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
//