ID A0A067MQV7_9AGAM Unreviewed; 640 AA.
AC A0A067MQV7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, 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=BOTBODRAFT_132759 {ECO:0000313|EMBL:KDQ14247.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ14247.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00011003}.
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DR EMBL; KL198039; KDQ14247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067MQV7; -.
DR STRING; 930990.A0A067MQV7; -.
DR HOGENOM; CLU_010345_0_0_1; -.
DR InParanoid; A0A067MQV7; -.
DR OrthoDB; 5480745at2759; -.
DR Proteomes; UP000027195; Unassembled WGS sequence.
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:UP000027195};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 243..450
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 69988 MW; 52C6E834C4851CE4 CRC64;
MSPNRLIEDA PNDDDFMNMD DSETGYNDTP TAPDPAPSVF STFSGVAQKN LFPMDNEELL
QFNMHTSSGR SAIIILEPSE SLAFIGTARL TLLRGFISLL GVPLHPSLDP HPVYAPRSHP
VPILTSLPNS PRGDTELPPR LQAYCGPESS VVLIQEMLTG VEGIGTICKS FERVFDNDDL
ELDEAWRIHG FTPIPPNILP PRDLQPFALP PSWQATLDLL IPEESQDMDE DTSLDPLVAL
VKGPKKSGKS TFARTLLSRL TTRYQKVAFL ECDMGQSEFT PGGMVSLHVI SRPVFGPPFT
HPSVPYRAHY VGASTPRSTP AHYLSSILAL LQTYRLELQY PIPGGEEEDD DRISSIIPLV
INTHGWVKGL GADLSRDIEE AAEATHVFLL ESDAPDDNSF NDFHHHPNQT HTSRLKSPKF
YSLEAIASTP LALRYTPADL RALSIISYFH ANFTSDAPHI ADSWSTAVPL CAQPPWEVDW
SVALDQVVLV GSGSEDVTPA ELPQALACGL VALVSAEADA DAPAKTEASL IPYTQGSSSP
PPSTSHCVGL ALIRGISPST HALHLLTPLP PVLLGKCRVL VKGELEMPVW GLLDHRKEEK
GKDLCGVEWS KVPYLQWGTM QGVGSTKKRV RRNLMRRGQM
//
