ID A0A1S3U5N2_VIGRR Unreviewed; 500 AA.
AC A0A1S3U5N2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN Name=LOC106762119 {ECO:0000313|RefSeq:XP_014501327.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014501327.1};
RN [1] {ECO:0000313|RefSeq:XP_014501327.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014501327.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 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}.
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DR RefSeq; XP_014501327.1; XM_014645841.2.
DR AlphaFoldDB; A0A1S3U5N2; -.
DR STRING; 3916.A0A1S3U5N2; -.
DR GeneID; 106762119; -.
DR KEGG; vra:106762119; -.
DR OrthoDB; 1110531at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
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:UP000087766};
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 500 AA; 55315 MW; D92A7FE8B26CB7B2 CRC64;
MVLAELGGSI SRALQQMSNA TVIDEKVLND CLNDITRALL QSDVQFKLVR DMQTNIKNIV
NLDDLAAGHN KRRIIQQAVF NELCKILDPG KPSFTPKKGK TSVVMFVGLQ GSGKTTTCTK
YAYYHQKKGW KPALVCADTF RAGAFDQLKQ NATKAKIPFY GSYMESDPVK IAVEGVERFK
EENCDLIIVD TSGRHKQEAA LFEEMRQVSE ATKPDLVIFV MDSSIGQAAF DQAQAFKQSV
AVGAVIVTKM DGHAKGGGAL SAVAATKSPV IFIGTGEHMD EFEVFDVKPF VSRLLGMGDW
SGFMDKIQEV VPMDQQPELL QKLSEGNFTL RIMYEQFQNI LKMGPISQVF SMLPGFSAEL
MPKGREKESQ AKIKRYMTMM DSMTNEELDS SNPKLMNESR IMRIARGAGR QIREVMEMME
EYKRLAKIWS KMKGLKIPKK GEMSALSRNM NAQHMSKVLP PQMLKQIGGM GGLQNLMKQM
GSAKDMMGMG GLFGGGGGGD
//
