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GRC3_ASPFU
ID   GRC3_ASPFU              Reviewed;         841 AA.
AC   Q4WID9; A4D9U7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Polynucleotide 5'-hydroxyl-kinase grc3;
DE            EC=2.7.1.-;
GN   Name=grc3; ORFNames=AFUA_2G02190;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EBA27309.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000008; EBA27309.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001481647.1; XM_001481597.1.
DR   AlphaFoldDB; Q4WID9; -.
DR   SMR; Q4WID9; -.
DR   STRING; 746128.CADAFUBP00001881; -.
DR   GeneID; 5076960; -.
DR   KEGG; afm:AFUA_2G02190; -.
DR   VEuPathDB; FungiDB:Afu2g02190; -.
DR   eggNOG; KOG2750; Eukaryota.
DR   HOGENOM; CLU_010345_1_2_1; -.
DR   InParanoid; Q4WID9; -.
DR   OrthoDB; 1217334at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; ISS:UniProtKB.
DR   GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045116; Clp1/Grc3.
DR   InterPro; IPR032319; CLP1_P.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12755; PTHR12755; 1.
DR   Pfam; PF16575; CLP1_P; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   rRNA processing; Transferase.
FT   CHAIN           1..841
FT                   /note="Polynucleotide 5'-hydroxyl-kinase grc3"
FT                   /id="PRO_0000087588"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..132
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         338..345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   841 AA;  92574 MW;  28BE249025D2A7E6 CRC64;
     MKRKAEKQQA TAPVSAFAAR KARQQQARLL EPEKTAQNEP AVEPPSKRAR RSPEEGAARQ
     AANENDRVQT RRSARTKAET LSSAELAEKQ PQESAAAARA QTAERTPPPE KGDADTFDAA
     EEEEEEEKEE DILERENGVG VIAVEDDAEG YESPADDVPQ VQNFPLSKTR LNKSNIVSSD
     ERTLCVRIKE KMTLVLLGHY DLWVKRGVIS LMGAKLHPSP RLYRVYAPST HSLPVIKCVA
     GVDGESEIEV KSCNSGIYRL RHLSPLYQRI WNGKHTAADK LTLKKVSAST KRTFSVLYTS
     SDDSWNRHLR PLHLEKQWSS AIRSLSQRGG RLKVLICGPK ASGKSTFSRY LLNHLLSPAP
     QTENNHRNTD GVAFLDLDPG QPEFCPMGQV YLAHLRSPFF GPPFTHPSLA ESQDGSIIRS
     HHIGAISPKE DPDHYVLAAM DLMDRYRALL ASYPQCPLII NYPGWIFGLG LEVATWLVKS
     LGLSDVVYMS EKGPAEVVEP LGHAAQEARV PLTTLPSQPT DFVSRSSAQL RSMQVQSYFH
     MSHPSEIHNP QWLDTTMSRT RPLVVDYAGP RQGIRGIMVM GSQISPNLLH EALDGALVGV
     VAVESPNAIM GQADAAGFSG SSHGDATQGA EDLSSAASDI DMNDVTDACH GDVAPTSSSS
     FESMIIRTPN EDLPYLFVGS GSCNPLDPKA SNCLGLALVR SIDVPSRKLE LITPIPASKL
     RDALEQGHGI VLVRGMLDNP SWAISEDYYA ARAAERRHQE LVAKARKETN TRDGQDAAVD
     ADTQGMVSAL LKDRIRRASN VPWMTVIEDN SRRHREAAQR KKSLWKLRKK AYPGSESETD
     W
 
 
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