ID J9IW88_9SPIT Unreviewed; 474 AA.
AC J9IW88;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE SubName: Full=Dual specificity phosphatase, catalytic domain containing protein {ECO:0000313|EMBL:EJY86497.1};
GN ORFNames=OXYTRI_13603 {ECO:0000313|EMBL:EJY86497.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY86497.1};
RN [1] {ECO:0000313|EMBL:EJY86497.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY86497.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY86497.1}.
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DR EMBL; AMCR01002121; EJY86497.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IW88; -.
DR EnsemblProtists; EJY86497; EJY86497; OXYTRI_13603.
DR OrthoDB; 5472710at2759; -.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR46642; DUAL SPECIFICITY PHOSPHATASE, SUBGROUP, CATALYTIC DOMAIN; 1.
DR PANTHER; PTHR46642:SF3; PHOSPHOGLUCAN PHOSPHATASE DSP4, CHLOROPLASTIC; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 42..178
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT DOMAIN 318..474
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 401..453
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 474 AA; 54824 MW; 2C1620C2DB675237 CRC64;
MEHRRNYDQN HYSHNLASNE EFNLFSNNSS TNGHENLSVV SAPHTKCYQV QFQINYQTDY
GQDVYIIGSI PELGKNSQNN LLTLSFKEVG NHLLRNQNGQ LQDNRCIYIY FDQGHNWVSN
VLTVAKDFFE YKYVIVETSS KKAIRWEQGF NRIADLKLLD QQQTNSTNHL IQKDEWDRFT
IVFSIFYPLK DENEYMRING DIEQLGMWNK GTGPERLVQG EEITWLTGQK VRPWEYRVRV
QQSDFKQRIT YKYSIRNDLK DYTIWEREPS RYAQIQEPGF YLGELGDSGS SKWPNVDNVF
IVNGMINKAD ANFVGGLSFD KIADTKLFIG PYPQLEEDVI AMAEAGVTGV LNVQTDIDIA
HRGINWPRML EYYAQHKVTA VHYPIHDFNE EDLKAKIKGG ADILNQMINQ QGLDVYVHCT
AGMGRAPAVV LTYLCLYKGM DPDEADLFVK THRKVSVPNM RAVREIVSKH RAMI
//
