ID T1J5T7_STRMM Unreviewed; 1080 AA.
AC T1J5T7;
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=protein phosphatase methylesterase-1 {ECO:0000256|ARBA:ARBA00013111};
DE EC=3.1.1.89 {ECO:0000256|ARBA:ARBA00013111};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR008993-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR008993-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000906};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIa family.
CC {ECO:0000256|ARBA:ARBA00009331}.
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DR EMBL; JH431868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1J5T7; -.
DR STRING; 126957.T1J5T7; -.
DR EnsemblMetazoa; SMAR008993-RA; SMAR008993-PA; SMAR008993.
DR eggNOG; KOG1818; Eukaryota.
DR eggNOG; KOG2564; Eukaryota.
DR HOGENOM; CLU_286252_0_0_1; -.
DR OrthoDB; 169198at2759; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd15749; FYVE_ZFY19; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.91.10; Cytochrome c oxidase, subunit VIIa; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036539; Cyt_c_oxidase_su7a_sf.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14189:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 1.
DR Pfam; PF12697; Abhydrolase_6; 2.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF81419; Mitochondrial cytochrome c oxidase subunit VIIa; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 139..198
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..424
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 121521 MW; DD040D0784D1B9B6 CRC64;
MYYKFSAMAN RLIATNIMQA YHPQGLIPLN KVKIIPIQFS YKPIHITQVE GIPRPPERLP
LGPTLGGERE ISTSGALGQQ MPQFPRLSPS GVPYGPKDPS LIAKQKHFQK NDGLPIHLKG
GQMDYVLYYG LKPRVFLRKI TSMPCTSCGT EFGIFRKEHG CKNCGFSFCG NCLVHKALIP
KLDQKKHSVC ATCFELLSGK KSGEATGRIS PPAALQRRID AAKEKHKNTN SEDQKLKMRL
DRLREAKRGK LPSDQELEER LARLKDIPAA APASTQPPAY IPRDNRSATE QSSSLLQQMT
DEVRLDAERP KPEDEITRRF NQLKSDNGLW NDLNNPGQIR TTEAKTSNVP SDPNLMCNNF
MQNFPMNIGE NSNENVDDFN EVHKLMEATR RVAEADAEKA IRGLEAEKRK MNELKANCNR
SSKTLLCNED SSDDDEDENK LADKVIEKLL AESALDDRTN DYKFRSEKKE INTPSSDISN
LTNFLGVTYA MKTQLFVAMD VMENYIAIVV SKNVTIRTTC EHILRSITLH RKELLKFLIT
FGNELLFYSM VDTQIVDIFR KCAFGRHTNG RHAFCRHANG RHPHLVVDQM CAMSCRPFAC
RPNAMSTICC RPEARFQHFS ILWSRSSSMV ALSEDSEHLQ HLLTNMSALQ REMLRPKLPI
PSGSSRILGS RGAIRRRDYT PTKWNKYFET YEDVIINDSD VFRVYRSGNK GPMLFFLHGG
GYCGLTWATL TTSILELIEC QIAAMDLRGH GDTVTSNDED LSAQTLSDDV SNVIMKLFGE
NSPEIILIGH SMGGAVAVHT AYRELVPQLI GLAVIDVVEG TAMDALQSMQ SFLRSRPTTF
RSIEASIEWC IRSGQVRNYE SAKVSMPGQI KNIYTHKSAT TDLEFEESTS SEHSSNESSK
ILKVPSSNNS IPEEQEEVNT IFEEKKDEEK ETVSPRNSGV DLATGHGDGS NEAMTSREQT
KTMDDSFIYP FKLSDGNRYT WRIDLSKTEK YWPSWFHGLS SMFLSCSPPK MLLLAGIDRL
DKDLTIGQMQ GKFQMQVLPQ CGHAVHEDVP EKVAEVLATF MVRHKFAIAT EEFTPSLPAC
//
