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Database: UniProt
Entry: I1KLI0_SOYBN
LinkDB: I1KLI0_SOYBN
Original site: I1KLI0_SOYBN 
ID   I1KLI0_SOYBN            Unreviewed;       956 AA.
AC   I1KLI0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=100819722 {ECO:0000313|EnsemblPlants:KRH50009};
GN   ORFNames=GLYMA_07G194800 {ECO:0000313|EMBL:KRH50009.1};
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:KRH50009.1};
RN   [1] {ECO:0000313|EMBL:KRH50009.1, ECO:0000313|EnsemblPlants:KRH50009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH50009};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH50009.1};
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:KRH50009}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH50009};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH50009.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH50009.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CM000840; KRH50009.1; -; Genomic_DNA.
DR   RefSeq; XP_003529311.2; XM_003529263.3.
DR   AlphaFoldDB; I1KLI0; -.
DR   STRING; 3847.I1KLI0; -.
DR   PaxDb; 3847-GLYMA07G31430-1; -.
DR   EnsemblPlants; KRH50009; KRH50009; GLYMA_07G194800.
DR   GeneID; 100819722; -.
DR   Gramene; KRH50009; KRH50009; GLYMA_07G194800.
DR   KEGG; gmx:100819722; -.
DR   eggNOG; KOG0323; Eukaryota.
DR   HOGENOM; CLU_010333_0_0_1; -.
DR   InParanoid; I1KLI0; -.
DR   OMA; MCSEDIN; -.
DR   OrthoDB; 1200617at2759; -.
DR   Proteomes; UP000008827; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.30.160.20; -; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR23081:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 1.
DR   PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          131..379
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          701..767
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          836..907
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          513..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   956 AA;  106733 MW;  94C2C5FAB7A7B042 CRC64;
     MRMYKSVVYQ GEVVVGEVDV YPEENNNYKN FHVKEIRISH FSQPSERCPP LAVLHTVTSC
     GVCFKMESKT QQQDGLFQLH SLCIRENKTA VMPLGGEEIH LVAMHSRNVD RPCFWGFIVA
     LGLYDSCLVM LNLRCLGIVF DLDETLIVAN TMRSFEDRID ALQRKINSEV DPQRISGMQA
     EVKRYQDDKN ILKQYAENDQ VVDNGRVIKV QSEIVPALSD SHQPIVRPLI RLQDKNIILT
     RINPQIRDTS VLVRLRPAWE DLRSYLTARG RKRFEVYVCT MAERDYALEM WRLLDPDSNL
     INSKELLGRI VCVKSGLKKS LFNVFQDGLC HPKMALVIDD RLKVWDEKDQ PRVHVVPAFA
     PYYAPQAEAS NTIPVLCVAR NVACNVRGGF FKDFDDGLLQ KIPQIAYEDD IKDIPSPPDV
     SNYLVSEDDG SISNGHRDPF LFDGMADAEV ERKLKDALSA ASTIPVTTAN LDPRLTSLQY
     TMVPSGSVPP PTAQASMMPF PHVQFPQPAT LVKPMGQAAP SEPSLHSSPA REEGEVPESE
     LDPDTRRRLL ILQHGQDTRD HASAEPPFPV RHPVQTSAPH VPSSRGVWFP AEEEIGSQPL
     NRVVPKEFPV DSGPLGIAKP RPHHPSFFSK VESSISSDRI LHDSHQRLPK EMYHRDDRPR
     LNHMLSSYRS FSGDDIPFSR SFSSHRDLDS ESGHSVLHAD TPVAVLQEIA LKCGTKVDFI
     SSLVASTELQ FSMEAWFSGK KIGHRVGRTR KEAQNKAAED SIKHLADIYL SSAKDEPGST
     YGDVSGFPNV NDSGYMGIAS SLGNQPLSKE DSASFSTASP SRVLDPRLDV SKRSMGSISS
     LKELCMMEGL DVNFLSAPAP VSTNSVQKDE VHAQVEIDGK VFGKGIGLTW DEAKMQAAEK
     ALGSLRSKLG QSIQKRQSSP RPHQGFSNKR LKQEYPRPMQ RMPSSARYPR NAPPIP
//
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