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Database: UniProt
Entry: A0A452IGM8_9SAUR
LinkDB: A0A452IGM8_9SAUR
Original site: A0A452IGM8_9SAUR 
ID   A0A452IGM8_9SAUR        Unreviewed;       713 AA.
AC   A0A452IGM8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Serine/threonine-protein phosphatase with EF-hands {ECO:0000256|PIRNR:PIRNR000912};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000912};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000026919.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000026919.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482,
CC         ECO:0000256|PIRNR:PIRNR000912, ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|PIRNR:PIRNR000912,
CC       ECO:0000256|RuleBase:RU004273}.
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DR   AlphaFoldDB; A0A452IGM8; -.
DR   Ensembl; ENSGAGT00000030595.1; ENSGAGP00000026919.1; ENSGAGG00000019599.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:UniProtKB-UniRule.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.60.21.10; -; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF2; SERINE_THREONINE-PROTEIN PHOSPHATASE WITH EF-HANDS 2; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF000912; PPEF; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000912};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000912};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          624..659
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          664..699
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          322..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  82431 MW;  B150B21CBE2DFEB3 CRC64;
     MEQTKPLETL GTRQKIRHAF KAAVLIQRWY RRYVARLEMR RRCTWRIFQS IEYSCEQDQI
     KLHNFFSYLM DHFTPSSSKE RDFISRMLTE EESYKDTELE KLCDYESVEV LDSYTGPHLS
     FPLLPDHATA LLEAFKQKQQ LHAHYVLKLL HETRRHLMQL PNINHVSTCY SEEITICGDL
     HGRLDDLFLI FYKNGLPSPE KSYVFNGDFV DRGKQSVEIL IILFAFLLVY PKEVHLNRGN
     HEDHMVNLRY GFTKEVMQKY KVHGKKILKM LQNVFCWLPL ATLIDQKVLI VHGGVSDMTD
     LELLAKIQRH KFVSVLRGKK RKEKSRHMDS KVINGESPVG VDPPRSSSFP GSCLQPGLAS
     MASRTELSQW VRQTVEEELE KCRRQVGFSE TPGDKELTCV SSVTMTESEL ESCETSESSQ
     GEWKQIVDLL WSDPMPQEGC KMNTVRGGGC YFGPDVTENI LQKHSLQLLI RSHECKQEGY
     EFCHNRKVLT IFSASNYYEI GSNRGAYYQA NKTAHTLTLR QRISRVEESA FRALREKLFA
     HTSDLICAFK GYDQEETGTI TLSDWATAVE SVLHLGLPWR MLRPQLVHST AGGLLEYKSW
     LDYLAVEQRS KEHIQSSLLE TIYRNRSNLE TIFRIIDSDH SGLISFEEFH QTWTLFSSHM
     NIELTDDGIS DLARSIDFNK DGNIDFNEFL EAFRLIEHTH CDDKAALPTS DGC
//
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