ID A0A1A9ZYX9_GLOPL Unreviewed; 1277 AA.
AC A0A1A9ZYX9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI029296-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI029296-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI029296-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A1A9ZYX9; -.
DR STRING; 7398.A0A1A9ZYX9; -.
DR EnsemblMetazoa; GPAI029296-RA; GPAI029296-PA; GPAI029296.
DR VEuPathDB; VectorBase:GPAI029296; -.
DR Proteomes; UP000092445; 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:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR CDD; cd05041; PTKc_Fes_like; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 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:SF418; TYROSINE-PROTEIN KINASE FER; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
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..162
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 912..1003
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 1015..1270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 603..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 481..540
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1044
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1277 AA; 146490 MW; A14B0C97BC9C8B6D CRC64;
MMLKHIKLMQ IASYIAYSAY RSPQKSNLTD EVVRKKTEYQ KHLEGYKALR TRFEEHYIKS
GRSGRKLDDV RDKYQKACRK LHLTHNEYVL SITEAIEVEK DFRNILLPGL LEHQQSVQES
FILLWKNILQ EASQHGDLTS DKFKEIQKRI DNVISSVNPN EEYREFTEKH RTSPTSPVVF
QFDEALIGDI PGKLQSSTLA VDNLTVDWLR TRLLDLELSV KDCQEKQLKM IEHVDGGAPV
IANGSLSSNG TNGMQSSKEN QNRHCKDLNA LRCQEKQKQR LVDMIKFALN EVGCEELPSG
CDDHLTLDQN FIEDSFNNHQ QNSNSTSVSI MTELKRRGGV LTLLRGRHFK RKSTPQPTTP
TTACRAKRFN TKMKPRSQSL GSLSVICPNT PYRYEPIFTN VPLRMAASDE ANNNQDFLHD
LSELKEDMYS LKFVPSKLRR SLSHGSVCVQ VEVVRVVAEM RGDNNTNSHS MAMNNNHIYA
ELDLKEEREV NEEKLNEMKQ NINPTVERTS TAKKTEREQI KKIKENMPNQ RKINEQIKQK
SFEEKPKTSA IVSEAMQNSI DAHLDKIDAL NRALDNRLKC TGSPQQETDL DAIESAELQD
VVARSSNDTN QTSNKRVSSS NSDKEVRISD AVSYNIIDNK TKKRSLSFSQ KSINALLCNI
KEFSKSPLTK MHRSQDSKDS FPGSPETSFA NLQKSHNEIK SNTDVVDVNP QKLSTTLPPP
ENHSISLNNA VEPFHKQLEH TCTVTSNPSK IDTNLITSKL KFKVPKIQKK SKALRQTFRS
KFLHFQLKRG NQCQTCTKKR RIYPSKSVFD FAKEFNLNED NDEFCTCPRS YHSVPKIMQN
KTGVGDDAGD DDNSSDDVLS IKDHCYCVPS LSTSQNNYKT YESYFQMNSC YFQRFFTQMS
LTTNRPLYEE EWFHGVLPRE EVVRLLNNEG DFLVRETIRN EESQIVLSVC WNGHKHFIVQ
TTADGHFRFE GPPFPSIQEL IMHQYQSELP VTVKSGAILR RPICRERWEL SNDDVVLLEK
IGRGNFGDVY KAKLKSSSLD VAVKTCRMTL PDEQKRKFLQ EGRILKQYDH PNIVKLIGIC
VQKQPIMIVM ELVPGGSLLN NLRKNSNHLT IRQQMGMCRD AAAGMRYLES RNCIHRDLAA
RNCLVDFENC VKISDFGMSR EEEEYIVSDG MKQIPVKWTA PEALNFGKYT SLCDVWSYGI
LMWEIFSRGD TPYSGMSNSR ARERIDAGYR MPAPENTPPE MYRLMLKCWS AEPESRPHFD
EIFNVVDALI LRLDNSH
//
