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Database: UniProt
Entry: D9YID1_BACDO
LinkDB: D9YID1_BACDO
Original site: D9YID1_BACDO 
ID   D9YID1_BACDO            Unreviewed;       507 AA.
AC   D9YID1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 45.
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:ACU32444.1};
OS   Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Bactrocera; Bactrocera.
OX   NCBI_TaxID=27457 {ECO:0000313|EMBL:ACU32444.1};
RN   [1] {ECO:0000313|EMBL:ACU32444.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22105664; DOI=10.1002/arch.20446;
RA   Suganya R., Chen S.L., Lu K.H.;
RT   "CDNA cloning and characterization of S6 kinase and its effect on yolk
RT   protein gene expression in the oriental fruit fly Bactrocera dorsalis
RT   (Hendel).";
RL   Arch. Insect Biochem. Physiol. 78:177-189(2011).
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; GQ203802; ACU32444.1; -; mRNA.
DR   AlphaFoldDB; D9YID1; -.
DR   EnsemblMetazoa; XM_029549633.1; XP_029405493.1; LOC105224794.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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:SF230; 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   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          74..335
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          336..406
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-50"
FT   BINDING         80..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51"
FT   BINDING         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   507 AA;  57201 MW;  C67A8FECF8B88E0D CRC64;
     MADVTDASGV FDLELHEEEN PRDSDDDRIE LDDVDLEPEL SINNIQEEVE GQETIQLSEE
     TVNPGKIKLG PKDFELKKVL GKGGYGKVFQ VRKTAGRDAN KYFAMKVLKK ASIVTNQKDT
     AHTRAERNIL EAVKHPFIVE LVYAFQTDGK LYLILEYLSG GELFMHLERE GIFLEDTTCF
     YLSEIILALG HLHKLGIIYR DLKPENILLD AQGHVKLTDF GLCKEHIQEG IVTHTFCGTI
     EYMAPEILTR NGHGKAVDWW SLGALMFDML TGMPPFTAEN RKKTIETILK AKLVLPAYLT
     PEARDLVRRL MKRQVPQRLG SGPEDAAAVQ SHPFFKHVNW DDVLARRLEP PIKPILRSED
     DVSQFDTRFT RQIPVDSPDD TTLSESANLI FQGFTYVAPS ILEDMQRANR MPARSPRRTP
     RQHHEGSYRM QFPPQRGIYP RATPPHLQAF PPRPSPQDEM MDVQGVPIVQ LKADGNCKPT
     LATASARAKT NTRPKNINDG GSSAKEN
//
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