ID A0A074Z0R2_9TREM Unreviewed; 916 AA.
AC A0A074Z0R2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dual specificity phosphatase, catalytic domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=T265_15277 {ECO:0000313|EMBL:KER20626.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER20626.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER20626.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL597038; KER20626.1; -; Genomic_DNA.
DR RefSeq; XP_009175640.1; XM_009177376.1.
DR AlphaFoldDB; A0A074Z0R2; -.
DR STRING; 6198.A0A074Z0R2; -.
DR GeneID; 20329442; -.
DR KEGG; ovi:T265_15277; -.
DR CTD; 20329442; -.
DR OrthoDB; 2901840at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF540; TYROSINE-PROTEIN PHOSPHATASE VHP-1; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..216
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 317..459
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 386..437
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 99918 MW; 2C3F356871596D6F CRC64;
MPHKREIRWC SNSPLGPSER EFTDRKVRGS NPTSATRLPL SGPGQPGSIP ALVLPSGGML
MDESSLQSTV QLVDPGCLAE RIRMDQSFIL LDVRSFVDYN TNHITQAVNI GGNRGFRRKF
LQLMVCSMFT ILYAVLVFQV PIDVFIQRLM GLPHDTDALH ATPVVVYDHC LDDLRNLSPD
CFLHSVLGQL SKKFCSIFLL KGGFLTFHAL YPELCWESPK RLAGEDVAEY HHSDCDLEHI
LASCEETVPS TALVSSSSVA ESSDIFRSSA SFTPMTATPQ LTQSTHMSKS VKRASGIHSG
YQKETSFPGL SSSDSPRPSP ILPHLVLGSQ LDALSAAVCH QYGITHVINV SVDGSAPPHI
PVENFYRIAV NDNYTDRMRP YFEQAFQFID QVKANRGRVL VHCSAGISRS PTLAIAYLMY
TCRISLRKAY SIIKNGRATI APNFNFLGQL VEFERELFPA SEPSSGEPHA VLSSLDVEST
IPATLALVAD KIDSPTASTP TTATCVRPIV RRPSFVVASR SSLSPKHSMM KKRDRPTYLS
LEAPGCSTTS RTYLPGNNLD ISPTEGKRSR VSCLTTFSRG SASLLPSPCT VLSRLELSSP
SDVYSHSVVS AQQLAFPATS DHNCKRKPYD ITTALFIHPS TSLDKLYFEP CSVSDYHHPR
RDRLLRSVTS LPVPPRRPTL LAERRLSSQA SAPTTPQSSS IDCPLLPIPR PLHPKNEATA
FSRPTSTNPT IPLPVSFAHN ESASLLTKQK AKVDSSSSTE APGRVLSSTY CDIRPPGFTD
TRSCSVDSLC RTSTRKLLFC SARSNSASGR GSRVSFSAPA GPTNTPISPF MTPNLRNSVS
AGQDVSWSSL YPGATPLLTV RRARGPLRPT AFESCRQEQQ QLFHQSSSSS SSNLSCSSTG
PNPTHNGSHF NPYPVS
//
