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Database: UniProt
Entry: I1NJ79_SOYBN
LinkDB: I1NJ79_SOYBN
Original site: I1NJ79_SOYBN 
ID   I1NJ79_SOYBN            Unreviewed;       438 AA.
AC   I1NJ79;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Protein CLP1 homolog {ECO:0000256|HAMAP-Rule:MF_03035};
GN   ORFNames=GLYMA_20G242900 {ECO:0000313|EMBL:KRG92999.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG92999.1};
RN   [1] {ECO:0000313|EMBL:KRG92999.1, ECO:0000313|EnsemblPlants:KRG92999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG92999};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG92999.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG92999}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG92999};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG92999.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG92999.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-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}.
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DR   EMBL; CM000853; KRG92999.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1NJ79; -.
DR   SMR; I1NJ79; -.
DR   STRING; 3847.I1NJ79; -.
DR   PaxDb; 3847-GLYMA20G38670-1; -.
DR   EnsemblPlants; KRG92999; KRG92999; GLYMA_20G242900.
DR   Gramene; KRG92999; KRG92999; GLYMA_20G242900.
DR   eggNOG; KOG2749; Eukaryota.
DR   HOGENOM; CLU_018195_1_0_1; -.
DR   InParanoid; I1NJ79; -.
DR   OMA; VQYVNCH; -.
DR   Proteomes; UP000008827; Chromosome 20.
DR   ExpressionAtlas; I1NJ79; baseline and differential.
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:UP000008827}.
FT   DOMAIN          22..113
FT                   /note="Clp1 N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF16573"
FT   DOMAIN          133..321
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
FT   DOMAIN          326..437
FT                   /note="Pre-mRNA cleavage complex subunit Clp1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06807"
FT   REGION          110..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03035"
FT   BINDING         68
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   438 AA;  47632 MW;  3C87E9E7FFB5B71D CRC64;
     MAYGGAGPVG GSGSASTIKQ VKLERESELR IEVGNDAPLR LRLLNGTAEI FGTELPPEIW
     LNFPPRLKFA VFTWYGATIE MDGATETDYT ADETPMVSYV NVHAVLDGRR SRAKASSPDD
     SGSSQGPRVI VVGPTDSGKS TLSRMLLSWA AKQGWKPTFV DLDIGQGSIT IPGCIAATPI
     EMPIDPVEGI PLEMPLVYYY GHATPSNNVE LYKVLVKELA GMIERQFTGN AESRASGMVI
     NTMGWIEGVG YDLLLHAIRT FKANVVLVLG QEKLCSMLKD VLKSEPKVDV VKLQRSGGVV
     SRNAKVRQKA RSYRIREYFY GLSNDLSPHS NIANFSDLFV YRVGGGPQAP RSALPIGAEP
     AADPTRVVPV NINRDLLHLV LAVSFAKEPD EIISSNVAGF IYVTDVDIQR KKITYLAPSA
     GELPSKYLIM GSLTWLET
//
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