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Database: UniProt/TrEMBL
Entry: A0A010SCH0_9PEZI
LinkDB: A0A010SCH0_9PEZI
Original site: A0A010SCH0_9PEZI 
ID   A0A010SCH0_9PEZI        Unreviewed;       997 AA.
AC   A0A010SCH0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-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=CFIO01_01863 {ECO:0000313|EMBL:EXF82403.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF82403.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF82403.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF82403.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF82403.1}.
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DR   EMBL; JARH01000321; EXF82403.1; -; Genomic_DNA.
DR   RefSeq; XP_007593983.1; XM_007593921.1.
DR   EnsemblFungi; EXF82403; EXF82403; CFIO01_01863.
DR   GeneID; 19031713; -.
DR   KEGG; cfj:CFIO01_01863; -.
DR   KO; K10777; -.
DR   Proteomes; UP000020467; 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; 2.
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; 2.
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:UP000020467};
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:EXF82403.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT   DOMAIN      436    559       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      726    812       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      893    996       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   997 AA;  114223 MW;  1F089525826B64FF CRC64;
     MSQRKRQKSP DAAAIDEEER HYAIGGTTLD ELNEKYPNRP RNHSKTMRFS ELFQSLFNPL
     NENKKQPAGR GPPRSKKGPH GPHKPSPQEQ RRHLIERFIS RWRNEVGNDI YPALRLILPD
     KDRDRGVYGL KENAIGKILV KLMKIDKNSE DGHNLLHWKL PGQTTFSRLA GDFAGRCFEV
     LSKRPMRTEV GDMTIAEVNE LLDKLAASTG ELENLEVFEI FYERMNAEEL MWLIRIVLKQ
     MKVGATERTF LDLWHPDGEA LFSVSSSLRR VCWELFDPRI RLEQENTGVT LMECFQPQLA
     QFQMPSSFQK MVDYLRTTEE DPEFWIEEKL DGERMQMHMA EDPSVSGGLR FCFWSRKAKD
     YTYLYGNGLK DEKGALTRHL ADAFSEGVRN VILDGEMITW DPEVDKIMPF GTLKTAALAE
     QNNPYNNTGP RPLYRVFDIL LLNDQPLTQY TLRDRHRALE KAVKGVHRRL EIHEYESATT
     PEAIEPLLRK VVAEASEGLV LKNPRSMYRL NSRNDDWLKV KPEYMSEFGE SLDCVVIGGY
     YGSGHRGGAI SSFLCGLRVS ENHIQAGANP EKCFSFFKVG GGFTAADYAE IRHRTDGKWT
     TWDPKKPPVE YIELAGGDRQ FERPDVWIRP SESVVVEAKA ASIGNSDQFA LGFTLRFPRF
     RKLRTDKNWD EGLSVQEFLD LRRRVEAEAK EKTMSVENRK RKSVKRVKRE VVIAGTENMP
     AQFQADKSKV FEGLEFCVLS ESLKPFKKTK AQLETLIKEN GGQVSQRAVP QSGMILLADK
     NVVKVASLVK EGQKGSGVDI IRPKWIQDCL EQADDSLLVP YEERHLLHAT EALKTVALQN
     TDMYGDSYAR DISLVELREV LNMMPKKEPD TEPFNKTQFL NQLEERGRGV GPMKGSMFHR
     CAVHLVNVEE GDEDEIKMLK LRNYLTFGGA RLISDVDDTE ATHMVVVGAD TRRKDAAAAL
     REEVSRRRKI PHIVTAEWIE DCWREKTLLD EEKYTRV
//
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