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Database: UniProt
Entry: A0A1Q7USA1_9CHLR
LinkDB: A0A1Q7USA1_9CHLR
Original site: A0A1Q7USA1_9CHLR 
ID   A0A1Q7USA1_9CHLR        Unreviewed;      1057 AA.
AC   A0A1Q7USA1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OLE07132.1};
DE   Flags: Fragment;
GN   ORFNames=AUG82_02720 {ECO:0000313|EMBL:OLE07132.1};
OS   Ktedonobacter sp. 13_1_20CM_4_53_11.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE07132.1, ECO:0000313|Proteomes:UP000186213};
RN   [1] {ECO:0000313|EMBL:OLE07132.1, ECO:0000313|Proteomes:UP000186213}
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   -!- 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:OLE07132.1}.
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DR   EMBL; MNIY01000057; OLE07132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7USA1; -.
DR   STRING; 1805225.AUG82_02720; -.
DR   Proteomes; UP000186213; Unassembled WGS sequence.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47691:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR RV0890C-RELATED; 1.
DR   PANTHER; PTHR47691; REGULATOR-RELATED; 1.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF46894; C-terminal effector domain of the bipartite response regulators; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT   DOMAIN          1..163
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          990..1055
FT                   /note="HTH luxR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50043"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OLE07132.1"
SQ   SEQUENCE   1057 AA;  115200 MW;  92F0E7D175A7B8BD CRC64;
     SQLPLDTVVS YVTQIAEALQ YAHDQKVIHR DIKPENILLG RNNEVLLSDF GIAIMTQSSA
     SQHPQDAAGS IAYMAPEQIQ AHPGPASDQY ALGIVIYEWL SGDRPFHGSF TEIAIKHALT
     PPPSLREKVS TIPPAVEQVV LKALAKNPKQ RFERVQAFAE ALEEASKEEA SGRTLFVSGS
     DIPGQHPAES EPTAGQWKAR PHNLPAQLTS LIGREEEIQV LCTLLQRPEI RLVTLTGTGG
     VGKTRLALQV ATDLLDDFAG DICFVPLAPV SDPNLVVPTI VQALGLEVSG DQPLLDLLKV
     SLRDKRLLLL LDNFEQVLGA APGLSELLSV CPHLKILVTS RAVLHIRGEH EFLVPPLRLP
     DLTHLPESEV LSQYAAVALF LQCAKAAKPD FQMTPANIRA VAEICVSLDG LPLAIELAGA
     RAKVLPPQAL LTRLRHRLQV LTIGARDVPA RQQTLRNTLA WSYDLLGVKE QLLFRRLSVF
     VGGCTLGAVE AMYSTLSDRP AYVLDGIASL IDKSLLRQTE QEGEEPRLLM LETIREYGLE
     VLTTSGEMQN ARRAHALYYL SLAEDAETEV GGPQQAVWLD RLEREHDNLR AALQWSLGQT
     GDDESVEKEQ DLEIALRLGG ALRSFWRVHG HITEGRSFLE RALAASKGAA AFVRAKALIA
     AANLAFIQSD YDSMEILCKE SLALYQELED LPGIAHSVYL LANVAWTRGD TATARSLLTE
     AQSLARAIDD EEYVAWSLFV QGLLESSQGN YPRARTLFEE SLKIHRQLQN KRGIAHSLSQ
     LAQVLFVSQS DQERVPSLLE ECLALSEEIG FKEGVAASSW LSGQVALRQG DLVKARSLAE
     KGVALYREMG HRHGMAESLP ALGKVLAAQG DYPTARTLYE EGLAISGELG EKWVVAQCLV
     GLGEVVAAQR QLAWAAQLWG VAEALRDAID VPLPPVERTS YDRSVAATRA HLGEGAFATA
     WAQGRSMTPE QVLVAQGRKP GPPPKTIIPP PTYPDGLSAR EVEVLCLVAA GLTDVQIAEK
     LILSPRTVHA HTSSIYSKLD ITSRSAATRY AIEHHLA
//
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