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Database: UniProt
Entry: T0ZEF9_9ZZZZ
LinkDB: T0ZEF9_9ZZZZ
Original site: T0ZEF9_9ZZZZ 
ID   T0ZEF9_9ZZZZ            Unreviewed;       290 AA.
AC   T0ZEF9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Signal recognition particle protein {ECO:0000313|EMBL:EQD43458.1};
DE   Flags: Fragment;
GN   ORFNames=B1B_13810 {ECO:0000313|EMBL:EQD43458.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD43458.1};
RN   [1] {ECO:0000313|EMBL:EQD43458.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD43458.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EQD43458.1}.
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DR   EMBL; AUZY01009107; EQD43458.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0ZEF9; -.
DR   GO; GO:0048500; C:signal recognition particle; 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:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd18539; SRP_G; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR036225; SRP/SRP_N.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR   PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 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   PROSITE; PS00300; SRP54; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          269..282
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   NON_TER         290
FT                   /evidence="ECO:0000313|EMBL:EQD43458.1"
SQ   SEQUENCE   290 AA;  30698 MW;  9CA2CB937F228DF5 CRC64;
     MFETLSQRLG ATVERLRGRG RLTEENIRES LREVRIALLE ADVALPVVQA LIERVKVRAV
     GQEVLKSLTP GQALVKVVRD ELTALMGTAN AALDLAATPP AVVLMAGLQG AGKTTTVAKL
     ARFLKERAKK KVLVVSCDVY RPAAIEQLRV LAAQVEVGFV SAAAGAKPVD IARAALAQAR
     REVADVLIVD TAGRLAIDAA MMDEIRALHA ALQPVETLFV VDAMTGQDAA TTAKAFAEAL
     PLTGVILTKT DGDARGGAAL SVRYVTGRPI KFLGAGEKTD ALEPFHPDRL
//
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