ID A0A061EQY0_THECC Unreviewed; 841 AA.
AC A0A061EQY0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=TCM_021715 {ECO:0000313|EMBL:EOY07246.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY07246.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY07246.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001883; EOY07246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061EQY0; -.
DR EnsemblPlants; EOY07246; EOY07246; TCM_021715.
DR Gramene; EOY07246; EOY07246; TCM_021715.
DR Proteomes; UP000026915; Chromosome 5.
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:UP000026915};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 133..384
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 684..751
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 93406 MW; 5E2E8BA73496DC47 CRC64;
MSRLGFKSVV YHGDVCLGEL DTIPVSDTNF QFPNNEIRIH HISPPSERCI PLSVLHTVSS
FPVRCKLESS SPVEQPHLIH LHASCFYELK TAVVLVGDEE VHLVPMPSKQ KKFPCFWCFS
VPTGLYNSCL GMLNLRCLAI VFDLDETLIV ANTMKSFEDR IEALRGWLAR ETDTIRHLGM
SAELRRYIDD RMLLKQYTES DCVVDNGKMF KVQMEEVPPL SDGHEKVVRP VIRLQERNIV
LTRINPEIRD TSVLVRLRPA WEELRSYLTA KGRKRFEVYV CTMAERDYAL EMWRLLDPEA
HLIGSKQLLD RVVCVKSGSR KSLLNVFRDG KCHPQMAMVI DDRSKVWEDK DQPRVHVVPP
FAPYYAPQAE TANAVPVLCV ARNVACNVRG LFFKEFDENV IRKISEVFYE DEVVNLPLAP
DVSNHLMLED AGFAPNGNGG APISEGMNGV EVERRLNQLE EKHVSDSSTH LVMNNPELRY
ETSQPPVAIV PNVVGPASLT APLPSQKPSL LGAPGLLSAP TLLGASVRRE SNTIDSDYDM
KRRALGSKQT LDLRNQSSVQ PPLLSKVPAQ ISSSSILPQG GWLVEEDNNK AHLNDRSSGS
AQEFDATKSD KLRNQNPFSH SAPGSVSTGL PSHASQVKVE EAHAGLDTQK QNVPPAGHLS
EIGGTQNHVS STEGGKLNLL PSHLSISVLQ EIGRRCGSKK VEFRTVVSTS KDLQFSVEVL
FTGEKIGVGM GKTRKDAQQQ AAELALHNLA EKYLAYIAPR SGAVDRDFNK LSLGTENGFL
WDVNPASSEA LREDGLPKDS TSEGMWARNF QIRGSGYLER NHSSLDFALH QDVRAITLKG
E
//
