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Database: UniProt
Entry: A0A3E1NNV6_9BACT
LinkDB: A0A3E1NNV6_9BACT
Original site: A0A3E1NNV6_9BACT 
ID   A0A3E1NNV6_9BACT        Unreviewed;       847 AA.
AC   A0A3E1NNV6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=DUF5117 domain-containing protein {ECO:0000313|EMBL:RFM29603.1};
GN   ORFNames=DXN05_01055 {ECO:0000313|EMBL:RFM29603.1};
OS   Deminuibacter soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Deminuibacter.
OX   NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM29603.1, ECO:0000313|Proteomes:UP000261284};
RN   [1] {ECO:0000313|EMBL:RFM29603.1, ECO:0000313|Proteomes:UP000261284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM29603.1,
RC   ECO:0000313|Proteomes:UP000261284};
RA   Wang C.;
RT   "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT   soil.";
RL   Submitted (AUG-2018) 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:RFM29603.1}.
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DR   EMBL; QTJU01000001; RFM29603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1NNV6; -.
DR   OrthoDB; 9776599at2; -.
DR   Proteomes; UP000261284; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000261284};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..847
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017757990"
FT   DOMAIN          47..96
FT                   /note="DUF5118"
FT                   /evidence="ECO:0000259|Pfam:PF17162"
FT   DOMAIN          105..306
FT                   /note="DUF5117"
FT                   /evidence="ECO:0000259|Pfam:PF17148"
FT   DOMAIN          437..747
FT                   /note="EcxA zinc-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16313"
FT   REGION          22..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  94293 MW;  20F77BA16AE3038F CRC64;
     MKHVVLSCAL AATVFSSLHA QRHKPVNPAP AKDTTHLPPV PAPRQGPKPY KDVVTAKAVT
     HKGLFTVHQV DDKWYFELPD SMFNRDIMAI TRYSKTPGGG GVYGGELVNQ QTIEWEKGPA
     NTVFMRVITL VNMADSTSSI YKAVTNSNLN PIAAAFDIKA VSADSAGVVI DVTDFFKGDN
     QAVSLSPNAK RRLNVSALSS DRSYIDYIHT YPINTEVKTV KTFSATASAG FSLFGPSQPP
     LPAASAIGAI TMELNTSFIL LPKQPMQRRF ADARVGFFAD DYTVYGDDQQ KVQNQVFIVR
     WRLEPKPEDV ARWEKGELVE PQKPIVYYID PATPKQWRKY LVQGVNDWQQ AFEKAGFKNA
     VMAKEWPDSA GMSTEDARFS MIRYFASDIE NAYGPNVHDP RSGEIIESHI GWYHNVMKLV
     HDWYMIQAAA VDPAARKMKF DDELMGQLIR FVSSHEIGHT LGLRHNWGSS STIPVEMLRN
     KAWLDVHGHT PSIMDYARFN YVAQPEDHIP QADLFPHIGE YDRWAIQWGY TSTHTATPEA
     DRKIVNRWIV DSLAANPRLW FGAETHPTDA RSQNEDLGDD AMKASAYGIK NLQRILAQLP
     VWTSEEADTY TNLKDMYTQL TGQFSRYMGH VLKNVGGINE TPKSVEQGGN VYEPTPKAKQ
     KEAVAFLNKQ LFETPFWLLD KNVLNKFSNP ADAERVAAIQ TNTLKGLLSA ARINSMLTGS
     ERFGVAQTYT AAEMLDDAKK GVWSELSSKK PVEMYRRNLQ KAYIAALVEL AKTDADNSDF
     VIVLGRSGAA GSNTNAASSD ASSLARAQLA ALRTEINAAM PGFTDKMTRY HLQDIADRIK
     KALDPSH
//
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