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Database: UniProt
Entry: A0A316UBV3_9BASI
LinkDB: A0A316UBV3_9BASI
Original site: A0A316UBV3_9BASI 
ID   A0A316UBV3_9BASI        Unreviewed;       720 AA.
AC   A0A316UBV3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=P-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:PWN21941.1};
GN   ORFNames=BCV69DRAFT_281846 {ECO:0000313|EMBL:PWN21941.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN21941.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN21941.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN21941.1,
RC   ECO:0000313|Proteomes:UP000245942};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(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}.
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DR   EMBL; KZ819324; PWN21941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316UBV3; -.
DR   STRING; 1684307.A0A316UBV3; -.
DR   OrthoDB; 5475029at2759; -.
DR   Proteomes; UP000245942; 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   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   Hydrolase {ECO:0000313|EMBL:PWN21941.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245942}.
FT   DOMAIN          692..705
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          176..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..358
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  75455 MW;  D4C23CDFD363AF78 CRC64;
     MLDNFTVLHT SGIVLWSKSF TPTFASNSPI GPLVRTAFIE SRSTGSADDE RYDVGGYSCR
     WSLANDYGLA FVAVHQRILH LAYVPALLAQ VRALFLDLFK PFLGAILANT KPIGGGGDGS
     ASLASKLTGE ARARFAAALK DWDAIFTSTL RKLEREANLQ ARSAAKSSGG AIAAAGAANA
     ETPASPKTSA DKVGKKGATP SAGNDDQAIA KNIEALKARL KGVEIGPGGS RGPAGTAARR
     KMGSRVSSGV GTPGGGAESP TASPGGKKKG GAGKEMRKWD ANGNAIVVGD VGQLDFSNDG
     GPSTPADERE QGTLEGWVDE KSLGKVGQDG LYEVADALDN GDEEASDEEE DEEDEEDQAV
     TNGKATSGGG FLSGLTSKSS GATSLFSRLT GSGHSLTQAD LQPTLAAMQS HLQSKNVAAD
     VAQRLCASVG RSLEGKTLST FGSVKKEVRL ALEDAITRVL TPRNSTDLLL EINDKLGRQA
     SKGDPASTTR QPYALAFVGV NGVGKSTNLA KVCFWLLQNQ KRVLIAACDT FRSGAVEQLR
     VHVRNLGELN VGGSQVKEPL PSGGQKLELY ERGYGKDAAG IAASALSYAR AQGFDVVLID
     TAGRMQDNEP LMRSLAKLVA TNEPDRVIFV GEALVGNEAV DQLTRFDKSL RDFSGKSAQD
     ARGLDGMLLT KFDTIDDKVG TALTATSVTG LPIYFVGVGQ TYTDLKQLKV KHIVNALMRD
//
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