ID U6GDY0_EIMAC Unreviewed; 1172 AA.
AC U6GDY0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Dual-specificity phosphatase, catalytic domain-containing protein, related {ECO:0000313|EMBL:CDI78476.1};
DE EC=3.1.3.16 {ECO:0000313|EMBL:CDI78476.1};
GN ORFNames=EAH_00033870 {ECO:0000313|EMBL:CDI78476.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI78476.1};
RN [1] {ECO:0000313|EMBL:CDI78476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI78476.1};
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:CDI78476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI78476.1};
RA Aslett M.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the type-I AFP family.
CC {ECO:0000256|ARBA:ARBA00006358}.
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DR EMBL; HG670874; CDI78476.1; -; Genomic_DNA.
DR RefSeq; XP_013251296.1; XM_013395842.1.
DR AlphaFoldDB; U6GDY0; -.
DR EnsemblProtists; CDI78476; CDI78476; EAH_00033870.
DR GeneID; 25271457; -.
DR VEuPathDB; ToxoDB:EAH_00033870; -.
DR OrthoDB; 5472710at2759; -.
DR GO; GO:0050825; F:ice binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000104; Antifreeze_1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF519; TYROSINE-PROTEIN PHOSPHATASE VHP-1; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR00308; ANTIFREEZEI.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Antifreeze protein {ECO:0000256|ARBA:ARBA00023076};
KW Hydrolase {ECO:0000313|EMBL:CDI78476.1}.
FT DOMAIN 894..949
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 37..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 119265 MW; D11A9137B45340FE CRC64;
MSDEAAAAHN RLHIPYSPYT PAGAGVSLLL PLPPTPRCLE KGPPAAAARG AEQQGAPGGP
RGGPPRARSA PRAVSTIKEY TRRSLCNPNT PRAPVEGAPF YRASGGAPFA VAAKETPGTR
LRRSGVRTPP KQQQQQQQQQ QQQQMSTRRL SASPARACQG MGAPRGAPIG GPPSGDCSVA
ALAEALERNQ RELSKLNLNL QEKLIGIDST ANKREAGGGP PKPFASCRGA PNPEAYGSSK
RPFSVGGPHP TAAAAAAAPA AAAAATTTAA ARARAGSRGP LQGTGKAGGA PTPSRVVYRG
APRGPPEEIT EGERIRFMLA LETAERQFGE RLQQCVSVLP QELSKKVAEA GPLEEKLQQL
QGALLLLLNK QPLDRGLSPS EREGLRTLGL QKKREGKLQA ALSETRAKLE ATRQQVAALR
RLLLPLQHSI GAYAALQRGN GGAAAAAAAA GGAAAAAARP YSPYRPAVPA LLASEEGPPY
QPNLFKDMQT AAQTNEGSTP RPYREAAEGG PQTSIGAPPN PLHRRGAPHS AGAPWGGPHG
GPPGGPPAEE EAVGAPSEAS EEAGRYSLKG GGPLQTDGGP PLEYEGSGFN VCDKKGRRSK
DKEILFKEFK AVEQHIAASS NSSSSSSSSS SKQSFEATLS NERRHYEAET AEEKTQVRDL
SAAESSSLFT WDQDEDDVKW ASEFLKRQEL GVGGCYRGPS AEEASKTLEE KKSSPASPLH
ARVLSPGYEG PPWAVGPPGP PQGPGGAPQG TRGAPQGPQV PRGAPQGTRG GAPPQGTLPG
TRGGAPQGTR GGAPQGPPGA PRGLQAAGSP MGRRAIGPPG APGAPGAPLH SGGGPLGRGY
SMGPHNMPPR LGWVYKEDAA VAAAAGEIYA YVASLPAACT SSKLGPGLAM RFEQMPLGAV
REALVRGCNV LIHCEKGISR SVAVCMAYLI LYEGHSFRSA YLAVRRHRPI ARPNVGFIQQ
LLQLEATVSS RGAPGGPRAL QQQQQQQQQD AKHRTRINQY LTYKQQDPAA AAAAAAAAAT
AATAAAATAA TAAAAAAAAA TPATLATAPP VTPAALAAPA AAPAAAPEEA AAAPAAEAAA
PAPAAAAPAA ATTTAAAATA AEAHRRELHQ HTQDLINSAV AATSAAAAAA AVAAAAARRS
GSATPSGPQQ GPAAAALHRG APTRALKGGG AR
//