ID A0A1Q9NEL6_9ARCH Unreviewed; 432 AA.
AC A0A1Q9NEL6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Methyl-accepting chemotaxis protein McpC {ECO:0000313|EMBL:OLS20549.1};
GN Name=mcpC {ECO:0000313|EMBL:OLS20549.1};
GN ORFNames=HeimC3_40070 {ECO:0000313|EMBL:OLS20549.1};
OS Candidatus Heimdallarchaeota archaeon LC_3.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=1841598 {ECO:0000313|EMBL:OLS20549.1, ECO:0000313|Proteomes:UP000186063};
RN [1] {ECO:0000313|EMBL:OLS20549.1, ECO:0000313|Proteomes:UP000186063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC_3 {ECO:0000313|EMBL:OLS20549.1};
RX PubMed=28077874; DOI=10.1038/nature21031;
RA Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA Baker B.J., Spang A., Ettema T.J.G.;
RT "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL Nature 541:353-358(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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:OLS20549.1}.
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DR EMBL; MDVS01000093; OLS20549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9NEL6; -.
DR Proteomes; UP000186063; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 3.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029095; NarX-like_N.
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 Pfam; PF13675; PilJ; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..231
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 215..431
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 432 AA; 47412 MW; 96747B8CC09C04BA CRC64;
MGVMMLYSTN LSRSDAVVIN VAGRQRMLTQ KMIQKSLAIY FHTDFTLQSE TIAELNQARL
EFEKAHIGLR NGDSDLGIPG TDDNNVLKNW NAVDEYYSNN FKQLIINIEN SQGNVSETMI
SSVITEEEPL IERLQSMVLS FQQFAENKIA FADLLAIIFP FGIFAISIFA GFMLNYTISR
PLIRISDDSK AIADGDLTIL IDSNQQNRKD EIGVLSKNFG LMVINLKKAV TDIQKGSTTI
ATNSQEMASS AEEVNATSEE ISSITQQMSR GSQEQSVKSS ESTMLVEELQ KSFSEKIKNI
EELSGLIEDI TGKVNMLALN ASIEAARAGE YGRGFAVVAE NIRQLAEEGK KSVSKVNEIT
SDIQTYLQSS IKTIYGSIQE VASISEETAS GAEEATAATE EQTATMQEMS SSAQELANIA
SDLENAVKKF TI
//
