ID A0A182K096_9DIPT Unreviewed; 1811 AA.
AC A0A182K096;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR004178-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR004178-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR004178-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
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DR STRING; 43041.A0A182K096; -.
DR EnsemblMetazoa; ACHR004178-RA; ACHR004178-PA; ACHR004178.
DR VEuPathDB; VectorBase:ACHR004178; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin 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 GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd14513; DSP_slingshot; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
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; PTHR45864:SF2; PROTEIN PHOSPHATASE SLINGSHOT; 1.
DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS51998; DEK_C; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 480..535
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 539..680
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 601..658
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1811 AA; 193725 MW; 070A11B4DED3EE8E CRC64;
DKKSAHDEET QSKIIDGRSE CQKFSTSQGS IALMLGSNEH LRAASEDQLP ATGITAACTF
VDVSDASGST VDSVVSNNDA ANTNAAGAVE AGESKVEGKT PSRPASSCSS GSSSSSSDIQ
QHLQSMFCLL RPEETLKMAV KLESLRTGRT RYLVVVSRTV TSKRHNTGTP YLTGSGSNSS
IGNNTSSTWQ MSAPPTVTTS VATVASQPLG RITATSTGTS GQHMRHGSCS SETFSGSDTY
VSSLDNCVLS VGSTSGGRLP SGNATCRSDQ CDSKANSRLI SSTVSADVLT SGTSSDYVCA
PVSSPSADDT ALSDKRNCSN ESACAFDQGD PQAQHQQHPN SSNSAIPVEG GKKIEESCLL
GIDCNERTTV GLVLKVLADT SIWLDGDGGF SVSSCGKQHI FKPVSVQAMW SALQTLHKAS
FKAREHNFFA GGPSHDWVTY YEAHIDSDRS CLNEWNAMDS LESRRPPSPG SIRNKPTERE
ETESVIRSKL KEVMMSVDLD DVTSKFIRGR LEELLDMDLG EYKPFIDAEM LVILGQMDAP
TEIFDHVYLG SEWNASNLEE LQRNGVHHIL NVTREIDNFF PGLFHYCNVR VYDDEKTDLL
RHWDNTFKFI SRAKMEGSKV LVHCKMGISR SASVVIAYAM KANGWDFEHA LRHVKEKRSC
IKPNKNFLMQ LETYQGMLDA MKNKEKLQRS KSETNLKLTG AKEGRSLPGS EPTPLIQALN
GAGGKKHTSP TAHLSPVGKE TDLSGGIGME KIESDTSDEG TDEGDAGPSR GRTRTRQIKQ
QAALHQHHIH QDEAACTGNQ PHPKEDNPML ANNPEAISKA TKLFANLFLP PASCKPWNAC
DGRICTRGSG ALKRHKSLSP ESLNPRWPDN YDFETSSLAY AEKSFTEKSK ASRTRTMLEL
DSAVESCAVS GPSGSGRRKQ QSYSLEHLHG GALEMRSPCT ETKTIRMPCG NGQNYSVSPN
QIVHLQDKMP TSCVRKAVSS MKPTNNVNTT NLKQTRTGSF LRKLFPANSN YNSSSNSDSP
SSNAETSHVL ADSSIQSLTT TVPSTIPSAS ASLVSTVKTI VNELECNSSS SGNIPIAPPP
LLTDPGAALT ASVPIPIASV AAEAAAVAVA SAIREASRKN VVQDSAERRT SPTPDPNSTD
AHGGWKSANN PEQWDPGETT VPSSNESKNE PICWTSSAQI IQQCLAPEFP EPAAPIDSGS
SVEICERIVD SETSSCATGK SPEQGVMRQC SWSSCDSNCT GLIDEPRVVG SYVSCFSQRC
LPISQPPGAV CSGSAPPIEE KEDIPWHPGT VKRTKKRIEE RGTNAAVGTL KWNTSSILST
EKSAVVQEGG SIASCPAAHP TRHVPSQKNQ PPDLGQADGY HPPTRERQGM VSSSYARLSA
SAPDSYNLYA GPGNRAGSIG SNVTTDPMPA KRQTKLSHQH SFAGAVDSLA RIGEPVPYCL
RVSFRGSSSQ STNRQSQHQE TEDATEEDSF NAGKVRNLKM NFEAKSSVRR QGQKKVRSLP
SSPVAVHVSM GSQTKRTPAQ SVSTGVSSTV CSIMPSASSS VVSSSTSSPP SAVSVSSTIK
NNNQTKTPPE DVTVRDLVDR YEEHGPRMRQ IGSNSLSRAQ RPRSVFEPLK QTGGVGGGKP
FVQTSSLLSH STSQLRLEDS MRPPVPPIVR GLVIPQVSGS GGGSSSAHYN NNNSRTSNST
SINCNVQSGR VSSCAFGISA NSNSNAKNNN NSKPILQQPG GAAAEAGIAP GTTGGRRTQQ
HGRTHPLAKI SPNARHHHHH LHVHHHHHLV HQYTVGQLQQ HRHIGATPGS GVSGTTGPSA
TTVTANAYNT M
//
