ID Q535V4_AEDAE Unreviewed; 550 AA.
AC Q535V4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000605};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000605};
GN Name=S6K {ECO:0000313|EMBL:AAW21700.1};
GN Synonyms=5566289 {ECO:0000313|EnsemblMetazoa:AAEL018120-PA};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:AAW21700.1};
RN [1] {ECO:0000313|EMBL:AAW21700.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15788394; DOI=10.1074/jbc.M500712200;
RA Hansen I.A., Attardo G.M., Roy S.G., Raikhel A.S.;
RT "Target of rapamycin-dependent activation of S6 kinase is a central step in
RT the transduction of nutritional signals during egg development in a
RT mosquito.";
RL J. Biol. Chem. 280:20565-20572(2005).
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL018120-PA, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL018120-PA,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AAEL018120-PB}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL018120-PA};
RG EnsemblMetazoa;
RL Submitted (OCT-2022) 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 ECO:0000256|PIRNR:PIRNR000605};
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,
CC ECO:0000256|PIRNR:PIRNR000605};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily.
CC {ECO:0000256|PIRNR:PIRNR000605}.
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DR EMBL; AY700377; AAW21700.1; -; mRNA.
DR RefSeq; XP_001650653.1; XM_001650603.1.
DR EnsemblMetazoa; AAEL018120-RA; AAEL018120-PA; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RB; AAEL018120-PB; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RC; AAEL018120-PC; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RD; AAEL018120-PD; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RE; AAEL018120-PE; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RF; AAEL018120-PF; AAEL018120.
DR EnsemblMetazoa; AAEL018120-RG; AAEL018120-PG; AAEL018120.
DR GeneID; 5566289; -.
DR KEGG; aag:5566289; -.
DR VEuPathDB; VectorBase:AAEL018120; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR OrthoDB; 5489497at2759; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05584; STKc_p70S6K; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016238; Ribosomal_S6_kinase.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000605; Ribsml_S6_kin_1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000605};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000605};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000605};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000605};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000605}.
FT DOMAIN 67..328
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 329..399
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 401..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..442
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000605-50"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000605-51"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000605-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 550 AA; 62019 MW; 2A74CA81067D7F26 CRC64;
MAGVFDLELH EEDNIRDSDD DVIEVDEVDL EPELHINSNL DAEGSETIPL SEEIVNPGRM
KLGPQDFELK KVLGKGGYGK VFQVRKTTGA DANSYFAMKV LKKASIVRNQ KDTAHTRAER
NILEAVRHPF IVELVYAFQT GGKLYLILEY LSGGELFMHL EREGIFLEDT TCFYLCEIIL
ALEHLHNLGI IYRDLKPENV LLDAQGHVKL TDFGLCKEHI QEGIVTHTFC GTIEYMAPEI
LTRSGHGKAV DWWSLGALMF DMLTGMPPFT ADNRKNTIDA ILKGKLNIPA YLAADSRDLI
RRLMKRQVSQ RLGSGPTDGQ AVRSHSFFKN VNWDDVLARR LDPPIKPVLR SEDDVSQFDT
KFTKQIPVDS PDDSTLSESA NLIFQGFTYV APSVLEEMQQ PRVVTARSPR RTPRPHHGSH
HHHHHHMGSH SSHHHHGGHG HHRMGGAIGN GVITLEDEQM LSMPRSQAMP SSHQPQPMPH
HMMFQQQQHQ QQQQQSQPQQ QPPQQQSAAR STQFVAGPNA RHTPAHLQPF APRPSPQDEM
MEVYPELPIS
//
