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Database: UniProt/TrEMBL
Entry: G0S6M3_CHATD
LinkDB: G0S6M3_CHATD
Original site: G0S6M3_CHATD 
ID   G0S6M3_CHATD            Unreviewed;      1032 AA.
AC   G0S6M3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   20-DEC-2017, entry version 31.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=CTHT_0026720 {ECO:0000313|EMBL:EGS20834.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS20834.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; GL988041; EGS20834.1; -; Genomic_DNA.
DR   RefSeq; XP_006693130.1; XM_006693067.1.
DR   EnsemblFungi; EGS20834; EGS20834; CTHT_0026720.
DR   GeneID; 18256710; -.
DR   KEGG; cthr:CTHT_0026720; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000617};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008066};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT   DOMAIN      459    582       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      758    844       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      926   1031       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   COILED      704    724       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1032 AA;  116646 MW;  2966B9E52BD0E987 CRC64;
     MSATKKRTKS PDPEAVEEDE KQYGNGPLTL EELDQQPRNH SKTFLFSELY KSLFNPLIEC
     KPHPPGAATT ATTAAAKGRP GRRGANPSKV SYHEQRRHII ERFMARWRAD VGDDFYPAMR
     LILPDKDRDR GVYGLKESAI GRLLVKVMKI DRHSEDGYAL MHWKLPGGAG GWKFGGGGGG
     GGGGGGNGKG AGTAGDFAAR CYEIVGKRAM RTEPGNLTIA DVNVMLDRLA RANGEAEQLP
     IFEEFYRRMN AEELMWLVRI ILKDMKVGAT ERTFFNLWHP DAEALFSVSS SLRRVCWELY
     DPEFRLEQEE TGVTLMSCFQ PQLAQFQMQG SFAKLVANLG VTEEEPEFWI EEKLDGERMQ
     MHMMEDESVP GGFRFAFWSR KAKDYTYLYG NSLEDDKSAL TRHLKNAFHP GVRNLILDGE
     MITWDPEVDK IMPFGTLKTA ALEQQKNPFA SGPRPLYRVF DILLLNDKSL TDYTLADRRR
     ALERAVKGVP RRLEIHPYEK ATSADAIEPA LRKIISESSE GLVLKNPRSR YRLNSRNNDW
     IKVKPEYMSE HGESLDCVII GGYYGSGRRG GTLSSFLCGV RVSENFTRSG AASKTEKCLS
     FCKVGGGFKG EDYAEIRHHT EGKWKDWDPS NPPSEYIELG GGERLQHERP DVWIRPSESV
     VISIKAASFG PSDQFATGYT LRFPRFRALR LDKAWDQAMD VDECDAIRTK VKEEEQERKA
     MEIENRKRRP TKRQKREIVV AGTDPNASAP LEFAVPLTNK QLFKGLEFCV LSEGLRPRKI
     SKPELEELIK KHGGTIKQKV DPASVRGGGT IVLADKNVVR AASLKKAGGV DIVRPRWVFD
     CLERTGGEGY LLPFETDRHL LHATEGMKLV ARDNTDAYGD SYARDVGIDE LREILDRMNL
     PERSKEFDAG LFLDQLEEHG HGLEEMRSFL FRRCRVYFAV AEGKEGSETE VIRLGYYIRF
     GNGEIVESIK DRKDITHMVV VAGSKEQERI VAVDMRYKVS SWRAIPRIVT PKWVEDCWKE
     GTVVDEEAYA PC
//
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