ID   A0A1Q3S2X4_9FLAO        Unreviewed;       543 AA.
AC   A0A1Q3S2X4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidase M1 {ECO:0000313|EMBL:OJV70731.1};
GN   ORFNames=BGO42_14550 {ECO:0000313|EMBL:OJV70731.1};
OS   Flavobacterium sp. 40-81.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1896169 {ECO:0000313|EMBL:OJV70731.1, ECO:0000313|Proteomes:UP000185767};
RN   [1] {ECO:0000313|EMBL:OJV70731.1, ECO:0000313|Proteomes:UP000185767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=40-81 {ECO:0000313|EMBL:OJV70731.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV70731.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MKTM01000022; OJV70731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3S2X4; -.
DR   STRING; 1896169.BGO42_14550; -.
DR   Proteomes; UP000185767; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
FT   DOMAIN          263..468
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   543 AA;  63075 MW;  DB8707D562E3C752 CRC64;
     MKNIILSAMV VLGMQQVSAQ LITEKETFTR RDSLHGGLRP ERTDYDVQRY DLNITINPGE
     RSITGYNDIT FKLIYNTNKI QVDLFENMKV DSIVFEKKKL DYIRDNDAVF IAFPNRLTRD
     STHKIRFYYS GKPTVAKNAP WDGGFVFSKD VQGKDWIAVA VQGTGASLWY PVKDSQTDEP
     DKGATIKVAV PNGLMNVSNG RFLGSEDLKN GYTRWDWEVI NPINNYDITV NIADYAHIHD
     NYKGLDLDYY VLRENESKAR KHFEEVKPMM DCFQSKFGKY PFWEDSYKLV ETPYLGMEHQ
     SAVAYGNKYR KGYLGHDNSG TGIGMTFDFI TIHESGHEWF GNSITSKDIA DMWIHEAFTT
     YTEAVFVECT LGYDKALAYV NGQSRNVRND RPIIGFYGVN KEGSGDMYYK GSLLLNTIRH
     IINNDAKWWK LLLDYSETYK KQIIDTETVI AFFNKETGMN LTPLFDQYLR YKDIPALELR
     TENQKVEYRW KTNVTDFQMP IEYSYNGKTS RVNVTNEWQQ FDKKTDLNKL KFNTQKMYYT
     VVK
//