SRP54_ASPNG
ID SRP54_ASPNG Reviewed; 534 AA.
AC Q00179;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Signal recognition particle 54 kDa protein homolog;
GN Name=srpA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8566805; DOI=10.1016/0378-1119(95)00669-9;
RA Thompson S.A., Golightly E.J., Yaver D.S.;
RT "Nucleotide sequence of the Aspergillus niger srpA gene.";
RL Gene 167:337-338(1995).
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 -!- 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; L38317; AAB04946.1; -; Genomic_DNA.
DR PIR; JC4572; JC4572.
DR AlphaFoldDB; Q00179; -.
DR SMR; Q00179; -.
DR STRING; 5061.CADANGAP00008025; -.
DR VEuPathDB; FungiDB:An09g06320; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1115095; -.
DR VEuPathDB; FungiDB:ATCC64974_8040; -.
DR VEuPathDB; FungiDB:M747DRAFT_287874; -.
DR eggNOG; KOG0780; Eukaryota.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:EnsemblFungi.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..534
FT /note="Signal recognition particle 54 kDa protein homolog"
FT /id="PRO_0000101199"
FT REGION 1..296
FT /note="G-domain"
FT REGION 297..534
FT /note="M-domain"
FT BINDING 109..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 534 AA; 57117 MW; 1B21E3A48CCB3BA6 CRC64;
MVLQDLGRRI NAAVNDLTRS NNLDEKQAFD DMIKEICAAL LSADVNVRLV QSLRKSIKSS
VNFASLPPAV NKKRLIQKAV FDELVSLVDP HAEPFRPKKG RSNVIMFVGL QGAGKTTTCT
KLARHYQMRG FKTALVCADT FRAGAFDQLK QNATKAKIPY YGSLTQTDPA IVAAEGVAKF
KKERFEIIIV DTSGRHKQEE ELFTEMTQIQ TAVTPDQTIL VLDSTIGQAA EAQSSAFKAT
ADFGAIIITK TDGHAAGGGA ISAVAATHTP IIYLGTGEHL MDLERFEPKA FIQKLLGMGD
MAGLVEHVQA VTKDSASAKE TYKHISEGIY TLRDFRENIT SIMKMGPLSK LSGMIPGLSN
LTAGLDDEDG SMKLRRMIYI FDSMTAAELD GDGKMFVEQP SRMVRIACGS GTTVREVEDL
LSQHRMMAGM AKRVGGQKKQ MQRAQNMLKG GNKEQQLAAM QKRMAAMGGA GGGGFPGMPG
MGDMAKMMQM LQGQGGGGGG GLPGLGGMDL QSMMSQMSGL MGGGGGGGGR GRGR