ID L5KIQ6_PTEAL Unreviewed; 647 AA.
AC L5KIQ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN ORFNames=PAL_GLEAN10025020 {ECO:0000313|EMBL:ELK11549.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11549.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}.
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DR EMBL; KB030673; ELK11549.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KIQ6; -.
DR STRING; 9402.L5KIQ6; -.
DR eggNOG; KOG0194; Eukaryota.
DR InParanoid; L5KIQ6; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF227; TYROSINE-PROTEIN KINASE FER; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
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 1..84
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 285..375
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 388..641
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 127..212
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 647 AA; 74303 MW; AFB7AE9FF8C16434 CRC64;
MKLHMLHNQY VLALKGAQLH QNQYYDTTLP LLLDSLQKMQ EEMIKALKGI FDEYSQITSL
VTEEIVNVHK EIQMSVEQID PSTEYNNFID VHRTSAAKEQ EIEFDTSLLE DNENLQANEI
MWNNLTAESL QAMLKTLAEE LMQTQQLLLN KEEAVLELEK RIEESSQTCE KKSDIVLLIS
QKQTLEELKQ SVQQLRCTEA KFTAQKELLE QKVQENDGKE PPPVINYEED ARSVTSMERK
ERLSKFESIR HSIAGIIRSP KSALGSSAFC DTVPVSEKPL AEQDWYHGAI PRIEAQDLLK
QQGDFLVRES HGKPGEYVLS VYSDGQRRHF IIQFVDNMYR FEGTGFSNIP QLIEHHYTTK
QVITKKSGVV LLNPIPKDKK WVLNHEDVTL GELLGKGNFG EVYKGVLKDK TDVAVKTCKE
DLPQELKIKF LQEAKILKQY DHPNIVKLIG VCTQRQPIYI IMELIPGGDF LSFLRKKKDD
IKLKQLVKFS LDAASGMSYL ESKNCIHRDL AARNCLVSEN NVLKISDFGM SRQEDGGVYS
SSGLKQIPIK WTAPEALNYG RYSSESDVWS FGILLWETFS LGVCPYPGMT NQQAREQVER
GYRMSAPQNC PEDIFKIMMR CWDYKPENRP KFSELQKELT VIKRKIT
//
