GenomeNet

Database: UniProt
Entry: M4AKE7_XIPMA
LinkDB: M4AKE7_XIPMA
Original site: M4AKE7_XIPMA 
ID   M4AKE7_XIPMA            Unreviewed;       549 AA.
AC   M4AKE7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Protein phosphatase 1G {ECO:0000256|ARBA:ARBA00040767};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014941.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000014941.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014941.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBUNIT: Interacts with NOL3; may dephosphorylate NOL3.
CC       {ECO:0000256|ARBA:ARBA00038798}.
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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   RefSeq; XP_005804266.1; XM_005804209.2.
DR   AlphaFoldDB; M4AKE7; -.
DR   Ensembl; ENSXMAT00000014961.2; ENSXMAP00000014941.1; ENSXMAG00000014897.2.
DR   GeneID; 102223390; -.
DR   KEGG; xma:102223390; -.
DR   CTD; 5496; -.
DR   eggNOG; KOG0699; Eukaryota.
DR   GeneTree; ENSGT00940000158427; -.
DR   HOGENOM; CLU_013173_13_1_1; -.
DR   OrthoDB; 11028at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
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:SF876; PROTEIN PHOSPHATASE 1G; 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:UP000002852}.
FT   DOMAIN          23..520
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          172..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..331
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  58946 MW;  94E54711B4E01EB9 CRC64;
     MGAYLSQPNT TKTSSDGGNT SMSYGFSAMQ GWRVSMEDAH NCIPDFDEET AMFAVYDGHG
     GEEVALYCSK YLPDIIKEQR TYKDGKLQKA LEDAFLAIDG RITTEEVIKE LVQISGRPVE
     EPPSEKVAEE DDLDNEEAAL LHEEATMTIE ELLVRYGQNL NAVKHAAAAA SGAAKKASAQ
     NAEVSKDKGE DAEKKGVNGE VNEEEGDGKV KEGAACGSKL RACRRTGGSE GSSSAVSGES
     GSSNGEEKAG KAEGDAGPSC SSASSKATGD SKSRFFDDSE ESEEGEEEEE EGSDEEDGSD
     EEEADTSELE EEDTEEGEED SEDEEEEMCL PGMDGKEEPG SDSGTTAVVA LIRGKQLIVA
     NAGDSRCVVS ERGKAVDMSY DHKPEDEVEL TRIKNAGGKV TMDGRVNGGL NLSRAIGDHF
     YKRNKSLPPE DQMISAMPDV KVLTLNEEHD FMVIACDGIW NVLSSQEVVD FISERIKPDQ
     DGKTRALSSI VEELLDHCLA PDTSGDGTGC DNMTCMIVTF RAQSDNTKKR MLPEGGEEAG
     NNSKKARSD
//
DBGET integrated database retrieval system