ID A0A1L9PPR0_ASPVE Unreviewed; 827 AA.
AC A0A1L9PPR0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase GRC3 {ECO:0000256|ARBA:ARBA00019824};
DE AltName: Full=Polynucleotide 5'-hydroxyl-kinase grc3 {ECO:0000256|ARBA:ARBA00018706};
GN ORFNames=ASPVEDRAFT_30005 {ECO:0000313|EMBL:OJJ03491.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ03491.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC {ECO:0000256|ARBA:ARBA00003798}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00011003}.
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DR EMBL; KV878130; OJJ03491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9PPR0; -.
DR STRING; 1036611.A0A1L9PPR0; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_30005; -.
DR OrthoDB; 5480745at2759; -.
DR Proteomes; UP000184073; 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; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF3; POLYNUCLEOTIDE 5'-HYDROXYL-KINASE NOL9; 1.
DR Pfam; PF16575; CLP1_P; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 327..529
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91675 MW; 6D076BFFD92E21A6 CRC64;
MMKRKAEKQQ AAAPLSAVAA RKARMQQTQT TVTTDTTTHT EPAGEPPSKR PRRSLEESQS
QSTSERQRTT RATKRAAVNA EKVQQKVENG TREPRSKKTT VEVEDRGSQT SSEEEEEDDD
AVEENAAGVM AVPEGTEDGY ESPADTPSLT MEFPLSKMRL NKSNIVYSDE HTLCVRIREK
MSIVMIGHYD LWVKRGLVSL MGAKLHPSPR VYRVYAPSTH SLPVIKCITG VDGAAEVEFK
SCHSGLTRLR DMSPLYQRVW NSGNSPADKL SLKTVRQDVR RTFSVLHTSS DDSLNRHLRP
LHLEKQWSAA IKVLSQRSGR LQALICGPKA SGKSTFGRYL LNHLLSPAPQ TETNYHNTDG
VAFLDLDPGQ PEFSPMGQVY LAHLRTPVFG PPFTHPSLDN ERDGSIVRAH HIGASSPKED
PDHYVLAITN LMEQYHALLA TYPQCPLIIN YPGWIFGLGL EVATYLIKTL GLSDVVYMSE
KGPMEVVEPL SQAASVSKTP LTILPSQPTE FVSRSSAQLR SMQMQSYFHM SQPKGINYPM
WLETPVFKNR PFRIQYSGPN RGIHGIMTLG SQISSDLLCE SLEGAIVGVV AVESPNALPS
QPDTQNITEN NPNAGDEEEE STSDIDMDAD TDVENTTAAT STSITTALTR LTTPTKESLP
YLTTGPGSDT PLHPTSSHSL GLALIRSINT TTQTLDLLTP IPPARLAQSL EQGHALVLVR
GALDNPNWAV SEEYYAARAE ERRFRRGLRS RNSNNQDGDE GEDGLDEDEK KRMHALLKER
IRRAKDVPFM TVVEDHGRRR QDEARAQRAL WKLRKKAGPE SESEVGY
//
