ID Q5F390_CHICK Unreviewed; 644 AA.
AC Q5F390;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=SRP54-type proteins GTP-binding domain-containing protein {ECO:0000259|PROSITE:PS00300};
GN ORFNames=RCJMB04_28a6 {ECO:0000313|EMBL:CAH65394.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:CAH65394.1};
RN [1] {ECO:0000313|EMBL:CAH65394.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB {ECO:0000313|EMBL:CAH65394.1};
RC TISSUE=Bursa {ECO:0000313|EMBL:CAH65394.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ851760; CAH65394.1; -; mRNA.
DR RefSeq; NP_001034366.1; NM_001039277.1.
DR AlphaFoldDB; Q5F390; -.
DR SMR; Q5F390; -.
DR GeneID; 419713; -.
DR KEGG; gga:419713; -.
DR CTD; 6734; -.
DR VEuPathDB; HostDB:geneid_419713; -.
DR PhylomeDB; Q5F390; -.
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 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170}.
FT DOMAIN 616..629
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 156..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71197 MW; EDD84F161B8A9D54 CRC64;
MLDFFTIFSK GGLVLWCFQG VRGPASAATA PVNALIRSVL LQERGGNNSF THEALTLKYK
LDNQFELVFV VGFQKILTLT YVDKLIDDVH KEFRDKYRNE FQQKGALGIL NGTFDFKDDF
LRLLREAEES SKVRAPTVMK TFEQSVKSQK TVKCMIETRG EKPKEKVKNK KNKGSKKEGN
EAVTASNKTA PGEKQSSAAG DKEELTKDEI LQKNREEFFK RHMKAGEKSS KSPKPDAQKE
KGKKPRVWDL GNSNAKVLDY SNSTTNGNSE ASPMEDFDPD MALRDRNREP GRLYDLEYES
DEEAEEEKII QNTSKPSTKK GGLGGMFGML KGLVGSKSLT RQNMDPVLEK MKDHLIAKNV
AAEIAVQLCE SVAKKLEGKV MGTFTTVTST VKQALQEALV QILQPQRRVD VLRDVMDAQR
HRRPYVVTFC GVNGVGKSTN LAKISFWLIE NGFSVLIAAC DTFRAGAVEQ LRTHTRRLNA
LHPPESHGGR TMVQLYEKGY GKDAAGIAME AISYARNQGF DVVLVDTAGR MQDNAPLMTA
LAKLIAVNAP DLVLFVGEAL VGNEAVDQLV KFNKALADHS MAQTPRLIDG IVLTKFDTID
DKVGAAISMT YITSKPIVFV GTGQTYCDLR SLNAKAVVAA LMKA
//
