ID I3KLK7_ORENI Unreviewed; 381 AA.
AC I3KLK7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=ppm1k {ECO:0000313|Ensembl:ENSONIP00000022002.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000022002.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000022002.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR RefSeq; XP_003452260.1; XM_003452212.4.
DR AlphaFoldDB; I3KLK7; -.
DR Ensembl; ENSONIT00000022021.2; ENSONIP00000022002.2; ENSONIG00000017445.2.
DR GeneID; 100701392; -.
DR KEGG; onl:100701392; -.
DR CTD; 503713; -.
DR GeneTree; ENSGT00940000156633; -.
DR HOGENOM; CLU_013173_1_3_1; -.
DR InParanoid; I3KLK7; -.
DR OMA; CHTHMKK; -.
DR OrthoDB; 202023at2759; -.
DR Proteomes; UP000005207; Linkage group LG6.
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; 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; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF226; PROTEIN PHOSPHATASE 1K, MITOCHONDRIAL; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 103..355
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 42257 MW; DD337B2D7B11E8A7 CRC64;
MSATCLARLA RCSGLHVGRA GLVQMSLGPL PVQHDSHFQF IFRKPLHTPS ETRHSNTRFD
PDSSGRPTTW DSFGIWDDRI DEPILLPPSI RYGKPIPKVS LSKVGCASLI GQRKDNEDRY
RVSELTDRVL YFAVFDGHGG SEAADFCEKY MEKYITNLLA DEENLELVLT KAFLEVDKAL
ARHLHFSPNA PGMNAGTTAT VALLRDGIEL VVGSVGDSRA MLCRKGKALK LTVDHTPERK
DEKDRIKKSG GFITWNSLGQ PNVNGRLAMT RSIGDFDLKK TGVIAEPETK RVTLHHVHDS
FLALTTDGIN FIMNSQEICN VINQCHEPKE AAQRISEQAI QYGSEDNSTI IVVPFGAWGK
HKSSDTSFSF SRSFVSSGRW A
//
