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Database: UniProt
Entry: A0A1D1UR03_RAMVA
LinkDB: A0A1D1UR03_RAMVA
Original site: A0A1D1UR03_RAMVA 
ID   A0A1D1UR03_RAMVA        Unreviewed;       340 AA.
AC   A0A1D1UR03;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=RvY_01261-1 {ECO:0000313|EMBL:GAU88588.1};
GN   Synonyms=RvY_01261.1 {ECO:0000313|EMBL:GAU88588.1};
GN   ORFNames=RvY_01261 {ECO:0000313|EMBL:GAU88588.1};
OS   Ramazzottius varieornatus (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX   NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU88588.1, ECO:0000313|Proteomes:UP000186922};
RN   [1] {ECO:0000313|EMBL:GAU88588.1, ECO:0000313|Proteomes:UP000186922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU88588.1,
RC   ECO:0000313|Proteomes:UP000186922};
RX   PubMed=27649274; DOI=10.1038/ncomms12808;
RA   Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA   Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA   Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA   Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA   Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT   "Extremotolerant tardigrade genome and improved radiotolerance of
RT   human cultured cells by tardigrade-unique protein.";
RL   Nat. Commun. 7:12808-12808(2016).
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,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAU88588.1}.
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DR   EMBL; BDGG01000001; GAU88588.1; -; Genomic_DNA.
DR   Proteomes; UP000186922; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000186922};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186922}.
FT   DOMAIN      126    131       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      309    340       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    324    340       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   340 AA;  38713 MW;  DDB79DAE422B2A91 CRC64;
     MGLKKLKLVS LLDNLIQRLW QCRNDDHVVR ITNFTYQEAQ ILCNAAIGVL KSQPMLLRLK
     APVVIAGDVH GQFNDVLRMF EENGRPEKGQ RYLFLGDYVD RGPQSVECMC LLLAYKIKYP
     HDFYLIRGNH EERQLNSLYG FLEECQAHHS LKLWDMLNRV FDYLPMGGVV SNKVFCAHGG
     IGPNLDNLSQ IDAIRRPNKG TAGKGVACDL MWADPDPNTS VWRRNEARNV SYMYGKNQVH
     DFLLKNNLKF ICRAHEQPDS EGYAYPFYPD TTVLTIFSAP GYENSGSDGA VVHLDAECVP
     TIKTLQYIKT QSREAPHKGN QPRSSASRKR ELEVDHDHES
//
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