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Database: UniProt
Entry: A0A498HD31_MALDO
LinkDB: A0A498HD31_MALDO
Original site: A0A498HD31_MALDO 
ID   A0A498HD31_MALDO        Unreviewed;       426 AA.
AC   A0A498HD31;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Protein CLP1 homolog {ECO:0000256|HAMAP-Rule:MF_03035};
GN   ORFNames=DVH24_037150 {ECO:0000313|EMBL:RXH69366.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH69366.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH69366.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH69366.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RXH69366.1}.
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DR   EMBL; RDQH01000343; RXH69366.1; -; Genomic_DNA.
DR   RefSeq; XP_008341533.1; XM_008343311.2.
DR   AlphaFoldDB; A0A498HD31; -.
DR   STRING; 3750.A0A498HD31; -.
DR   EnsemblPlants; mRNA:MD17G0041000; mRNA:MD17G0041000; MD17G0041000.
DR   GeneID; 103404408; -.
DR   Gramene; mRNA:MD17G0041000; mRNA:MD17G0041000; MD17G0041000.
DR   KEGG; mdm:103404408; -.
DR   OrthoDB; 56092at2759; -.
DR   Proteomes; UP000290289; Chromosome 17.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
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   CDD; cd01983; SIMIBI; 1.
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:UP000290289}.
FT   DOMAIN          11..102
FT                   /note="Clp1 N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16573"
FT   DOMAIN          121..309
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
FT   DOMAIN          314..425
FT                   /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06807"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         124..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
SQ   SEQUENCE   426 AA;  46628 MW;  CBFA8C901A7BC557 CRC64;
     MAHGGGARQV KLDRESELRI EVGNDAPLKL RLLNGTAEIF GTELPPDFWL TFPPRLKFAV
     FTWNGATIEM DGSTETDYTA DETPNISYVN VHAVLEERRH RAKPLPPDDP NSQGPRVIVV
     GPTDSGKSTL SKMLLSWAAK KGWKPTFVDL DIGQGAITIP GCIAATPIEM PIDPVEGIPL
     DIPLVYFYGH TTPSNNVDLY KVLVKELAQV VERQISGNAE SRASGMVINT MGWIEGQGYE
     LLLHAIDTFN ANVVLVLGQE KLWSMIRNVL KNKPGVDVVK LQKSGGVVSR NAKFRQKSRS
     HRIREYFYGL ANDLSPHSNI ANFSDFSVFR IGGGPQAPRS ALPIGAEPAA DPLRLAPVNI
     NRDLLHTILA VSFAKEPDQI ISSNVAGFVF VTDVDIQRKT ITYLAPSAGE LPSKYLIAGT
     VTWLET
//
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