ID A0A1Q7I6D4_9CHLR Unreviewed; 417 AA.
AC A0A1Q7I6D4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE Flags: Fragment;
GN ORFNames=AUH89_06395 {ECO:0000313|EMBL:OLC59255.1};
OS Ktedonobacter sp. 13_1_40CM_4_52_4.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805230 {ECO:0000313|EMBL:OLC59255.1, ECO:0000313|Proteomes:UP000186693};
RN [1] {ECO:0000313|EMBL:OLC59255.1, ECO:0000313|Proteomes:UP000186693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:OLC59255.1}.
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DR EMBL; MNFP01000121; OLC59255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7I6D4; -.
DR Proteomes; UP000186693; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR026870; Zinc_ribbon_dom.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13240; zinc_ribbon_2; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}.
FT DOMAIN 15..321
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 417
FT /evidence="ECO:0000313|EMBL:OLC59255.1"
SQ SEQUENCE 417 AA; 45725 MW; C858193D33109862 CRC64;
MMETVPSGTI LHGRYRIERV LGSGGFGHVY LAIDLITNQQ YAIKEYFVTG ASGQAQLQHE
ARVLSQLHHP NLPAFQEAFD QRGHYFVVLS YIEGSDLTDR IRIARQRNEI IPLPQIMGWI
LSICDAVQFL HSQQPVVIHR DIKPDNIRIM LDGTAILVDL GNAKATADGA RTLFFIRHQG
TPGYAPQEQY PGGTGTDVRS DIYALGATLY FALTSHEPPS VSLRNQSIQQ GLPDLPSLQE
ILAKNPPENN AEANAGRQFR LGVTKPTKPV PRHLRHLAQL GSLPPPLLDQ LNAIIKRAMA
MKQKDRYPTV AEFSNDLNRV MAALPAPPSA PTQRPVDPNS TQPDLPLLYE TIQRAKENAD
KASPGEANNP PAQPANRPAP TPVCPRCGES LLQQSSFCPR CGSSLNNVFK ASASTTV
//
