ID A0A346Y1N4_9ACTN Unreviewed; 1049 AA.
AC A0A346Y1N4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transcriptional activator of maltose regulon, MalT {ECO:0000313|EMBL:AXV08381.1};
GN ORFNames=DVS28_a3708 {ECO:0000313|EMBL:AXV08381.1};
OS Euzebya pacifica.
OC Bacteria; Actinomycetota; Nitriliruptoria; Euzebyales.
OX NCBI_TaxID=1608957 {ECO:0000313|EMBL:AXV08381.1, ECO:0000313|Proteomes:UP000264006};
RN [1] {ECO:0000313|EMBL:AXV08381.1, ECO:0000313|Proteomes:UP000264006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY32-46 {ECO:0000313|EMBL:AXV08381.1,
RC ECO:0000313|Proteomes:UP000264006};
RA Xu L., Wu Y.-H., Xu X.-W.;
RT "Complete genome sequence of Euzebya sp. DY32-46 isolated from seawater of
RT Pacific Ocean.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP031165; AXV08381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346Y1N4; -.
DR KEGG; euz:DVS28_a3708; -.
DR Proteomes; UP000264006; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13428; TPR_14; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF81901; HCP-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000264006};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..267
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 278..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..559
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1049 AA; 111409 MW; CE63937BA2E35D13 CRC64;
MKLAGFERLS EIGSGAFGTV YRAWQVDFQR EVAIKVLHDT RASEEDISRF ERERRVLGGL
SSHPHIVTVH AAGTTETGHR YIVMAFLDRG DWAGRIASTT RLDVPEVLDV GVKLCGALAT
AHDAGIVHRD IKPDNILLDE FAEPQLADFG IARTQQTRQL TVQGGLLGTV AYMAPEAFDG
AVTPSTDLWS LAATLHHALL GSPAYRRAEM IQTMYAILND ELPSLVEMGV PPVVEEAVAA
GLARSPSDRP ADAAAFGRLL QQAQATLGLS PTRLLQRGVQ PGPLPTAQAV GPSPPTRVAG
EATDGPPITS GPATVPVPGL ARLEEARVRW LTGDVPSAEQ LLAELAADDN GMVADRARVG
LAEIEAARGD VGAAIRHLRP LVSEHSPARE HAAITLSRLL AAMGDPDGAM TSLARASAWP
GEGRGDLLAE YADLLQRMGE EREARDLIGA AADLPDGQGQ GALLLGAALD LATGDLGRAE
AVSTRLEFEA KDAETAGLAL IVQGNCAERV DPDRAIACYR RVVDGDFPPE PVAIALLELQ
ALHRDLDDAE EATAMARRLV DGGHPVAGPL AGVLEAAELA GRGDLSAAEG WLRTAEDRGR
HPSNRPVLAY GRAALAAARD DRAGVEAALE PLFAAYATEH GAALQAVAAQ LLADAGDPVK
ARALLERALD RGGPEHRAER LLVLGLLTEA DGDHERADRL FRDALAVGHP TASRQAQVAL
GRRALISGDV DTAEAHLRRV IASGDWALAP EASVGLAEAM LMKGRWSRAR ALLETASEAR
SVHVSARAMA ILADELGHRG ERAPAEELLT RAAARAESDT DAFVLVMRIR AALHSLVGEH
DGARQAYLRA AERATLGDRE DLLLEAALTY VDEDDDVMAV TALGQLLESV DDPTVLDHAT
LFHAHARLRL GEQDARRTIR QVADGGGPAA VKALVGLAEL YEDEGRPEEA RHLYERWRDH
APADPEPLRR IAQVLLGAGR ASEAKDAAKT ALDIGGPEDM EPTLLVMGDV HRALGDHEAA
AACWRRVLKS ADPDLAEHAD ERLRSLGSG
//
