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Database: UniProt
Entry: A0A0Q3PNI3_AMAAE
LinkDB: A0A0Q3PNI3_AMAAE
Original site: A0A0Q3PNI3_AMAAE 
ID   A0A0Q3PNI3_AMAAE        Unreviewed;      1018 AA.
AC   A0A0Q3PNI3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   ORFNames=AAES_204868 {ECO:0000313|EMBL:KQK82635.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK82635.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK82635.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK82635.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001149,
CC         ECO:0000256|RuleBase:RU362096};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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:KQK82635.1}.
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DR   EMBL; LMAW01001781; KQK82635.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3PNI3; -.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05070; PTKc_Fyn; 1.
DR   CDD; cd12006; SH3_Fyn_Yrk; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035750; Fyn/Yrk_SH3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013568; SEFIR_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF443; TYROSINE-PROTEIN KINASE FYN; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF08357; SEFIR; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS51534; SEFIR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|RuleBase:RU362096}.
FT   DOMAIN          82..143
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          149..277
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          299..552
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          878..1018
FT                   /note="SEFIR"
FT                   /evidence="ECO:0000259|PROSITE:PS51534"
FT   REGION          15..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1018 AA;  113735 MW;  A7768BB035FA42A8 CRC64;
     MGCVQCKDKE ATKLTDERDG SLTQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHATGGQG
     LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
     EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
     TKGRLANAIL TANENIYEKN CAKIVKYCFQ WYEGAYSLSI RDWDDMKGDH VKHYKIRKLD
     NGGYYITTRA QFETLQQLVQ HYSEKADGLC FNLTVIATNN TPQTVGLAKD AWEVARDTLF
     LEQKLGQGCF AEVWRGTWNG NTKVAIKTLK PGTMSPESFL EEAQIMKKLK HDKLVQLYAV
     VSEEPIYIVT EYMSKGSLLD FLKDGEGRAL KLPNLVDMAA QVAAGMAYIE RMNYIHRDLR
     SANILVGNGL ICKIADFGLA RLIEDNEYTA RQGAKFPIKW TAPEAALYGR FTIKSDVWSF
     GILLTELVTK GRVPYPGMNN REVLEQVERG YRMPCPQDCP ISLHELMIHC WKKDPEERPT
     FEYLQGFLED YFTATEPQYQ PGDNLLLENP GIAVRQLTLI SGVTTKLGNG LCVSVSSPTF
     SGTSVGHSIP VEIDESMPWS PFPKHILEKT LQSSGEDTKD EESQRPCVAP TPEPVANASC
     LCRAPACHQS VPSMEPGSSL WSRYNDPDVD VRFCSPSESI AGVVASKMHL VAMDKSGMRP
     RSQLSADTGH NSRKSEQSLS DAPEDSLEES SQWSSGSQQH SGNRPPAELG TVDTGYNSQS
     RDVMGIRHLD PPLPLVSMLN PQDLPGPLIS RVFSGPEHQQ CPMCQHLPHP NASSQAHGCF
     EHXCLAKQHP QGPSAIPRPL SNPAAKGTLR TSNLPEELRK VFITYSVDTA VEVMKFVNFL
     LVNGFQTAID IFEDTVRGID IIKWMERYLG DKTVMIIIAI SPKYKQDVEG AESQLDRDEH
     GLHTKYIHRM EHVPTWLQNT HIYNWPKNKK NILLRLLREE EYIAPPIGPL PTLQVVPL
//
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