ID A0A0E0AWN9_9ORYZ Unreviewed; 624 AA.
AC A0A0E0AWN9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=SRP54-type proteins GTP-binding domain-containing protein {ECO:0000259|PROSITE:PS00300};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM08G19170.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM08G19170.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM08G19170.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004347}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family.
CC {ECO:0000256|ARBA:ARBA00008531}.
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DR AlphaFoldDB; A0A0E0AWN9; -.
DR STRING; 40148.A0A0E0AWN9; -.
DR EnsemblPlants; OGLUM08G19170.1; OGLUM08G19170.1; OGLUM08G19170.
DR Gramene; OGLUM08G19170.1; OGLUM08G19170.1; OGLUM08G19170.
DR eggNOG; KOG0781; Eukaryota.
DR HOGENOM; CLU_009301_8_2_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005785; C:signal recognition particle receptor complex; 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:0005047; F:signal recognition particle binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd14826; SR_alpha_SRX; 1.
DR CDD; cd17876; SRalpha_C; 1.
DR Gene3D; 3.30.450.60; -; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007222; Sig_recog_particle_rcpt_asu_N.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF04086; SRP-alpha_N; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 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; SSF64356; SNARE-like; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 597..610
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 122..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 68721 MW; EFFB5D66F1857131 CRC64;
MLEELLIFTR GGLILWSSCR ALGGAALKGS PIDALIRSCL LEERSADASF SQDTYALKWT
FNNDLGLVFV AVYQRMLHLL YVDDLLAAVR KEFSQIYDPK RTSYDDAFNE VFRQLHLEAE
ARSEEMKKNK QVTGSRPTKV TTKTNRGDTQ GSGGGRKKGD SGKDDSDGDS GKEHTLPNGN
SKMQENSLKD NSHARSVVVK GKENGDPNDG AFDVNKLQKM RNKGNKKNEV ASNVAKNTSK
ANTKKNLKKN RVWDDTPDDK KKLDFTDPAD ERGDEVIDQV VVKQGESMMD KDDVVSSDSD
EEEEDGEENS GASQKKKGWF SSMFKSIAGN NVLEKSDIQP ALKALKDRLM TKNVAEEIAE
KLCESVAASL EGKKLGSFTR ISSTVQTAME EALLRILTPR RSIDILRDVH AAKERGKPYV
IVFVGVNGVG KSTNLAKVAY WLLQHNLSVS LAACDTFRSG AVEQLRTHAR RLQIPIFEKG
YEKDPAVVAK EAIQEATRNK SDVVLVDTAG RMQDNEPLMR ALSKLINLNS PDLVLFVGEA
LVGNDAVDQL TKFNQKLAEL SAVPTTRLID GILLTKFDTI DDKVGAALSM VYISGAPVMF
VGCGQSYTDL KKLNVKSIVK TLLK
//
