ID U9VH96_9CYAN Unreviewed; 583 AA.
AC U9VH96;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=N836_28150 {ECO:0000313|EMBL:ESA32029.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA32029.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA32029.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA32029.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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:ESA32029.1}.
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DR EMBL; AWNH01000117; ESA32029.1; -; Genomic_DNA.
DR RefSeq; WP_023077056.1; NZ_AWNH01000117.1.
DR AlphaFoldDB; U9VH96; -.
DR STRING; 1385935.N836_28150; -.
DR PATRIC; fig|1385935.3.peg.7378; -.
DR eggNOG; COG1293; Bacteria.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000017515; 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; 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:UP000017515};
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 458..552
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 583 AA; 66853 MW; CBB4232BC9540A5A CRC64;
MQPVDITTFR AVCHELTAEW LPARCEQVVQ QDRNTICLAL RTFDRRGWLT ISWHPQAARI
HIGAAPPKRP DTFTFSQQLK HQFSGLALTK ISFLAPWERA VDLQFARRPD ESAEWHLYVE
IMGRYSNVLL TNAQQEIVTA AHQVNEQQSS VRTIRTGGQY RPPPAIVGTL PRLDEPFVDW
QERISLVPGK LSKMMVKSYS GLSTALAKQL IDVAGLDSNQ ITDSLTGDDW QQLYVQWQRW
LQCLEKNDFQ PAYTANGYAV LGWAGEPATG SIQQLLNNYY TSHLNQQIFS QLHHQLIQKT
KTLTGKLRQK AANFYRRLDD SDQAEHYRIQ ADLLMAYLHE WRPGMSSIQL QDFESGQPVT
LALNPEKNAV QNAQALYKRH QKLKRTRDAV MPLLEQVETE LHYLEQVESA LSQTAEYTNA
DDLMALEEIR DELVQQGYLD DPYQRQDKQR SRDRLPNFYR FQTPSGTEVW VGRNNNQNEA
LSFRAANDYD LWLHTQEIPG SHVLLRLEPG AKASDDDLAF AANMAAWFSR ARQSEQVPVV
YTKPKHVYKP KGARPGMVIY KHEQVLWGQP QQAKAYLAAV GDQ
//