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Database: UniProt
Entry: B3RWM4_TRIAD
LinkDB: B3RWM4_TRIAD
Original site: B3RWM4_TRIAD 
ID   B3RWM4_TRIAD            Unreviewed;       461 AA.
AC   B3RWM4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
DE   Flags: Fragment;
GN   ORFNames=TRIADDRAFT_13008 {ECO:0000313|EMBL:EDV24721.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV24721.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV24721.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV24721.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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DR   EMBL; DS985245; EDV24721.1; -; Genomic_DNA.
DR   RefSeq; XP_002112611.1; XM_002112575.1.
DR   AlphaFoldDB; B3RWM4; -.
DR   EnsemblMetazoa; TriadT13008; TriadP13008; TriadG13008.
DR   GeneID; 6754261; -.
DR   KEGG; tad:TRIADDRAFT_13008; -.
DR   CTD; 6754261; -.
DR   eggNOG; KOG1323; Eukaryota.
DR   HOGENOM; CLU_029072_2_0_1; -.
DR   InParanoid; B3RWM4; -.
DR   OMA; YKEHIEW; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; B3RWM4; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF354; GM14138P; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          96..461
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EDV24721.1"
FT   NON_TER         461
FT                   /evidence="ECO:0000313|EMBL:EDV24721.1"
SQ   SEQUENCE   461 AA;  52144 MW;  0FDFADE5901C266F CRC64;
     SIVDIMGGKA SIPSQHNHLS SQSYDFAPAK FRYNRPEFLR LTEEDLQKSK DRTCREIISP
     SYQLPRFTGF AECINSGKSH LNEDQAAVGI YMLRLQTSLK LQSLSNKNVM KLVYDTLYNY
     DILAMKAYNT SLSRILPYQY FAIFDGHGGT EAAIYAANSL HLIIYQKLTE AHNFYATLPS
     INSELSTVKL EALIIGAIEE AFRELDQQIG NERQSCSISG GCTAIMALYF EKHLYVANAG
     DCRALIIKQG IMEQLSTDFN PITDRQRLQY LAYLQPELLH AYYNRLYFKQ RIRKTDVGKP
     VVYKDMDMVG WGTKIASEED FELVPMIRGG GKQCRLLDII STTRGFGDFD LKCQEGGPYL
     KPFLTSCPEV KSLALDQDSY GPDDILILGC DGLYESLSNE EIGKIVLDCL QKCGREDNFR
     YAKAAKTLVE TCRGMYDGRH WMKNDVELAS QDDISAFIIP L
//
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