ID A0A4D9DYD0_9SAUR Unreviewed; 636 AA.
AC A0A4D9DYD0;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=DR999_PMT15133 {ECO:0000313|EMBL:TFK02559.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK02559.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK02559.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK02559.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK02559.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK02559.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK02559.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK02559.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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:TFK02559.1}.
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DR EMBL; QXTE01000185; TFK02559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9DYD0; -.
DR STRING; 55544.A0A4D9DYD0; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
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 CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF77; DUAL SPECIFICITY PROTEIN PHOSPHATASE CDC14A; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703}.
FT DOMAIN 198..355
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 280..342
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 71223 MW; BCA798665D1660C8 CRC64;
MSSELPRASP LRALFKMEPA PSASELLVGA SEFLKDRLYF ATLRNKPKST VNTHYFCTDE
ELVYENFYAD FGPLNLAMLY RYCCKLNKKL KSFSLSRKKI VHYTSFDQRK RANAAFLIGS
YAVIYLKKIP EEAYRALLSG SNPPYLPFRD ASFGNCTYNL TILDCLQGIK KAFQHGFFDF
KTFDVDEYEH YERVENGDFN WIVPGKFLAF SGPHPKTKIE NGYPLHAPEA YFPYFRKHNV
TSIIRLNKKI YEAKRFTDAG FEHYDLFFID GSTPSDNIVR RFLNICENAE GAIAVHCKAG
LGRTGTLIAC YIMKHYRFTH AEVIAWIRIC RPGSIIGPQQ HFLEEKQAAL WIQGDFCRSK
QKQRSADDGT VNKIISGLDD LSVSGSFSKV QNLDQCVEND FEDNAEMESK NGMTQGDKLR
ALKSQRQPRS ATTGALRLED MKLHTRSVSQ PFRLNSSSSS QGSMSPLKSS KVAAAVSPSA
KRISRSPTSL GSNLKSVSVN SRLGSSLGNL YAASDDTESK MMSSSSRTGF SVNHISSHLN
GSLQLPTRNY HELNNNLYNR SSNNGTNLNS HASSHGTGTD DDYSIYQPSF MGLTASPARY
LSRSIPVSSQ PQKPSQGHDR SLSTLLLQPK LSQKNS
//