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Database: UniProt/TrEMBL
Entry: A1CBF1_ASPCL
LinkDB: A1CBF1_ASPCL
Original site: A1CBF1_ASPCL 
ID   A1CBF1_ASPCL            Unreviewed;      1029 AA.
AC   A1CBF1;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-SEP-2017, entry version 68.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   ORFNames=ACLA_015070 {ECO:0000313|EMBL:EAW13069.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 /
OS   NCTC 3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13069.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW13069.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027049; EAW13069.1; -; Genomic_DNA.
DR   RefSeq; XP_001274495.1; XM_001274494.1.
DR   ProteinModelPortal; A1CBF1; -.
DR   STRING; 5057.CADACLAP00001394; -.
DR   EnsemblFungi; CADACLAT00001413; CADACLAP00001394; CADACLAG00001413.
DR   GeneID; 4706930; -.
DR   KEGG; act:ACLA_015070; -.
DR   EuPathDB; FungiDB:ACLA_015070; -.
DR   HOGENOM; HOG000176213; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000006701; 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; 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:UP000006701};
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:EAW13069.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   DOMAIN      418    552       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      721    806       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      915   1024       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   1029 AA;  117611 MW;  12350CBF4A8E68BA CRC64;
     MNSDDIGPDE GHPRAPVENE ESDLDEKYPN RPRNHSSTLP FHELFQTLFN PLSEIKKKPA
     GAVAARRKVG PHGQSAANLN PLERRRDVIE RFISRWRKEV GDDIYPAFRL ILPDKDRDRA
     MYGIKEKAIG KMLVKIMKID KNSEDGFNLL NWKLPGQAAA TRMAGDFAGR CYDVLSKRPM
     RTDVGDMSIE EVNEKLDNLS AASKEEQQLP ILAEFYRRMN PEELMWLIRI ILRQMKVGAT
     ERTFFDVWHP DAENLYSISS SLRRVCWELH DPNIRLDAED RGISLMQCFQ PQLAQFQMQS
     LDKMVSRMRP TEDDPVFWIE EKLDGERMQL HMESDDSVPG GRRFRFWSRK AKEYTYLYGN
     GIYDENGSLT RHLKDAFADG VDSLILDGEM ITWDPEQDAP APFGTLKTAA LAEQRNPFST
     TGARPLFRVF DILYLNGRDL TGYTLRDRRN ALQKSVRPVH RRFEIHPYEE ATTKDEVEVA
     LRKVVAEASE GLVLKNPRSP YRLNERHDDW MKVKPEYMTE FGESLDLIVI GGYFGSGRRG
     GNLSSFLCGL RADDTHASQG SNASKCYSFC KVGGGFNAAD YANIRHHTDG KWVEWNPKKP
     PTAYIELAGK DAQYERPDMW IKPEDSVVVC VKAASVSVSD QFRIGLTLRF PRFKRLRMDK
     DWRSALSVQG FLDLKSNVEQ EHREKEFSVD NFRRKRIKRT TKKPLAVAGY DADEEAKYAG
     PSGHIFEGLN FYILTDANAP VKKSKQELEQ LVKANGGKFY QTNNAAPHTV CIADRRTVKA
     ASLQKSGNVD IIRPSWLLDC VKQNEIDAGL PDLLLPMEPK HMFFARPEKQ EEVAANVDQF
     NDSYARNTTS EELKNVLFLP NWWLRKTSAD CFKTLHQMMK EHRFKGSQCP EGIAKLTERI
     QERVHSGYEI PCGWLFKGLT ILFQHRSMDD TGSSGNTVPS DHSYRLRLAI NTARFAGANI
     ASSPNQASIT HVVVDPESPS SEISSLRGTW SKKQGQKVPH IVAVDWIEES WKERTLLDEE
     RFQPKRSKA
//
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