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}.
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; 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
//