ID A0A1I7RSB5_BURXY Unreviewed; 347 AA.
AC A0A1I7RSB5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0361900.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0361900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 -!- SIMILARITY: Belongs to the MPI phosphatase family.
CC {ECO:0000256|ARBA:ARBA00011065}.
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DR AlphaFoldDB; A0A1I7RSB5; -.
DR WBParaSite; BXY_0361900.1; BXY_0361900.1; BXY_0361900.
DR eggNOG; KOG3772; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
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};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 206..315
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 347 AA; 39885 MW; 2A89B0DB14189F4D CRC64;
MICCLRMEVE NHDENAQCPF GSDPPLCLAT SILDEMLPAA SNDSGVGSSC SAWSIHEDKT
NFMVPGTSNS FEDVQMDEAK VSPIRRPLRD VSNDTPLKGK RFNRIPFRNN PISTRKLSTR
VPMKKIEGRF LKRPPPRLPS SVVSLEKGVS KSMVNMRRFG RCTSPESIHT YSLRYLTKPQ
VESSAFKSID GSILASLIKE MGNEKFLETF MLIDCRYPYE FEGGHIINSI NMFQFDQVCQ
KFYSEENGSF HAIQNKIPIF YCEFSQARGP KMATALRRFD RKLNESNYPH LDYPEIYVLD
SGYQGFFKQK EHSDLCTPRH YVRMQDTAFL EGLKRFHYHK KGVNHQI
//
