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Database: UniProt
Entry: A0A2Y9K633_ENHLU
LinkDB: A0A2Y9K633_ENHLU
Original site: A0A2Y9K633_ENHLU 
ID   A0A2Y9K633_ENHLU        Unreviewed;       638 AA.
AC   A0A2Y9K633;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Signal recognition particle receptor subunit alpha isoform X1 {ECO:0000313|RefSeq:XP_022368568.1};
GN   Name=LOC111153704 {ECO:0000313|RefSeq:XP_022368568.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368568.1};
RN   [1] {ECO:0000313|RefSeq:XP_022368568.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022368568.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_022368568.1; XM_022512860.1.
DR   AlphaFoldDB; A0A2Y9K633; -.
DR   STRING; 391180.A0A2Y9K633; -.
DR   KEGG; elk:111153704; -.
DR   OrthoDB; 5475029at2759; -.
DR   Proteomes; UP000248482; Unplaced.
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,
KW   ECO:0000313|RefSeq:XP_022368568.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT   DOMAIN          610..623
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          132..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   638 AA;  69786 MW;  B8D4D2F72BAAE149 CRC64;
     MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN
     QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ RSALSLLNGT FDFQNDFLRL
     LREAEESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKP KEKAKNSKKK GAKKESSDGP
     LATSKAVPAE KSGLAVGPEN GVELSKEELI RRKREEFIQK HGRGLEKSSK SMKSDAPKEK
     GKKVPRVWAL GGCANKEILD YSTPTTNGAP EDAPPEDISL IRGTGPGGQL QDLDCSSSDD
     EAAAQNTTKP SATKGTLGGM FGMLKGLVGS KSLSREDMES VLDKMRDHLI AKNVAADIAV
     QLCESVANKL EGKVMGTFST VTSTVKQALQ ESLVQILQPQ RRVDMLRDIM DAQRHQRPYV
     VTFCGVNGVG KSTNLAKISF WLLENGFSVL IAACDTFRAG AVEQLRTHTR RLSALHPPEK
     HGGRTMVQLF EKGYGKDAAG IAMEAIAFAR NQGFDVVLVD TAGRMQDNAP LMTALAKLIT
     VNTPDLVLFV GEALVGNEAV DQLVKFNRAL ADHSMAQTPR LIDGIVLTKF DTIDDKVGAA
     ISMTYITSKP IVFVGTGQTY CDLRSLNAKA VVAALMKA
//
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