ID   Q6BZ22_DEBHA            Unreviewed;      1102 AA.
AC   Q6BZ22;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 102.
DE   SubName: Full=DEHA2A05192p {ECO:0000313|EMBL:CAG84502.2};
GN   OrderedLocusNames=DEHA2A05192g {ECO:0000313|EMBL:CAG84502.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG84502.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG84502.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CR382133; CAG84502.2; -; Genomic_DNA.
DR   RefSeq; XP_456547.2; XM_456547.1.
DR   AlphaFoldDB; Q6BZ22; -.
DR   STRING; 284592.Q6BZ22; -.
DR   MEROPS; M16.008; -.
DR   GeneID; 2899926; -.
DR   KEGG; dha:DEHA2A05192g; -.
DR   VEuPathDB; FungiDB:DEHA2A05192g; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; Q6BZ22; -.
DR   OMA; WIFDEMK; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
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:UP000000599};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          68..205
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          232..409
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          418..702
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          731..900
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1102 AA;  127359 MW;  B0548681666E9268 CRC64;
     MYSAKGLSRI INYKSGFNLQ QVFYSSISKL RMQSDKYTVL ADNSNVEKPI LDDRSYRLIK
     LNSNDLHVLI INDASTDKAA ASLDVNVGSF ADKNYQVPGL AHFCEHLLFM GTSKYPEENE
     YSSYLSKHSG HSNAYTAAEH TNYYFELSSD YLEGALDRFS QFFISPLFSK SCKDREIKAV
     DSENKKNLQN DMWRFYQLDK STSNPQHPYN GFSTGNYETL HEEPTSQGLN VRDILLDFYK
     NHYSSNLMSL VILGKEDLDT LTSWAIDKFS EVPNSNLPRP NYDGELIYNP DHLGKIIKAK
     PIMDSNKLEL SFMVPSDQEA NWDSKPASYY SHLLGHESSG SILHYLKQKG WVNELSAGNM
     KVCQGNSIFV LEFDLTPNGL KNWEAIVVNV FEYLKLVLNG EPKLWLWEEL SNMSTINFKF
     KQKQRAAQTV SKMSNSLYKF TEGSYIPPQY LLSSSILREF KSQEIKEYGS FLNPDNFRIL
     LTSQSLPDLD KSEHWYGTQY SYESISNNLK DQIESAETNE NFHYPIPNKF IPKDFTVSKP
     KSENPLPHPY LIEDNNKFQV WYKQDDQFQI PKGAIEIVLH LANANTSCKS SIYTMLLSQL
     IDDELNEIVY YASMVGISFT INHWRDGLLI RVSGYNDKLP VLLEQILQKL ITFKPKEDRF
     EVFKFKLNQE FKNFGFEVPY SQIGTHFLTL LNDKTYPYDL KIDTLNKEIN FGELLEFSTN
     KIWEQGVFGE VLIQGNFNDT KAFEISRAIQ GHFTEFKTIR DSQEEINEIV KLKTHIVPSN
     QRIRYEVALQ DKNNINSCIE YFIQISDSFD DVRLRVLTDL LGTVIHEPCF NQLRTKEQLG
     YVVFSGTRLT RTTLGFRILI QSERSSEYLE YRIEEFINQF DKFVKKGLTD ENFAKFKQAL
     KDKKLTKLKN LSEEVSKFWN SIISGYYDFQ EREKHVEVLE SITKDEFIKF YNDYISADSN
     VSSRIIVHLK SPSVPKLEKS KLLHSSINNY IYRNEFSISS DVLDSLIEAN ADDVAKLVEV
     LTNAIAEKKE NNVSNKDRLK SDLSETINRE LTTPVPPQYP SGKLVENVDQ FKSTYPVGDI
     PRPVEPLSNF YYSKQPEDHA HL
//