GenomeNet

Database: UniProt
Entry: I4F1S2_9ACTN
LinkDB: I4F1S2_9ACTN
Original site: I4F1S2_9ACTN 
ID   I4F1S2_9ACTN            Unreviewed;       522 AA.
AC   I4F1S2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=MODMU_4188 {ECO:0000313|EMBL:CCH89585.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH89585.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH89585.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH89585.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO203431; CCH89585.1; -; Genomic_DNA.
DR   RefSeq; WP_014742154.1; NC_017955.1.
DR   AlphaFoldDB; I4F1S2; -.
DR   STRING; 477641.MODMU_4188; -.
DR   KEGG; mmar:MODMU_4188; -.
DR   PATRIC; fig|477641.3.peg.3910; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OMA; DISWPAY; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   CDD; cd06577; PASTA_pknB; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF03793; PASTA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CCH89585.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CCH89585.1};
KW   Transferase {ECO:0000313|EMBL:CCH89585.1}.
FT   DOMAIN          12..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          307..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..474
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..496
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  54153 MW;  CE7B06D0D88523A0 CRC64;
     MEPNGRLLGG RYELTALIAT GGMGQVWQGR DTVLNRDVAV KVLRDEYTGD PTFLARFRAE
     AQLAAGLVHP NIATLFDYGE VAPADPRGEH LAYLVMELVR GESLSALLRR QRRLPPERTL
     AILRQSAAGL AAAHAAGVVH RDVKPGNVLL GNDGSVKITD FGVAVSAASV PLTRTGQVIG
     TAHYLSPEQA QGHRASAASD VYALGVVGYE CLSGHRAFDA ESSVQVALMH IRDNPEPLPD
     DVPAPVRALV EAAMVKDPAD RFPDGAAFRD AIDQVMAGRG FSGPVAAAGP AATTVMPVVA
     APTAEFPATQ PRGAWSSEAA QDWSPEPAEE DREDSRRRRL LVPLLALLVV AAVALGGWQM
     LTSGGDDDRT ATAPTTSATS SAPTSSAPAQ PTVQLVDLTS TDYVGRPVGD VQAELTGRGL
     VVTLAAQETS DVADGLVTGV TPDGPLTPNS PVTVSYAVAP PPPPPTPTPT PTPTVEDPGA
     DESEPAETEP EETEPEQQLP GDGNGDGNGW GNGRGNGRGG NG
//
DBGET integrated database retrieval system