MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene lig (MPN357)
Name 
lig
Stable ID 
MPN357
Location 
425535 - 427511 -
Sequence 
    1  ATGGCAAAGG TCGCACAAAT TCGAGCAATA GTTGAACAGT TAAAACGCTA TGATTACCAT
   61  TACTATGTTT TGGACGATCC GCTGGTCAGT GACTTTGAAT ACGACCAGTT ATACAAACAG
  121  CTGCAAGCGT TGGAACAAGC CCATCCTGAG TTAATCCAAC CCGATTCACC AACCCAACGT
  181  GTTGGGGGAA TTGTAGTGGA AGCATTTAAT AAGTTTCCTC ACCAAAATCC AATGCTTTCC
  241  CTAGACAATG CCTTCGACAC AGCAACAATT GCTAGTTTTA TTGCCAACAT TAACAACTTA
  301  ACTGGAGTGC AAAACCGCTT TGTGGTGGAA CCCAAAATTG ATGGTGTAAG CATCTCTTTA
  361  ACTTACGAAA ACGGATTGTT AACTCGGGCT TTAACCCGCG GTGATGGACT TGTGGGTGAG
  421  GATGTTTTGA GTAATGTTAA AACGATTAAG AGCATTCCCC TAACGATTCC CTTTCACAAA
  481  CAGGTGGAAA TCCGCGGTGA GATCTTTGTC GATAAAAAAA CATTTGCGCA AATTAACGAG
  541  AATTTAGCAA AACCGTTTGC CAATGCCCGC AATTTAGCAG CAGGTACACT ACGGAACCTC
  601  AACAGTGAGG TGAGTGCCAA GCGCAAACTT AAGGCCTTCT TTTACTTTGT TCCCAACGCC
  661  TTAACTTTGG GTTGTAGGAG TCAAAGTGCC GTGTTAGCAC AGTTAAAGCA GTGAAACTTT
  721  CCAGTGTCCA AAGCGGTGGC TAGCTTTGAT CGACCCGAAG CATTAATTGA ATACCTCGAG
  781  CAGTTTGACC AAACACGTGA TCAGTTGAAC TTCCAAGTCG ATGGCCTAGT GGTTAAACTA
  841  GATAACTTTC ACTTTTACGA CCAGTTAGGG TTTACTAGTA AGTTTCCCCG TTGGGCGTTG
  901  GCGTACAAGT TTAAACCGAA GTTTGTCCAA ACCAAACTGC GTGGTGTCTT GGTAACAGTG
  961  GGACGCACTG GCAAGATTAA CTATACCGCG CAGTTAGATC CAGTTAACTT AGAGGGGACA
 1021  GTAGTATCAG CAGCCACACT GCATAACTTT GACTACATTA AGGAGAAGGA CATTCGTTTA
 1081  AACGATACAG TGATAATTTA CAAAGCGGGG GAAATTATCC CTAAGGTATT GGAGGTGTGT
 1141  TTACCGTTAA GAACAGCAGC GAATCAACCG ATTCCCGAAC AAACCCACTG TCCGGCATGT
 1201  CAAGCCCCGT TAGTGCAGTA TAAGGATGAG GTAGATCAGT ACTGTACCAA TGAACGTTGT
 1261  GACCAGCGTA ACCTTGAAGC GATTAATTAC TTTGTGTCCA AAACGGCTAT GGACATCCAG
 1321  GGGCTAAGTA TCCAGACCAT TAGTAAGCTG TATGAAAATA ACTTAGTGCG CAGCGTCGTT
 1381  GATTTATACC ACTTAAAGGA GCACAAAGCC GCGGTGTTAG CCTTGGAACT TAAAATTGGT
 1441  GAAGTGCTGT TCAATAAACT AATCAGCAGC ATCGAACAGT CCAAAACCAA GGGGATGGCA
 1501  CGCTTGTTAA CTGGGCTTGG CATTAAACAT GTGGGGCAAG TGTTAGCCAA AAGCTTAACG
 1561  AAGCACTTTG AAAACATCGA TGCCTTACAA TCCGCCAGTA TGGAAACACT GTTAGAACTC
 1621  CCTGATGTGG GACCGACTGT GGCAGAATCG TTGTTTAACT GGTTTCACAA TGACAATAAC
 1681  TTACAGCTGT TAGCTGCACT TAAAGCAGTT GGAGTGCAAA TGGATGCTTT AAAGAGCAAC
 1741  ACTAACTTTG ACACCGCGAG CATTTACTTT CAAAAGAGTT TTGTTATTAC TGGCAGCTTT
 1801  CCAATTAGTC GCGATACCAT TAAAAACTTG CTCGTCAATA AGTATGATTG TCGTTTTACA
 1861  AATAACGTCA CTAGTAAAGT TGATTTTGTG TTAGCTGGCA TTAAGGCTAC ACCTCGTAAA
 1921  CTTGAACAAG CTAAAGCCCT CAATATTCCC ATTATTAATG AACCAATTTG AACCTAA
Download Sequence
Operon 
OP452
Operon location 
424230 - 427650
Protein (mpn357)
Name 
DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD+])
Stable ID 
Mpn357
Molecular Weight 
72380
Isoelectric Point 
8
Localization 
SIGNALP
Comment (RN:R00382) NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m = AMP +nicotinamide nucleotide + (deoxyribonucleotide)n+m
Sequence 
MAKVAQIRAIVEQLKRYDYHYYVLDDPLVSDFEYDQLYKQLQALEQAHPELIQPDSPTQRVGGIVVEAFNKFPHQNPMLS
LDNAFDTATIASFIANINNLTGVQNRFVVEPKIDGVSISLTYENGLLTRALTRGDGLVGEDVLSNVKTIKSIPLTIPFHK
QVEIRGEIFVDKKTFAQINENLAKPFANARNLAAGTLRNLNSEVSAKRKLKAFFYFVPNALTLGCRSQSAVLAQLKQWNF
PVSKAVASFDRPEALIEYLEQFDQTRDQLNFQVDGLVVKLDNFHFYDQLGFTSKFPRWALAYKFKPKFVQTKLRGVLVTV
GRTGKINYTAQLDPVNLEGTVVSAATLHNFDYIKEKDIRLNDTVIIYKAGEIIPKVLEVCLPLRTAANQPIPEQTHCPAC
QAPLVQYKDEVDQYCTNERCDQRNLEAINYFVSKTAMDIQGLSIQTISKLYENNLVRSVVDLYHLKEHKAAVLALELKIG
EVLFNKLISSIEQSKTKGMARLLTGLGIKHVGQVLAKSLTKHFENIDALQSASMETLLELPDVGPTVAESLFNWFHNDNN
LQLLAALKAVGVQMDALKSNTNFDTASIYFQKSFVITGSFPISRDTIKNLLVNKYDCRFTNNVTSKVDFVLAGIKATPRK
LEQAKALNIPIINEPIWT
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation VGGIVVEAFNKFPHQNPmLSLDNAFDTATIASFIANINNLTGVQNR 61 107 M
Oxidation TAmDIQGLSIQTISK 435 450 M
Oxidation AVGVQmDALK 569 579 M
Oxidation aVGVQmDALK 569 579 M
GENE/PROTEIN lig (Domains Overview)
Click on the features to jump to domain info

 ExportIMG
Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-305 SSF56091 (n.a.) NULL 0
1-658 PIRSF001604 (IPR001679) NAD-dependent DNA ligase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
2-436 SM00532 (IPR013840) NAD-dependent DNA ligase, N-terminal Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
3-307 PF01653 (IPR013839) NAD-dependent DNA ligase, adenylation Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
5-60 G3DSA:1.10.287.610 (n.a.) NULL 2.3e-23
6-654 PTHR11107 (n.a.) NULL 0
6-654 PTHR11107:SF5 (n.a.) NULL 0
10-657 TIGR00575 (IPR001679) NAD-dependent DNA ligase Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
112-141 PS01055 (IPR018239) NAD-dependent DNA ligase, active site Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
116-241 G3DSA:3.30.470.30 (n.a.) NULL 3.89561e-43
306-391 SSF50249 (IPR016027) Nucleic acid-binding, OB-fold-like 1.3e-27
310-379 G3DSA:2.40.50.140 (IPR012340) Nucleic acid-binding, OB-fold 2.7e-29
310-389 PF03120 (IPR004150) NAD-dependent DNA ligase, OB-fold Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

2.9e-30
320-335 PS01056 (IPR018239) NAD-dependent DNA ligase, active site Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0
392-577 SSF47781 (IPR010994) RuvA domain 2-like 0
396-420 PF03119 (IPR004149) Zinc-finger, NAD-dependent DNA ligase C4-type Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006260'>'DNA' == '' ? '': 'DNA'; 'replication' == '' ? '': 'replication'; ('GO' == '' ? '': 'GO';:0006260) <'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003911'>'DNA' == '' ? '': 'DNA'; 'ligase' == '' ? '': 'ligase'; ('NAD' == '' ? '': 'NAD';+) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003911)

0.0000083
425-494 G3DSA:1.10.150.20 (n.a.) NULL 3.5e-19
434-453 SM00278 (IPR003583) Helix-hairpin-helix DNA-binding motif, class 1 Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003677'>'DNA' == '' ? '': 'DNA'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0003677)

180
495-575 G3DSA:1.10.150.20 (n.a.) NULL 1.2e-28
535-554 SM00278 (IPR003583) Helix-hairpin-helix DNA-binding motif, class 1 Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006281'>'DNA' == '' ? '': 'DNA'; 'repair' == '' ? '': 'repair'; ('GO' == '' ? '': 'GO';:0006281)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003677'>'DNA' == '' ? '': 'DNA'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0003677)

0.12
582-654 SSF52113 (IPR001357) BRCT Cellular Component:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0005622'>'intracellular' == '' ? '': 'intracellular'; ('GO' == '' ? '': 'GO';:0005622)

0.00000016
588-654 G3DSA:3.40.50.10190 (n.a.) NULL 0.0000000000024
590-654 PF00533 (IPR001357) BRCT Cellular Component:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0005622'>'intracellular' == '' ? '': 'intracellular'; ('GO' == '' ? '': 'GO';:0005622)

0.0013
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
6 654 648 - b2411 Escherichia coli 7 662 <1e-50 37.6506 1128
6 569 563 - b3647 Escherichia coli 33 552 2e-22 21.2329 251
1 657 656 - MARTH_orf373 Mycoplasma arthritidis 1 659 <1e-50 35.3204 988
7 654 647 - MAG2820 Mycoplasma agalactiae 10 645 <1e-50 37.5 1027
6 657 651 - MCJ_004700 Mycoplasma conjunctivae 9 663 <1e-50 34.9776 964
6 654 648 - MCAP_0712 Mycoplasma capricolum subsp. capricolum 9 656 <1e-50 40.2736 1245
7 657 650 - MYCGA7000 Mycoplasma gallisepticum 15 715 <1e-50 41.2268 1417
6 658 652 - MG254 Mycoplasma genitalium 7 659 <1e-50 66.3093 2296
1 654 653 - MHP7448_0266 Mycoplasma hyopneumoniae 7448 1 679 <1e-50 34.6264 980
13 654 641 - MHO_2000 Mycoplasma hominis 20 659 <1e-50 34 968
4 654 650 - MMOB1950 Mycoplasma mobile 17 664 <1e-50 37.6328 1053
6 654 648 - MSC_0764 Mycoplasma mycoides subsp. mycoides SC 9 656 <1e-50 40.2736 1238
6 657 651 - MYPE1840 Mycoplasma penetrans 25 699 <1e-50 44 1532
7 654 647 - LIC_13282 Leptospira interrogans serovar Copenhage 21 663 <1e-50 35.7143 1008
14 654 640 - MS53_0567 Mycoplasma synoviae 17 685 <1e-50 33.9706 999
6 654 648 - Rv3014c Mycobacterium tuberculosis 16 676 <1e-50 35.503 1022
5 654 649 - Lactococcus lactis subsp. lactis KF147 5 648 <1e-50 38.9908 1147
4 551 547 - Caulobacter crescentus NA1000 15 595 <1e-50 35.3846 848
3 654 651 - Bacillus subtilis subsp. subtilis 4 659 <1e-50 41.4781 1257
3 654 651 - Bacillus subtilis subsp. subtilis 4 659 <1e-50 41.4781 1257
12 654 642 - Mycoplasma pulmonis 17 671 <1e-50 36.4865 926
277 633 356 - Mycoplasma pulmonis 1 355 <1e-50 36.1878 527
External IDs
COG 
COG0272L
EC number 
6.5.1.2
Gene ID 
876856
GI 
13508096
GO 
DNA replication, recombination and repair
Home COG 
L
InterPro 
IPR013839|NAD-dependent DNA ligase, adenylation
InterPro 
IPR013840|NAD-dependent DNA ligase, N-terminal
InterPro 
IPR010994|RuvA domain 2-like
InterPro 
IPR008994|Nucleic acid-binding, OB-fold
InterPro 
IPR004150|NAD-dependent DNA ligase, OB-fold
InterPro 
IPR004149|Zinc-finger, NAD-dependent DNA ligase C4-type
InterPro 
IPR003583|Helix-hairpin-helix DNA-binding, class 1
InterPro 
IPR001679|NAD-dependent DNA ligase
InterPro 
IPR001357|BRCT
InterPro 
IPR000445|Helix-hairpin-helix motif
Old MP number 
MP479
Pathway 
Division, DNA maintenance
PDB homologs 
1v9p_A
PDB homologs 
1dgs_A
PDB homologs 
1b04_A
Pfam 
PF03120
Pfam 
PF00533
Pfam 
PF01653
Pfam 
PF03119
Pfam 
PF00633
PID 
g1674170
RefSeq 
NP_110045.1
Swiss-Prot protein ID 
DNLJ_MYCPN
phylomeDB tree 
DNLJ_MYCPN
UniProt 
P78021
Transcription
IMAGE BROWSERS

OPERON OP452 (Genomic Overview)
Region:424230-427650

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STRING image

STRING of Mpn357STRING legend

PDB image(s)

1v9p

PDB 1v9p

1dgs

PDB 1dgs

1b04

PDB 1b04
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