ID I1ZCS4_9ACAR Unreviewed; 444 AA.
AC I1ZCS4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
DE Flags: Fragment;
GN Name=Srp54k {ECO:0000313|EMBL:AFJ22055.1};
OS Aeroglyphus robustus (warty grain mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Glycyphagoidea; Aeroglyphidae;
OC Aeroglyphus.
OX NCBI_TaxID=474095 {ECO:0000313|EMBL:AFJ22055.1};
RN [1] {ECO:0000313|EMBL:AFJ22055.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23417682; DOI=10.1093/sysbio/syt008;
RA Klimov P.B., OConnor B.;
RT "Is permanent parasitism reversible?--critical evidence from early
RT evolution of house dust mites.";
RL Syst. Biol. 62:411-423(2013).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER).
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of SRP19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- DOMAIN: The NG domain, also named G domain, is a special guanosine
CC triphosphatase (GTPase) domain, which binds GTP and forms a guanosine
CC 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in
CC the SRP receptor subunit SRPRA. The two NG domains undergo cooperative
CC rearrangements upon their assembly, which culminate in the reciprocal
CC activation of the GTPase activity of one another. SRP receptor
CC compaction upon binding with cargo-loaded SRP and GTPase rearrangement
CC drive SRP-mediated cotranslational protein translocation into the ER.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|RuleBase:RU364034}.
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DR EMBL; JQ001004; AFJ22055.1; -; Genomic_DNA.
DR AlphaFoldDB; I1ZCS4; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:UniProtKB-UniRule.
DR CDD; cd17875; SRP54_G; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 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; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR NCBIfam; TIGR01425; SRP54_euk; 1.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU364034};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU364034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364034};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU364034};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU364034};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW ECO:0000256|RuleBase:RU364034}.
FT DOMAIN 242..255
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFJ22055.1"
FT NON_TER 444
FT /evidence="ECO:0000313|EMBL:AFJ22055.1"
SQ SEQUENCE 444 AA; 49188 MW; 3B9DFE778761E933 CRC64;
LDSLLKEICT ALIESDVNIM LVKKLRENVR SVIDFEEMAA GLNKRRMIMM AVFTELVKLL
DPGVKPWQPV KGKVNVIMFV GLQGIGKTTT CTKMAYYYMR KGWRCALVCA DTFRAGAFDQ
LKQNATKARI PFYGSYTESD PVVIASEGVE KFTNENFEIV IVDTSGRHKQ ESSLFEEMLA
ISAAIQPNLV VYVMDASIGQ ACEAQAKAFK SKVDVGAIII TKLDSHAKGG GALSAVAATK
SPIIFIGTGE HIDEFEQFKV KPFISKLLGM GDIEGLIDKV SELKLDDNEE LIEKLKHGEF
TIRDMYEQLT NIMKMGPFNQ ILNMIPGIGA ELSKCASEAE SMSRLKRMMT IMDSMSDSEL
DSREGAKLFS KQPTRIVRVS RGSGVTQREV QELLSQYTKF AAVVKKMGGI KGLFKSGDLT
KNVNPAQMAK LNQQMAKMID PRIL
//
