ID A0A4Y0BQG8_ANOFN Unreviewed; 1505 AA.
AC A0A4Y0BQG8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN020462-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN020462-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN020462-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=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
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DR STRING; 62324.A0A4Y0BQG8; -.
DR EnsemblMetazoa; AFUN020462-RA; AFUN020462-PA; AFUN020462.
DR VEuPathDB; VectorBase:AFUN020462; -.
DR VEuPathDB; VectorBase:AFUN2_003750; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR CDD; cd06366; PBP1_GABAb_receptor; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF489; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 934..958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1001..1273
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 722..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1033
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1505 AA; 170402 MW; 2D489A8AB8496BC3 CRC64;
MLSVDETTRV TSVNTLQTIY CGKLPSKTRQ MKALLKHLKI FPPKMKLAVH HPGVRFQTFI
LLLLYASTIG IVSCQLQRNS KIKSFEQYEF ECFPASAKEN LTPRFASSNQ TDSISLQVSH
RYTHQILSRI YAIFLREVLG YRNVKLVEIR DDLPTSETER MRQFCTMEHL SSRGDQWPDP
TIDVEVWLLS DYHYIPEDIR EAGAITNPGR FGLFIPKALI RKEDAFSKPL IYTMFQEDTN
DRRYYDLIKK FDIPDAVLGS IYGYAERKCG NDCDEYGMFI PSHCTMGRKC ALVLAPHYDD
THFLVKHILE MEFQLKVIWL GDKLRLGIRQ LMSVYGSDRK NAKKFLVFHW TPSEVISSRT
MEYVPVTMPR CEDMIASNDT GCKYEMTPLL KYYGKKFREA NYAFNSLVML HFKDESMQHT
FDLYDQYEDQ ILKAREEADA DQLGVTRYYD QIACDWMHTQ ESFWKAWKPP TPLEEIYVGG
IFPLSGMGLT YLGIAPAALM AQGDINNNHT ILANHRLTVQ QNDGQCRADT VMKSFISYYM
QQTRMIGILG PACSETVEPI AGVSKHFRMA VISYSAEGAF LSDREKYPYF FRTIGENRQY
EHVYAQLLPR LNWHRVAALT EDGQKATEYI SYMETLLKEH SIELISNKKF PRDRTDNEMN
RYLVDLKLKN AKIIIADVDD KVAQVIMCEA YKLEMTAENG YIWFLPIWLS NVWNLSSEVR
RPGENDGGGV PPSTPNNSTR GCTNSELLRA MNGHFSLSHA PYADDDSRLD VDGSTVREWK
QRYLQNLSQM GYTASDYAGY AYDAVWVYAL AFDRLLREDP SYFSNLHSQH TTKRLMQLIR
ATDFQGVSGR IRFNEAGSRY TIINVLQFVN GTANIVGHFT PNISAEYQLI GGDLMLNESA
IMWMTRDGRA PDDGAIVCAF ESFVRIFGIG CDDVTLIVIT MVSIISILIL SVASFLFWKE
RYDRKMKTSA KYLQKLGIDL LSPSAIPFNT LDKWEIPKDR VVINRRLGEG AFGTVYGGEA
QIEDEGWTAV AVKTLKVGST TEDKVDFLSE AEAMKRFDHN NIVRLLGVCL QSEPVYTIME
FMLYGDLKTY LLARRHLVNS KQSEDSDISN KRLTMMALDV SRALSYLAEQ KYVHRDVACR
NCMVNAQRVV KLGDFGMARP TFENDYYRFN RKGMLPVRWM APESLALGFF TPASDVWSYG
VLLYEIITFG SFPFQGLTNN QVLEHLKNGT TLTIPAGVKP QLEGLMKACW NQDYKKRPSA
SEVSEFISNY PRLLNPCLDV PLASVEMVDT DSDQFELLPG LCKYKDDSQP TADLLVGTQP
MNDLNNGYNN VSIMSTGGAQ RNNRQRAINL NDLNVATDFT TVNPLPPLED YEDEPSTRQQ
LGSNQQRQTT SANHLNVYNP IEPLLQRDTE VTKSNNSLLR YVPMFGFGKS KTVTIGGTTI
VTGSACKTVP VTTAIHCTTS LGAMGSTGGD VGGGTNSPQS PTGSVLGMSG GTMIVNARST
STTIL
//
