ID A0A099Z1Z6_TINGU Unreviewed; 608 AA.
AC A0A099Z1Z6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE Flags: Fragment;
GN ORFNames=N309_14079 {ECO:0000313|EMBL:KGL75727.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75727.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL75727.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75727.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750}.
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DR EMBL; KL888311; KGL75727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099Z1Z6; -.
DR STRING; 94827.A0A099Z1Z6; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14606; PTPc-N6; 1.
DR CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR CDD; cd10340; SH2_N-SH2_SHP_like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR PANTHER; PTHR46257:SF4; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Receptor {ECO:0000313|EMBL:KGL75727.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 6..102
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 112..226
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 257..528
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 443..519
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 564..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL75727.1"
FT NON_TER 608
FT /evidence="ECO:0000313|EMBL:KGL75727.1"
SQ SEQUENCE 608 AA; 68600 MW; 89D572FAF12D1170 CRC64;
ISSARWFHRD LSGLEAEALL KGRGVHGSFL ARPSRKNQGD FSLSVRVGDQ VTHIRIQNTG
DFYDLYGGEK FATLSELVEY YTQQQGSLQD KDGTIIDLRY PLNCSDPTAE RWYHGHLSGS
AAESLLQAKA TPWTFLVRES LSKPGDFVLS VLTDQPKPGS DAAPAGATSG SGPRLKVTHI
KIMCENGRYT VGGAEVFDSL AELVEHFKKT GIEEVSGSFV YLKQPYYATR VNAADIENRV
QELNKKSLAE ESSKAGFWEE FDSLQKQEAK HLYDRHEGQR PENKSKNRYK NILPFDHSRV
ILQGRDPNIP GSDYINANYV KNNLISPDEC TKTYIASQGC LDATVNDFWQ MVWQENTRII
VMTTREVEKG RNKCVPYWPE VGNTKEYGPY LVQNAGEHDA LEYKLRQLCV WPKNDGESMR
QIWHYQYLSW PDHGVPSEPG GVLSFLDQIN QKQESIPCAG PILVHCSAGI GRTGTIIVID
MIVETISTKG LDCDIDIQKT IQMVRAQRSG MVQTEAQYKF IYMAICQFIE TTKKKLEVIQ
SQKGKPNESE YGNIAYPPAV RNTHAKAMRK SSKQKEESTV YENLGKKEEK VKKQRSSEKK
LKGSLKKK
//
