ID C5XY22_SORBI Unreviewed; 439 AA.
AC C5XY22;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Protein CLP1 homolog {ECO:0000256|HAMAP-Rule:MF_03035};
GN ORFNames=SORBI_3004G092400 {ECO:0000313|EMBL:EES04747.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EES04747.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EES04747.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- FUNCTION: Required for endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {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; CM000763; EES04747.1; -; Genomic_DNA.
DR RefSeq; XP_002451771.1; XM_002451726.1.
DR AlphaFoldDB; C5XY22; -.
DR STRING; 4558.C5XY22; -.
DR EnsemblPlants; EES04747; EES04747; SORBI_3004G092400.
DR GeneID; 8082954; -.
DR Gramene; EES04747; EES04747; SORBI_3004G092400.
DR KEGG; sbi:8082954; -.
DR eggNOG; KOG2749; Eukaryota.
DR HOGENOM; CLU_018195_1_0_1; -.
DR InParanoid; C5XY22; -.
DR OMA; VQYVNCH; -.
DR OrthoDB; 56092at2759; -.
DR Proteomes; UP000000768; Chromosome 4.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
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:UP000000768}.
FT DOMAIN 21..112
FT /note="Clp1 N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF16573"
FT DOMAIN 134..322
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
FT DOMAIN 327..438
FT /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06807"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT BINDING 137..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ SEQUENCE 439 AA; 47612 MW; AF5EB32563C3535F CRC64;
MAAATAAGAG AATPQPPRQY KLAPQSELRV EVLPDAPLRV RLVTGTAEIF GTELPPEGWV
PVPPRSKIAI FTWHGATVEL DGVSESEYSS DETPMVIYVN THAILDARRA RARAAAAQGG
DMEASQGPRV IVVGPTDSGK STLCKMLLSW AAKLGWKPTY VDLDIGQGSI TIPGCISATP
IEKPIDIVDG IPLEMPLVYF YGHSSPSINA DVYKVLMKEL AKTLEKQFSG NAESRAAGMV
INTMGWVEGL GYELLLNAIE TFKANVVLVL GQEKLWKMLK DAVQSKSNID VVKLHKSEGV
VLRNTKYRQK TRSFRIREYF YGIANDLAPH SNIVNFSHVS VYKIGGGHQA PRSALPIGAE
PVADPTRLVA VNISTDMIHT VLAISYAKEP DEIISSNIAG FIHVTDVDIQ RKKLTYIAPC
PGDLPSRLLI ASSLTWYEA
//
