ID K1XLM5_MARBU Unreviewed; 525 AA.
AC K1XLM5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
GN ORFNames=MBM_08462 {ECO:0000313|EMBL:EKD13379.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13379.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13379.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13379.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921450; EKD13379.1; -; Genomic_DNA.
DR RefSeq; XP_007296351.1; XM_007296289.1.
DR AlphaFoldDB; K1XLM5; -.
DR STRING; 1072389.K1XLM5; -.
DR GeneID; 18764397; -.
DR KEGG; mbe:MBM_08462; -.
DR eggNOG; KOG0780; Eukaryota.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; K1XLM5; -.
DR OMA; GMTGQDA; -.
DR OrthoDB; 1110531at2759; -.
DR Proteomes; UP000006753; 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:UP000006753};
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 525 AA; 56278 MW; 751AE1EA0C90E66E CRC64;
MVLQDLGRRI NAAVSDLTRS SNLDEKAFDG MIKEICAALL EADVNVRLVG NLRKSIKASV
NFKDQAPGVN KKRLIQKAVF DELVKLVDPH AEPFKPKKGK ANVIMFVGLQ GAGKTTTCTK
LARHYQSRGF KACLVCADTF RAGAFDQLKQ NATKAKIPYY GSLTQTDPAV VAKEGVEKFK
KERFEIIIVD TSGRHRQEDA LFQEMVDIQT AVKPDQTIMV LDASIGQQAE AQSKAFKETA
DFGAIIITKT DGHASGGGAI SAVAATHTPI VFIGTGEHML DLERFAPQQF VSKLLGMGDM
QGLVEHVQSL KLDQKDTMKH IAEGVFTVRD LRDQLSNIMK MGPLSKMAGM IPGMSGMMQG
MDDDEGSMKL KRMIYICDSM TAKELDSDGK MFIEQPTRMT RIAYGSGTSV HEVEDLLTQH
KMMAGMAKKM GGNIKNLQKA QGAMGGGNKQ QQMAAMQKRL ASMGGGGAGG GMPDMGSLMK
MLGGGGGGGA GGMPGMPGMP GGMDMQAMMK QMSGMMGGAG RGGRR
//
