ID L5MES8_MYODS Unreviewed; 799 AA.
AC L5MES8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=MDA_GLEAN10010658 {ECO:0000313|EMBL:ELK37109.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37109.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|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|RuleBase:RU004273}.
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DR EMBL; KB100892; ELK37109.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MES8; -.
DR eggNOG; KOG0377; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
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; 2.
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|RuleBase:RU004273};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 688..723
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 728..763
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 341..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 91596 MW; 6316B30420C68CEE CRC64;
MLPPRQRLHY PTFQGCCILA ITPVFISSSE SWQSSLFIST HVNIFIKKWE SNTPPVIGAE
PRAFKAAVLI QRWYRRYMAR LEMRRQCTWS IFQSMEYAGQ QDQVKLHDFF SYLVDHFTPS
SHSERDFLNR MFTEERVPRD SEVEKCSDYE SIEVPDNYTG PHLSFPLLPD HATALVEAFR
LKQQLHARYV LNLLHETRKH LVQLPNISRV STCYSEEITV CERAYVFNGD FVDRGKDSVE
ILMVLFAFML VYPKEFHLNR GNHEDHMVNL RYGFTTEVMQ KYKTHGKKIL QRLQDVFCWL
PLATLVDEKV LILHGGVSDM TDLELLSKLD RHKIVSTLRC KTRKEKEKQA EEKGKAKQTS
SAGSLSPWFL PQSRSLPSSP LHLSSHKTHK TGRSSSVPSS ILLDPRGLSR QARRSVDLEL
ERCRQQAGFP VIKEKEEPWV FNPEADSAAG DLLEPSQEEW RQVVDILWSD PMAQEGCKAN
TVRGGGCYFG PNVTKRLLQK YDLQLLIRSH ECKPEGYEFC HSRKVLTIFS ASNYYAVGSN
RGAYVKLGPA LTPHIVQYQA NKATHMLTMR QRQDFPMSDF RKAELWISRV EESALRALRG
KLFAHSSDLL EEFKKRDNGN TGLITLSDWA AAVESVLHLG LPWRMLRPQL VNSSTGNMLE
YKSWLEDLAK EQLSHENIQS SLLETLYRNR SNLETIFRII DSDHSGFISL DEFRQTWKLF
SSHMKMDITD DGICDLARSI DFNKDGHIDI NEFLEAVRLV EQSCSEGNAS DCPQASNAKG
SGSWPPTEDS LVSVTQVAS
//
