ID T1E8M1_ANOAQ Unreviewed; 351 AA.
AC T1E8M1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Putative a kinase anchor protein {ECO:0000313|EMBL:JAA99518.1};
DE Flags: Fragment;
OS Anopheles aquasalis (Malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=42839 {ECO:0000313|EMBL:JAA99518.1};
RN [1] {ECO:0000313|EMBL:JAA99518.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole body {ECO:0000313|EMBL:JAA99518.1};
RG Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG University of Sao Paulo);
RA Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA Silva-Neto M.A.C., Capurro M.L.;
RT "Transcriptome sequencing and developmental regulation of gene expression
RT in Anopheles aquasalis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GAMD01002072; JAA99518.1; -; mRNA.
DR AlphaFoldDB; T1E8M1; -.
DR VEuPathDB; VectorBase:AAQUA_008101; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR CDD; cd22395; KH-I_AKAP1; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR InterPro; IPR047368; KH-I_AKAP1.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:JAA99518.1}; Membrane {ECO:0000256|SAM:Phobius};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Transferase {ECO:0000313|EMBL:JAA99518.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..350
FT /note="K Homology"
FT /evidence="ECO:0000259|Pfam:PF00013"
FT REGION 30..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAA99518.1"
FT NON_TER 351
FT /evidence="ECO:0000313|EMBL:JAA99518.1"
SQ SEQUENCE 351 AA; 37496 MW; 2B20180F17A34311 CRC64;
SGRPLLFLSL PGLALIVGLV WYRRKYKPDV GDSRGGEKRR GDECESTVGG ASCHAELEPD
VRQSSSLPIQ SVAAGNGAME SWDNCSGSGH SSAGSSRSAP IDIVPNKSPS KGGDAGLCDP
FGHSRLVDDQ EEFSFSPSVD LPDSVSRYKP NLRKFNQMLE KAQEPVIIRP TKPASLQSCQ
FKVADANGNS TPVKPKQKSQ TKAKAQAQTQ SQSQSQQQPQ KQQQTASDKA NGNTVTGSGN
AALSKRNHVE EAFDERTEQT ASPPLSICSV RSEDSGKGSS PPHSVGHASS IYEFLLPAYL
VAGMLGKEGV FVKQIKQKTG VNVIIKRNPN THTSKICTLQ GAPDDIQKAL K
//
