SR543_HORVU
ID SR543_HORVU Reviewed; 493 AA.
AC P49970;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Signal recognition particle 54 kDa protein 3;
DE Short=SRP54;
GN Name=SRP54-3;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root, and Shoot;
RA Chu B., Brodl M.R., Belanger F.C.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the signal sequence of presecretory protein when
CC they emerge from the ribosomes and transfers them to TRAM
CC (translocating chain-associating membrane protein).
CC -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule of
CC 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19,
CC SRP14 and SRP9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
CC domain binds the 7S RNA in presence of SRP19 and also binds the signal
CC sequence.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; L48286; AAA79356.1; -; mRNA.
DR PIR; T06187; T06187.
DR AlphaFoldDB; P49970; -.
DR SMR; P49970; -.
DR PRIDE; P49970; -.
DR ExpressionAtlas; P49970; baseline and differential.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11564; PTHR11564; 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; SSF47364; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..493
FT /note="Signal recognition particle 54 kDa protein 3"
FT /id="PRO_0000101209"
FT REGION 1..294
FT /note="G-domain"
FT REGION 295..493
FT /note="M-domain"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 53824 MW; F478C70C5DFACA98 CRC64;
MVLADVGGSI SRALAMSSAA VVDESVLREC LNEIARALMQ SDVRFKTVCD LQANIRKTVN
LEALAAGTNK RRIIETSVGK ELCKMLDTGK PAFVPKKGKP NVVMFVGLQG SGKTTTCTKY
AHYHQRKGFK PSLVCADTFR AGAFDQLKQN ATKAKIPFYG SYMESDPVKI AVEGLEKFRQ
EKSDLIIIDT SGRHMQEAAL FEEMRQVAEA TKPDLVIFVM DGSIGQAAFD QAQAFKQSAS
VGAVIVTKLD GHAKGGGALS AVAATKSPVI FIGTGEHIDD FDVFNVEPFV ARLLGRGDLP
GLIDKMESIV PADQQSELVA KLSEGAFTLR LLYEQFQNLL KMGPMSQIFS MLPGFSSELM
PKGQEKQSKE KFKRYMTIMD SMTPAELDST NPKLMTESRI IRVARGSGRK VKDVMEMLEE
YKRLAKMWSK RNVSKLIPQN GKMSAQAIQK MLKVMPPQVV QQMGGKSGLE ALLKQLGGGK
DTSKMLAGMR GGA