ID A0A091TUG2_PHALP Unreviewed; 610 AA.
AC A0A091TUG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000604};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000604};
GN ORFNames=N335_05392 {ECO:0000313|EMBL:KFQ81407.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ81407.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ81407.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ81407.1};
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,
CC ECO:0000256|PIRNR:PIRNR000604};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000256|PIRNR:PIRNR000604}.
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DR EMBL; KK465147; KFQ81407.1; -; Genomic_DNA.
DR Proteomes; UP000053638; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd05116; PTKc_Syk; 1.
DR CDD; cd10401; SH2_C-SH2_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; 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:SF231; TYROSINE-PROTEIN KINASE SYK; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000604, ECO:0000256|PIRSR:PIRSR000604-
KW 2}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000604};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000604,
KW ECO:0000256|PIRSR:PIRSR000604-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000604};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000604}.
FT DOMAIN 14..99
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 160..251
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 346..610
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT BINDING 352..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 610 AA; 69985 MW; 03F3743771A4369D CRC64;
MASNTTNPAN HLPYFFGNIT REEAEEYLMQ GGVSDGLYLL RQSRNYLGGF ALSLAHGRKV
HHYTIERELS GSXXXXXXXL INYHSEEADG LICLLRKPFN RPPGVEPKTG PFEDLKENLI
REYVKQTWNL QGHALEQAII SQKPQLEKLI ATTAHEKMPW FHGRISREES ERRILIGSRS
NGKFLIRERD SNGSYALCLL NDGKVLHYRI DRDKTGKLSI PDGKRFDTLW QLVEHYSYKP
DGLLRVLTIP CPQLGSENGK LFLWAGGGII SRLKSYTFPK AGSKKVPYIV FVGFCLRLRC
HQKSITSLNS DQREALPMDT EVYESPYADP DEMKPKNVTL DRNLLTLEEG ELGSGNFGTV
KKGFYKMKKG AKPVAVKILK NESNDPAIKD ELLREANVMQ QLDNPYIVRM IGICEAEAWM
LVMEMAELGP LNKFLQKNRH VTEKNITELV HQVSMGMKYL EENNFVHRDL AARNVLLVTQ
HYAKISDFGL SKALSADENY YKAQSHGKWP VKWYAPECMN FYKFSSKSDV WSFGVLMWEA
FSYGQKPYKG MKGGEVAQMI ERGERMERPE VCPTEVYDLM KLCWTYNVDD RPGFVAVELR
LRNYYYDISH
//
