ID M7AXY2_CHEMY Unreviewed; 581 AA.
AC M7AXY2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Signal recognition particle receptor subunit alpha {ECO:0000313|EMBL:EMP29614.1};
DE Flags: Fragment;
GN ORFNames=UY3_13272 {ECO:0000313|EMBL:EMP29614.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP29614.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB555015; EMP29614.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AXY2; -.
DR STRING; 8469.M7AXY2; -.
DR eggNOG; KOG0781; Eukaryota.
DR Proteomes; UP000031443; 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:EMP29614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 553..566
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 76..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP29614.1"
SQ SEQUENCE 581 AA; 64394 MW; 82140EE9525500B8 CRC64;
FQVGFQKILT LTYVDKLIDD VHKEFRDKYR NEFQQKGTLG LLNGTFDFKE DFLHLLREAE
ESSKIRAPTA MKTFEQSVKS QKTVKSMIET RGEKPKEKVK NKKNKGSKKE ASGTEAATVP
SKAAPDAKQN PLAATGDREE LTKDEILQKN REEFFKKRLK GGEKSNKSPK PETQKEKGKK
PRVWELGNSN AKVLDYSNST TNGNTDTCPT EEYDPDMALG DRDREPGRLY DLEYESDEEE
PEEEKVIQNP SQPRAKKGGL GGMFGMLKGL VGSKSLTRED MDSVLEKMKD HLIAKNVAAD
IAVQLCESVA KKLEGKVMGT FTTVTSTVKQ ALQESLVQIL QPQRRVDMLR DVMDAQRHRR
PYVVTFCGVN GVGKSTNLAK ISFWLIENGF SVLIAACDTF RAGAVEQLRT HTRRLNALHP
PESHGGRTMV QLYEKGYGKD AAGIAMEAIL YARNQGFDVV LVDTAGRMQD NAPLMTALAK
LIAVNTPDLV LFVGEALVGN EAVDQLVKFN KALADHSMAQ TPRLIDGIVL TKFDTIDDKV
GAAISMTYIT SKPIVFVGTG QTYCDLRSLN AKAVVTALMK A
//
