ID A0A0L7KE47_PLAFX Unreviewed; 500 AA.
AC A0A0L7KE47;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN ORFNames=PFHG_03384 {ECO:0000313|EMBL:KOB61623.1};
OS Plasmodium falciparum (isolate HB3).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=137071 {ECO:0000313|EMBL:KOB61623.1, ECO:0000313|Proteomes:UP000054289};
RN [1] {ECO:0000313|EMBL:KOB61623.1, ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB3 {ECO:0000313|EMBL:KOB61623.1};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Kodira C., Zeng Q., Oleary S., Yandava C., Alvarado L., Wirth D.,
RA Volkman S., Hartl D.;
RT "The genome sequence of the Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) 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 {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
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 EMBL; CH672012; KOB61623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7KE47; -.
DR SMR; A0A0L7KE47; -.
DR EnsemblProtists; KOB61623; KOB61623; PFHG_03384.
DR VEuPathDB; PlasmoDB:PfHB3_140055800; -.
DR OMA; GMTGQDA; -.
DR Proteomes; UP000054289; 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 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:UP000054289};
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; 55979 MW; 183FF7F2768151DD CRC64;
MVLTELGTQI TNAFRKLQTS TLADDVVIEE CLKEIIRALI LSDINVSYLK DIKSNIKNNI
EKNIDIYGNN KKKLVQKYVV EELIKLLEGK KEGYNPVKGK RNVILFVGLQ GSGKTTTCTK
YAHYYQKKGF KTALVCADTF RAGAFDQLKQ NAAKVKIPFY GSYSEVDPVK IATDGVNAFL
KDKYDLIIVD SSGRHKQENE LFEEMIQVEN SIQPEEIIFV IDSHIGQSCH DQAMAFKNSV
SLGSIIITKI DGHAKGGGAL SAVAATGCPI TFIGTGEHVN DFEKFEAKSF VSRLLGLGDI
SGLVSTIKEV IDIDKQPELM NRLSKGKFVL RDMYDQFQNV FKMGSLSKVM SMIPGFGNNL
ISKGTEKEGI DKIKKFMVIM DSMTNEELDC IKPLNDSRCL RIVKGSGTRL QDIKELLEQF
KFLQKMVVKM GKLGLRENNI SNLMRNQKQF MSKMNNIMDP NMLKQLGGAN NMVNILKEFT
KMDDLGVSMA NMMKQMGLKK
//
