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Database: UniProt
Entry: R4VUF6_9EURY
LinkDB: R4VUF6_9EURY
Original site: R4VUF6_9EURY 
ID   R4VUF6_9EURY            Unreviewed;       514 AA.
AC   R4VUF6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=L593_04445 {ECO:0000313|EMBL:AGN00840.1};
OS   Salinarchaeum sp. Harcht-Bsk1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Natronoarchaeaceae; Salinarchaeum.
OX   NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00840.1, ECO:0000313|Proteomes:UP000014072};
RN   [1] {ECO:0000313|EMBL:AGN00840.1, ECO:0000313|Proteomes:UP000014072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00840.1};
RX   PubMed=23868130;
RA   Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA   Toshchakov S.V.;
RT   "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT   Isolated from Hypersaline Lake Baskunchak, Russia.";
RL   Genome Announc. 1:E00505-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP005962; AGN00840.1; -; Genomic_DNA.
DR   RefSeq; WP_020445734.1; NC_021313.1.
DR   AlphaFoldDB; R4VUF6; -.
DR   STRING; 1333523.L593_04445; -.
DR   GeneID; 16180941; -.
DR   KEGG; sali:L593_04445; -.
DR   PATRIC; fig|1333523.5.peg.906; -.
DR   eggNOG; arCOG02333; Archaea.
DR   eggNOG; arCOG02359; Archaea.
DR   HOGENOM; CLU_000445_114_58_2; -.
DR   OrthoDB; 8127at2157; -.
DR   Proteomes; UP000014072; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AGN00840.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014072};
KW   Transferase {ECO:0000313|EMBL:AGN00840.1}.
FT   DOMAIN          5..77
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          287..506
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          393..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  56370 MW;  D081D65D16E3B086 CRC64;
     MVVETAATFE ALVDVYAGAV FVVDREGRYR EVIEGSEGSD VLYDLPESLT GQEFRDVLPP
     ETAERFHRVV REAIDSGTPS IVEYELEVQA GHRWFEATVS PIEDEELVVW AARDVTERKQ
     YERALAALHE AGPRLTASDS VADVCEEAIY AAETILDFDQ SMIALERDGV LQAEATSEQL
     PADATTTVPI DDGIAGRTYR TGESYLTPDL AETDAALDHV EFRAGLSVPI GDHGVFQAVA
     ERPDAFDETD LELAELFVGQ VDATITRLEH ERALERQNER LDEFASIVSH DLRNPLTVAN
     GRLELAAEEC DSEHLEHVAD AHDRMQGLID DLLTLAQSGE DVAVEPVDLA HLVRECWQLI
     ETEDATLDVA VERPIEANRT QLRQLLENLL GNAVEHGSTG PGSQARQDAV EHGSTSPRSQ
     AHEDAVEHGD DGVTITVGDL EDGFYVEDDG PGIDDVDRDR LFEAGYSSAD GGTGIGLHIV
     GSVAERHGWT VELDEEYEDG ARFEITGVER PDEY
//
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