ID A0A1V6SNC7_9EURO Unreviewed; 820 AA.
AC A0A1V6SNC7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=PENFLA_c033G04998 {ECO:0000313|EMBL:OQE15169.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE15169.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC {ECO:0000256|ARBA:ARBA00003798}.
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:OQE15169.1}.
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DR EMBL; MLQL01000033; OQE15169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SNC7; -.
DR STRING; 254877.A0A1V6SNC7; -.
DR OrthoDB; 5480745at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 334..536
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 90051 MW; EE8C6C5DDE367E60 CRC64;
MVKRKAEKQQ SAGPVSAVAA LAARRARQQQ AQSANVPQDA PPAIIESERP LKKSRQSLEG
PEATETNEER HGTRTKAAKK QDEPLPAEIT PERPVRATRP QKLEVKREVG NTPKHPEDEQ
SENDQVEDAG DMDEDDIASV VGDADGYESP TETPAELQNF PLSKARLSKS NIVYSDESTL
CVRIKERTNL ALLGHYDIWV KRGVVSLMGA KLHPSSQLHR VYAPSTHSLP IIKCVAGVDG
EAEVEIKSCT SGISRLRDLS PLYQRIWAGE NTAADKITLK GASKDSKRTF SVLYTSADDS
LNRHIRPLHL DKKWSASMKA LSQRQGQLRV LICGPKASGK STFSRYLLNH VLSPTPETEN
GYTNTDGVAF LDLDPGQPEF APMGQVYLAR LRSPFFGPPF THPSLDDSRD GEIVRAHHIG
AASPKEDPDH YALAVMDLMD QYRSLLEKHP QCPLIINYPG WIFGQGLEVA TWLVRSLGLS
DVVYMSEKGP SEVVDPLGLA AQEARVPLTI LPSQPTDFVS RSSAQLRAMQ IQSYFHMSYP
NDLRTSLWSD VPLSRTRPIT VDYAGARQGI LGVMVMGSQI SPDLLHETLE GAIVGVVAVE
SPKAIMGGMA TSETPIDEDH EDIDMDSANP SAGNSAELSI ADSIVRTSED LPYLFVGSGS
CIPLDPNASN CLGLALVRSI DTSSRKLELS TPIPSSHLEK AIEQGHGIVL VRGQLDNPNW
AISEEYYAAR AAERHYQQST SGPRKAGGSG SDQAHELDPA EHNRTLALLR ERVRRASNVP
WMTVVEDNSR HQREVAARRE KSLWKLRKKA YPVSESEADY
//