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Database: UniProt
Entry: I1ZD32_9ACAR
LinkDB: I1ZD32_9ACAR
Original site: I1ZD32_9ACAR 
ID   I1ZD32_9ACAR            Unreviewed;       460 AA.
AC   I1ZD32;
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:AFJ22163.1};
OS   Rallicoptes aff. gallinulae AD992.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Laminosioptidae; Rallicoptes.
OX   NCBI_TaxID=1111363 {ECO:0000313|EMBL:AFJ22163.1};
RN   [1] {ECO:0000313|EMBL:AFJ22163.1}
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; JQ001112; AFJ22163.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1ZD32; -.
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   SMART; SM00963; SRP54_N; 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          258..271
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFJ22163.1"
FT   NON_TER         460
FT                   /evidence="ECO:0000313|EMBL:AFJ22163.1"
SQ   SEQUENCE   460 AA;  50987 MW;  58A780B5B3DFBCD3 CRC64;
     TALRSLGNAT IINQEVLDSL LKEICTALIE SDVNIMLVKQ LRENVRSVID FDEMAAGLNK
     RRMIMMAVFK ELVKLLDPGV KSWQPIKGKT NVIMFVGLQG IGKTTTCTKM AYYYMKKGWK
     CALVCADTFR AGAFDQLKQN ATKARIPFYG SYTESDPVVI ASEGVEKFKK ENFEIVIVDT
     SGRHKQETSL FEEMMAIQSA IQPNLVIYVM DASIGQACEA QARAFKNKVD VGAIIVTKLD
     GHAKGGGALS AVAATKSPII FIGTGEHIDE FEQFKVKPFI SKLLGMGDIE GLIDKVNELK
     LDDNEELIEK LKHGEFTIRD MYEQLTNIMK MGPFNQILNM IPGFGAELAK CASEAESMSR
     LKRMMTIMDS MSDSELDSRE GAKLFSKQPT RIIRVSRGAG VTQREVQELL SQYTKFAAVV
     KKMGGIKGLF KSGDLAKNVN PAQMAKLNQQ MAKMIDPRVL
//
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