ID A0A2G9HJE4_9LAMI Unreviewed; 621 AA.
AC A0A2G9HJE4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Signal recognition particle receptor, alpha subunit {ECO:0000313|EMBL:PIN17651.1};
GN ORFNames=CDL12_09684 {ECO:0000313|EMBL:PIN17651.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN17651.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- SUBCELLULAR LOCATION: 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}.
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:PIN17651.1}.
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DR EMBL; NKXS01001626; PIN17651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HJE4; -.
DR STRING; 429701.A0A2G9HJE4; -.
DR OrthoDB; 5475029at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:PIN17651.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 594..607
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 123..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 68348 MW; 5BB8281A2A618DAA CRC64;
MLEQLLIFTR GGLILWSCKE FGNALRGSPI DTLIRSCLLE ERSGAASYNY DAPGASYTLK
WTFHNELGLV FVAVYQRILH LLYVDELLSM VKQGFSEIYD PKRTSYNDFD EIFQQLKKEA
EARAEEMKKS KQVGKPMNNH LGRKQGQAQN GSTDGGNKKK SGGENDGGDG DKLRGRTLEN
ENPNNNHVGK GEVPTKVNAN GKGNGTSNNG AFDVNKLQKL RSKGGKKTET VASKVTKAEP
KKKITKKNRV WDDSPKDTKL DFTDPVSENG EENISVVAAD QGESMMDKEE IISSDSEIEE
EDTGKDNKVD SKKKGWFSSM FQSIAGKANL EKSDLEPALK ALKDRLMTKN VAEEIAEKLC
ESVAASLEGK RLASFTRISS TVQAAMEDAL VRILTPRRSI DILRDVHAAK EQGKPYVVVF
VGVNGVGKST NLAKVAYWLL QHNIKVMMAA CDTFRSGAVE QLRTHARRLQ IPIFEKGYEK
DPAIVAKEAI QEASRNGSDV VLVDTAGRMQ DNEPLMRALS KLIYVNDPDL ILFVGEALVG
NDAVDQLSKF NQKLGDLSPS PNPRLIDGIL LTKFDTIDDK VGAALSMVYI SGAPVMFVGC
GQSYTDLKKL NVKSIVKTLL K
//
