ID K8EGE6_9CHLO Unreviewed; 1015 AA.
AC K8EGE6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Bathy06g02640 {ECO:0000313|EMBL:CCO17227.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO17227.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO17227.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO17227.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) 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}.
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; FO082273; CCO17227.1; -; Genomic_DNA.
DR RefSeq; XP_007512627.1; XM_007512565.1.
DR AlphaFoldDB; K8EGE6; -.
DR STRING; 41875.K8EGE6; -.
DR GeneID; 19015244; -.
DR KEGG; bpg:Bathy06g02640; -.
DR eggNOG; KOG0323; Eukaryota.
DR eggNOG; KOG1245; Eukaryota.
DR OrthoDB; 298319at2759; -.
DR Proteomes; UP000198341; Chromosome_6.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.20.1270.220; -; 1.
DR Gene3D; 2.30.30.1150; -; 1.
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 InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
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; PF17035; BET; 1.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS51525; NET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 889..941
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 937..1015
FT /note="NET"
FT /evidence="ECO:0000259|PROSITE:PS51525"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..316
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 179..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 114432 MW; D807966DAB119A60 CRC64;
MAFQTSIAFK DLERAKNDQS SMRVSVHQLS VEASVFNDAG GTNGDDGDDG GNDEKNQMSF
ANVYKKESEL VVAGFWFPTK GEKVTCDVLD VFLLLCPNGA SVAMRNVVAE GEDEVNGKAL
KRLHEEMLSK NKSAVVMLPN ERELHIVAVR KDGMMKEEKE KKSNVAGAPN ATTGEKKISV
GFYEDDEDED NEKKKKKKEE EDASSTLKSE SESYFLGFEI PSKSVFEANL LLENSQFVVI
LDLDETLLQA ASEGTLERAI ENERRKMIEL DGKIETLSKG GGGINNNIDE NNRDELSKYR
RERQETEQRR RFLMEDHRML KEFREGNAVR QGALLNAKNE KALVVDKLNP NELKMIERPV
VRLASKYRGG LNGFTMFTRI DPNDPNSSIL VHVRPGWFGP HGLKEALSGI NRASKKRLAE
VYVCTTAEKE YAMEMWRILD GDFSLIDERD VRRRVVSLYG LGGGARKSFK MAWEGNAKKW
PHALSLIIDD RSNVWAETEQ PHVITVHPFL PNGYIEPESN SIEKDADAAN SNGNNSNSHN
VNPAAVLRRE RETFLERELP GKGGVLGSAL GMLNAARTRW FYEFQKYRKD KRMRMFEESF
ESNDTDDGKV EAEKEDAQNV SAPPAENGAP GGDGGSPAQK MSKNASLELP SLNKILPEIM
AKEAQELASA LKARAGVSRT ATGAGSALDS ILAPLHRSIV ENEKMKKEKR EKEEREKREQ
MQKEKEEREK REREEHEAAE AKERAEREAE EARWEEERVR RKKEREEKDE AEEQKRKEKK
RISGGGGSGK KLDKDETLDE AGQILEDAKK KERAAEVALK KAKKEQQRML KELEVEKSRK
AAAEKRKATR EAKNGSASKK KKKKDGEEET GLVLDDEMDP EAWNATLDEI PCKVCKSKDD
DEKMLLCDGC DCGFHIFCLK PPMKKIPEGD DDWFCKPCKA GVERMTKSVE AKVALRVAMQ
ELPESYQEEA IKICKVANGL DEDADEEIVI DVAELEPKTL WRLNLVCDRA KDEQT
//
