ID A0A1D7XTL9_9FLAO Unreviewed; 828 AA.
AC A0A1D7XTL9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glutaminyl-tRNA synthetase {ECO:0000313|EMBL:AOR26673.1};
GN ORFNames=FORMA_15180 {ECO:0000313|EMBL:AOR26673.1};
OS Formosa sp. Hel3_A1_48.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR26673.1, ECO:0000313|Proteomes:UP000094318};
RN [1] {ECO:0000313|EMBL:AOR26673.1, ECO:0000313|Proteomes:UP000094318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR26673.1,
RC ECO:0000313|Proteomes:UP000094318};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP017259; AOR26673.1; -; Genomic_DNA.
DR RefSeq; WP_069675035.1; NZ_CP017259.1.
DR AlphaFoldDB; A0A1D7XTL9; -.
DR STRING; 1336795.FORMA_15180; -.
DR KEGG; foh:FORMA_15180; -.
DR PATRIC; fig|1336795.4.peg.1455; -.
DR OrthoDB; 9776599at2; -.
DR Proteomes; UP000094318; Chromosome.
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:AOR26673.1};
KW Ligase {ECO:0000313|EMBL:AOR26673.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094318};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..828
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009102234"
FT DOMAIN 48..96
FT /note="DUF5118"
FT /evidence="ECO:0000259|Pfam:PF17162"
FT DOMAIN 104..291
FT /note="DUF5117"
FT /evidence="ECO:0000259|Pfam:PF17148"
FT DOMAIN 426..734
FT /note="EcxA zinc-binding"
FT /evidence="ECO:0000259|Pfam:PF16313"
SQ SEQUENCE 828 AA; 94073 MW; 3553E14A759D31B6 CRC64;
MRFFKKISIL LLTVFLVHSC AISIKTTSSK KSKAPAVEKP KPKKGDLKPY DEIITEDAVS
DSGLFTVHKI DADFFYEIPD SLFDKEMLMV TRISKTASGI GFGGGKQNTQ VLRWQKKDKK
VLLRVVSYEV FAADSLPVHQ AVVNSNFEPV LYTFPVETIS KDSTATVINV TELFDKDVKA
LGLPSYRRKQ YKVSRLESNK SFIESIKSYP KNIEARHVKT YAASNAPSNS STGAISIEIN
NSMILLPENP MKRRYFDERV GWFTRGQVDY GLEDQRSREL TYLDRWRLEV KDEDIQKFKA
GELVEPKKQI VYYIDRATPK KWRKYIKQGI EDWQVAFEAA GFKNAIIAAD PPSIEEDPEW
SPEDVRYSVV RYLASPIPNA NGPHVSDPRT GEILESDINW YHNVMTLLRG WFFVQTAAIN
PDARGAEFED EVMGRLIRFV SAHEVGHTLG LPHNMGSSCA YKVEDLRSAS FTQKYGTAPS
IMDYARFNYV AQPEDKGVAL MPNIGVYDKY AIAWGYKPIL DKTAEEEKET LNGWITTHAG
DPMYRFGHQQ VGDVVDPSSQ TEDLGDDAVL ASTYGIKNLQ RIVPNLIEWT TKDGETYDDL
AQMYGQVLSQ FNRYMGHVAN NVGGVYEHYK TADQEGAVYT HVAKEKQAEA LAFLDKELFQ
TPAWLLDKSI FERIEYSGSV ERIRSLQERT LKNLLSLGKM ARLIENQTLN GSDAFLVSDL
TKTLRNSIWS ELKKGTEIDT YRRQLQRAHV ERLAYLMTAE NQSKRRGSDY IKSTAVNTNQ
SDIRAVVRAE LSTLKSMVRR GLNRTSNTMS RIHLKDILER IEAVLDPK
//
