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Database: UniProt
Entry: A0A316W1Z4_9BASI
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ID   A0A316W1Z4_9BASI        Unreviewed;       622 AA.
AC   A0A316W1Z4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=IE81DRAFT_311554 {ECO:0000313|EMBL:PWN43810.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN43810.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN43810.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN43810.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR   EMBL; KZ819366; PWN43810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316W1Z4; -.
DR   STRING; 1522189.A0A316W1Z4; -.
DR   InParanoid; A0A316W1Z4; -.
DR   OrthoDB; 56092at2759; -.
DR   Proteomes; UP000245783; 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   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:UP000245783}.
FT   DOMAIN          7..106
FT                   /note="Clp1 N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16573"
FT   DOMAIN          222..434
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
FT   DOMAIN          486..621
FT                   /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06807"
FT   REGION          551..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         176..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   622 AA;  66689 MW;  824DCAD8B45808CE CRC64;
     MTIRRVTLPP RGEYRFELEN EEKLSIRLVP STGDAEIFGS SLISSTSSDR WYNFGEEAKA
     AICSWSGCEL ELAGSASVEY LADSLSPTFG AYTNLHLYLE QERLKARNEL RSASRETLED
     IKDRALRAAN PTVPLEVDSK DDTGVAELLT GGEKSGQAIY ENIGQGPRVL VVGPESAGKT
     SLANLLANYA LKSPAVCEIP HMKAQEDNEN KRDGEAESAL TGWWPVIANL DPSAGAPTLP
     CTFSLLPLSP SPSVSLTTAS PAYPFGLTLP TTGLFTTTSL NPVSSIPAQT LWLGKEDVRT
     NEVHSKRVVD WLGAALERRL ARDYRARCSG VIVDSMGVNS KDARKGYSFL KHVVRTLYID
     TIIVLGHEKL HIELTRLFAS ATPGGEASAA SSASSSTHKP IQVIKLPKSG GVVELDETYK
     ARLRSLQIRN YFYGGSVDKK STSAKTGADH VASSLAPAVV DDRMQEATNN EGGPTDGTPL
     GGLPPLNPLT TSIPFDLLEI YRVGQESMAP TSALPIGMGR TVTETQLLKL DIVNSLADQN
     SILHNVLALV EPPHGGGGPG QPDSQTVPPP EDDAIIGANV LGFLHVVGID TQRKKLNILS
     PNPTKRLPSK TALLGTLDWQ DA
//
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