ID U6MYB4_9EIME Unreviewed; 1550 AA.
AC U6MYB4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Dual specificity phosphatase, catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ENH_00066340 {ECO:0000313|EMBL:CDJ69232.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ69232.1};
RN [1] {ECO:0000313|EMBL:CDJ69232.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ69232.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ69232.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ69232.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; HG725685; CDJ69232.1; -; Genomic_DNA.
DR RefSeq; XP_013437699.1; XM_013582245.1.
DR GeneID; 25476769; -.
DR VEuPathDB; ToxoDB:ENH_00066340; -.
DR OrthoDB; 49652at2759; -.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14498; DSP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR46381; MKPA PROTEIN; 1.
DR PANTHER; PTHR46381:SF4; MKPA PROTEIN; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 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 796..1005
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 936..983
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 165640 MW; 06314228C937845F CRC64;
MGGVSSTVHF ERPALGPNRS TGPLAPPEKR EEGPSSVSAS LASGKKPSMS LWLTQDGDRT
LDAVIHALRQ WGSTSAHLAP VESSCLESLS GCLLQQHQML LAWKMSRIGA PGRCGCCETL
LPLGVSPKGV TGTSNATDKG QRRPCSSNST TSIRSDSPAE DVNLTGGGKS GGERGQASEG
WRRTIGANIP HPDPSSCYLI IHAYTAAQQQ QEISSTLEGP TDRRRSLSPP RARGTTRNPS
LPGDPQCNFD GRNYNSRVAA ELMSGDVASL LSQAESLIAL DTRRHSVWHA VHCCACCSLN
QQQRRHVTRD DACRRGECSA QCYEADVSDS RKGEQLQPEE QQPQRKQQHL WAVYLWEGVE
APRYILDHAR LRTLRLVDAF ESCEQRGFPI LPEVLLPWAS FAILRPDREG PRCWPVVRAC
PVGGVSASQT EQEPVFLDAG ALLERNVLLL RLLLRPPRLA YRTPPSVLPA PAEPATASQS
AAEIGNRADE IRNSSASTGG DERATQQHQQ QQRDRPSQTI PVVPPLALPS KGLPQLQHPE
AGNKRDGEGR PLRIDSSALR RVAPGRGGLQ LHATDCAGSD DNSFPSSFCD SPVASGEISP
SESPSAERAG QDIQRVSHRN TDGGPLRQRN FRLQGVPKLV IPRLGGGEPT VSPAGCAPSG
EVGGSLSPPF RAVGGSSSSF LQCTEGEASK SFSLAFGTSS AASRETATAS SSLKQQQQQV
LPAGARLSGV SVGSVGGLHH SGLLSSPAAS FAGLQRLGSD GSSAGSSREA FGSRRRRIDD
DGMGLYSRTR QQQLVNFRRV ISDVYEGCLF VSGAAAACDL QCLKQAGITH VVNTIGDICP
NVFAPLLIYK TYYLKDTRQQ DIMCVFYDCI RFIYEAIGEN TRGVAAPLSP RESIRANTDA
SGAASLAAVS GVCNPDASKK SRKQNSDESC SSFSNNSGSR KPHKVLIHCK EGVSRSATLA
IAFLMWKLRL PFAEAFERLR SRRAICSPNT GFTFQLLLLQ KRLGLKPHRA AFSCRNQAHS
RDGQEALKTP PTLRSIPSEG PSSPGPVSDR QWTSGKGLKR AGSPLESRAS PRPSVGSEEL
PPGAPGSPGA LSPHSAQERC SHSPVGEHLS SDGSHLEVSD AVVTLRGLRP HSPRVCAPPR
PGGDSSENEA GSEVGPQRES PSSSVEAAIT ARGRISSAEE DCVLLLHLVV HSAHSPDFLL
WSEMTEWRPG VVPAMSEKGA YMLRCNGQGW VWMDASKCLR TAAQVEAAAS NYQENVALVE
GRSIRLHFIT AGSEPADFWL AFGVGAETPH PHLGVPNVLS GLEPMVPEKS EEPFRWRDYC
AFDLPGDWAE GDFPAGSADG DAMEAVVSQD LFAVPGEIVL EGTPEEPCQA GDETHIRYQS
NSSCSSASSC VPSLRRSFKA FGHAANRASA GAPPEEVATV AGTHAKGTAK LFCLPDLEEP
LDLFDSEDLF SDKVYLLVAD SNDSTGRLPR AASPVPATAA TGAVTAWLWV GSEAALDSQN
DYEAVKAQVM DAFHLQPGQL QLSVEVSALA SLLLLLFLFM PRAVQRSSPA
//
