ID T1ISL8_STRMM Unreviewed; 409 AA.
AC T1ISL8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=M-phase inducer phosphatase {ECO:0000256|RuleBase:RU368028};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU368028};
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:SMAR004098-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:SMAR004098-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- FUNCTION: Functions as a dosage-dependent inducer in mitotic control.
CC Tyrosine protein phosphatase required for progression of the cell
CC cycle. {ECO:0000256|RuleBase:RU368028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001490,
CC ECO:0000256|RuleBase:RU368028};
CC -!- SIMILARITY: Belongs to the MPI phosphatase family.
CC {ECO:0000256|ARBA:ARBA00011065, ECO:0000256|RuleBase:RU368028}.
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DR EMBL; JH431441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1ISL8; -.
DR STRING; 126957.T1ISL8; -.
DR EnsemblMetazoa; SMAR004098-RA; SMAR004098-PA; SMAR004098.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_585710_0_0_1; -.
DR OrthoDB; 12481at2759; -.
DR PhylomeDB; T1ISL8; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR10828:SF17; CDC25-LIKE PROTEIN PHOSPHATASE TWINE-RELATED; 1.
DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU368028};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|RuleBase:RU368028};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368028};
KW Mitosis {ECO:0000256|RuleBase:RU368028};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU368028};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT DOMAIN 225..329
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 409 AA; 47446 MW; 220260CE346281BD CRC64;
MSSNNKIKLR SPYLSLNFDD CMSTPKRRIS WSPKICTSIV EEICDSAFGT PEMNRKSLEL
NDSFCTNFEL SPLLKENEDD FAWSNGWDSE FTNNTPKSIS QLLEKPLVNS ESKTEKRSKI
ATKKPINVLD TNNDTPRRKS KEKKAFSLIG RRKPSVLIDK FNRGYSESEK ISIMNAVQIS
SEDPDLIGDF TRPHALPLIA GKHEDMKSIS IETMRRVLNG DFHSRVKEFI VIDCRFPYEY
QGGHIRGAVN IHSKDSLEQN FLRPLQMDSK CVVLIFHCEF SSNRGPSMYR FLRGKDREVN
EYPNLHYPEI YVLDGGYKAF FERCEELCEP KSYKPMLHAD HREELKFFRT ESKMLIKEKS
KIGFRRCSKT QDVVASVDEV SVVDDSTRLK SLFNWSVFVF KFFLCFCKK
//