ID A0A0N8KP84_9CYAN Unreviewed; 584 AA.
AC A0A0N8KP84;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=HLUCCO16_11990 {ECO:0000313|EMBL:KPQ38626.1};
OS Phormidium sp. OSCR.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ38626.1, ECO:0000313|Proteomes:UP000050461};
RN [1] {ECO:0000313|EMBL:KPQ38626.1, ECO:0000313|Proteomes:UP000050461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSCR {ECO:0000313|EMBL:KPQ38626.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ38626.1}.
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DR EMBL; LJZT01000045; KPQ38626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KP84; -.
DR STRING; 1666905.HLUCCO16_11990; -.
DR PATRIC; fig|1666905.3.peg.2095; -.
DR Proteomes; UP000050461; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844};
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 455..548
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 584 AA; 66721 MW; 15F63714CCE16A62 CRC64;
MQPVDFTTLC AIYADFRTSW LPARLEQVIQ SDRTQLALAL RTLDRRGWLR LCWHRQAAHL
CLSSPPPKVP DTFTFSDQLR HQLKGLALVD VSPLSPWERV LDFQFARRPG DPLQGHLYVE
IMGKYSNVIL TNAENLIITA AHQVSAQQSR LRPILTGQPY EPPPAMTGAT PRLDESFERW
QERISLIPNA LRRNLLTPYR GLSSALVRSL CARANLDPET PTDQLSDADW QRLFASWQEW
LTILETQNFQ PGWTESGYSV LGWDAHTPVD DVQGLIDRYY RDRLNQQLFQ QLRHQLSQKL
SQTLKKLQTK RQTFLDKLQQ SHDADQQRQQ ADLLMAHLQD WTPGLNEITL ADFETGDPIT
IPLDPEKNAV SNAQALYKQH QKLKRAKQAV QPLLSATEAE ISYLQQVEAA LDQLGPYQQP
DDLSALEDIR DELVEQDYLS SPQHRPQRES APDPFHHFQT PSGLEILVGR NNRQNDQLSF
RIATEYDLWF HTQEIPGSHV LLRLPPGTHP DPKDLQFAAD IAAYYSRARD SDAAPVVYAE
PKYVYKPKGA KPGMAIYKHE TVLWGNPGQV ERQLESRGRG PASR
//
