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Database: UniProt/TrEMBL
Entry: K9GB89_PEND1
LinkDB: K9GB89_PEND1
Original site: K9GB89_PEND1 
ID   K9GB89_PEND1            Unreviewed;       974 AA.
AC   K9GB89;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   07-JUN-2017, entry version 24.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=PDIP_59620 {ECO:0000313|EMBL:EKV10581.1};
OS   Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV10581.1, ECO:0000313|Proteomes:UP000009886};
RN   [1] {ECO:0000313|Proteomes:UP000009886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the
RT   main postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EKV10581.1}.
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DR   EMBL; AKCU01000405; EKV10581.1; -; Genomic_DNA.
DR   RefSeq; XP_014533188.1; XM_014677702.1.
DR   EnsemblFungi; EKV10581; EKV10581; PDIP_59620.
DR   GeneID; 26234278; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000009886; 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; IPR021536; DNA_ligase_IV_dom.
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   Pfam; PF11411; DNA_ligase_IV; 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:UP000009886};
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:EKV10581.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      396    521       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      686    771       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      863    972       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   974 AA;  111804 MW;  99B99AE936AAEEC4 CRC64;
     MDSDEILSQE LLGQEKEEDI KANELKKKLS GPAPARRKVG PNGKGAASLN PFERRRDVIE
     RFISRWRKDV GNDIYPALRL ILPDKDRDRP MYGIKEKAIG KMLVKIMKIN KESEDGYNLL
     NWKLPGQGAT TRMAGDFAGR CFDVLSKRPM RTEPGDMTID EVNEKLDKLS AASKEDEQLP
     ILTEFYRRMN PEELLWLVRI ILRQMKVGAT ERTLFDVWHP DAENLYSISS SLRRVCWELH
     DPNIRLEGEE RGIALMQCFQ PQLAQFQMHS FEKIIARMKP TEDDHVFWIE EKMDGERMQL
     HMAPDDSIQG GRKFGFWSRK AKEYTYLYGN GIYDENGALT RHLKDAFVDG VQSIILDGEM
     ITWDPEQDAM VPFGTLKTAA LAEQRNPFSN APRPLFRVFD ILHLNGRDLT KYALRDRRNA
     LEKTIRPVYR RFEIHSYEEA TTTTEVEKAL RKVVAEASEG LVLKNPRSPY RLNERHDDWM
     KVKPDYMTEF GESLDVVVIG GYYGSGHRGG ALSSFLCGLR VDDSTQAAEK CWSFCRVGGG
     FTAADYQEVR HHTEGKWKVW DAKKPPTNFI ELAGGDAQHE RPDMWIKPSD SIVLCAKAAS
     VAISDQFRMG LTLRFPRFKK LRKDKDWKSA LSVQEFLDLK SNAEQEHREK EFSVDNSRKK
     RVKRATKKPL TVAGYDDNID VQYLEPSGHI FDELNFFVMT ESTSPEKKTK LQLEQLVKAN
     GGKIYQTKTA AVDTLCVADR RTVKVASLQR SGEQNIIRPS WLIDCIKQNE IDIGLPDLLL
     PFEPRHMFFM REDEEEEVVA NVDQFMDSYA RDTTVEELKE VFKQMEQNQE QPDHALDPET
     IQRVEARIQE KINAGYTVPC GWLFRGLKFY FHSNGDRQDE SASQELWKKS QPLYLARNTA
     RFAGAESASS LKSSGTTHVI VDPETLSSAD ISSLRKSLAE KPGAKMPHLV SASWVDECWK
     NRTLLDEERF PVPR
//
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