ID   Q6CPG4_KLULA            Unreviewed;      1004 AA.
AC   Q6CPG4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   SubName: Full=KLLA0E05105p {ECO:0000313|EMBL:CAG99262.1};
GN   ORFNames=KLLA0_E05105g {ECO:0000313|EMBL:CAG99262.1};
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG99262.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAG99262.1, ECO:0000313|Proteomes:UP000000598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37 {ECO:0000313|Proteomes:UP000000598};
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; CR382125; CAG99262.1; -; Genomic_DNA.
DR   RefSeq; XP_454175.1; XM_454175.1.
DR   AlphaFoldDB; Q6CPG4; -.
DR   STRING; 284590.Q6CPG4; -.
DR   MEROPS; M16.008; -.
DR   PaxDb; 284590-Q6CPG4; -.
DR   GeneID; 2893763; -.
DR   KEGG; kla:KLLA0_E05105g; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; Q6CPG4; -.
DR   OMA; WIFDEMK; -.
DR   Proteomes; UP000000598; Chromosome E.
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:UP000000598};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          74..207
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          236..414
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          420..700
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          704..886
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1004 AA;  115802 MW;  7F855E64E371B5A9 CRC64;
     MLAAVQGILS QPTSLLASKI SVSCLLTSRY RFLHYNTKMS NKYRTLGTDS EFLKPDLDDR
     KYRYIQLPNN LKALLISDAE ADKAAAALDV NIGSFQDPEH LPGLAHFCEH LLFMGNEKYP
     DENDYSSFLS KHGGSSNAYT GSQNTNYYFH LNHENLYPAL DRFSGFFSCP LFNKASTDKE
     INAVDSENKK NLQNDIWRMY QLDKSLTNWE HPYHKFSTGN IKTLGDIPKL KGIDIRNELL
     DFHKNNYSAN LMKLCVLGRE DLDTLADWVY ELFKDVPNLN KQVPYYPARL YTESQLKKMV
     YCKPVKDLKK IEFTFPTPDM DPYWESKPNH YLSHLIGHEG NGSLLAFLKE KGWAVELSAG
     SHTISKDNAV FGIEIDLTDD GMNHVNEIII STFQYLEMLK VTLPEEWIHN ELKSTSVSSF
     KFKQKDPPSS TVSNMARCLE KEYIPVVDIL STSLIREYNP SMIKKYVQSL NWENSRIMLT
     GQNLPVDCKE QWYGTEYKVT DYPESLLKKL PNVGLNPKFH LPRPNEFICT KFEVNKLDNV
     KPLDEPFLLK DDHYSKLWYK KDDRFWVPKG HIYVSMKLPH TFSSVVNSML TSLYVDMIKD
     ALVDLQYDAS CADLRITLGK TNQGIDIQAS GYNEKLTILL TRFLEGIKSF QPKESRFNVI
     KNRLLQKLSN QQYDVPYNQI SNVFNSLVNE RSWTTKAKLD VTKDLTFEHL KSFVPTIYEQ
     LFHESLVLGN FSVEMAYEIN QLVDILVVDR IPNLEVKNNK LRSYILPEES AFRYEYMLED
     KANVNSCIQY LIQLGAYSEE LAAKASLVSQ LIHEPCFDTL RTKEQLGYIV FSAVANTHGT
     TNLRVLVQSE RDSAYVESRI VKFLNSFGEA LKEMPEEAFE KHKSGLIKNL LQKLTNLRQE
     YDRFTTAIYL ADYNFCSYQR RADIITKLSK EDMVEFYKNF VLSPRSSRLA IHLKSQIEKK
     STEEVVEGFP TGTLISDIDE FKSNLFLAPV RQAVKQYEPT NARL
//