ID A0A2K1IJW4_PHYPA Unreviewed; 1600 AA.
AC A0A2K1IJW4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PHYPA_028263 {ECO:0000313|EMBL:PNR29569.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR29569.1};
RN [1] {ECO:0000313|EMBL:PNR29569.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_18380V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR29569.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_18380V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c23_18380V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABEU02000023; PNR29569.1; -; Genomic_DNA.
DR STRING; 3218.A0A2K1IJW4; -.
DR PaxDb; 3218-PP1S49_248V6-1; -.
DR EnsemblPlants; Pp3c23_18380V3.1; Pp3c23_18380V3.1; Pp3c23_18380.
DR EnsemblPlants; Pp3c23_18380V3.3; Pp3c23_18380V3.3; Pp3c23_18380.
DR Gramene; Pp3c23_18380V3.1; Pp3c23_18380V3.1; Pp3c23_18380.
DR Gramene; Pp3c23_18380V3.3; Pp3c23_18380V3.3; Pp3c23_18380.
DR OMA; MANDSRR; -.
DR Proteomes; UP000006727; Chromosome 23.
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; PF03031; NIF; 1.
DR Pfam; PF12738; PTCB-BRCT; 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:UP000006727}.
FT DOMAIN 1282..1462
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1505..1598
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 24..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1600 AA; 178485 MW; 53EE688ED6491FDA CRC64;
MDEDAVVLTQ NDDKVVDTVE DRLEGLNFSN NDPGEDQEEG ELSEKEDMNE EIKAAEPDIE
EDVGVNVEVA SKRIKHNLDD LSGRATMGLR GKDDYSQRSG TENLGKDNED NLWLRDKMTF
RSAATSYAPN LYNFAWAQAV QGNQGFKLVE KQDGDEEADA LPDNGASFDG DDEMEDGLPE
SLADMTLKIP EGYDMRQVLY DRRLMTNASW NSRLGDTRRE KTWIDSEDGM DSRRRFDRDE
RGGSRSGGGG RREMRSPSRR RDSRSERERG GVKSRLSEFE RQRARDRERE RENGRERGER
NDNILRPTSS DESDYSRRNA PSGAIGRQSQ SNDNIVDVRE EGEIEEGEIE LPTDNLRSRS
SSREKSQDPR AESLIEDGIS NGNLRKSLSS RLSFRNSSSS HPRSLSRESS FRRLQDGDLR
HRLTKDVERE KPRQDVLLRE DRREQIAHLT AVMKSVTVKD AQKAFINTCL RLDNAVKILQ
AFAMQRIPSS GLPADDIPRD LSKMATKVFQ GLRAVYAVWN TANGREQERD RDTFPRLLQF
VTESCLTYFS PKQARELEVF MDHVTKTARK IRMEGSLWHA QAVMKSAEAM QEPGVREREF
VNASVSNSKM APSGASTLEG NSEHNADSKD AIAEATIAAA ALAYAQSSAA ALANFTHGST
YNQSMKDHPI IGMDHWAWNG SNGPFERSMS PGLPPGYSGV SHAGRSLVAH GAVAHINSST
NSHGVAARPP NTSANGWISA NKKLAYDAKS PYGPGFLEED WEELSPPSQA PAYEFTTRKV
VKLDERGFSI SSSETINTFA PPSKMGNLPV SVNFRLASPT PSDGDDDHEN QNTASAGVNG
QLGHKPLHSL PKPSSSMPPV TSPFYKTSNT HVDDTGRVHY ASAPMVSPAS VDQELSLNFE
QPKNQPVSGP VLSSLRSRDP RKQLQNGYLE AEGSLHQSTA QIKYQWPSAL QTMDKKREGE
TYANMTEPSK RLKLLGSSNG MQNANLFAST SAIGGWLDEG AVVSAGHENH GAQSMDIDFD
SPTPSERKHC LKDEFPGMNS NISEVSSASG SFEMLVSGTA ASTRDKPPSD PFTSNSTNPE
DQTGEEDVGR HRMRPRDPRR ILLENAVETA QVNPMNVPVN DAAGSEMTLQ YTNRSPEVAD
VSPNLNNQPS TNTLGNPPNQ RDPRLNPYES SQSDSAVVSI QLSTEHKTTE WKTLDERIKE
SERDSNRNQG SEVSSGESTG DKGDHLHPWD PLLRKPRFGP SHWGGNDMHR DFEQLLEDLD
EKQRIAIQNE RKRRLQEQDR MFIAGKLCLV LDLDHTLLNS AKFSEIEPEW EARLRQAENM
ERSRALKDPS MKQELYRFPH MSMWTKLRPG IWKFLAKASE LYELHVYTMG NKAYATEMAK
LLDPTGTLFA GRVISKGDEV DGSDKSKDLD GVLGMESAVV IIDDSSRVWP HHRENLIVVE
RYMYFPSSRR QFGLLGPSLL EVGHDERAAD GMLSSASGVI DRIHKNFFSN KRLREVDVRA
ILAAEQRRVL DGCRVLFSRI FPVGEANPHL HPLWRLAEQF GASCCLHIND KVTHVVAISL
GTDKVNWAAA TGRPVVRPAW LEASAILYRR ANEQDFPVLP
//
