ID A0A166IM05_9AGAM Unreviewed; 744 AA.
AC A0A166IM05;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PENSPDRAFT_602671 {ECO:0000313|EMBL:KZV73603.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV73603.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV73603.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV73603.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00011003}.
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DR EMBL; KV424488; KZV73603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166IM05; -.
DR STRING; 1314672.A0A166IM05; -.
DR InParanoid; A0A166IM05; -.
DR OrthoDB; 5480745at2759; -.
DR Proteomes; UP000077086; 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.
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:UP000077086};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 365..523
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 79895 MW; 9C3AB663BA8731CC CRC64;
MLSAVAARKL KQGQQDPAAP SPTTVQPAAP IPSILNGSPS KQHASSSKKT NNKPSSKRKP
SGHPAPKSAS KKPRRSRSKG KDKATPRYFA EPVHADASDD DAVISVDEDE EDEREGMLVG
PNTDPLPSST KRAYSPSRPV EEDSSDDDVP APSAPLRLKS VQRQPAPVTV STFEPSLDQN
MFVLTADERS ILALGDENAI VLLLSAQETF SFIGTSRLHV LRGSVVMHGT TLRASNISHP
VFAPRSSPVP SLQAITTPDG SSEQASVALP SRIKRLSKGA AAIVALREMF TGVEGLGHVV
RTFDGVFRPS LDDSVLELPL VGAAMCVRSS RDIQPFVMPS SWEDALQEVT SAEGSGAPPV
YFVKGPKNSG KSTLARTMVN RLTARYRRVA YLDCDIGQSE FTPGGMVALT VVERPLFGPP
FTHMTVPYQA HYLGSSSPRS SPSHYLSCIE ALLHAYRIDL QYGAVVDVDD DAEDGRIPES
IPLVVNTMGW AKGLGADLTL KIEHLAAPSA VFSFYPDPPP EEYDGPPLHL LDPIAPPTHV
PRYTAADHRA LALLSYFHSI FPSSDRTVAQ RTAEKWDTRL PLCATPPYEL DMRATIQNVV
LAGAGMEDVV PTEILRVLNG ALVGLVKSDD DGAPYTSEGW ALPYSQAAPP PDPTASHCTA
LAVIRAVSPD GSKIHLLTPL PSSANTFVKG ELEIPVWGML DFRDGGAGEE TGLPFLRWGK
AGADGAIGGE RRRIRRNLMR KGQM
//