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Database: UniProt
Entry: A0A452RSW7_URSAM
LinkDB: A0A452RSW7_URSAM
Original site: A0A452RSW7_URSAM 
ID   A0A452RSW7_URSAM        Unreviewed;       524 AA.
AC   A0A452RSW7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000605};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000605};
GN   Name=RPS6KB1 {ECO:0000313|Ensembl:ENSUAMP00000022429.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000022429.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000022429.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004294}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804, ECO:0000256|PIRNR:PIRNR000605}.
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DR   STRING; 9643.ENSUAMP00000022429; -.
DR   Ensembl; ENSUAMT00000025067.1; ENSUAMP00000022429.1; ENSUAMG00000016594.1.
DR   GeneTree; ENSGT00940000154203; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR   GO; GO:0045948; P:positive regulation of translational initiation; IEA:Ensembl.
DR   GO; GO:0031929; P:TOR signaling; IEA:Ensembl.
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:SF48; RIBOSOMAL PROTEIN S6 KINASE BETA-1; 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   3: Inferred from homology;
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:UP000291022};
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          91..352
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          353..423
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..48
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-50"
FT   BINDING         97..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000605-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   524 AA;  59245 MW;  2A7D42B138A135A8 CRC64;
     MRRRRRRDGF YPVPDFQDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL NESMDHGGVG
     PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG GYGKVFQVRK VTGANTGKIF
     AMKVLKKAMI VRNAKDTAHT KAERNILEEV KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL
     FMQLEREGIF MEDTACFYLA EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC
     KESIHDGTVT HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK
     TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP FFRHINWEEL
     LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL SESANQVFLG FTYVAPSVLE
     SVKEKFSFEP KIRSPRXFFF FFNLQDPVKF SPGDFWGRGA SASTANPQTP VEYPMETSGV
     EQMDVTMSGE ASAPLPIRQP NSGPYKKQAF PMISKRPEHL RMNL
//
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