GRC3_ASPNC
ID GRC3_ASPNC Reviewed; 819 AA.
AC A2QNQ8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase grc3;
DE EC=2.7.1.-;
GN Name=grc3; ORFNames=An07g06640;
OS Aspergillus niger (strain 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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: 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=CAK39510.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270135; CAK39510.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; A2QNQ8; -.
DR SMR; A2QNQ8; -.
DR EnsemblFungi; CAK39510; CAK39510; An07g06640.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW rRNA processing; Transferase.
FT CHAIN 1..819
FT /note="Polynucleotide 5'-hydroxyl-kinase grc3"
FT /id="PRO_0000289952"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 819 AA; 90438 MW; 6AD0A39BF395E229 CRC64;
MKRKAEKAQA AAPVSAFAAR KARQQQAQAT AAAVKPPVAE PVVEPPPKRA RRSLEEPVVP
VAPEENRVQT RRSSRRKEEQ AKVEKPTPKA RNDQPPKASK KLPEHDTSKA TEDQAPSDEE
SEEPDVVVGN TGVIGLEPIQ NEEEGYESPA DTAVQVQDFP LSKARLNKNS IVYSDEHRMC
VRIKEKMSLV MIGHYDLWVK RGVVSLMGAK LHPSSQVYRV YAPSTHSLPV IKCVSGVNGE
AEVEFKSCHS GIYRLKELSP LYQRIWNGKN TTADKLTLKG TPQSTKRTFS VLYTSADDSF
KRHLRPLHLE KQWSSAIKSL SQRGGRLKTL ICGPKGSGKS TFSRYLLNHL LSPAPQTETK
YFNTDGVAFL DLDPGQPEFA PMGQVYLAHL RSPVFGPPFS HPSLDGSRNG TIVRSHHIGA
TSPKEDPDHY VLAAMDLMDR YRALQASYPQ CPLIINYPGW IFGLGLEVAT WLVRSLGLSD
VVYMSEKGPT EVVQPLGQAA YQAKIPLTIL PSQPTDFVSR SSAQLRSMQM QSYFHMSRPN
GINNSLWLEQ PLSRTKPFRV HYSGPQQGIQ GIMVMGTEIH PDLLHEVLDG SIVAVVAVES
PNAILGQNSG PMFANNANAE TDGDHDVDMQ DSADAVPVIG TSTIESSITR TPNEDLPYLF
VGAGSSNPLD PKVSHCLGLA LVRSVNVASR QLELVTPITG STLRGVLEQG HSIVLVRGLL
DNPNWAISED YYAARAAEKR HRELIEKLKK DKGAAAAEDA TLESEKQVLK DRIRRASKVP
WMTVVEDNSR RQREAAQREK SLWKLRKKAY PGSDSEGDW