ID A0A0F8UF78_9EURO Unreviewed; 814 AA.
AC A0A0F8UF78;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ARAM_001622 {ECO:0000313|EMBL:KKK18329.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK18329.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK18329.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK18329.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK18329.1}.
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DR EMBL; JZBS01002519; KKK18329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8UF78; -.
DR STRING; 308745.A0A0F8UF78; -.
DR OrthoDB; 5480745at2759; -.
DR Proteomes; UP000034291; 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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000034291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 328..530
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 89625 MW; ADA4B6E581D64CF8 CRC64;
MKRKAEKQQA AAPVSAFAAR KARQQQAQAQ AVEASVKPAH TESAGEPPSK KPRRSLDDKT
IAQPIVEERQ TRSQKQKALK TEEVPLKKNE DITRKARDRK PEPVVSSDHE EQGPSDEGSE
DEDAIVEEAG VMSVSENGDG YESPADTPVQ TVEFPLSKAR LNKNNIVYSD EDTLCVRIRE
KLSFVLIGQY DLWVKRGVVS LMGAKLHPSP RVYRVYAPST HSLPVLKCVS GVDGAAEVEF
KSCHSGIYRL RELSPLYQRV WNHKNTPADK LSLQKVGGAS KRTFSVLHTS GDDPLNRHLR
PLHMEKQWSA AIKSLSQRGG RLQVLICGPK ASGKSTFGRY LLNHLLSPAP QTESQYRNTD
GVAFLDLDPG QPEFSPMGQI YLAHLRSPVF GPPFTHPALD SRREGTIIRA HHIGATSPKE
DPDHYVLAAT NLLEHYRALL ASYPQCPLII NYPGWIFGLG LEVATYLVRS LGLSDVVYMS
EKGPMEVVEP LSQAARAAKT ALTILPSQPT EFVSRSSAQL RSMQMQSYFH LSHPTEIANP
LWLEGPVSRT KPFLVHYAGP KQGIYGIMGS GSQISLDLLA ESLEGALVAV VAVESPTAIP
VAGPTPLPNS HHHDDYAGHD EMDMDAKPST TTTTTTTMPT LESNITRTSK EHLPYLFVGA
GSSTPLDPKS SRSLGLAIVR SIKATSHQLE LITPIPGSQI RGAVEQGHGI VLVRGLLDNP
NWAISEEYYL AQAAERRFRS RVRPGRHSNP KSTGDLGDEQ VRILGTLQDR IRRAQNVPWM
TVVEDRRHVV QRGQEGALWK LRKKAYPDSG SEAE
//