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Database: UniProt
Entry: S7MFB7_MYOBR
LinkDB: S7MFB7_MYOBR
Original site: S7MFB7_MYOBR 
ID   S7MFB7_MYOBR            Unreviewed;       499 AA.
AC   S7MFB7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=D623_10010011 {ECO:0000313|EMBL:EPQ02466.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ02466.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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|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. PP-5 (PP-T)
CC       subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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DR   EMBL; KE161231; EPQ02466.1; -; Genomic_DNA.
DR   RefSeq; XP_005857889.1; XM_005857827.2.
DR   RefSeq; XP_014403462.1; XM_014547976.1.
DR   AlphaFoldDB; S7MFB7; -.
DR   GeneID; 102243677; -.
DR   KEGG; myb:102243677; -.
DR   eggNOG; KOG0376; Eukaryota.
DR   OrthoDB; 1107740at2759; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          28..61
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          96..129
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          300..305
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  56849 MW;  134C253D111053F7 CRC64;
     MAMAEGERAE CPDPPQDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF YSQAIELSPS
     NAIYYGNRSL AYLRTECYGY ALADATRAIE MDKKYIKGYY RRAASNMALG KFRAALRDYE
     TVVKVKPHDK DAKMKYQECN KIVKQKAFER AIAGDEHKRS VVDSLDIESM TIEDEYSGPK
     LEDGKVTITF MKELMQWYKD QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC
     GDTHGQFYDL LNIFELNGLP SDTNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
     RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG
     VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR GVSCQFGPDV TKAFLEENHL
     DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLRGSDLR PQFHQFTAVP
     HPDVKPMAYA STLLQLGMM
//
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