(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7X0_ASPNC

ID   A2Q7X0_ASPNC            Unreviewed;       242 AA.
AC   A2Q7X0;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Ribonuclease P protein subunit {ECO:0000256|PIRNR:PIRNR027081};
GN   ORFNames=An01g02230 {ECO:0000313|EMBL:CAK43593.1};
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:CAK43593.1, 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).
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DR   EMBL; AM269955; CAK43593.1; -; Genomic_DNA.
DR   RefSeq; XP_001388661.1; XM_001388624.1.
DR   PaxDb; A2Q7X0; -.
DR   EnsemblFungi; CAK43593; CAK43593; An01g02230.
DR   GeneID; 4977688; -.
DR   KEGG; ang:ANI_1_294014; -.
DR   HOGENOM; HOG000175595; -.
DR   KO; K03538; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:InterPro.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
DR   Gene3D; 2.30.30.210; -; 1.
DR   HAMAP; MF_00754; RNase_P_1; 1.
DR   InterPro; IPR002730; RNase_P/MRP_p29.
DR   InterPro; IPR016848; RNase_P/MRP_p29-subunit.
DR   InterPro; IPR036980; RNase_P/MRP_p29_sf.
DR   InterPro; IPR023538; RNP1.
DR   InterPro; IPR023534; Rof/RNase_P-like.
DR   Pfam; PF01868; UPF0086; 1.
DR   PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR   SMART; SM00538; POP4; 1.
DR   SUPFAM; SSF101744; SSF101744; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7X0.
DR   SWISS-2DPAGE; A2Q7X0.
KW   Nucleus {ECO:0000256|PIRNR:PIRNR027081};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR027081}.
FT   DOMAIN          123..237
FT                   /note="POP4"
FT                   /evidence="ECO:0000259|SMART:SM00538"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   242 AA;  27702 MW;  20838A1FCBAFB054 CRC64;
     MTTPKPHIAH TLLSRAHSPD TASQLFTERI KQKPLYVRPT SPTPADNRSR RRLHRLRKKE
     YFLRKQKPQP LSARQKRASG LYNLPKEECK YAVFQELHAM WVRYMQDMLD LGAKKFKPPM
     TPLSHGSKLS SADFHGAEVE VVRSRCEGRV GVKGIVVRDT KFTFVVVTRG DEVKTIPKEQ
     TIFRFSVPLP EADDADGAAV TGETSADSAK KELVFELHGS QFQNRPVDRA NKKFKWRNVD
     YI
//

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