GenomeNet

Database: UniProt
Entry: A0A182M0L4_9DIPT
LinkDB: A0A182M0L4_9DIPT
Original site: A0A182M0L4_9DIPT 
ID   A0A182M0L4_9DIPT        Unreviewed;      1701 AA.
AC   A0A182M0L4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA006547-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA006547-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA006547-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   EMBL; AXCM01000338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 139723.A0A182M0L4; -.
DR   EnsemblMetazoa; ACUA006547-RA; ACUA006547-PA; ACUA006547.
DR   VEuPathDB; VectorBase:ACUA006547; -.
DR   OrthoDB; 2880940at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   CDD; cd06611; STKc_SLK_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR022165; PKK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46538:SF3; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF12474; PKK; 2.
DR   SMART; SM00220; S_TKc; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          37..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          320..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1431..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1606..1635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1657..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1020..1106
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1295..1344
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        336..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..581
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..872
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1606..1626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1657..1684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1701 AA;  188574 MW;  9717C41596876E6C CRC64;
     MSFLNNLKKV FHLGSGEAKK KRIFNNIRMD TDPADFWDMI GELGDGAFGK VYKAQNRDTK
     QLAAAKMCTL EDEENLSDHM VEIDILSEIK HPNIVGLYEA FSIDDKLWML IEYCDGGALD
     SIMVELEKPL TEAQIAYVCK HMCAGLNHLH KNKVIHRDLK AGNVLLTMDG GVKLADFGVS
     AKNKHTMQKH DTFIGTPYWM APELVLCETF RDNPYDFKVD IWSLGITLIE FAQMEPPNSE
     MSPMRVLLKI QKSEPPKLDQ PSKWTKHFND FLARALVKDP QQRPSTDVLM GLPFISGNLD
     SKPIKDLLLE YKADVVEEEL VDEEAEEPRN SALPLDLDDD SSSLQSQETD KLPDTPTSLS
     KSSRDSKEST PVPATEDHSS KPKIGPIPTP IGAAGPPGTT PLEKTPGSVD TKSEMKKSQP
     APPIVPAAAS PISGDVSAQP MIKSSSSSSN ISGGAVNVPT PVLPVPKEII PEGVKMITST
     STPSAVRNQL PHHATLMNSS SSSSTTSITI NDATVLSDPS NSLASNVAQV TVVTSHPPVI
     IDNSIPLPPT AAAAVASSGT SSSASSTKSF GSSQQRRSRV ISPPGTGAHD EVIIVSNELN
     KTHVNESSTD DDFQSLDSLE NVSPRHHPIR TPSQSAGGRA IARKLDESEV LIVSSGFDDR
     REVLLVDDTN AGSPDRDVDA YGDGDLFNAS GNNLLNNSSK LLLDTSHVSV VTVGEEEIKV
     KDSSQHHPQL INNPHTSPHH YHHDSTSDLS NFHESREDVS IIVNKRKIEK SRISPDSSVG
     SLEGGGSIRS ASTPIHQNHH PHQHGGAAGV MVAGNHHQRT GSIGTVPVTK HLHDRSDAES
     IATTTSHDSR EHAAVDLEEE VTLRRKPVSS LELEDGKGSS SVGGTLSSGS STLVSTAGDN
     SIATTTAGTP GVAGTAVAST GGTAAAGGNG TAGIKQKANR NFTKEELHLQ NLKKKTRKRT
     RKFEIDGVQV TTTTSKVIYS DEDNNKLYDD HLFRKQELRE LKMLQKQEKK QFYDLQGKEA
     IAKEQQEKKF EQERLQLERT FEGDMDVLAR QHRQTVEKFE QQQEAELRNT SKKIRAEQER
     DLKLFRDSLK QEIRLLKQEV DLLPKEKRKD EFRKRKTQME FEHEEREKSF LSSLSENHEL
     ALRRISEIYR EKLSATDKGY LQQKQTAMRT REAMLWELEE KHIHDKHQLA KRHVKDICFM
     QRHQMIIRHE KELDQIKRMI TRKEEELLKR QTIERRALPK RIRAERKARD MMFRESLRIS
     MTTDPEVERD KLKKFQEQEK KRYNQEQLRF ETKHSKQLEE LRATSEGSIR ELEQLQNEKR
     KQLLEHETAK LRECDEALQK ELREWKAQLM PRKQAIEKHL SRMVDEYEDH WGPVDRREFD
     GDFTVPPELR NRTNSLNTLS LRLLNITRSR TFLTLPTMAN GGVAGGGVYG GSGNGGNSNR
     NSIHSSVPDL SRSMPNTPNS GHKLSLASSY DSVLEENEGE NQPPTMDVGR NGGGRGSSYQ
     HQSAIKYIHT NDPVVSGNVH VRRKSEDMLS GKSRSTRVPI KSFLYSNTSN RYEYGGSSAY
     YGGDYGGSRG SSNGPMAYYS DSKDRVVSIR VNNQAINRKP ANVFEGMTNR SNIPQSHTSS
     GGTMPRRTSA GWGPSRLGEN TFTTASDANI NRLTTFSSAR GGLPLPTANG SSGRNTTNPG
     LKLSPSTPVL LAPSKDDDTV V
//
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