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Database: UniProt
Entry: L0I8B3_HALRX
LinkDB: L0I8B3_HALRX
Original site: L0I8B3_HALRX 
ID   L0I8B3_HALRX            Unreviewed;       798 AA.
AC   L0I8B3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGB15805.1};
GN   OrderedLocusNames=Halru_1189 {ECO:0000313|EMBL:AGB15805.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15805.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CP003050; AGB15805.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0I8B3; -.
DR   STRING; 797302.Halru_1189; -.
DR   KEGG; hru:Halru_1189; -.
DR   eggNOG; arCOG02320; Archaea.
DR   eggNOG; arCOG02362; Archaea.
DR   HOGENOM; CLU_000445_107_19_2; -.
DR   OrthoDB; 8523at2157; -.
DR   Proteomes; UP000010846; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.250.1910; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          322..374
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          395..448
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          467..703
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          513..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          362..400
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          545..579
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          608..642
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        727..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..777
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   798 AA;  87002 MW;  4958D7A0F7113197 CRC64;
     MSKRLSASPI RALRSSFLRK LSLLFLLVLL LVAAVGGAIY LQTESSLQDS TEQEMTQSTT
     LQANTISEWV DRTREKTQYL SASGQVAGGD SAEIADYLRS EQQDSSASIA GIHYYDTGEQ
     EVLTSTEASA DGVNYRDADI EWALEGLALE TPDQTRVTHP YLDPTTETNA VAFVSQVPEN
     PDRAIVVIVD LESQVQQLER PTATDESFTH IVDSRGTVVM SHHAMDINTQ NMGPENEYVA
     ESEAVKRGID GKSGYTEMEM AHGDHAEMAM GYAPIPGTDW VIMTHTPVDT AFALQDDITR
     SVLALVVLSM LSLGAVGVVI VRNTSRPITR LADRASELEA GNLEAELSSN RPDEIGQLYN
     AFDSMRASLR GQIQEAEEAR QEAEEERSRT DRINTHLEAK ADEYSSVMRA CGEGDLSRRM
     DPESQNDAMT EIALEFNQML SNLEETVERV SQFADEVAAA SEEVTASTEE VHTASTQVTE
     SVQEISDGAE RQNESLQAVN GEMNELSTTT EEIASSSHTV ADLAERTAKT GNEGRDVARS
     AIDGMNEIET ESEGAVDAIE SLEEEVAQID ELVEFITEVA EQTNMLALNA NIEASRATQS
     NDGFSAVADQ VKELSEDTQK AARDIEERIE EIEEETNYAA GEVRQTSERI ARHRQAVEDT
     VDALEEIAEY ASETSDGIQE ISAATEQQAA TTQEVVSMVD QAATISEETT TEAETVAAAA
     EEQTTAITEV SRSASDLSQQ AAELSSKLDE FETGHHADQG SKSDDADEFS FAEHGETSSE
     SDDEDEEPRT ADVNDRER
//
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