ID   A0A3F3QJL1_9EURO        Unreviewed;      1037 AA.
AC   A0A3F3QJL1;
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=Metalloenzyme, LuxS/M16 peptidase-like protein {ECO:0000313|EMBL:RDH39325.1};
GN   ORFNames=BDQ94DRAFT_156135 {ECO:0000313|EMBL:RDH39325.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH39325.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH39325.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH39325.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-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; KZ852032; RDH39325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QJL1; -.
DR   STRING; 1341132.A0A3F3QJL1; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000253729; 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; IPR007863; Peptidase_M16_C.
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; PF05193; Peptidase_M16_C; 2.
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:UP000253729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          38..196
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          225..400
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          410..694
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          703..881
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1037 AA;  118077 MW;  07339D344BA7E7C3 CRC64;
     MGEALPFGSI KLISDRMEKP LLDNRSYRVI QLSNQLEVLL IHDPDTDKAA AAMDVNVGSF
     SDPDDLPGTA HAVEHLCFMG TKKYPAESEY STYLAKHGGY SNAYTASTST NYFFELSASS
     TSNSPGSVAT VEQSNVTITK DKVPLYGALD RFSQFFIQPL FLPDTLDREL RAVHSENKKN
     LQSDTWRLEQ LGRSTSSEKH PIRKFATGNY QCLHEEPVSR GIDIRKRFIE FHEAHYSANR
     MKLVVLGREA LQELESWVQE LFSDVPNKNL HRLRWDNIPV LNESELMTQI FVKPVTEQRQ
     LNIDFTYPDE EELVDSHPSQ YLAHLIGHGG PGSALAYLKE LGLADSLSAG ASALCPGTAL
     FCIDVMLTEK GVRQYRDVLR VVFQYIAMLR ENPPSAWISD EMSRLAEVDF KFRQKSPPSR
     TVSDLAQLMQ NACIPREHLL SPFLIRKFDP ESIQSGLSHL LPDNFRFFLV DQQFPGNWDA
     KEKWYGTEYK LEKIPKEFMK ELWKAAQAPI TESPSILHLP AVNEFIPRRL DVDRKDVTEP
     ARHPTLVRHD DHVRVWFKQD DRFWVPKANI KILLRSPIVS ITPMYAVMTR LYVELVEDSL
     IEYAYNADKA GLSYAISESS QGLNIELKGF NDKMSMLLEK VLLAVRDLKI KQEQFDVAKD
     RVWKAYKNFD YMEPYRQINA FSRMLINERS WTPFLLVEEL PAVTAEDINS YYPHLLRQMH
     IEILVHGNLN KEDALNLIGL VESTLRPRRL PESQWLSRRT IALPSGANYL YERGLRNPDN
     VNNCLEYIIS VGSVSDRSQR AKLLLFSQIA EVPCFSTLRT KEQLGYIVNS AIGVYVTTGT
     WRILVQSERD CKHLEERCDA FLVNFEHYLR AMTDETFEEH KVGLINKRLE NLKNLNQETS
     RFWTHITSEA LDFEQVYHDV EHIEPLTKED ILQFFDQHIH PSSPTRAKLA IHLIAQASAT
     AEAASGDSAV AVGNPDALAL PETQDAVAAN AYEPSVSPAI IPIKIDNVRT WKASLPLSPA
     ATPVKGLAKF KEFNSKT
//