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Database: UniProt
Entry: W9SRW8_9ROSA
LinkDB: W9SRW8_9ROSA
Original site: W9SRW8_9ROSA 
ID   W9SRW8_9ROSA            Unreviewed;       740 AA.
AC   W9SRW8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-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=L484_015578 {ECO:0000313|EMBL:EXC23668.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC23668.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) 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; KE346002; EXC23668.1; -; Genomic_DNA.
DR   RefSeq; XP_010109623.1; XM_010111321.1.
DR   AlphaFoldDB; W9SRW8; -.
DR   STRING; 981085.W9SRW8; -.
DR   eggNOG; KOG0323; Eukaryota.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
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   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:UP000030645};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          133..397
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          662..728
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          442..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  83007 MW;  52E255D47AB62E3B CRC64;
     MSRLGFKSVV YHGDLCLGEL DVIPMKDKNF QFPNNEIRIH RISPQSERCP PLSILQAISS
     FSVCCKLESS SPVEQPHLIN LHASCHYELK TAVVLVGEEE IHLVAMLSKQ KKYPRFWCYL
     VPKGLYNASL GMLNLRCLSI VFDLDETLIV ANTMKSFEDR IELLRGWVAR EIDPIRLAGM
     HAEMKRYMDD RLILKQYLES DTVMDNGRMF KVQMEEVPPL SDNHERFFRP IIRLPEKNIV
     LTRINPEIRD TSVLVRLRPA WEDLRSYLTA KGRKRFEVYV CTMAERDYAL EMWRLLDPEA
     HLIGSRKSLI NVFQNGICHS KMAMVIDDRL KVWEDKDQPR VHVVPAFTPY YAPQAETANA
     VPVLCVARNV ACNVRGCFFK EFDENLLRRI TEVFYEDDVL NLPPAPDVSN YLMSEDAGFV
     PNGIPPLINE GMYGVEVERR LSQSDDRPVM ESASHSSTNN VELRSETFQA SAPILPNAIP
     ASLGPLLPSQ RPGLLGTPVR RDGFSDRDHD MKKGVSTLKY GVEMRNQSSG EPPLLSRLPT
     HLSMPPVQAH GGWLVEDDIN RGPLRNRPSG LVQESDVLKP EKQRAHQNSS SYTTSCYTPT
     GLLSQTPEVK SEEGHNGNSL QKQNLPIVSQ LSDAGVSQNQ AASNSRDVHP EGGKLNLLPS
     PLSIGVLQEI ARRCSSKVEF KSVLSTSKDL QFSVEVLFTG EKIGVGMGKT RKDAQQQAAE
     NALHNLAAIG PSSISVFSIS
//
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