(data stored in SCRATCH zone)

SWISSPROT: Q75CS4_ASHGO

ID   Q75CS4_ASHGO            Unreviewed;       697 AA.
AC   Q75CS4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=AGOS_ACL155W {ECO:0000313|EMBL:AAS51073.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51073.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51073.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={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; AE016816; AAS51073.1; -; Genomic_DNA.
DR   RefSeq; NP_983249.1; NM_208602.1.
DR   STRING; 33169.AAS51073; -.
DR   EnsemblFungi; AAS51073; AAS51073; AGOS_ACL155W.
DR   GeneID; 4619369; -.
DR   KEGG; ago:AGOS_ACL155W; -.
DR   HOGENOM; HOG000036006; -.
DR   InParanoid; Q75CS4; -.
DR   KO; K10747; -.
DR   OMA; PYPDWKP; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006284; P:base-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IBA:GO_Central.
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:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 1.
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; IPR012340; NA-bd_OB-fold.
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   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CS4.
DR   SWISS-2DPAGE; Q75CS4.
KW   ATP-binding {ECO:0000256|RuleBase:RU000617};
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:UP000000591}.
FT   DOMAIN          441..578
FT                   /note="DNA_LIGASE_A3"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          45..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  76963 MW;  95E4EBF0F2CDB522 CRC64;
     MSAPKKQATL GRFFTALKRP QDGATAAATV KKSKVEAAEC LAAPAGHEQD AEVKNSLPEL
     ADKPAPGGVL PQAASAVPRA QSSPVKPAAS TSVMYADLCA VFEAVEATSS RLSITKLCAD
     FMYSVLKCDP GHLIPVTYLF INRLGPDYEP GLELGLGEGI LIKTISDACG KSAAQVRSSY
     RECGDLGTVA QQARVVQPTM FKPKPLTVRD VFSTLQAIAQ AEGKDSQGKK IRLIKKMLTA
     CQGMEAKYLI RSLESKLRIG LAEKTVLVAL SKAILTHEHD GKEPSPEQVD AAEALVRDTF
     CQVPNYEMII NAALQYGIMN LPQHCVLTPG IPLKPMLAKP TKSITEVLDR FQGQRFTCEY
     KYDGERAQVH LMEDGTIRIY SRNSENMTER YPEIQFHQFL ANPQTTRSLI IDCEAVAWDN
     EKQKILPFQV LSTRKRKGVE LKDVKVRVCL FAFDLLYLNG ESLLKCSLAD RRKHLYSVLK
     VVPGELQFAN EITTMELSEL QTYLEQSVSA SCEGLMVKML DGEESQYEPS KRSRNWLKLK
     KDYLEGVGDS LDLAVLGAYY GRGKRTGTYG GFLLGCYNPD LEEFETCCKI GTGFSEEVLQ
     SLHAQLKDTV IAAPRGDVSY DDSSPPDVWF EPAMLFEVLT ADLSLSPVYK AGRDVYGKGI
     SLRFPRFLRI REDKSVTDAT SSDQIVEFYQ RQANSSG
//

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