ID A9V5U3_MONBE Unreviewed; 853 AA.
AC A9V5U3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN ORFNames=MONBRDRAFT_27624 {ECO:0000313|EMBL:EDQ87175.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ87175.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ87175.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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|PIRNR:PIRNR000606};
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|PIRNR:PIRNR000606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000606};
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:PIRNR000606}.
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DR EMBL; CH991561; EDQ87175.1; -; Genomic_DNA.
DR RefSeq; XP_001748118.1; XM_001748066.1.
DR AlphaFoldDB; A9V5U3; -.
DR STRING; 81824.A9V5U3; -.
DR EnsemblProtists; EDQ87175; EDQ87175; MONBRDRAFT_27624.
DR GeneID; 5893310; -.
DR KEGG; mbr:MONBRDRAFT_27624; -.
DR eggNOG; KOG0603; Eukaryota.
DR InParanoid; A9V5U3; -.
DR OMA; ILEHSWV; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; IPR016239; Ribosomal_S6_kinase_II.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF175; CHROMOSOMAL SERINE_THREONINE-PROTEIN KINASE JIL-1; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000606; Ribsml_S6_kin_2; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000606};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000606};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000606};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000606}.
FT DOMAIN 49..319
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 320..389
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 527..785
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 831..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT ACT_SITE 642
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 533..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 853 AA; 94162 MW; 993A702DAEF62C97 CRC64;
MALPADFCLP GEGSSDFDFS NFGEDSEIFP ITEASMHPSD GERVGPADFE LLRVLGSGAY
GKVMLTRKVT GNDTGTLYAM KVLKKAAIVR QAKMTEHTRA ERNILESIRH VPFVVQLHYA
FQDESKLHLV LDYVNGGELF THLRRRVMFL EREARFYVAE ILVALDALHR LGVIYRDLKL
ENILLDKEGH VRLTDFGLSK EHIQSPAART YSYAGTTEYL APEIAGEHPE GHGLSVDWWS
LGCLLYELVQ GHTPFVNYPG DTDNSNSAIA RRILTKPAVL HKSMSKPLRG LLTGLLEKRA
EKRLGAHRDA AELMEHAFFK PLKWEDLRDK KVPPPIVPVI ANELDTQNFD SEFTDQDPVL
TPAPPTSPTA RMLFRGFSFV GPNVLFNSGL FDPEASQNAT ALQSSLQNVV SVQQVVPQAN
HNSLPQFSAE IPASAPFVPP MDASGNNTQQ STASLQTQAT MPEDMPQDES ANMGFVDVGM
ARAEPRQPLK TALGAIPPSA LTSQGATASS SPIIDSERTF HMEYTIPAGE RELGLGSFST
CRKCIRKSDN AAFAVKIVSN RGQTQEAEML RRVQGHPNII QLIDVFQDPV HTYIVMELCT
GGELFYRIAQ HGNLSEREAR NIFKQLVSAV QYSHNNNVVH RDLKPENIVF QEASVDSPVK
IIDWGFAKLT DTQQTLQTPL FTFKFGAPEV TARLKSSAPA YTSACDMWSL GVILYTMLTG
ATPFEVPANF QDADAWDKVL RKELQFTQPI WQHISAEAKQ LLQRLLSHNA HLRPTATLAA
RDPWLTEAAL SNQPLPSPAI LAKEETAGRG KRGILAANVA ALSDASRLAP VEDAKLAKRR
KQRDKSTSSV SSA
//
