ID A0A0F0HU21_9PSEU Unreviewed; 652 AA.
AC A0A0F0HU21;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:KJK59009.1};
GN ORFNames=UK12_07050 {ECO:0000313|EMBL:KJK59009.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK59009.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK59009.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK59009.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK59009.1}.
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DR EMBL; JYJF01000011; KJK59009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HU21; -.
DR PATRIC; fig|1427391.3.peg.578; -.
DR Proteomes; UP000033409; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KJK59009.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033409};
KW Transferase {ECO:0000313|EMBL:KJK59009.1}.
FT DOMAIN 8..63
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 80..132
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 238..373
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 382..650
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT REGION 158..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 70405 MW; D0DE0673EBD3E332 CRC64;
MLAALRASES RFRAAFADAG IGMALIDSDD RIIEANPAFA AMIGHDLADL VRTHIHDIIE
PEENHRQHYL ELVRGERDRL RVEKRLKHRD GRAVWSNVTI SLIRDGSGYP LYTMAMVEDV
TEQRLLGDRL AYQALHDPLT RLPNRTLFFE RLNAAFMPGN GDAPPNPQGA AAAKPGSEEP
AEPASAIGAT PSAPEASVPG DSRTGLLGTA ATTVPATMAT AAPGPGPTAG PGSSRPTRRV
GLCYVDLDGF AAINETLGHH VGDQLLVAVA ARLERGFSRD QESLVARLGG DEFAVLVADS
ASSEQLTRLA SDLIAALEQP FDIAGQQLVV TASVGVVERP VQETTPTDLL KDADATLYWS
KADGRARWTL YDPDRGAHQL TRQRLATALR PALERGEFTV EYQPLVGLAD GAVHGAEALV
RWCHPRYGTL SPDRFIPLAE ESGAIVPLGK WVLEESCRQA RQWLTEFPDT ETFVSVNLAA
RQIWDSDVVA DVAQVLERTG LPPRLLQLEI TESAVLGPGG RPVQALQALA DMGVRIAIDD
FGTGYSNLAY LSRLPVHVLK LDGSFIEGFR DPAPGGRPDN RFRRADADEQ IVGAMVQLAH
ALGLTVTAEG IENASQAERL RLTGCDTAQG WYFAKPGEAE RVAAMLRARQ AR
//
