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Database: UniProt/TrEMBL
Entry: C1GEB6_PARBD
LinkDB: C1GEB6_PARBD
Original site: C1GEB6_PARBD 
ID   C1GEB6_PARBD            Unreviewed;      1021 AA.
AC   C1GEB6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PADG_05602 {ECO:0000313|EMBL:EEH49523.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis;
OC   Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH49523.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH49523.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH49523.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A.,
RA   Goldberg J., Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M.,
RA   Grynberg M., Gujja S., Heiman D.I., Henn M.R., Kodira C.D.,
RA   Leon-Narvaez H., Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L.,
RA   Morais F.V., Pereira M., Rodriguez-Brito S., Sakthikumar S.,
RA   Salem-Izacc S.M., Sykes S.M., Teixeira M.M., Vallejo M.C.,
RA   Walter M.E., Yandava C., Young S., Zeng Q., Zucker J., Felipe M.S.,
RA   Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G., Puccia R.,
RA   San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(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; KN275962; EEH49523.2; -; Genomic_DNA.
DR   RefSeq; XP_010760812.1; XM_010762510.1.
DR   EnsemblFungi; EEH49523; EEH49523; PADG_05602.
DR   GeneID; 22584501; -.
DR   KEGG; pbn:PADG_05602; -.
DR   EuPathDB; FungiDB:PADG_05602; -.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000001628; 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; 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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 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   Complete proteome {ECO:0000313|Proteomes:UP000001628};
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:EEH49523.2};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT   DOMAIN      425    550       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      719    804       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      937   1020       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   1021 AA;  116675 MW;  56B11B30838C9D91 CRC64;
     MDSDVENEVD DVRQGADTEA DLDEKYPNRP RNHSPTLPFH DLFLTLFNPL NENKKRPTGP
     AVARRKVGPH GLGAAVHLSP QELRRDIIQR FISRWRKEVG NDVFPAFRLI IPEKDRYRAM
     YGLKEKAIGK LLVKVMKIDK NSEDGFSLLN WRLPGQTFAS RMAGDFAGRC FEIISKRPMR
     TEVGDMTIEE VNEQLDKLSA ASKEDEQVPI LEYFYRRMNP EELMWLIRII LRQMKVGATE
     RTLFNLWHPD AEALFSISSS LRRVCWELYN PNVRLEGDEA KVTLMQCFQP QLAQFQVQSF
     DRMIQRMRLA EDDPTFWIEE KLDGERMQLH MQTDDSIPGG KRFVFWSRKA KDYTYLYGNG
     LLDENGALTR HLQNAFADGV QSIILDGEMI TWDPEHDAIV PFGALKTAAL AEQRNPCSTG
     QRPLFRIFDI LYLNGRALTR YILRDRRRAL EASVIPVHRR FEIHTYEIGR STADIEPLLR
     KVVAEASEGL VLKNPNSPYR LNERHDDWMK VKPDYMTEFG ESLDCVVVGG YYGSGRRGGA
     LSSFLCGLRV DGAHAKKGDK PTKCYSFCKV GGGFTAADYA NIRHHTDGKW MDWDPKRPPT
     EYIELGGDDA QHERPDVWIK PEDSVVLCIK AAQVTPSDQF RLGLTLRFPR FKRLRMDKNW
     QSALTVQEFM DFKSNVEKEV KEKELRFDDT RRPRHKKSTK KPLTVAGYEG GKKTAYASPS
     GKLFDGLNFF IITESMQEPK KTKAQLEQLV KANGGKLYQT NTAAENTICI ADHRTVKVAS
     LQKNAKENVV RPSWLFDCLK QNEIDQGLPD LLIPLEPKHM FFTTADQEEE IAGNVDKYSD
     SYARDVDVSE LTKLLDEMPT VPNTTFSSIS QLESHIGHML DQTASFNNSS KGWLFKGLVI
     YFAAPQPASP SLCSSLQNDN LKEEKQRLPQ CLYLASNLVK FAGGQVITDD NDMTDPRITH
     IVIDANTDDK TIMATEISAI RRKIATRTGI NKRIPHLVGV EWVEESWRKK TLVDEDRFAP
     K
//
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