ID A0A0K9PVW3_ZOSMR Unreviewed; 1239 AA.
AC A0A0K9PVW3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=ZOSMA_154G00320 {ECO:0000313|EMBL:KMZ73089.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ73089.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ73089.1}.
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DR EMBL; LFYR01000604; KMZ73089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PVW3; -.
DR STRING; 29655.A0A0K9PVW3; -.
DR OMA; MRDLYKY; -.
DR OrthoDB; 11699at2759; -.
DR Proteomes; UP000036987; 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; IBA:GO_Central.
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:UP000036987}.
FT DOMAIN 920..1100
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1143..1236
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 139100 MW; 593B123740782838 CRC64;
MMATPAKDIK PSADRDDGGG VRDYNSDSSI EEIPESSFKQ RIGKGNPKPK PNPNLIGGEG
GGTIFSHRTH RSVSTTNANN RAWKGGDAAL HHSQQYPNIN NTNFTSNLYN FAWAQAVQNK
PLGFSNQPSA IVPSEHCIVL DDEQREEGEL EEGEIGDLDS EELELQGECD SKDQNNDGEE
KAENIMVVEE GSPRPIEDNN DGPEIIEVVE DDDSDDGGDN HDDDDDDDDE KMDDFDIRLI
TIIEELEILP EDVEKSFDDA CSQMHKALEK LKKIVLDGPL DVVIQQAFIG VQTIHSVFLK
RKEQHRYVFK RLLEYIERQK PKLFSSEQMK EIYSMLQSAS PDHITDSIPL IETKQIFSRD
SNGESTGLPL SKSCKLESLI IPKNRFEFKP LLDPRANHDE GSLPSPTHET AYPPLIQRSI
YSGSNVTASQ PTTCRREETS YGSKTAVYET DALRAVCSYQ KKYDRISYLS ENRLPSPTPS
DESNNDKIDS HSEVSSITNN KTISSFGVDN SKNITSGFRP ELHHSSYISN SDAKVSSKSR
DPRLRIANLN TVNSQDFNKQ PATIGCEASK NGFPGDIVMD SRKQNIMNGY SINCQSMKRQ
KYDCSGYTNP QMASIGKAGY LEKHNINTTL RTDNNHPMEV MGQGKLSNVN SDAYTRQDIH
GHIKGENIQR KNIQSMDAVS KVSFPALLKE ITTNPTMLIH LLKEQHRLTA EGQQKSANLN
QDATNSMAVF SPNIYIKSSE SEEKLDAKAQ SIFQLTMSEA GKPRMKPRDP RRILHNNMVK
KIESLGSESV PSLNANGRDS IIVREQGEKQ QISGMPSQTQ SIQDITSQFV NNKKNVVDTM
STKQNNPAVA FHPINSQPVS KSANNASSIQ RSTEVSMPAT SQLPNQWGDV DYLLDGYDDK
QKAAIQRERA RRIEEQSKMF NARKLCLVLD LDHTLLNSAK FVEVDQFHDE ILRTKEEQDR
DQPQRHLYRF QHMAMWTKLR PGVWNFLEKA SKLFELHLYT MGNNVYATEM AKILDPKGAL
FAGRVISKGD DGDSPDGDDR LPKSKDLDGV LGMESAVVII DDSIRVWPHH KLNLIVVERY
MYFPSSRRQF GLPGPSLLEI DRDERPEDGS LASSLAVIER IHQNFFSRPS LNNVDVRNIL
AAEQHKILGG CRIVFSRIFP VGEINPQRHP LWQTAEQFGA ICTNQLDDQV THVVTNSPGT
NKVNWALSMG KFVVYPGWVE SSALLYRRAS EHDFSVSKL
//
