ID A0A2A2J9M5_9BILA Unreviewed; 897 AA.
AC A0A2A2J9M5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=WR25_26673 {ECO:0000313|EMBL:PAV58212.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV58212.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV58212.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV58212.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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}.
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:PAV58212.1}.
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DR EMBL; LIAE01010594; PAV58212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2J9M5; -.
DR STRING; 2018661.A0A2A2J9M5; -.
DR Proteomes; UP000218231; 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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT DOMAIN 647..788
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 712..766
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 263..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..258
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 793..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 102518 MW; DA7BCA5CD48C8A06 CRC64;
MPPSSDPVND PFYQKLFRLF SHFADVLPEG TLRPSQGEFL LDELLREAGR PTTSKKVSFP
DDVSFRELLN LLEVLFPDRL ELEPAAERVF ERIIGHLIRK GFILYRQMYR KRGCLPQKKV
SWSPGWCTIE PGTLTLYPLA KNSKHFQILL NKEVAIEYCG YLDGRFICTV RNGNNRIDLA
HFDDLAIKTF IRDRHVDIEV AQRQALEKEK QKLEKELESE RQNLRDEEIV RGLATRMLEE
EKQKSEQMEK VLYELQMKLE GRSSRREFRG EGDDGNEEDT EIEETLEEIP ENEMDKEHRR
EEELRNYAYH LESSNYDADD EDGRSSPFVS QSVGMSIVQV QRTPSPSVGD ESESFDFDDS
RCSSRNRSIS ECYFAVKGAA VILPHSQSPP VGTRDSFSAS EIQEHLPLMI KLLRQNDSLN
MAVCLQTNVP EHIRYLVIVT TNQATEGNDK DARTLLIGMD YFEGNISIGV VLPLLWCSEV
KLTGDGGVVV YGSARTPKKA DNTLLFRPTS VQTMWFVFQF LHRELERTIR EMTGRKMKEP
SLATEHYMDR INSPVVLCAQ WQQSPLDEDE DYGLGADVVR QQGSPGDSLS MQSEIRGELR
HVMQSLDLEQ VTSRDIKEAL TQELGNVDAY KEFIEIEMLV ILGQMEKPSQ IFDYLYLGNE
WNASNYDELM SNEVGYILNM TREVDNFFPQ QFCYRKYLVS DEPSTQLLSH WNETTEFIKL
AKESGKKCLV HCKKGVSRSS STVIAYIMKE YGWALDKAVD HVKKRRNCIT PNRGFMDQLR
QFAGALEASR HRHSAVFNRE DNNRISNRRD RSAEPRPQPS SSSSFSSSSS SRLPVSVRGG
VTLRSPRSRA ASATPPSQRS PIGSMTANRA STGNSVRCIV DQLERTTRTS IQERVGS
//
