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Database: UniProt
Entry: A0A0M8PAL7_9EURO
LinkDB: A0A0M8PAL7_9EURO
Original site: A0A0M8PAL7_9EURO 
ID   A0A0M8PAL7_9EURO        Unreviewed;       646 AA.
AC   A0A0M8PAL7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=SRP54-type proteins GTP-binding domain-containing protein {ECO:0000259|PROSITE:PS00300};
GN   ORFNames=ACN38_g405 {ECO:0000313|EMBL:KOS48676.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS48676.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS48676.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS48676.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS48676.1}.
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DR   EMBL; LHQQ01000003; KOS48676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8PAL7; -.
DR   STRING; 229535.A0A0M8PAL7; -.
DR   OrthoDB; 5475029at2759; -.
DR   Proteomes; UP000037696; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037696}.
FT   DOMAIN          619..632
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          133..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  69961 MW;  AC45EC43B5068C8F CRC64;
     MLEAFEILTT SGVVLWSKAY APVGAHVINS LINDVFIEEK VVPQNTTASG VSPAYKKEKY
     TLKWKRVKEF DLIFVAVYQS LLHLGWIDKL LENISTIFID LYKDQVKGNR ARIQTYRFDQ
     YFEQQVRELE DNTGGFVEEN VPEKGEKKDT LVSSDNGGPP PPPVPGLVKA QPRAALAGAT
     SDEGTPPATP EISRSSTPQG HLLTAKAGPG GRGSRRSRKA ANSSANASSG DDARKGKSAK
     TPVKKMRRWD ASGMADEDDG EILDYSAPAE EEAAAPAVEA VSEEDWGRRT GKGQFVLKEL
     GEEVQSILDQ ADAEKSKATA SSGVVGSGFN AIGGFFRNIV GGKVLTESDL EKPLKAMEEH
     LLKKNVAREA AVRLCEGVKG EMIGKKTGNF QSTDAALHVA MESSLRNILT PTSSLDLLRE
     INAVVAPTTK QQAPRPYVMS IVGVNGVGKS TNLSKICYFL LQNKYRVLIA ACDTFRSGAV
     EQLRVHADRL KELSVRENAG DVEIYQKGYG KDAANVAKDA VDYAAANKFD VVLIDTAGRR
     HNDQRLMSSL EKFAKFANPD KIFMVGEALV GTDSVMQARN FNQAFGTGRN LDGFIISKCD
     TVGDMVGTLV SMVHATGIPI VFLGVGQHYG DLRGLSVPWA VSLLMK
//
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