ID B9RZ63_RICCO Unreviewed; 978 AA.
AC B9RZ63;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=RCOM_0935770 {ECO:0000313|EMBL:EEF43243.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ973834; EEF43243.1; -; Genomic_DNA.
DR RefSeq; XP_002519032.1; XM_002518986.2.
DR AlphaFoldDB; B9RZ63; -.
DR STRING; 3988.B9RZ63; -.
DR GeneID; 8279473; -.
DR KEGG; rcu:8279473; -.
DR eggNOG; KOG0323; Eukaryota.
DR InParanoid; B9RZ63; -.
DR OrthoDB; 1200617at2759; -.
DR Proteomes; UP000008311; 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; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 152..400
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 723..789
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 859..929
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 540..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..45
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 555..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 109796 MW; 577D0739FD6F8ECA CRC64;
MYKSVVYKGD ELLGEVEIYA QQEQKLQQQE ELQEQEQELK KKRVIDEILK GIRISHFSQA
SERCPPLAVL HTITTNGICF KMESKNSVSL DTPLHLLHSS CIQESKTAVV LLQGGEELHL
VAMFSRNDER QYPCFWAFNI SSGLYDSCLV MLNLRCLGIV FDLDETLIVA NTMRSFEDRI
EALQRKISTE LDPQRISGML SEVKRYQDDK TILKQYVDND QVVENGRVIK TQFEVVPALS
DNHQTIVRPL IRLQERNIIL TRINPQIRDT SVLVRLRPAW EELRSYLTAR GRKRFEVYVC
TMAERDYALE MWRLLDPESN LINSKELLDR IVCVKSGLRK SLFNVFQDGI CHPKMALVID
DRLKVWDEKD QPRVHVVPAF APYYAPQAEA NNAVPVLCVA RNVACNVRGG FFKEFDEGLL
QRIPEISFED DMNDIPSPPD VSNYLVPEDD AFTSNGNRDP LSFDGMADAE VEKRLKEAIS
ISSAFPSTVA NLDARLVPPL QYTMASSSSI PVPTSQPAVV TFPSMQLPQA APLVKPLGQV
VPSEPSLQSS PAREEGEVPE SELDPDTRRR LLILQHGQDL RDPAPSESPF PVRPSNSMQV
SVPRVQSRGN WVPVEEEMSP RQLNRAVTRE FPMDTEPMHI DKHRPHHPSF FPKVESSIPS
ERMPHENQRL PKVAPYKDDR LRLNQTMSNY QSLSGEENSL SRSSSSNRDL DVESDRAVSS
AETPVRVLHE ISMKCGAKVE FKHSLVNSRD LQFSVEAWFA GERVGEGFGR TRREAQSVAA
EASIKNLANI YISRAKPDNG ALHGDASKYS SANDNGFLGH VNSFGSQPLP KDEILSYSDS
SEQSGLLDPR LESSKKSMSS VNALKEFCMM EGLGVNFLAQ TPLSSNSVQN AEVHAQVEID
GQVMGKGIGS TFDEAKMQAA EKALGSLRTT FGRFPPKRQG SPRPVPGMPN KHLKPEFPRV
LQRMPSSARY PKNAPPVP
//
