ID I0Z0G5_COCSC Unreviewed; 1029 AA.
AC I0Z0G5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=COCSUDRAFT_41430 {ECO:0000313|EMBL:EIE24134.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24134.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE24134.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE24134.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
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:EIE24134.1}.
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DR EMBL; AGSI01000006; EIE24134.1; -; Genomic_DNA.
DR RefSeq; XP_005648678.1; XM_005648621.1.
DR AlphaFoldDB; I0Z0G5; -.
DR STRING; 574566.I0Z0G5; -.
DR GeneID; 17042132; -.
DR KEGG; csl:COCSUDRAFT_41430; -.
DR eggNOG; KOG0323; Eukaryota.
DR OrthoDB; 1200617at2759; -.
DR Proteomes; UP000007264; 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 Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT DOMAIN 116..334
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 421..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 109044 MW; 30E0327196132737 CRC64;
MAMAFSMTPG RWPRNKTCKK DVRLVLHVLT GGSCVALLPS PQLTPEGTKV LEEQHAQCLG
ENKAAVVAAS DKLDLLLVAE RALDGETPVP VFLGYVVARG TAETARGGAE AAAALIENMR
LPLVLDLDET LLEAFTANQL RKHIKDLSAE IDGGNWSNVE KKLQLKREKA FKEEDYNLLV
QFIQTNSVTL NGQIHKAWPG RERFEVYVCT TADRSYALEA WRHLDPSALL IPYADRRKRF
HNVHQDKDSK DKDGNVKPVK DLAHVMGLLG HPWSAPCTPP NSAMPLAVII DDQPAVWTAE
SQGQLYQVEK FNPQRLAGVH DGVAMHDQEH VRSLAEELEG VQDVLCKTRG WMYNTMEGHP
RDSLRKQILD AKPLKIRDIR EGRPFARHQW PRICHLLSKA KKGTLEAVPL ELSPANSYGA
TVNAGTGQPP AAAAAARKPV DSRRGCLPDG QPGAAALFAR GAPAGAAAGC KQNPAPPPRG
SAAPAAAAAA ADLTRRGSNA AAGPSGAPPK QFGNLRAAVD PRMMAVAPAG AQSKPPGQGV
KPRGQPPPGR GRVQPAAPGR APAPGAKAGT AVPAKPAASR AAPQQAGQGM AAGSSAQPGR
KRSLEGQDDA AADKAKRPMI HANGRRRPSL SPNLEMTWMQ LKDKPHAESA APAAAATAAS
AAGTGGAAEG APQASRPAAA GATQGQQPQM LSVQLPSDED GAGPVPMEAS PYRTPAKPPA
GPSAQQIGQA TPEGIPLGFG GSNLPLRSPG SSKGRGRRPS ASPAATSAAR RRASAPAGPT
DTPNGPNDAS DGTPAQPPRQ QGDSSPLPAS VRATQTTSFP PECQFGSLDE LPAAVREHAV
LRQRRLQYHT WKVEDWCCAR VLLGPKVLGF GVHRELQPAK DSCIKKACDK VEEGMKRGLT
WLDDEQPVDA RSAINRAEHL YPGRLQWASD NRDGDNKKAV RLSLDNGALT AEAWAQTEVQ
AKRKVALCVL LELGCPLDDT EDKPDSFSAL PSVHARGTRA QSGTEAEQRA EQCTAAMQGQ
SVVQQYKEP
//
