ID A0A2S4UBA0_9BASI Unreviewed; 647 AA.
AC A0A2S4UBA0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=signal-recognition-particle GTPase {ECO:0000256|ARBA:ARBA00035672};
DE EC=3.6.5.4 {ECO:0000256|ARBA:ARBA00035672};
DE AltName: Full=Signal recognition particle 54 kDa protein homolog {ECO:0000256|ARBA:ARBA00034905};
GN ORFNames=PSTT_16772 {ECO:0000313|EMBL:POV94578.1};
OS Puccinia striiformis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27350 {ECO:0000313|EMBL:POV94578.1, ECO:0000313|Proteomes:UP000239156};
RN [1] {ECO:0000313|EMBL:POV94578.1, ECO:0000313|Proteomes:UP000239156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-210 {ECO:0000313|EMBL:POV94578.1,
RC ECO:0000313|Proteomes:UP000239156};
RA Xia C.;
RT "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT fungi.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POV94578.1}.
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DR EMBL; PKSL01000406; POV94578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4UBA0; -.
DR VEuPathDB; FungiDB:PSHT_15397; -.
DR VEuPathDB; FungiDB:PSTT_16772; -.
DR Proteomes; UP000239156; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; 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 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; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
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};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000239156};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135}.
FT DOMAIN 287..300
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 68894 MW; EC9EEEE1A63B16E2 CRC64;
MVLADLGKKI NAAFSELQRT PLIDDKALDL LLKGISSALL SSDVNVTLVA NLRNRVKSKL
LPQLEKLIQS PAKQKQLVHK TVFDELVALV SPAGSASDHA SSSSRPAEYA PWQPKKGKPN
FIMFVGLQGS GKTTSCTKLA VYYRRKGFKT ALVCADTFRA GAFDQLKQNA TKAKIPFYGS
HTETDPISIS MAGVTRFKRE RFEVIIVDTS GRHRQETELF EEMKQISAGV TPNLTIMVLD
GAIGQAAESQ TRAFKEAADF GAIIVTKMDG HAKGGGAISA VAAAQTPIMF IGTGEHLHDL
ERFAPEPFIS KLLGMGDISE FLETMQDLQS ATPNQNREEM RQRIERGIFT VRDLRDQMSN
LTQMGSIGKI ASMIPGMSNM MAGLGGGDGD EMSQKMKRMV FIFDAMTPQE LDSDGSMFRR
KRRKGDNNNQ LADGEPREPH PRVLRIARGS GTSVDEVEGM LAQHAMFATM VKGAGGKRKW
EQQQALKQAQ QQSKAMMGGS RGGKVKQQQV TIEQLVKMAP AQRAQVLRQA PANVRKQIED
AGGVDAFYAL SQAAQRSGGQ PSAATRARRA AAAMAGGGTG GGAGAGGLGS LLGGLGGLGG
LGGLGGLGGL GGGQMPDPET MRKMMEQMGM GDLGSMFGAG GPGPGNH
//
