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Database: UniProt
Entry: R5LZJ1_9FIRM
LinkDB: R5LZJ1_9FIRM
Original site: R5LZJ1_9FIRM 
ID   R5LZJ1_9FIRM            Unreviewed;       578 AA.
AC   R5LZJ1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE            Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN   Name=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN   ORFNames=BN569_01314 {ECO:0000313|EMBL:CCY78422.1};
OS   Butyrivibrio crossotus CAG:259.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY78422.1, ECO:0000313|Proteomes:UP000018300};
RN   [1] {ECO:0000313|EMBL:CCY78422.1, ECO:0000313|Proteomes:UP000018300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the ribosome quality control system (RQC). Recruits
CC       Ala-charged tRNA and directs the elongation of stalled nascent chains
CC       on 50S ribosomal subunits, leading to non-templated C-terminal Ala
CC       extensions (Ala tail). The Ala tail promotes nascent chain degradation.
CC       May add between 1 and at least 8 Ala residues. Binds to stalled 50S
CC       ribosomal subunits. {ECO:0000256|HAMAP-Rule:MF_00844}.
CC   -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00844}.
CC   -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00844}.
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:CCY78422.1}.
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DR   EMBL; CAYU010000107; CCY78422.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5LZJ1; -.
DR   Proteomes; UP000018300; Unassembled WGS sequence.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.50; -; 1.
DR   Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR   HAMAP; MF_00844_B; RqcH_B; 1.
DR   InterPro; IPR008532; NFACT_RNA-bd.
DR   InterPro; IPR043682; RqcH_bacterial.
DR   PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   PANTHER; PTHR15239:SF6; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   Pfam; PF05670; NFACT-R_1; 1.
DR   Pfam; PF18297; NFACT-R_2; 1.
DR   Pfam; PF05833; NFACT_N; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000018300};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00844};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00844}.
FT   DOMAIN          459..551
FT                   /note="NFACT RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05670"
SQ   SEQUENCE   578 AA;  65981 MW;  E52FD086B5080111 CRC64;
     MAFDGITIRS LIFELNNKIL NGRIDKIAQP EKDELLLTIK TPSGQQRLML SVNASLPLAY
     LVSSNKPSPL TAPNFCMLLR KHINNGRITE ISQPGLERII DFKIEHLNEL GDMCTKHLMV
     ELMGKHSNII FIDDNNKIID SIKRINASVS SVREVLPGFD YFIPNTTDKA DVLAMSEPEI
     TEAIKDKALP VSKILYQSFT GISPQVNNEI CDISGVEARK SVTGLYNNEL THFVRTFYNI
     LDTVKSNDFN PVIITNGKDK IYDVINYGTS ACDTVKYDSV SRMLEDYYKD KNISDRIRQR
     SADLRQIVST ALVRNYKKYD LQQKQLDDTS KRETYRIYGE LLNVYGYEIP KDAKSCEVLN
     YYTNENITIP LDPQLSALEN SKKYFAKYNK LKRTYEALSE LVLSTKAEID HLESINTALD
     IAVSYEDLGQ IREELIEYGF IKKNLSKKGK EKKVKCVPFH YISSDGFDIY VGKNNIQNEE
     LTFKFATGND WWFHAKNMPG SHVIVKCDKK ELPDKTYEEA AALAAYYSKG RTYEKVEVDY
     VERKQLKKVT GGAPGFVIYH TNYSMNISPD ISKIKEVK
//
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