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Database: UniProt
Entry: A0A1H4CVS5_9FIRM
LinkDB: A0A1H4CVS5_9FIRM
Original site: A0A1H4CVS5_9FIRM 
ID   A0A1H4CVS5_9FIRM        Unreviewed;      1070 AA.
AC   A0A1H4CVS5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Zn-dependent peptidase, M16 (Insulinase) family {ECO:0000313|EMBL:SEA64491.1};
GN   ORFNames=SAMN05216349_12053 {ECO:0000313|EMBL:SEA64491.1};
OS   Oribacterium sp. KHPX15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=1855342 {ECO:0000313|EMBL:SEA64491.1, ECO:0000313|Proteomes:UP000199483};
RN   [1] {ECO:0000313|EMBL:SEA64491.1, ECO:0000313|Proteomes:UP000199483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHPX15 {ECO:0000313|EMBL:SEA64491.1,
RC   ECO:0000313|Proteomes:UP000199483};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNRG01000020; SEA64491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4CVS5; -.
DR   Proteomes; UP000199483; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199483}.
FT   DOMAIN          564..797
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
FT   REGION          41..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  121136 MW;  7C75BC993040C163 CRC64;
     MSIIHKIYKS QINHYTLKKI TGVILAASMV ITMAGCEATS VPEPNPIPES VSEETTAAGN
     KETVPGIEET TPDTEEVKRQ AVEQDENGYP YLSEEVDEEY QNDLFKEGNS YLDYKVERTG
     TVKALRADTA VLKHETSGAT LYLIRNDDKE LGFDISYRVP QLNNADIPHI FEHSILAASD
     KYPATDLFFD MSNTTYNTFT NAITYNTCTS YPFSTLSQGQ FIKLLDGYMS CMTSPKVLEN
     ENYFKREALR YQLYDIDDPI TLSGVVFSED MGGMTSGQDI SCYAVNESLY PDSIMSYANG
     RCYTDLENLN YSNLHEVYNS YYRFDNSLMI LYGDMDYKAV LEYLDREYLS KYPEKEEPVN
     IPEIVVPDGY VETEYDIPVY EDDTSGSQNS ITYAFDLSGF TPEEERELLV FTALMMDSSS
     VFMKALREEG LQWNTFSTLS PYNAWYPVYQ VMVYTQGEDI DKNVIKKIFD DSLLEVSENG
     FPKEIYDVVI KERELQDAFE REKVTFIDTL SEAIAVPWTR TGDPMVMETD EAAFEKLIQD
     PDQTRVKGLA KKLMEVDRKA LIYCKEKPGL AEKKEQEIED YLKNLKVDMS ESELLKLIED
     TRDFDEWNEE NVTNKNTVIN VSDLPEPMKY DTPEITNLGE CTVAAVPIEQ EDIYSVSLFY
     DTSTLKQEEL FDLVLYLNLL GNVSTTERSK EEFDRESNLN GSISTGLSGT DFKEPFDRLY
     LEVSLGGFTK DFSNNLSLME EMLTKSDYKM EEVQEIVQIL KNNSDPSNIS ANKAAVTLAR
     ALSGTSTGFE YYIMKGMHDY LTGIETALSE NDGAIEELAE RMKNIRDKIW HSDHMIMGIA
     ASPKGIAEIK SECGKLIDSM PSGTGDDYRE SYDYGIPDEK RVGIIVSSPL QSMCGGYILE
     DSEFKGRYLP FLEALNDRYI IPEMRYRNGA YGADVNYRIE KRVVSIGTSS DPNCKTTLEV
     LDEAPSALRE MSLTGEDIDT YTVSAFNNVI KPMGDISRAE SGIYTFFAGN DPDYLIKIAE
     DMKKATLEDR NGAADVMEKV VGDGYFVMAG NKAKLEEDKD CFDKVFSFSE
//
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