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Database: UniProt
Entry: A0A367J0C2_RHIST
LinkDB: A0A367J0C2_RHIST
Original site: A0A367J0C2_RHIST 
ID   A0A367J0C2_RHIST        Unreviewed;       437 AA.
AC   A0A367J0C2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Polynucleotide 5'-hydroxyl-kinase GRC3 {ECO:0000256|ARBA:ARBA00019824};
DE   AltName: Full=Polynucleotide 5'-hydroxyl-kinase grc3 {ECO:0000256|ARBA:ARBA00018706};
DE   Flags: Fragment;
GN   Name=CLP1 {ECO:0000313|EMBL:RCH83171.1};
GN   ORFNames=CU098_001342 {ECO:0000313|EMBL:RCH83171.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCH83171.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCH83171.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCH83171.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RCH83171.1}.
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DR   EMBL; PJQM01004835; RCH83171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367J0C2; -.
DR   STRING; 4846.A0A367J0C2; -.
DR   EnsemblFungi; RCH83171; RCH83171; CU098_001342.
DR   Proteomes; UP000253551; Unassembled WGS sequence.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
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:0031124; P:mRNA 3'-end processing; IEA:InterPro.
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};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253551}.
FT   DOMAIN          15..103
FT                   /note="Clp1 N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16573"
FT   DOMAIN          118..317
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
FT   DOMAIN          323..436
FT                   /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06807"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RCH83171.1"
SQ   SEQUENCE   437 AA;  48231 MW;  323C01B6CC9B52A3 CRC64;
     MPNNGNTETQ REIKLGPDHE FRFEVDFQTK ASVKLTQGTG EIFGTELALG VEYNFTGRKA
     AVYTWHGCTL QINGQFSVEY IANETPMTSY LNTHLALEQL RQRLKAEKEL GPRVLVVGPH
     DVGKTSLCKI LASYSLRQGG TPIYLSLDTS EGSITMPGAI TATSIQHIID VEEGFGSSAT
     TAASVGSATM PLAYYYGFES PAENVKLYKL VTTKLAEAVK SRMAVDEDCR TSGLIIDTSG
     LVDQVGYETI QHAVQAFSVN VVIVLGHERL YSDLHRILSS NADLSIIKLS KSGGVVERDK
     QFKNMLQRTK VHEYFYGTPK CELSPYSMLI NYGDINVWRV GDVIAPSSAL PLGMEGSSNE
     TQIVKVDSYE MCLHSVMAIL NAPPDEHENK LLESNVVGFI YISDINEEKR KLTVLSPSPG
     RLPRQHLLMG SFKWMES
//
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