ID A0A0B3AME8_9ARCH Unreviewed; 448 AA. AC A0A0B3AME8; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 08-MAY-2019, entry version 19. 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}; RN [1] {ECO:0000313|EMBL:KHO49894.1} RP NUCLEOTIDE SEQUENCE. 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 RT from 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 CC signal sequence of the ribosome-nascent chain (RNC) as it emerges CC from the ribosomes. The SRP-RNC complex is then targeted to the CC cytoplasmic membrane where it interacts with the SRP receptor CC FtsY. {ECO:0000256|HAMAP-Rule:MF_00306, CC ECO:0000256|SAAS:SAAS00871663}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. Archaeal CC SRP consists of a 7S RNA molecule of 300 nucleotides and two CC protein subunits: SRP54 and SRP19. {ECO:0000256|HAMAP- CC 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 CC is responsible for interactions with the ribosome, the central G CC domain, which binds GTP, and the C-terminal M domain, which binds CC the RNA and the signal sequence of the RNC. {ECO:0000256|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 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|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00306}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 264 277 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 105 112 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 185 189 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT NP_BIND 243 246 GTP. {ECO:0000256|HAMAP-Rule:MF_00306}. FT COILED 311 331 {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 //