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Database: UniProt/TrEMBL
Entry: W3WI38_9PEZI
LinkDB: W3WI38_9PEZI
Original site: W3WI38_9PEZI 
ID   W3WI38_9PEZI            Unreviewed;       998 AA.
AC   W3WI38;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PFICI_14546 {ECO:0000313|EMBL:ETS73600.1};
OS   Pestalotiopsis fici W106-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS73600.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
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; KI912121; ETS73600.1; -; Genomic_DNA.
DR   RefSeq; XP_007841318.1; XM_007843127.1.
DR   EnsemblFungi; ETS73600; ETS73600; PFICI_14546.
DR   GeneID; 19279559; -.
DR   KEGG; pfy:PFICI_14546; -.
DR   KO; K10777; -.
DR   Proteomes; UP000030651; 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; 2.
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   Complete proteome {ECO:0000313|Proteomes:UP000030651};
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, ECO:0000313|EMBL:ETS73600.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT   DOMAIN      429    563       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      729    808       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      893    997       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   998 AA;  114820 MW;  4838C299EE47326A CRC64;
     MSQRRAKERD AGAVEEEVRQ YTFGGHTLEE FDENYPNRPK NHSRTLRFAE LFQNLFNPLN
     ENKKKPPGPA ARRKQRGGRG PSQLSPHEQR RAIIERFMSR WRAEVGNDFY PAMRLILPNQ
     DRDRGVYGLK ESAIGKLLVR TLKIDKYSTD GQSLLQWKRP GQKASQTAGD FAGRCLEVIA
     KRPMRSSPGD MRVAEVNEML DKLSAASGEA EQLPIIEDFY QKMSPEELMW LIRIILKEMK
     VGATERTFFD IWHPDAEALF NVSSSLRRVC WELYDRDVRL NDDDTGVTLM QIFQPQLAQY
     QYFGSWKKMV DQLTRDKENN TIREDAEFWI EEKLDGERMQ MHMMEDKTVP GGFRFGWWSR
     KAKDYAYLYG TGLRDRDSAL TQHLKNAFVP GVRSIILDGE MVTWDMQLDK IMAFGTLKSA
     ANAGKRNPYD EVGARCLYRV FDIVYLNGQE LTRYTLQDRR NALEKAVPGV HRRLELHDHL
     VSTSAADIEP HLRQVVENRS EGLVIKNPLS VYSLNQRNDD WIKVKPEYIK EYGEAVDVVI
     IGAYYGTGHR GGAHSSFLCG LRVTDDDIER GADPEKCFSF IRVGGGFALQ DYREIANRTQ
     GKWTDWNSKR PPSKYIELAG GERQWWKPDQ WIRPKDSVVI AVKAASSVPS DQYAKQITLR
     FPRFQKLRDD RDWDTALDWR QFEDLKTQIA VKQEEKEMNF ERRRRNTKRI KKEMVIMGQE
     ATPVEFGGPK TKLFQGLEFC VLSESVQPKK SKTQIEVLIK ENGGRISQRA IPNADMILIG
     DKKVLKVASL IKAGPVDIIS PKWVLDCVAQ SDASAGFLLP YEPRHLFHVS DEMKEQAQEN
     LDDYGDSYAR DIDVAELKAL LQDMPKNEII DEPFHSGAFV EQLEAHGHDI GNIKGHMFKR
     VVAHFATADN VLDISVLKYK NWVRFGGGII VDDLEDRSVT HVVVVAKDDD PRAERDLSAE
     IRSVISKRTQ IPRLVTRKWL EDCWTEGTML DEERFSPQ
//
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