(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8L0_ASPNC

ID   A2Q8L0_ASPNC            Unreviewed;       500 AA.
AC   A2Q8L0;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 57.
DE   RecName: Full=DNA primase large subunit {ECO:0000256|PIRNR:PIRNR009449};
DE            EC=2.7.7.- {ECO:0000256|PIRNR:PIRNR009449};
GN   ORFNames=An01g04720 {ECO:0000313|EMBL:CAK37007.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK37007.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {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   -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA
CC       primers for the Okazaki fragments made during discontinuous DNA
CC       replication. {ECO:0000256|PIRNR:PIRNR009449}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009449};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR009449};
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000256|PIRNR:PIRNR009449}.
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DR   EMBL; AM269963; CAK37007.1; -; Genomic_DNA.
DR   RefSeq; XP_001388899.1; XM_001388862.2.
DR   PaxDb; A2Q8L0; -.
DR   EnsemblFungi; CAK37007; CAK37007; An01g04720.
DR   GeneID; 4978025; -.
DR   KEGG; ang:ANI_1_610014; -.
DR   HOGENOM; HOG000212154; -.
DR   KO; K02685; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd07322; PriL_PriS_Eukaryotic; 1.
DR   InterPro; IPR016558; DNA_primase_lsu_euk.
DR   InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR   PANTHER; PTHR10537; PTHR10537; 1.
DR   Pfam; PF04104; DNA_primase_lrg; 1.
DR   PIRSF; PIRSF009449; DNA_primase_large_subunit; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q8L0.
DR   SWISS-2DPAGE; A2Q8L0.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR009449, ECO:0000256|PIRSR:PIRSR009449-1};
KW   DNA replication {ECO:0000256|PIRNR:PIRNR009449};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR009449};
KW   DNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR009449};
KW   Iron {ECO:0000256|PIRNR:PIRNR009449, ECO:0000256|PIRSR:PIRSR009449-1};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR009449, ECO:0000256|PIRSR:PIRSR009449-
KW   1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR009449,
KW   ECO:0000256|PIRSR:PIRSR009449-1};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR009449,
KW   ECO:0000313|EMBL:CAK37007.1}; Primosome {ECO:0000256|PIRNR:PIRNR009449};
KW   Transcription {ECO:0000256|PIRNR:PIRNR009449};
KW   Transferase {ECO:0000256|PIRNR:PIRNR009449, ECO:0000313|EMBL:CAK37007.1}.
FT   METAL           307
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   METAL           390
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   METAL           407
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   METAL           448
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
SQ   SEQUENCE   500 AA;  58518 MW;  8F441DA4BAD3CF1E CRC64;
     MIRQDFRRID PKRRATLDHK KKQFATPVFK QQDYPHRLNF YEVPPTDEIT LEQFEQWAID
     RLKVLAEIEA CSYRNKSPAE TEAHITPHLQ KYLPLSSNTS SSNGAADQRL KNERQKDHYS
     HFILRLAFSA TEELRRRFVR AETMLFRFRF QRDDTRERRA FIESLNLDWE PVDDEEKQRL
     AEQLLAASPG LRRIDDETWY KVDWEKVPEL VERRAVFLSK GKAYVPGREQ LSMIIAEFTA
     RLERALELTS RALPRLDEDD RLTPILNHLS KNFGSAESVY TENEGFVDGA PITANNIDRL
     SQHFPLCMRS LHMNLRKNNH LKHYGRLQYT LFLKGIGLSL EECIVFWRQG FKGLTDDEFN
     SRYKYNIRHA YGDVGGDQNR RGRGYPPYSC QKILGDSNPG VGQTHGCPYR HFSVDNLIGL
     LQSTGVNDRD VLRGVREDVE KMRFHIACNR VFEHTHKADI KRVKEDGTWN QTDLDTIVHP
     NTYFKRSYLL KQMGKAPKNA
//

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