GRC3_ASPTN
ID GRC3_ASPTN Reviewed; 815 AA.
AC Q0CKU1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase grc3;
DE EC=2.7.1.-;
GN Name=grc3; ORFNames=ATEG_05693;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CH476601; EAU33454.1; -; Genomic_DNA.
DR RefSeq; XP_001214871.1; XM_001214871.1.
DR AlphaFoldDB; Q0CKU1; -.
DR SMR; Q0CKU1; -.
DR STRING; 341663.Q0CKU1; -.
DR EnsemblFungi; EAU33454; EAU33454; ATEG_05693.
DR GeneID; 4321818; -.
DR VEuPathDB; FungiDB:ATEG_05693; -.
DR eggNOG; KOG2750; Eukaryota.
DR HOGENOM; CLU_010345_1_2_1; -.
DR OMA; PLYQRIW; -.
DR OrthoDB; 1217334at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW rRNA processing; Transferase.
FT CHAIN 1..815
FT /note="Polynucleotide 5'-hydroxyl-kinase grc3"
FT /id="PRO_0000289954"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 815 AA; 89374 MW; ABE004498765B2E0 CRC64;
MKRKAEKQQS AAPVSAFAAR KARQQAQIAA TPEPVKPPSA VETTEEPPSK KARTSPEEDT
PSQSVSPADR VQTRRSSRRK AEPSEIEKTP RRKTKTTPAT PPEHLTDGTV GRESGIQTPV
EEVSEPEGND VPLDDADRYE SPADTPALVE AFPLSKTRLN KSNIVYSDEH TLCVRIKEKL
SLVVIGHYDV WVKRGVISLM GAKLHPSPRL YRVYAPSTHS LPVIKCVSGV DGAAEVEIKS
CHSGIYRLRD LSPLYQRIWN GSNTSADKLT LKNAEPHARR TFSVLYTSTD DSLKRHLRPL
HLEKQWSSAI KSLSQKGGKL RALICGPKGS GKSTFSRYLL NHLLSPAPQT EPSYCNTDGV
AFLDLDPGQP EFAPMGQIYL AHLRSPVFGP PFSHPSLEGS QDGTVIRAHH IGASSPKDDP
DHYVLAATDL MDRYRALLAS YPQCPLIINY PGWIFGLGLE VATWLVRSLG LSDVIYMSEK
GPAEVVEPLG QAAAAARIPL TTLPSQPTDF VSRSSAQLRS MQMQSYFHMT RPADVSTPLW
LDQPMSRTRP FKVHYAGPHQ GIRGIMVMGS QIHPDLLHEA LDGSLVGVVA VESPNAILGH
SEVPGLANGV MGKQPSPAEE GSEDAVMDEA TEMVPTAPLA SIDSGITRSP HEDLPYLFVG
AGSCNPLDPK ASHCLGLALV RSVNVAARQL ELVTPIAASR IRDALQQGYG IVLVRGQLDN
PNWALSEEYY AARAAEKRHR RFVDSSRKDK VDDGTDDSAH TSAILKDRIR RASHVPWMTV
IEDNSRRQRE AAQREKSLWK LRKKAYPGSE SEGDW