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Database: UniProt
Entry: A0A2I3MGE5_PAPAN
LinkDB: A0A2I3MGE5_PAPAN
Original site: A0A2I3MGE5_PAPAN 
ID   A0A2I3MGE5_PAPAN        Unreviewed;      1054 AA.
AC   A0A2I3MGE5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=RPS6KC1 {ECO:0000313|Ensembl:ENSPANP00000034655.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000034655.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000034655.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000034655.2}
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   -!- 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   AlphaFoldDB; A0A2I3MGE5; -.
DR   Ensembl; ENSPANT00000031479.2; ENSPANP00000034655.2; ENSPANG00000017815.3.
DR   GeneTree; ENSGT00940000155656; -.
DR   OrthoDB; 5308056at2759; -.
DR   Proteomes; UP000028761; Chromosome 1.
DR   Bgee; ENSPANG00000017815; Expressed in postnatal subventricular zone and 67 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd02677; MIT_SNX15; 1.
DR   CDD; cd05576; STKc_RPK118_like; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR035053; STK_RPK118-like.
DR   PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00745; MIT; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50195; PX; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..120
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          782..1044
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          192..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  117498 MW;  162A40246130E842 CRC64;
     MTSYRERSAD LARFYTVTEP QRHPRGYTVY KVTARIIVWK RYSDFKKLHK ELWQIHKNLF
     RHSELFPPFA KGIVFGRFDE TVIEERRQCA EDLLQFSANI PALYNSKQLE DFFKGGIIND
     SSELIGPAEA HSDSLIDTFP ECSTEGFSSD SDLISLTVDV DSLAELDDGM ASNQNSPIRT
     FGLNLSSDSS ALGAVASDSE QSKTEEERES RSLFPGSLKP RLGKRDYLEK AGELIKLALK
     KEEEDDYEAA SDFYRKGVDL LLEGVQGESS PTRREAVKRR TAEYLMRAES ISGLYGKFQL
     DDVSQPPGSL SSRPPWNLRS PAEELKAFRV LGVIDKVLLV MDTRTEQTFI LKGLRKSSEY
     SRNRKTIIPR CVPNMVCLHK YIISEESVFL VLQHAEGGKL WSYISKFLNR SPEESFDIKE
     VKKSTLAKVH LQQPTSSPQD SSSFESRGSD GGSVLRALPL KSSLTPSSQD DSNQEDDGQD
     SSPKWPDSGS SSEEECTTSY LTLCNEYGQE KIEPGSLNEE PFMKTEGNGV DTKAIQSFPT
     HLADDSDSPS TQLRAHELKF FPNDDPEAVS SPRTSDSLSR SKNSPMEFFR IDSKDSASEL
     LGLDFGEKLY SLKSEPLKPF FTLPDGDSAS RSFNTSESKI EFKAQDTISR GSDDSVPVIS
     FKDAAFDDVS GTDEGRPDLL VNLPGELEPT REAAAMGPTK FTQTNIGIIE NKLLEAPDVL
     CLRLSTEQCQ AHEEKGMEEL SDPSGPKSRR MTEKHYAQDD PRMLFVAAVD HSSSGDMSLL
     PSSDPRFQGL GVVESAVTAN NTEESLFHIC SPLSGANEYI ASTDTLKTEE VLLFTDQTDD
     LAKEEPTSLF QRDSETKGES GLALEGDKEI HQIFEDLDKK LALTSRFYIP EGCIQRWAAE
     MVVALDALHR EGIVCRDLNP NNILLNDRGH IQLTYFSRWS EVEDSCDSDA IERMYCAPEV
     GAITEETEAC DWWSLGAVLF ELLTGKTLVE CHPAGINTHT TLNMPECVSE EARSLIQQLL
     QFNPLERLGA GVAGVEDIKS HPFFTPVDWA ELMR
//
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