SR541_HORVU
ID SR541_HORVU Reviewed; 497 AA.
AC P49968;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Signal recognition particle 54 kDa protein 1;
DE Short=SRP54;
GN Name=SRP54-1;
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; L48284; AAA79354.1; -; mRNA.
DR PIR; T06185; T06185.
DR AlphaFoldDB; P49968; -.
DR SMR; P49968; -.
DR ExpressionAtlas; P49968; 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..497
FT /note="Signal recognition particle 54 kDa protein 1"
FT /id="PRO_0000101207"
FT REGION 1..295
FT /note="G-domain"
FT REGION 296..497
FT /note="M-domain"
FT BINDING 108..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 497 AA; 54512 MW; 28647ABDCA372B95 CRC64;
MVLAQLGGSI SRALAQMSNA TVIDEKVLGE CLNEISRALL QSDVQFKMVR DMQTNIRKIV
NLETLAAGTN KRRIIQQAVF TELCNMLDPG KPAFTTKKGK PSVVMFVGLQ GSGKTTTCTK
YAYYHQRKGF KPSLVCADTF RAGAFDQLKQ NATKAKIPFY GSYMESDPVK IAVEGLERFR
KENSDLIIID TSGRHKQEAA LFEEMRQVAE ATKPDLVIFV MDGSIGQAAF DQAQAFKQSA
SVGAVIITKL DGHAKGGGAL SAVAATKSPV IFIGTGEHID EFEIFDVKPF VSRLLGMGDL
SGLMDKIQDV MPADQQPELL AKLAEGTFTL RLLYEQFQNL LKMGPIGQVF SMLPGFSSEL
MPKGHEKEGQ AKIKRYMTIM DSMTAAELDS TNPKLMTESR IIRIARGSGR QIRDVTDMLE
EYKRLAKMWS KMKGLKMPKN GKMSDLSQNL NIQQMTKALP PQVLKQMGGM GGLQALMKQM
GGKDMSKMLG GMGLGGD