ID A0A167BZC0_9ASCO Unreviewed; 632 AA.
AC A0A167BZC0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN Name=CMP2 {ECO:0000313|EMBL:ANB11012.1};
GN ORFNames=AWJ20_3807 {ECO:0000313|EMBL:ANB11012.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB11012.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB11012.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB11012.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) 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 ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC catalytic subunit and the B component confers calcium sensitivity.
CC {ECO:0000256|ARBA:ARBA00011112}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000256|ARBA:ARBA00009905}.
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DR EMBL; CP014500; ANB11012.1; -; Genomic_DNA.
DR RefSeq; XP_018733489.1; XM_018880838.1.
DR AlphaFoldDB; A0A167BZC0; -.
DR GeneID; 30035869; -.
DR KEGG; slb:AWJ20_3807; -.
DR OrthoDB; 1488111at2759; -.
DR Proteomes; UP000189580; Chromosome c.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
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:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR CDD; cd07416; MPP_PP2B; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041751; MPP_PP2B.
DR InterPro; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189580}.
FT DOMAIN 178..183
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 424..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 72712 MW; E7C3B47635BEE02C CRC64;
MSDERAKKLE NAIKAFQEKK PLPKVDFSVY KGDDGKELRT DERVIKTTPA PATKIPTDDE
LFLPGTSNPR LPNLAFLKDH LFREGRLHEE QAIYIINSAT KIIMEEPTLL EIDPPVTLCG
DIHGQYYDLM KLFEVGGDPR NTKYLFLGDY VDRGYFSIEC VLYLWALKLH YPKSVFFLRG
NHECRHLTDY FTFKLECKHK YSLNIYEACM MSFCTLPLAA VVNKQFFCVH GGLSPELHTL
DDVRKLDRFR EPPTHGLMCD LLWADPIENF GEEDNNRSFI HNNVRGCSYF YTYKAACDFL
VKNNLLSIIR AHEAQNAGYR AYLESRNTGF PSVMTIFSAP NYLDTYNNKA AVVKYENNVL
NIRQFKHSPH PYWLPNFMDV FTWSLPFVGE KITDMLISIL NICTREELEE DTVRYIQEKG
NTSKYGGIFG RKSPRSPRSP RSPSSPRSPR SPTSPRSPKK PIAGQTQQYD SDEDLPVKIP
EEVEPEEDYF QDAQSTAMDR DDDDLDQEDD EDEDDLEVRR DRFKNKILAI GRLSRMFQVL
RQESESVSEF KATTGTMLPA GTLMSGAEGI RKAITTFDEA RRVDLINEQL PPTADEKAQE
NERQRKEALN RAMKEADADV KIRNLARRLT GE
//
