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Database: UniProt
Entry: A0A1Q7QLD6_9CHLR
LinkDB: A0A1Q7QLD6_9CHLR
Original site: A0A1Q7QLD6_9CHLR 
ID   A0A1Q7QLD6_9CHLR        Unreviewed;       368 AA.
AC   A0A1Q7QLD6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   10-APR-2019, entry version 20.
DE   RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944};
GN   ORFNames=AUI58_02415 {ECO:0000313|EMBL:OLD52555.1};
OS   Chloroflexi bacterium 13_1_40CM_2_70_6.
OC   Bacteria; Chloroflexi.
OX   NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD52555.1};
RN   [1] {ECO:0000313|EMBL:OLD52555.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C.,
RA   Singh A., Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G.,
RA   Northen T., Pan C., Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S
CC       ribosomal subunit in a nucleotide-independent manner.
CC       {ECO:0000256|HAMAP-Rule:MF_00944}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00944}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00944}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OLD52555.1}.
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DR   EMBL; MNHK01000031; OLD52555.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   CDD; cd04867; TGS_YchF_C; 1.
DR   Gene3D; 1.10.150.300; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR   InterPro; IPR004396; ATPase_YchF/OLA1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR030389; G_FEOB_dom.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR023192; TGS-like_dom_sf.
DR   InterPro; IPR013029; YchF_C.
DR   Pfam; PF02421; FeoB_N; 1.
DR   Pfam; PF06071; YchF-GTPase_C; 1.
DR   PIRSF; PIRSF006641; CHP00092; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00092; TIGR00092; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00944};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00944}.
FT   DOMAIN        5     50       FeoB-type G. {ECO:0000259|Pfam:PF02421}.
FT   DOMAIN      284    367       YchF-GTPase_C. {ECO:0000259|Pfam:
FT                                PF06071}.
FT   COILED      158    178       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   368 AA;  39888 MW;  3C477E2F5AC48C19 CRC64;
     MGLTSAITGL PYVGKTTLFN LLTGAHAATG GFAGAEAETN VGVAKVPDER VDRLAPLFQP
     KKTTHAEITY RDLGLAKPAA PGQAISAQKL GDLRTADALV HVVRAFADAG VPHVEGTVDP
     ARDLATLELE LLFADHAVVE RRLERLEPEL RSAKGAERDA KEREKAVLEH ARSALDAERP
     LRDVDFDAEE LRVMRGFRFL TLMPTLVAAN LDEADVGRPD TVLAPLRAAT GKHRATAVVP
     VCAKIESEIA ELPPDEAAAF RADLGLAEPA LDRLIRATYE LLGLISFFTV GPDEVRAWTI
     PAGTRAQQAA GAIHSDLERG FIRAEVIEWD DLLRVGSETE AKRQALMRTV GKDWVVEDGW
     VMHVLFNI
//
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