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Database: UniProt
Entry: A0A285MW86_9FLAO
LinkDB: A0A285MW86_9FLAO
Original site: A0A285MW86_9FLAO 
ID   A0A285MW86_9FLAO        Unreviewed;       926 AA.
AC   A0A285MW86;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:SNZ00076.1};
GN   ORFNames=SAMN06265377_1893 {ECO:0000313|EMBL:SNZ00076.1};
OS   Allomuricauda parva.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1247520 {ECO:0000313|EMBL:SNZ00076.1, ECO:0000313|Proteomes:UP000219048};
RN   [1] {ECO:0000313|Proteomes:UP000219048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25885 {ECO:0000313|Proteomes:UP000219048};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; OBEH01000002; SNZ00076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285MW86; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000219048; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          47..168
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          488..610
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          642..820
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   926 AA;  104424 MW;  EF44578945FAD3C2 CRC64;
     MKRFFIFISM ALFCVQTQRA QNFQFKASEI EIPYKHYNLP NGLTLLVHED HKAPIAAVNV
     WYHVGSKNEK PGKSGFAHLF EHLMFNGSEN YNKDYFQALE SIGGTDLNGT TNSDRTNYFQ
     NVPISALDQV LFLESDRMGH LLGAIDHAKL DEQRGVVQNE KRQGENQPYG NQWNYLTKSM
     YPKGHPYSWT VIGEMEDLNA ASLEDVHEWF KSYYGAANAV VAVAGDVNPD EVYKKVLKYF
     GDIPAGPTIE RQEVNIPERN FDTYQVYEDR VPETRVLFCW NTPQFGDKED IHFDLISAIL
     TSGKNSRLYK KFVYEDQTAS AAVSFQASSE IASRFITWLN VKPGQDADKL RNQFEDEIRR
     FLAEGPTEAE LTRVKAAYFS NFIKGLERIG GFGGVSDILA SNQTYFGDAS YYKTVLKYVE
     DATIDDLKKT ANKWLSKGKH VLVCNPFPEY SVQKSTVDRS KLPELGTQKS SKFPILEKAQ
     LSNGLNIVLA KRTGVPTVVV NLVVNAGYKT DYLSSPGTAQ LAMNLMDEGT KNLNSLQISE
     KSELLGVSLN TFSNQDQSNV FMTTLKQSFG TSLELFSDVV LNPIFPEAEF NRLKNEQINN
     IKNEKSQPVS MALRVMNKYL YGEDHPYSNP YTGTGYEATV GKLTRDDVVG YYNTWVKPNN
     STIIVTGDIE MDDLKSKLQK TLGKWKKGDV PTIAFNEPKS NSKNTLYLMN RPESQQSVII
     AGHLTEKYGG VSEVALEQMV SILGGDFTSR INMNLREDKH WSYGAGGFVL GSKEVRPFIV
     YAPVQTDKTS ESVSEIRKEI SEFISTRPAT QQELDKVKTN QVLSLPGQWE TNSSVNTSIR
     NMIRYDLPDD YYQTYDQDVR NLSLDDVRTV SKKVVKPEAV NWFMVGDRAK IASKLDELGF
     DNIIEIDADG NPIVPAVKEP EIELKN
//
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