ID A5AAE3_ASPNC Unreviewed; 1038 AA.
AC A5AAE3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Contig An02c0310, genomic contig {ECO:0000313|EMBL:CAK44385.1};
DE EC=6.5.1.1 {ECO:0000313|EMBL:CAK44385.1};
GN ORFNames=An02g10370 {ECO:0000313|EMBL:CAK44385.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK44385.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK44385.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; AM270026; CAK44385.1; -; Genomic_DNA.
DR Proteomes; UP000006706; Chromosome 4R.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd08039; Adenylation_DNA_ligase_Fungal; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR029710; LIG4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR45997:SF2; ATP DEPENDENT DNA LIGASE DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_5G02430); 1.
DR PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAK44385.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 368..512
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 659..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 117449 MW; 750D1ABFEC6EA468 CRC64;
MGFKFARLCD LLSALEDNRI LKAAHEAKVV NPDIRAVSRW FAQNDKQIHD KDTDQLALLS
CIFPEKRTDR VYWLQDTSLA KIIARCLLLG CSRRQELERW RVSGGVDLGQ CVENVMRQAE
NHVTNGQDVT VEEIDKALAE IASRCKFSGP RVRRQRTAVK VDQTLSSLYR RLSSRDAKWL
TRMILKSYSP VSLXTNMILK RFHFLLPHLL LFQDSFEHAL SVLGTSPIRH FPPQPEPALA
KDLGSIALGH LSPAVGVKIG RPEYYKARSI KHCCRMVGNR RMSIERKYDG EYCQIHIDLS
KDSNWIQIFS KSGKDSTADR AGIHQVINES LNLRRPDFHK LRKFISRSGT FIGTESDSPP
QPYEHLMIVF FDILLIDDNV CLRLPHRERR LLLKDIIEPI PGRADISEQW VVDFSHHGGQ
SRLESVFHKG IDERWEGFVL KACEDPYFTI FSDDKDNPSF GRWIKLKKDY IPGLGDTVDL
AIIGARYNSR DAMAIKQVKK LLWTEFFIGC LVNKEMVVQC GAIPKFRVLD VINHKCMHVR
FMQFLNQYGE FCARSPDSEH GFNIEYGESV VSPMDVVFKT PFVVEMLGSG FEKPSGARYY
TLRFPRILKV LSDRSFEDAA SYRELQLLAE TARTVLDEDP GTHEYEAAKR MKLRDCTECT
PEGSQSFQTT QSPCLQSSTT AKDDSSNGAF VSLPNKASNA PDALPGSTRQ TKRRRESCAM
QRTIPIHVDL NRDPSPPVGH SVCGNYLTDN ENLSSHAAGQ RKNSTQPTDS SDAEKASRSC
RMPSPLTSLD KLQKHSLPVY TPLHCHIGSN VSQEICNRHR LGDEVVTAHL GQKPIRRILS
PLLHRLIYVH HGISSDHMAV SQSIPNALNI APTLKEFVCS LTRLESRTHP RTSNPHAVSH
YTACGLAMIP GKEDALCTVL PDLIKSIGNA FQSHKSNSHH HGGKVFILDS SFLKLKISNY
DTAIFPGQTW EDISKVFFYA CVSWTFNGTT GCGTFEKYQV GECDALYTRP KITVSFDRRE
LGRLEEIFRS ETPNTYPI
//
