ID A0A0D2MGD1_GOSRA Unreviewed; 815 AA.
AC A0A0D2MGD1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=B456_002G264300 {ECO:0000313|EMBL:KJB17087.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB17087.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB17087.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001741; KJB17086.1; -; Genomic_DNA.
DR EMBL; CM001741; KJB17087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2MGD1; -.
DR EnsemblPlants; KJB17086; KJB17086; B456_002G264300.
DR EnsemblPlants; KJB17087; KJB17087; B456_002G264300.
DR Gramene; KJB17086; KJB17086; B456_002G264300.
DR Gramene; KJB17087; KJB17087; B456_002G264300.
DR OMA; SERINCV; -.
DR Proteomes; UP000032304; Chromosome 2.
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; IEA:InterPro.
DR CDD; cd10845; DSRM_RNAse_III_family; 1.
DR Gene3D; 3.30.160.20; -; 1.
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:SF24; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 2; 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; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 133..384
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 688..754
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 454..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 90763 MW; 7FA6262D853DC39D CRC64;
MSRLGFKSMV YHGDFFLGEL NTIPITDSNF QFPNNEIRIH HISPTSERCI PLSILHTISS
FPVRCKLESP FPVEQPHLIH LHASCFYEFK TAVVLVGDEE VHLVAMPSKQ KKFPCFWCFS
VSTGLYNSCL GMLNLRCLAI VFDLDETLIV ANTMKSFEDR IEVLRGWIAR ESDPIRLSGM
SAELRRYIDD RLLLKQYAES DCVVDNGKMF KVQMEEVPPL SDGHEKVVRP VIRLQDRNIV
LTRINPEIRD TSVLVRLRPA WDELRSYLTA KGRKRFEVYV CTMAERDYAL EMWRLLDPGA
HLIGSKQLLD RVVCVKSGSR KSLLNVFRDG KCHPQMAMVI DDRSKVWEDK DQPRVHVVPP
FAPYYAPQAE TANAVPVLCV ARNVACNARG LFFKEFDENV LRKMSEVFYE DEVVNLPLAP
DVSNYLMSEE ASFASNGNNG APICEGMNGA EVERRMNQSE EKHVLDSSTR PVTNNPELRS
ETSQPPVTDI VGPASSVAPL PSQKPSILGA PGLLSNPMML GASVRRDNNG SEGDYDMKRR
ALGIKQSLDL RNQSSIQPPL LPKFPIQTSS SSVVPQGGWL VEEDINESHL NDRPSGTTQE
SDVLKSDKLR GYQNPFPHTA PGSVSTGLPS YASQVKIEEA RTGLDTPKQN VLPTAHLSEI
GGTQNHLPSI TRELQSEGGK MNLLPSHLSI GVLQEIGRRC GSKVEFRSVV STSKDLQFSV
EVLFTGEKIG VGMGKTRRDA QQQAAELALH NLAEKYVAYI APRSGAVDRD FNNLSLGTEN
GFLWDVNPAS NEAIKEGFPK DNTSEVGIPD DAFIT
//
