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Database: UniProt
Entry: A0A448YNQ1_BRENA
LinkDB: A0A448YNQ1_BRENA
Original site: A0A448YNQ1_BRENA 
ID   A0A448YNQ1_BRENA        Unreviewed;      1175 AA.
AC   A0A448YNQ1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=DEKNAAC103637 {ECO:0000313|EMBL:VEU22574.1};
GN   ORFNames=BRENAR_LOCUS3305 {ECO:0000313|EMBL:VEU22574.1};
OS   Brettanomyces naardenensis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU22574.1, ECO:0000313|Proteomes:UP000290900};
RN   [1] {ECO:0000313|EMBL:VEU22574.1, ECO:0000313|Proteomes:UP000290900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tiukova I., Dainat J.;
RL   Submitted (DEC-2018) 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; CAACVR010000023; VEU22574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448YNQ1; -.
DR   STRING; 13370.A0A448YNQ1; -.
DR   InParanoid; A0A448YNQ1; -.
DR   Proteomes; UP000290900; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000290900};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          32..157
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          545..764
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
SQ   SEQUENCE   1175 AA;  131256 MW;  E1C3345FA9A6EBF5 CRC64;
     MSYTFPNRFP VPCSAKGRSY KFIKLENGIR CLIISDPTED VASMSLSVAT GHHADPSAVP
     GLAHLCEHMV CVSSKEYPQV DLYKTMVHEV GGSWNAVTVN EKTSFFFRIP LIASSDDLDQ
     ESSFSKIIKV FASYFKHPLF DSNYADREVV AVDNENAKNC SLTSRISFHG LRLLANPNCQ
     FHRFSTGNYE TLHGISSTVS IKATLKAFFK AEYLPERMAV VLKGPQTLNY LQRVATSAFS
     SIGDQKKTGL SLFRKHTEIT SPHPREDLLQ SQVAADVWLR RYKTVTFPSR GGRFILIHKK
     GSGDTILRLF FPINLQSISF SAKQLEIFQS FWCHILGSES FGSLNSKYIS SQYVTELIAK
     VATISSSTNA LELQLALSRE GARNLDKVIR LFFDFTSLFS GDDPKFKRKL AKAFSQFNGI
     ELYNFYYAEA GAGGTDEIRA FSERLLSPLE VFGQWFFRGS PCFDSTDKGF AGSFHESESF
     WIREANKFIS FVNDIVSPDN LLFSYVGDTE LVGESLGSEN LPSFKDANFK FSYKMGRLAM
     SSHSGCSTAF SIPPPNAFAP SITDEQCNLL DMFKAIEESS LEAGLGYSVK NISAISLPQL
     AFSDDGTQFW IKKESDPIYM DKLFLSVELT SLVDRGKTTC SHVIVLELLC DLVKVKLRET
     LYPALVMGYS YDIFPSLKGD TGIVIHIAGP KSRILNVFSL IVYEAKAVSS DFKINVTPTE
     FRNSRIRIQK KYSAGQSLPS HSLVSLGLMA VMEENTWLLD TRMEALEDLN FATADSICSH
     LFDVCYSTFL IHGDVDDIMA SRYGVLDCLN SLVKEFKGQN DCFVPSTIHL PQNCNYIAKD
     TCKDPTNALA YFLQTSPRSD TPSRAITRLL AFILSNSLLS KLRIQYQLGY VVLVGSRVFR
     KVEGIHITIM SGQMGPEALE AKVEEIIMEW YEEFVKDLDE TKFKSLYVNK FLAAYSSINQ
     KMNTAGRAPS LTQGSLISGM SGSALAKQHQ GYWDQIVNRS YRFSQNLTGE DTIDVSVIEQ
     LRLDDFLSFI KARILPNSGS RIKVSAMLTT ERSREDVEQM LTPVRIYFFL SSVGLPIKKD
     ALVDILKTSG DSKIALCKNL LKYYRSQGKA LRLISAGLAK MSLAVLPGPG NLSVDFHRHS
     EPVHIDPVHL QEWQRGIGFI HGESLSVTLS RFSGR
//
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