ID A0A0B3AME8_9ARCH Unreviewed; 448 AA. AC A0A0B3AME8; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 29-SEP-2021, entry version 23. DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|HAMAP-Rule:MF_00306}; DE Short=SRP54 {ECO:0000256|HAMAP-Rule:MF_00306}; GN Name=srp54 {ECO:0000256|HAMAP-Rule:MF_00306}; GN ORFNames=QT01_C0001G0008 {ECO:0000313|EMBL:KHO49894.1}; OS archaeon GW2011_AR6. OC Archaea. OX NCBI_TaxID=1579368 {ECO:0000313|EMBL:KHO49894.1, ECO:0000313|Proteomes:UP000030994}; RN [1] {ECO:0000313|EMBL:KHO49894.1, ECO:0000313|Proteomes:UP000030994} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T., RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M., RA Taylor R.C., Williams K.H., Banfield J.F.; RT "Genomic expansion of domain Archaea highlights roles for organisms from RT new phyla in anaerobic carbon cycling."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic signal CC sequence of the ribosome-nascent chain (RNC) as it emerges from the CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic CC membrane where it interacts with the SRP receptor FtsY. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein translocation CC system, which is composed of SRP and FtsY. Archaeal SRP consists of a CC 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and CC SRP19. {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is CC responsible for interactions with the ribosome, the central G domain, CC which binds GTP, and the C-terminal M domain, which binds the RNA and CC the signal sequence of the RNC. {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily. CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|HAMAP-Rule:MF_00306}. 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:KHO49894.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JWKR01000001; KHO49894.1; -; Genomic_DNA. DR PATRIC; fig|1579368.3.peg.8; -. DR Proteomes; UP000030994; Unassembled WGS sequence. DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule. DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.10.260.30; -; 1. DR Gene3D; 1.20.120.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR036225; SRP/SRP_N. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR042101; SRP54_N_sf. DR PANTHER; PTHR11564; PTHR11564; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF47446; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135, KW ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 264..277 FT /note="SRP54" FT /evidence="ECO:0000259|PROSITE:PS00300" FT NP_BIND 105..112 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT NP_BIND 185..189 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT NP_BIND 243..246 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT COILED 311..331 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 448 AA; 50234 MW; BB5A4DF111FD570A CRC64; MILESLGDKL KAALKKVASA VFIDTRVIDD LVKELQRALL EADVDVELVF EISERIKEKA KEEPRPGISK KEQLIKIVHD ELISLLGKGR EIQVKDKPLK IMFVGLYGVG KTTSISKVAL YYSKRGYKVC MLGLDTHRPA ARDQLEQLGE KVKVPVFVDK QEKDPRKIWQ KFEQEAKRFD VILIDTAGRH SLDAELEKEI RELKEKIRPQ EVILTLSSDI GQAARKVVEG FHKACGTTGI FLTKMDGTAK AGGALAAASI TKAPVLFIGT GEKPQDIETF DTTSFISRLL GMGDLQALLE KAKISIDEKD AKKLEQRLEE GKFTLDDLYE QLKAMRKMGP LSKITEMIPG FSNMKLPSDM MQVQESKLKR WGHAMESMTK KEKENPDTIT GERIARISKG SAVPTSEIRE MLKQYKMVKG FFGMSKGKTM SQKDLQKIAR KMGARGGF //