ID A0A0J0YFI8_9FLAO Unreviewed; 824 AA.
AC A0A0J0YFI8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Glutaminyl-tRNA synthetase {ECO:0000313|EMBL:KLT68914.1};
GN ORFNames=AB674_15205 {ECO:0000313|EMBL:KLT68914.1};
OS Flavobacterium sp. ABG.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423322 {ECO:0000313|EMBL:KLT68914.1, ECO:0000313|Proteomes:UP000036173};
RN [1] {ECO:0000313|EMBL:KLT68914.1, ECO:0000313|Proteomes:UP000036173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABG {ECO:0000313|EMBL:KLT68914.1,
RC ECO:0000313|Proteomes:UP000036173};
RA Gimbel A.B., Miller J.R., Newman J.D.;
RT "Flavobacterium sp. ABG.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KLT68914.1}.
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DR EMBL; LEKS01000014; KLT68914.1; -; Genomic_DNA.
DR RefSeq; WP_047777956.1; NZ_LEKS01000014.1.
DR AlphaFoldDB; A0A0J0YFI8; -.
DR STRING; 1423322.AB674_15205; -.
DR PATRIC; fig|1423322.9.peg.3224; -.
DR OrthoDB; 9776599at2; -.
DR Proteomes; UP000036173; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd04276; ZnMc_MMP_like_2; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR033413; DUF5117.
DR InterPro; IPR033428; DUF5118.
DR InterPro; IPR032534; EcxA_zinc-bd.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR034032; Zn_MMP-like_bac.
DR PANTHER; PTHR38478; PEPTIDASE M1A AND M12B; 1.
DR PANTHER; PTHR38478:SF1; ZINC DEPENDENT METALLOPROTEASE DOMAIN LIPOPROTEIN; 1.
DR Pfam; PF16313; DUF4953; 1.
DR Pfam; PF17148; DUF5117; 1.
DR Pfam; PF17162; DUF5118; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:KLT68914.1};
KW Ligase {ECO:0000313|EMBL:KLT68914.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..824
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005247126"
FT DOMAIN 48..95
FT /note="DUF5118"
FT /evidence="ECO:0000259|Pfam:PF17162"
FT DOMAIN 108..296
FT /note="DUF5117"
FT /evidence="ECO:0000259|Pfam:PF17148"
FT DOMAIN 430..733
FT /note="EcxA zinc-binding"
FT /evidence="ECO:0000259|Pfam:PF16313"
SQ SEQUENCE 824 AA; 93616 MW; 936D481CCAF5ADDF CRC64;
MKKFYIFAAT TVFLLFPVSQ FAQSKKEKSK KGEAAVAPPE KKPESTIKEY SKVITKDAVS
DEGLFTVHKV DKKYYFEIPN KYLNKDMLLV SRLSKLPSNL GGGYVNAGSE TNEQLVVWQR
FQDKILIKSK SYNSVANDSL PISISVKANN YNPTLFAFDI VSFSKDSANV VVDVTKFYST
DVKAISGISP EMREVYKVKG LDESRSFVNT MKSFPMNIEV VQDMTYNASK PSMLEETESI
SVQMNQSMIL LPEVPMKPRL ADPRVGWFTM SQYDYGSNEL KSDLKTYIRR WRMEPKDPEA
YARGELVEPV KPIVYYLDPA TPVKLRKYIK QGIEEWQKPF ETAGFKNAII AKDAPTKEED
PDFSPEDVRY SVIRYVASTT RNAVGPSVSD PRTGEIIESD VIWYHNHLRS YRNRYLLETG
AANPSARTLQ TSDEEMGEMM RMVIAHEVGH ALGFPHNMGA SCAYDTESYR NGDFTQENGI
AASIMDYARY NYIAQPGDKN IRFIRKMGAY DHYALNWGYR VIPNAKTTQD ELPTLDKWIV
EKAGNPVYKY GKQSSSFDPT SQTEDVGNNS MKASSYGLKN LEYVAAHLNE WTSNVTNNYD
DLDELYKELL DVWSRYVGHV VTNVGGVYEN TKNPNQSGNV YEVVPKAKQI EAMNWLQTNA
FASPTWIVNV TTLKNTDFAG YTERFRGIQV RQLNSLLSLG RIGRLMDNEI LGADTYKALD
LFKDIRKGIW KEAGTAANVT IYRRNLQRAF IDRMGFLMTE EIKPTDRSAT YYNVSQSDVR
ALVRGELSAL RKTLSVAKAT AVNTETKYHY EDCIKRIDLI LNPK
//
