ID W9RM72_9ROSA Unreviewed; 1301 AA.
AC W9RM72;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=L484_013158 {ECO:0000313|EMBL:EXB81217.1};
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:EXB81217.1, 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; KE344834; EXB81217.1; -; Genomic_DNA.
DR RefSeq; XP_010100046.1; XM_010101744.1.
DR STRING; 981085.W9RM72; -.
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:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02250; FCP1_euk; 1.
DR PANTHER; PTHR23081:SF2; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645}.
FT DOMAIN 967..1147
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1190..1265
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..162
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 142671 MW; 001A4FADBDA5FD1F CRC64;
MGRIESGRVV EDVEEGEISD SASVEEISEE DFNKQEGNGT GSGKVMSVSD SNSKESKFGD
SRVWTMRDLY ANYPGFRGYT TGLYNLAWAQ AVQNKPLNEI FVMDVDADDS SRVVLSSASP
AVNSGRREGK NGVKEVEKVE KVVIDDSADE MEEGELEEGE IDLESEPTQK PAGEEAKDGD
LNCEAENVGG LEVDSRRDEL EKRVDLIWET LGSVNVVNAE KSFEEVCSRL QRTLESLRGV
LSEKEFSFPT KDVVIQMSIT AIQVVNSVFC SMSVNQKEQK KETLSRLFCS VKNCGTPLFS
PEQTKEIELM ISSLNPLNVL PSSGASDKEK ETQIIERLHE MDSNLTNANA ENASIERTSV
KLPQDCVASV VHSNPITLPE LLRPGTLAFK GRGLLLPLLD LHKDHDADSL PSPTREAPSC
FPVYKPLGVA DGIIKPVSTT AKVAPGAEES RLHRYETDAL KAVSTYQQKF GRGSFLMSDR
LPSPTPSEEC DEEDDINQEV SSSLTSGNLR TPAIPILRPS VVTSSVPVSS PTMQGPIAAK
NAAPVGSGSN STMKASARSR DPRLRFANSD AGALDLNQRP LTAVHNGPKV EPGDPTSSRK
QRIVEEPNLD GPALKRQRHA FVSAKIDVKT ASGVGGWLED NGTTGPQIMN KNQLVENAEA
DPRKSIHLVN GPIMNNGPNI GKEQVPVTGT STPDALPAIL KDIAVNPTIF MDILNKLGQQ
QLLAADAQQK SDSSKNTTHP PGTNSILGAA PLVNVAPSKA SGILQTPAVS LPTTSQVATA
SMQDELGKIR MKPRDPRRVL HGNMLQKSWS LGHEQFKPIV SSVSCTPGNK DNLNGPVQEG
QADKKQVPSQ LVVQPDIARQ FTKNLRNIAD LMSVSQASTS PATVSQNLSS QPLPVKPDRG
DVKAVVPNSE DQHSGTNSTP ETTLAVPSRT PNAWGDVEHL FEGYDDEQKA AIQRERARRL
EEQKKMFDAH KLCLVLDLDH TLLNSAKFVE VDSVHDEILR KKEEQDREKP QRHLFRFPHM
GMWTKLRPGV WNFLEKASKL YELHLYTMGN KLYATEMAKV LDPMGTLFSG RVISRGDDGD
PFDGDERVPK SKDLEGVLGM ESSVVIIDDS VRVWPHNKLN LIVVERYTYF PCSRRQFGLP
GPSLLEIDHD ERPEQGTLAS SLAVIEKIHQ NFFSHHSLDE VDVRNILASE QRKILAGCRI
VFSRVFPVSE VNPHLHPLWQ TAEQFGAVCT TQIDDQVTHV VANSPGTDKV NWALANGKFA
VHPGWSLTMM LTINATVVNI WLNLLSFKWI NYSALAVGAR W
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