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Database: UniProt
Entry: E3S2R0_PYRTT
LinkDB: E3S2R0_PYRTT
Original site: E3S2R0_PYRTT 
ID   E3S2R0_PYRTT            Unreviewed;       541 AA.
AC   E3S2R0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-NOV-2023, entry version 56.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN   ORFNames=PTT_16633 {ECO:0000313|EMBL:EFQ87728.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ87728.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ87728.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- FUNCTION: Signal-recognition-particle (SRP) assembly has a crucial role
CC       in targeting secretory proteins to the rough endoplasmic reticulum (ER)
CC       membrane. SRP is required for the cotranslational protein translocation
CC       for ER import and preferentially recognizes strongly hydrophobic signal
CC       sequences. It is involved in targeting the nascent chain-ribosome (RNC)
CC       complex to the ER and is proposed to participate in the arrest of
CC       nascent chain elongation during membrane targeting. SRP54 binds to the
CC       signal sequence of presecretory protein when they emerge from the
CC       ribosomes. SRP54 interacts with the scR1 RNA and mediates the
CC       association of the resulting SRP-RNC complex with the signal
CC       recognition particle receptor (SR) via its alpha subunit SRP101. Both,
CC       SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR
CC       complex, which dissociates upon transferring the signal sequence to the
CC       protein-conducting channel (translocon). After signal sequence
CC       transfer, SRP54 and SRP101 act as reciprocal GTPase-activating proteins
CC       (GAPs), thereby resolving their association.
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   -!- SUBUNIT: Fungal signal recognition particle consists of a 7S RNA
CC       molecule (scR1) and at least six protein subunits: srp72, srp68, srp54,
CC       sec65, srp21 and srp14. {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 and the signal sequence of
CC       presecretory proteins. {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 srp101. 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; GL536800; EFQ87728.1; -; Genomic_DNA.
DR   RefSeq; XP_003304165.1; XM_003304117.1.
DR   AlphaFoldDB; E3S2R0; -.
DR   STRING; 861557.E3S2R0; -.
DR   EnsemblFungi; EFQ87728; EFQ87728; PTT_16633.
DR   KEGG; pte:PTT_16633; -.
DR   eggNOG; KOG0780; Eukaryota.
DR   HOGENOM; CLU_009301_6_1_1; -.
DR   OrthoDB; 1110531at2759; -.
DR   Proteomes; UP000001067; 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; 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; 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|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:UP000001067};
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   541 AA;  57682 MW;  4BF20AD8B76235FF CRC64;
     MVLQDLGRRI NAAVTDLTRS PNLDEKAFDA MVKEISNALV EADVNVKLVM NLRQSIKRTV
     DFKHLAPGVN KKRLIQKAVF DELVKMVDPH AEPFKPRKGK SNVIMFVGLQ GAGKTTTCTK
     LARWYQARGF KACLVCADTF RAGAFDQLKQ NATKAKIPYY GSHTQTDPVV VAGEGVEKFK
     KERFEIIIVD TSGRHRQEKD LFDEMVQIQN VVTPDQTIMV LDGTIGQAAE SQARAFKEAA
     DFGAIIITKT DGAAAGGGAI SAVAATHTPI VFLGNGEHML DLERFAPQAF VSKLLGMGDV
     QGLVEHVQSL KLDQKDTMKH ITQGIFTIKD LRDQLSNIMK MGPLSKMAGM IPGLGNMMGG
     MDDEEGGMKL KRMIYICDSM TEKELESDGK MFVDQPTRMT RIARGSGTSV REVEELLTQH
     RMMAGMAKKM KGGMASMQKA QGAMGGGNKQ QQLAAMQKRM QSMGGAGGGG GMPDLGAMMK
     MLGGGRGGGG GMPDMSALAG MGGMGGMGGM DMGAMMKMMG GMGGMGGGAG SGGAGQGKGR
     R
//
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