ID A0A367AUU5_9ACTN Unreviewed; 688 AA.
AC A0A367AUU5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:RBY91943.1};
GN ORFNames=DQ237_19220 {ECO:0000313|EMBL:RBY91943.1};
OS Blastococcus sp. TF02-8.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY91943.1, ECO:0000313|Proteomes:UP000252403};
RN [1] {ECO:0000313|EMBL:RBY91943.1, ECO:0000313|Proteomes:UP000252403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-8 {ECO:0000313|EMBL:RBY91943.1,
RC ECO:0000313|Proteomes:UP000252403};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-8.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RBY91943.1}.
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DR EMBL; QOHK01000016; RBY91943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367AUU5; -.
DR OrthoDB; 118142at2; -.
DR Proteomes; UP000252403; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RBY91943.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252403};
KW Transferase {ECO:0000313|EMBL:RBY91943.1}.
FT DOMAIN 75..127
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 121..165
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 664..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 75699 MW; AB48E49534345D81 CRC64;
MELLDLARAA AGIGTFDWDL ITGRLSWDDR LLELFDLTPA TFDQTIEGFN ARVHPDDLGR
VSELLDRAIT TCGDYEAEYR VLCTDGSLRW IAARGRALCD EAGDAVRLLG AAWDVTDRRK
TQDRIARALE GMAVGYLVMD ADWRIGYVNA RAEKALGLPR AELVGGIIWE RFPGTVGTDF
EAGYRRAKDT GQPVTFDAYY PEPLNAWYEV RATPEGDGVA LYFLDITERY RTYQRNELLG
QTTHQLTGTL NAEEAVARLA QLVVPTLADW CLVSLVSDEQ HTNIRRALRD VGHWHTDPDE
RALVEAYARV RLAAATDEPF LARALSSGEP VVIERDASER IRAVLTAGEA TELLEQLAPE
SAAVLPLRGR GRTVGLLTLF NGPARGPIPP NDLSTATDIA GRAGMALDNA RLYREQRSLA
EGLQRSLLTA PPQPDHGQIV VRYVPASQAA QVGGDWYDAF LQPGGATVLA IGDVIGHDTQ
AAAAMGQIRT IVRSIGALDD QSPATILRRA DEVMERLMVR TAATIALARL EQTPDDLQRG
ITRLRWSNAG HPPPFVINPD GTVLPLTRVR ADLLLGVRPD SARHEAEVVL DHDAVVLLYT
DGLVERRDED LDQGTQRLQD TLEELAGRDL DELCDELLAR MLPHEPDDDV ALIAIRLFRR
DRPRPAQAGP NVVPPDVPPH RDVASHPD
//