ID A0A0M1J5U5_9GAMM Unreviewed; 446 AA.
AC A0A0M1J5U5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE Flags: Fragment;
GN ORFNames=TI05_16475 {ECO:0000313|EMBL:KOR28678.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR28678.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR28678.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR28678.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOR28678.1}.
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DR EMBL; JXSO01000652; KOR28678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1J5U5; -.
DR Proteomes; UP000036918; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR045269; Atg1-like.
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 PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000036918}.
FT DOMAIN 134..388
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 412..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 446
FT /evidence="ECO:0000313|EMBL:KOR28678.1"
SQ SEQUENCE 446 AA; 49666 MW; 77CC108E46C7145A CRC64;
MGRECWQALK NFQEEAAQEE RIMQLEQAAA LTPTEARDIA QAVIAELRRN GQQIASDQAE
AVQDIISVMP DQIRERTRAT LDHAQRLGTQ AIAALPVTDR FAIDEREAFY SGLYPRRRPQ
FRVGEPIPHY GFEWRLERLL GTGGFGEVWL AKHRRLRSKP MMAVKFCQDE TSSKLLKKEE
AILDKLIEQL PETMPNIVSL LELNLTEMPY WLAFEYIEGG TLESRIRLGA MDWPTAWSLF
EPILQGMAAV HDLGIVHRDL KPANILLDIE QQPAIADFGI GKLLATKTAA TQRSQRSQSL
TTRGYGSVGY MSPEQKAAID AHATDDVYAL GIILWQMLMG TCLQSPEYPD DIADLVVPDP
VKLVLSKCRF SRREKRPQNA GAMLQQLGGI QAQAAVKPDA ASSTVTSRIQ RILPGNATAN
SQSQSQSQGQ SSQSQNQSQN QSQGQS
//
