ID C7HU48_9FIRM Unreviewed; 582 AA.
AC C7HU48;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=FbpA {ECO:0000313|EMBL:EEU12828.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN ORFNames=HMPREF0078_0799 {ECO:0000313|EMBL:EEU12828.1};
OS Anaerococcus vaginalis ATCC 51170.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=655811 {ECO:0000313|EMBL:EEU12828.1, ECO:0000313|Proteomes:UP000003821};
RN [1] {ECO:0000313|EMBL:EEU12828.1, ECO:0000313|Proteomes:UP000003821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51170 {ECO:0000313|EMBL:EEU12828.1,
RC ECO:0000313|Proteomes:UP000003821};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RL Submitted (AUG-2009) 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:EEU12828.1}.
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DR EMBL; ACXU01000011; EEU12828.1; -; Genomic_DNA.
DR RefSeq; WP_004838828.1; NZ_GG700527.1.
DR AlphaFoldDB; C7HU48; -.
DR GeneID; 79022070; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000003821; 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; 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; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT 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 Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000003821};
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 461..557
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 308..335
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 582 AA; 67664 MW; 53E6367932AB2565 CRC64;
MSYDGLVTKA ITFEIKKLLL GGKIQKISQP SKNDIVLNIY SVGKSYKLLL SANNNEARVH
ITEKKYENPI SPPNFCMVLR KYLNQSKIVE IEQYKMDRVI IFHISSVDEM GFDISNKLIV
EIMGKYSNII LTDENYKIID SIKRVNFKMS SVREILPSLE YKFIESNKIN ILESDFSLDI
LKLDKNIADN QNPEKLLYEN YLGFSPTISK ELIYKSNIDP RINWGLVSED EKQLLNDNLY
ELRNSLINNT YSPVLYKNSR KYKEFYSFDL SGLGFEKILC NSMSNAIENF YESNKSNDRL
RQIKNNLLRK INSQIKLVNK KIDILNKNLS KEKNMDSIRM KGDLLAANVN KLNKGYKEII
LKDFYNNNKD IKISLDSRKN PWENVDSYYK RYKKIKNSID FAKDDLPKQN DLLEYLNQVS
DFVERSESIS DLDEIKEELI ENKIIKNTSR NKKKTKAKSK PMQFKTVDNS NIYVGKNSRQ
NDYITLKLAN KNDYFFHVRN APGSHVILKT NLLNENDIKI ASYLAASNSS QAKSNKVDVD
YTEKKNVNKA KGAKPGMVYY ENFKTVTVNM DENPKNLYEK IK
//
