ID K8ZL13_9ENTE Unreviewed; 564 AA.
AC K8ZL13;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, 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=C683_0599 {ECO:0000313|EMBL:EKU27268.1};
OS Catellicoccus marimammalium M35/04/3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Catellicoccus.
OX NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27268.1, ECO:0000313|Proteomes:UP000016057};
RN [1] {ECO:0000313|EMBL:EKU27268.1, ECO:0000313|Proteomes:UP000016057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27268.1,
RC ECO:0000313|Proteomes:UP000016057};
RX PubMed=23405330;
RA Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT Commonly Found in Gull Feces.";
RL Genome Announc. 1:E00019-12(2013).
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:EKU27268.1}.
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DR EMBL; AMYT01000017; EKU27268.1; -; Genomic_DNA.
DR AlphaFoldDB; K8ZL13; -.
DR STRING; 1234409.C683_0599; -.
DR PATRIC; fig|1234409.3.peg.549; -.
DR eggNOG; COG1293; Bacteria.
DR Proteomes; UP000016057; 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; 3.40.970.40; fibrinogen binding protein from staphylococcus aureus domain like; 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 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:UP000016057};
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 446..535
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 292..319
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 564 AA; 65313 MW; A3BA066A212D58F5 CRC64;
MKKMSFDGIF LHQVQQELQE LETGRITKVQ SPYENEIILT VRAKGKNHKL LLCTHAQYAR
IQCTTLPYLN QEQPSLFCMT LRKYIDGAFI EKIEQQGNDR VICLSLTRRD EIGDQKYYQL
ILEIMGRHSN LLLVEKETNK IIDCLKHVGI HQNSYRTLLP GAIYLSVPHQ DKKNPFQMTK
EEVFQFLHTE AHSAKEIQTA LQGIGKDTAH ELFLRLDEEK EKVMIWNQFF QELEKGTPTL
TTYEGKDYLL PMPYQSLPGE NEFFSSYSEL LDVYYGERVQ QARVQQQIGD IAHRLRHIVE
KNTLKIQKLE EQLSEANDAE QWRQYGELLT TYLHLVPKGA TEVSLPNYYN EEGKDAIIPL
DPAYSPNKNA QKYFQKYQKL KKSVKIVQQQ ITQTKEENQY LESILAQMEI ATPEDLPAIQ
EELYAQGFLK EKKHRRMKTK KSQPLQFHTS KGTPIYVGRN NLQNDELSLK KAQKNDYWLH
AKNIPGSHVI LKTSTPTDEE IVEAATLAAY YSKYQKAANV PVDYIQVKHL RKPNGAKPGF
VVYEGQKSTV VTPTKEKVEA LKDE
//