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Database: UniProt
Entry: A0A091P5Q3_APAVI
LinkDB: A0A091P5Q3_APAVI
Original site: A0A091P5Q3_APAVI 
ID   A0A091P5Q3_APAVI        Unreviewed;       600 AA.
AC   A0A091P5Q3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE   Flags: Fragment;
GN   ORFNames=N311_11826 {ECO:0000313|EMBL:KFP86900.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP86900.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP86900.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP86900.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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};
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DR   EMBL; KL380402; KFP86900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091P5Q3; -.
DR   Proteomes; UP000054244; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd10402; SH2_C-SH2_Zap70; 1.
DR   CDD; cd09938; SH2_N-SH2_Zap70_Syk_like; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035838; SYK/ZAP-70_N_SH2.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF369; TYROSINE-PROTEIN KINASE ZAP-70; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 2.
DR   PIRSF; PIRSF000604; TyrPK_SYK; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000604-
KW   2}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP86900.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000604-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          6..98
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          159..250
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          360..600
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        483
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT   BINDING         366..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT   BINDING         391
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000604-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP86900.1"
FT   NON_TER         600
FT                   /evidence="ECO:0000313|EMBL:KFP86900.1"
SQ   SEQUENCE   600 AA;  68141 MW;  3FEC70AFD9791F24 CRC64;
     AAHLPFYYGS IARAEAEEYL KLAGMSDGLF LLRQCLRSLG GYVLSMVYNL QFYHYSIERQ
     MNGTYAIAGG KAHCGPEELC EFYSKDADGL CCTLRKPCNR PSGVEAQAGV FDSMRDNMVR
     EYVRQTWKLE GDALEQAIIS QAPQVEKLVA TTAHERMAWY HGSIARDEAE RRLYSGAQPD
     GKFLLRQRKE TGAYALSLVY GKTVYHYRID QDKSGKYSIP EGTKFDTLWQ LVEYLKLKPD
     GLIFYLRETC PNPNMPGSDL LVPQWINVTA FQACWSNSAL QTLLFSKTQQ LKGNILSPAA
     VLERGTGKGT LFTVINNCLS WECAGNSRLL PMDTSVYESP YSDPEELKDK KLFLKRDHLM
     MDEVELGSGN FGCVKKGVYK MKKKQIDVAI KVLKSNNEKT VKDEMMKEAQ IMHQLDNPYI
     VRMIGVCEAE SLMLVMEMAS GGPLNKFLAS KKDEITVSNI VELMHQVSMG MKYLEEKNFV
     HRDLAARNVL LVNQHYAKIS DFGLSKALGA DDSYYKARTA GKWPLKWYAP ECILYHKFSS
     KSDVWSYGVT MWEAFSYGQK PYKKMKGPEV ISFIEQGKRM DCPTDCPAEI YALMQKCWTY
//
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