ID W5JHE3_ANODA Unreviewed; 1314 AA.
AC W5JHE3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=AND_004796 {ECO:0000313|EMBL:ETN63491.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN63491.1};
RN [1] {ECO:0000313|EMBL:ETN63491.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN63491.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN63491.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC004796-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; ADMH02001252; ETN63491.1; -; Genomic_DNA.
DR STRING; 43151.W5JHE3; -.
DR EnsemblMetazoa; ADAC004796-RA; ADAC004796-PA; ADAC004796.
DR VEuPathDB; VectorBase:ADAC004796; -.
DR VEuPathDB; VectorBase:ADAR2_011083; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR HOGENOM; CLU_007537_0_0_1; -.
DR OMA; HYKNTNL; -.
DR OrthoDB; 103262at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR PANTHER; PTHR22967:SF57; AUXILIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ETN63491.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW Transferase {ECO:0000313|EMBL:ETN63491.1}.
FT DOMAIN 36..309
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 463..643
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 649..785
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT REGION 323..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 140819 MW; 7090F8CC619829B5 CRC64;
MSDFLKSAMS YFNTAPSNGL DNEFVGQTVE VANVKLRIKR VIAEGGFAYV FVAQDVQSGT
EYALKRLLGT DKEECNNIIR EINVHKQVSG HPNVVKFVAA TFIDRTQTAN AQRRAEYLLV
SELCKGGSLY DCLEQDLAPE TVLRVFYQAT KAVAHLHSQS KPINHRDIKI ENFLIGSDGL
LKLCDFGSAS TDSYAPDVTW NAQQRDTLED ALTRCTTPMY RAPEQLDTWA NYPIGIKMDV
WALGCVLYLL CYRKHPFEDS AKLRIINANY TIPNDSRYAC FSETIRGCLQ VDPNQRFDTA
TVLERLAAIA ETKGWPLKAP LGLSGKPLNS PPSGVTPSPS PVHRVSNGGG GGGVGAAPER
PAPPRPTVGP PPGGAVPVGP DGTLNKNKYP QRPPDPVRVT VSGAAAHGGM VPPSHHIGGP
AYGQPAGSGG VVGGGGLFSS IKGGAGSFLK NLKDTSSKVM QTVQQSIART DLDLSYITQR
ILVMPCPSEG LESTYRTNNI EDVKVYLDTR YQPTKLSVYN LGPRSSPRMP PPVRTVEAGF
IYAPVPPSST GSGKAPLLTG LYSLVEDIYG FLSADPKTIV VIQSPDSGRA LAATVVCGLL
IYAGLVTEPE DAMQMFAIRR TPPNMRPSEL RYLYYLGDIV RSIPHLPHYK PVTLVSLAVA
PVPRMTKARD GCRMYVEVAT ADRTVFCTLQ DYERMRLYHS SEGKIALAMN VTVCGDVTIS
LYHARNALGG IGRPQGIRIC QLQFHTGYIP EEETLINYDR SELDEVPDLE HVPQKFSVAL
SVFVGDSERP PASQPPWRST KASRDPKILF ATQLEYEENV DNFITKPSSK PAASAAKPPP
PRPAPPSPQP AHRSVAGYGE AHEVIADREA DLLNLNKSGQ GSTGTGVVEQ QQQQQELHHP
VERPSNVEES FDLLGGLSPP VVNAPATAAT ESTVGNATAT KSAVLDDIFG AFEGAGPAVG
GATLTATKSS SDLNGLNLNF DHFGGVAQPA AGPTAGGGPF SNGSQTDVNA PNANNSFGFD
AFAGVGPQVF YNSAPTPMAQ QSQQQATQQS KDPFADIGNL TAGLVAGSTA NAAGGGSGGA
GWGSKGGMPS ATTPSPRSTQ FSSPTHHFSG ASTANPSPRA PSTPNHQQQQ MRSPNEGQSQ
RQPDYSRSHF AEPTAKGTTP NNGNGSNGNG ATGGRSGDIF GDILGQQGYS FGSSKNQGPR
TINDMRKEEL VKEMDPERLK LMEWTEGKKS NIRALLCTVH TVLWPGAKWT KCEMHQLVTA
ADVKKIYRKA CLAVHPDKHT GTENESMAKL IFMELNNAWT EFESDASQQN LFAN
//
