ID A0A218Q7Y1_9CYAN Unreviewed; 575 AA.
AC A0A218Q7Y1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=NIES3585_40300 {ECO:0000313|EMBL:GAX37984.1};
OS Nodularia sp. NIES-3585.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=1973477 {ECO:0000313|EMBL:GAX37984.1, ECO:0000313|Proteomes:UP000198352};
RN [1] {ECO:0000313|EMBL:GAX37984.1, ECO:0000313|Proteomes:UP000198352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3585 {ECO:0000313|EMBL:GAX37984.1,
RC ECO:0000313|Proteomes:UP000198352};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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:GAX37984.1}.
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DR EMBL; BDUB01000001; GAX37984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218Q7Y1; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000198352; 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};
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 457..550
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 297..324
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 65725 MW; 073239AF66CE142C CRC64;
MQPVDYTTLT ASCSELRAHW LPSRLEQVYQ RDRYTIAVAL RTLKQRDWLE ISWHPQAARI
CIGEPPPRLP DTFTFSQQLV HQLGGLALVD IQAIAPWERV VDLQFARRPG EEALYHIYVE
VMGKYSNAIL TDASQMIITA AHQVGQHQSS VRPIQTGQPY ETPPKLTGPV PSLNESPERW
QERVSLVPGA IKRQLLKSYS GLSSALVESM IVAADLAPET TTDHLKPEDW QKLFARLQEW
LQALESSKFQ PAWTANGYTV MGWGAVAPEK DIQTLLNRYY TDELNQQVFA HLRHQLNQKL
QNILVKLRNK AQTFSERLQQ SDQADEYRAK ADLLMSNLQK WQPGMKEIIL PDFETNQPIA
IALQPDKNAV QNAQRLYKQH QKLKRARAAV EPLLFDVKSE ISYLEQVEAA IAQIENYQTV
EDLQALEEIR DELIGQKYLE DPGYRSRSAN ETAATNFHRY RTPNGFEVLI GRNNRQNDQL
SFRVAGDYDL WFHAQEIPGS HLLMRLEPGA VPEAADLQFV ANLAAYYSRA RQSEQVPIVY
TQPKHVYKPK GAKPGIAIYK QERILWGQPQ LVISH
//