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Database: UniProt
Entry: T1KQ73_TETUR
LinkDB: T1KQ73_TETUR
Original site: T1KQ73_TETUR 
ID   T1KQ73_TETUR            Unreviewed;       497 AA.
AC   T1KQ73;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN   Name=107366200 {ECO:0000313|EnsemblMetazoa:tetur17g03110.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur17g03110.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur17g03110.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; CAEY01000348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015789268.1; XM_015933782.1.
DR   AlphaFoldDB; T1KQ73; -.
DR   STRING; 32264.T1KQ73; -.
DR   EnsemblMetazoa; tetur17g03110.1; tetur17g03110.1; tetur17g03110.
DR   GeneID; 107366200; -.
DR   KEGG; tut:107366200; -.
DR   eggNOG; KOG0780; Eukaryota.
DR   HOGENOM; CLU_009301_6_1_1; -.
DR   OMA; PIKFAGV; -.
DR   OrthoDB; 1110531at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
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; IPR036225; SRP/SRP_N.
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; SSF47364; Domain of the SRP/SRP receptor G-proteins; 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|ARBA:ARBA00022490, 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   Reference proteome {ECO:0000313|Proteomes:UP000015104};
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          269..282
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
SQ   SEQUENCE   497 AA;  54763 MW;  FDBC9FFE2CA3EF90 CRC64;
     MVLADLGRKI TNALRSLGNA TIIDQEVLEG LLKEVCKALL ESDVNIRLVK ELRENVRKVI
     DFDEMAAGLN KRRMIQMAVF KELVKLVDPG VKAWQPTKGK PNVIMFVGLQ GAGKTTTCTK
     MAYYYQRKGW KCCLVCADTF RAGAFDQLKQ NATKARIPFY GSYTEADPVV VAAEGVDKFI
     KEGFEIIIVD TSGRHKQESA LFEEMLSISN AVQPNLVIFV MDASIGHACE AQARAFKSKV
     DVGAVIVTKL DGHAKGGGAL SAVAVTNSPI IFIGTGEHMD DFEPFKVKPF VSKLLGMGDI
     EGLIDKVNEL KLDDNEELIE KLKHGEFTLR DMYEQFTNIM KMGPFNQILQ MIPGFGQELA
     RGASEADSMA RLKRLMTIMD SMSDGELDHR DGAKLFSKQP TRTTRVARGA GVTTREVQEL
     LTQFTKFAAV VKKMGGIKGF FRGGDMSKNV NAMQMAKLNQ QVAKMMDPRI LQQMGGISGL
     QTMMRQLQGA ASAAQHK
//
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