ID E1ZIE2_CHLVA Unreviewed; 912 AA.
AC E1ZIE2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=CHLNCDRAFT_135536 {ECO:0000313|EMBL:EFN54143.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN54143.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN54143.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
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 ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671}.
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DR EMBL; GL433848; EFN54143.1; -; Genomic_DNA.
DR RefSeq; XP_005846245.1; XM_005846183.1.
DR AlphaFoldDB; E1ZIE2; -.
DR STRING; 554065.E1ZIE2; -.
DR GeneID; 17353749; -.
DR KEGG; cvr:CHLNCDRAFT_135536; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; E1ZIE2; -.
DR OMA; PRMYATA; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000008141; 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:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041758; MPP_BSL_C.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141}.
FT DOMAIN 669..674
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 98271 MW; A13DC75F0EAB3E56 CRC64;
MEGGAPSPSS SAETPNSGPS VLDSVAPAPR VRAFPIVGTN PGPRCGHTLT TIAGPDGDLS
SAKLVLFGGA TALEGQAKGD APPSPGPSSA GIRLAGATND VHIMDVRSGK WEKVTPQGEP
PSPRAAHAAA AVGNMVVVQG GIGPAGLASE DLHVLDFTDL EKPRWHRVMV AGAGPSARYA
HTLALVANRF LVAVGGNDGK QTLADSWALD TSEKPYQWRK IPESGDDPPP RMYATAAARS
DGLLLLTGGR DVSGTPLADA FGLARHRDGR WEWASAPGTM PSPRYQHGAV FVGARLHIFG
GALGGGKMVD EASSVVVLDT AAGQWLTQAQ TGHSDDVMRR CRHAMASVGP YIFVHGGLKG
STLLEDVLLA DDSSGSELSV CDPRSPAWQQ WINSMHGSEA AAAALANAAA EEAAAAAALS
MRRVGNMEDL RCLDEDLDEN MRLNKLRAAN PDSPKSVTLA QRRRGEFPPT RDMPTPDVRL
YHRAVVVAQD VQGQLRGLVR QLSIDQFENE SRRVSMGAGA SEASTVRNKT PLFERTFSEP
GIHKAVLREF LNPRHWSPSA ARDFFFNYDQ ICQLCDQAER IFQQEPSVLK LRAPIKIFGD
LHGQFGDLMR LFEEYGTPST AGDITYIDYL VRWVVAFLGD FVDRGAHSLE TICLLLALKI
EHPRSVHLIR GNHEAADINA LFGFRLECLE RLGDQQGLKA WQRLNTLFNW LPLAALIEDK
VLCMHGGIGR SINSIEQIEE LQRPLTMEDG GIVLMDLLWS DPTTNDAVEG VQPSPRGPGL
VTFGPDRVME FCRNNDLQMI VRAHECVMDG FERFAQGHLI TLFSATNYCG TANNAGAILV
LGRDLVMVPK LIHPLPPSTP RTPGSAGGGD EIEEDPPTPH PGIADTWMAA LNEERPPTPP
RGRPQTHSLE TF
//
