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Database: UniProt
Entry: A0A1Q3C5B9_CEPFO
LinkDB: A0A1Q3C5B9_CEPFO
Original site: A0A1Q3C5B9_CEPFO 
ID   A0A1Q3C5B9_CEPFO        Unreviewed;       495 AA.
AC   A0A1Q3C5B9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN   ORFNames=CFOL_v3_18926 {ECO:0000313|EMBL:GAV75447.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV75447.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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       As part of the SRP complex, associates with the SRP receptor (SR)
CC       component SRPRA to target secretory proteins to the endoplasmic
CC       reticulum membrane. Binds to the signal sequence of presecretory
CC       proteins when they emerge from the ribosomes. Displays basal GTPase
CC       activity, and stimulates reciprocal GTPase activation of the SR subunit
CC       SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with
CC       the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement
CC       of SR drive SRP-mediated cotranslational protein translocation into the
CC       ER (By similarity). Requires the presence of SRP9/SRP14 and/or SRP19 to
CC       stably interact with RNA. {ECO:0000256|ARBA:ARBA00034655}.
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       As part of the SRP complex, associates with the SRP receptor (SR)
CC       component SRPRA to target secretory proteins to the endoplasmic
CC       reticulum membrane. Binds to the signal sequence of presecretory
CC       proteins when they emerge from the ribosomes. Displays basal GTPase
CC       activity, and stimulates reciprocal GTPase activation of the SR subunit
CC       SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with
CC       the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement
CC       of SR drive SRP-mediated cotranslational protein translocation into the
CC       ER. Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact
CC       with RNA. {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   -!- SUBUNIT: Component of a signal recognition particle (SRP) complex that
CC       consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC       subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9.
CC       {ECO:0000256|ARBA:ARBA00034796, ECO:0000256|RuleBase:RU364034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240, ECO:0000256|RuleBase:RU364034}.
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}.
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:GAV75447.1}.
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DR   EMBL; BDDD01001367; GAV75447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3C5B9; -.
DR   STRING; 3775.A0A1Q3C5B9; -.
DR   InParanoid; A0A1Q3C5B9; -.
DR   OrthoDB; 1110531at2759; -.
DR   Proteomes; UP000187406; 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   ECO:0000256|RuleBase:RU364034};
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:UP000187406};
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   495 AA;  55014 MW;  C7D76B096371E251 CRC64;
     MVLGELGGSI SRAIQQMSNA TIIDEKVLNE CLNEITRALL QSDVQFKLVR DMQTNIKKIV
     NLDDLAAGHN KRKIIQQAIF NELCKMLDPG KPSFTLKKGK TSVVMFVGLQ GSGKTTTCTK
     YAYYHQKKGW KPALVCADTF RAGAFDQLKQ NATKAKIPFY GSYTESDPVK IAVEGVERFK
     KESCDLIIVD TSGRHKQEAA LFEEMRQVSE ATKPDLVIFV MDSSIGQAAF DQAQAFKQSV
     AVGAVIVTKM DGHAKGGGAL SAVAATKSPV IFIGTGEHMD EFEVFDVKPF VSRLLGMGDW
     SGFMDKIHEV VPMDQQPELL QKLSEGNFTL RIMYEQFQNI LKMGPIGQVF SMLPGFSAEL
     MPKGREKESQ AKIKRYMTMM DSMTDEELDS SNPKLMNESR MMRIARGSGR QLREVQDMLE
     EYKRLAKIWS KMKGLKIPKK GDMSALSRNM NAQHMSKVLP PQMLKQIGGM GGLQNLMKQM
     GSAKDMMGMF GGGDK
//
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