ID A0A1G7NHQ2_9EURY Unreviewed; 586 AA.
AC A0A1G7NHQ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SDF73563.1};
GN ORFNames=SAMN05216218_1099 {ECO:0000313|EMBL:SDF73563.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF73563.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDF73563.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF73563.1,
RC ECO:0000313|Proteomes:UP000199076};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNBK01000009; SDF73563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7NHQ2; -.
DR STRING; 660518.SAMN05216218_1099; -.
DR OrthoDB; 8523at2157; -.
DR Proteomes; UP000199076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd01068; globin_sensor; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR044398; Globin-sensor_dom.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR039379; Protoglobin_sensor_dom.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF11563; Protoglobin; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}.
FT DOMAIN 257..493
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 168..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 229..256
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 419..464
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 257..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 63849 MW; C9D9CF778D7F70A8 CRC64;
MSDSPQYGRD DFGRGGLNDQ LDADSLVGEI GLDRSEIRWR KDFVGFTDDD VRRLRTYRDD
FADNADQVAE DFYDNLTDHE ETVEVIGRSP KTVEQLKRTQ SAYLVTLADG EYGTDYFRDR
ARIGKLHDIL DMPMKHYLGQ YGVYYDLILP LVGDRLVESL TERLTDAVTD GGTEPASGGG
EDALNPGPDL SRRAIETAVE EEVDDAVQDI LAILRVINLD MQVVTDTYIH SYSQQLEEEI
ERNERLMADV EEDVKQPVSD LQTSAEDVAE SATAISDAAT QQSERVDEIS SEVANLSATI
EEVASTADQV ESASDRSETL AEEGKESADT AAEVMDDIGD AINDVADDVT SLQNRVQQID
EFVDAIDGIA EQTNILALNA SIEAARAGKA GEGFAVVADE IKSLAKESQT HASDIETMVD
EIQTDAEDTA ANLADTTEQV DRGIEQVQDA MDSLTEIVEA VTETANGISE VADATDDQAA
AAEEIASMVD EVVDRTDRVA EEIESLAAAN EEQAAMVSEV EESVTRLSGE RSATDGGRDT
VTTTDSEQVS IPQDLPDDMP DFVIETLSEE QLREVAIGNR DPTDLL
//