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Database: UniProt
Entry: A0A0C9WUQ2_9AGAR
LinkDB: A0A0C9WUQ2_9AGAR
Original site: A0A0C9WUQ2_9AGAR 
ID   A0A0C9WUQ2_9AGAR        Unreviewed;       826 AA.
AC   A0A0C9WUQ2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=K443DRAFT_134254 {ECO:0000313|EMBL:KIJ96005.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIJ96005.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIJ96005.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIJ96005.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; KN838735; KIJ96005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9WUQ2; -.
DR   STRING; 1095629.A0A0C9WUQ2; -.
DR   HOGENOM; CLU_015120_0_0_1; -.
DR   OrthoDB; 277019at2759; -.
DR   Proteomes; UP000054477; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03875; M28_Fxna_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR048024; Fxna-like_M28_dom.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU361240};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT   TRANSMEM        341..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        383..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        420..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        499..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        538..557
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        564..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..316
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   826 AA;  90104 MW;  8F447DB17492071F CRC64;
     MGPTALTACI VARSHWCAVV GLQATSLSNP VTGLPQISEV RILDVVKNLS EDIGYRTVGT
     LEHALADKYM VAQAEEVKKN CEKLVAESGR KLECEVWRQE GSGSHRFDMM GKRLYKTYVN
     LTNIIVRVSD GTPEGKEHAV LVNSHLDSTL PSPGAADDAI SVGVMLECMR VLIETPTWSP
     KHAIIFLFNH AEECLQDGSH LYSTQHSTAP TVRAAINLEA AGTTGRELLF QATSEEMIKA
     YSQVPRPYGT TFANDIFSSG IILSDTDFRQ FETYLNVTGL DMAIIGNSYL YHMRKDLVEN
     IEIGVGQHMA ENALALLTYL SAPGSPLPSL NKGYSPVSTV YFAHIGGLFF MYTFTTAKIL
     YTFLFAASLI LRAGGFFQEQ RKGIIAVVAG AVGTMLVPNI VALVMRFVLK KGLSWFSNPF
     APMALYGPAA LLGELLGHLH EKTVFTSLLL MQSGLAILVQ LLKVGSAAMF FLSALPLFVV
     LLINPLFSGN TKTISLATYF LGQICPLLTG SLLTIPTIEV FVPLMGRVGA QAPADNMIAS
     LVSGLGAQSL PLVLPLAHRF GRRALLRGVL LLSMTTFVLM GIFAMRTPFD EMHQKRLFVL
     HLENITSQER HLHLAAADGA PGFELLVQDI VKDFGATDVA PTPVVMDDYN SDWDTLYPFS
     TFLTPYKVPL AMEPGYVSPW VKEQAFVVSA DNDVKDLVAG TRSLTIKVDH PGLIWTTIAF
     DAHVLKWSLD DSPPNEHARH HVKEASFYGT DTYTFDMVIK LTNDPGLSVN FIGVQEKGMW
     PGKKSVKAEG GLAMRLFEEL DSWLDVKTGG TVDALLMGCV AGSVIV
//
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