SRP54_GEOCY
ID SRP54_GEOCY Reviewed; 499 AA.
AC Q8MZJ6;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Signal recognition particle 54 kDa protein;
DE Short=SRP54;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P61011};
GN Name=SRP54;
OS Geodia cydonium (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX NCBI_TaxID=6047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Durajlija-Zinic S., Cetkovic H., Mueller W.E.G., Gamulin V.;
RT "Signal recognition particle 54 kD protein (SRP54) from the marine sponge
RT Geodia cydonium.";
RL Food Technol. Biotechnol. 40:233-237(2002).
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 (By similarity). As part of the SRP complex, associates with the SRP
CC receptor (SR) component SRPRA to target secretory proteins to the
CC endoplasmic reticulum membrane (By similarity). Binds to the signal
CC sequence of presecretory proteins when they emerge from the ribosomes
CC (By similarity). Displays basal GTPase activity, and stimulates
CC reciprocal GTPase activation of the SR subunit SRPRA (By similarity).
CC Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR
CC subunit SRPRA (By similarity). SR compaction and GTPase mediated
CC rearrangement of SR drive SRP-mediated cotranslational protein
CC translocation into the ER (By similarity). Requires the presence of
CC SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity).
CC {ECO:0000250|UniProtKB:P61010, ECO:0000250|UniProtKB:P61011}.
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:0000250|UniProtKB:P61011}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P61011}.
CC Cytoplasm {ECO:0000250|UniProtKB:P61011}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P61011}.
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 (By similarity). The two NG domains
CC undergo cooperative rearrangements upon their assembly, which culminate
CC in the reciprocal activation of the GTPase activity of one another (By
CC similarity). SRP receptor compaction upon binding with cargo-loaded SRP
CC and GTPase rearrangement drive SRP-mediated cotranslational protein
CC translocation into the ER (By similarity).
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of SRP19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY100457; AAM23234.1; -; mRNA.
DR AlphaFoldDB; Q8MZJ6; -.
DR SMR; Q8MZJ6; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..499
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101198"
FT REGION 1..294
FT /note="NG-domain"
FT /evidence="ECO:0000250|UniProtKB:P61011"
FT REGION 295..499
FT /note="M-domain"
FT /evidence="ECO:0000250|UniProtKB:P61011"
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 499 AA; 55175 MW; DA7A65507ECCD21A CRC64;
MVLADLGRKI TTALLPRQRT VINEEVLQAM LKEICTALLE ADVNVKLVGK LRQNVRAAID
FEDMGAGLSK RRIIQTSVFN ELCKLLDPGV PVWHPTKGHS NVIMFVGLQG SGKTTTCTKL
AYHYQKKGWK TCLVCADTFR AGAFDQLKQN ATKARVPFYG SYTEMDPVVI AQEGVEKFKE
DSFEVIIVDT SGRHKQEESL FEEMLQVSQA IDPDNIIFVM DGTIGQACES QARAFKEKVD
VASVIVTKLD GHAKGGGALS AVAATRSPII FIGTGEHIDE MEPFKTKPFV SKLLGMGDLE
GLMEKVSDLK LDENEELMDK LKHGQFTLRD MYEQFQNIMK MGPFNQIIGM IPGFSPDFMS
KGNERESMAK LKRLMTMMDS MNDGELDHPN GAKLFSKQPG RAARVARGSG TSVREVNELL
KQYSNFSATV KKMGGIKGLF KGGDLGKNVN PSQMAKLNQQ MAKMMDPRVL QQMGGMSGLQ
NMMRQFQQGA SNMPGFKGK
