ID A0A4T0WJ58_9PEZI Unreviewed; 455 AA.
AC A0A4T0WJ58;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 05-FEB-2025, entry version 19.
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 Name=CLP1 {ECO:0000256|HAMAP-Rule:MF_03035};
GN ORFNames=CH35J_000267 {ECO:0000313|EMBL:TID06897.1};
OS Colletotrichum higginsianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=80884 {ECO:0000313|EMBL:TID06897.1, ECO:0000313|Proteomes:UP000305883};
RN [1] {ECO:0000313|EMBL:TID06897.1, ECO:0000313|Proteomes:UP000305883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF305635-RFP {ECO:0000313|EMBL:TID06897.1,
RC ECO:0000313|Proteomes:UP000305883};
RX PubMed=31028389; DOI=.1093/gbe/evz087;
RA Tsushima A., Gan P., Kumakura N., Narusaka M., Takano Y., Narusaka Y.,
RA Shirasu K.;
RT "Genomic Plasticity Mediated by Transposable Elements in the Plant
RT Pathogenic Fungus Colletotrichum higginsianum.";
RL Genome Biol. Evol. 11:1487-1500(2019).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC {ECO:0000256|ARBA:ARBA00003798}.
CC -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000256|HAMAP-Rule:MF_03035}.
CC -!- SUBUNIT: Component of a pre-mRNA cleavage factor complex. Interacts
CC directly with PCF11. {ECO:0000256|HAMAP-Rule:MF_03035}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|HAMAP-Rule:MF_03035}.
CC -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03035}.
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:TID06897.1}.
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DR EMBL; MWPZ01000001; TID06897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0WJ58; -.
DR OrthoDB; 258143at2759; -.
DR Proteomes; UP000305883; Unassembled WGS sequence.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IEA:InterPro.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:TreeGrafter.
DR Gene3D; 2.60.120.1030; Clp1, DNA binding domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.330; Pre-mRNA cleavage complex subunit Clp1, C-terminal domain; 1.
DR HAMAP; MF_03035; Clp1; 1.
DR InterPro; IPR028606; Clp1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR010655; Clp1_C.
DR InterPro; IPR038238; Clp1_C_sf.
DR InterPro; IPR032324; Clp1_N.
DR InterPro; IPR038239; Clp1_N_sf.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF6; POLYRIBONUCLEOTIDE 5'-HYDROXYL-KINASE CLP1; 1.
DR Pfam; PF06807; Clp1; 1.
DR Pfam; PF16573; CLP1_N; 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, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03035};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03035};
KW Reference proteome {ECO:0000313|Proteomes:UP000305883}.
FT DOMAIN 25..119
FT /note="Clp1 N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF16573"
FT DOMAIN 133..340
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT DOMAIN 347..448
FT /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06807"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 136..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ SEQUENCE 455 AA; 49344 MW; 2BCA81E450AF6B46 CRC64;
MSIPGLGHLV APQPTSANQT RTIRLQPFWE WRFEVAFDTH IKLKLLSGTA EKDGTELALQ
HAYTFGGVKS KILTLQGCEL EVEGSLTTDS LAEYAKPQDS PANATLNLHF QLTAMRQRAA
AERREGPRIA ICGPPSTGKT SLVRTLTSYA TRVGAQPLVV NTDPKEGMLS LPGTLSASVI
GTILDVEAVD GWGTTPTSGP SQVPVKLPLV YYYGHASAEE DQKKYQELVS KMAATVTSRL
GKDAEVKSSG MIIDTPAVSE NSVNGMDILA HIVDELSVNI IIVLGSSHLN AELIKRFSTE
RTSLGEPYSI LLLDKSDGVV ERDVGFMQQA CEASIKEYFF GSIGQTLSPA TQQVDFDSLA
IFRIGDYSMY GNADGGLMRV DPAQLMAHWT LAIVYASVKD SPEAIRAANV MGYVYVADID
KEKRKLRILA PVSGRLGDRP LLMGKWPEPF INLLG
//
