ID A0A0C3BJG1_HEBCY Unreviewed; 888 AA.
AC A0A0C3BJG1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=M413DRAFT_448810 {ECO:0000313|EMBL:KIM36870.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM36870.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM36870.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
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 -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000256|ARBA:ARBA00003273}.
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}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|ARBA:ARBA00010918, ECO:0000256|RuleBase:RU361240}.
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DR EMBL; KN831801; KIM36870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3BJG1; -.
DR STRING; 686832.A0A0C3BJG1; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000053424; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar 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; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF56; VACUOLAR MEMBRANE PROTEASE; 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:UP000053424};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..290
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 508..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97490 MW; 733F67A3207F1D58 CRC64;
MLRFTQASTS AFLIAVYAAV FTVVLVSNST PKIPGDTLGL DLSEAYYDLH QIATRPHPFN
SHANDVAREY ILARLNNITY SFDHITVEDD LTSAATWVSK SHAVSFEGSN VLVKVEGTDP
EFSKSGGVLF SAHFDSVPTA PGVTDDGIGV ATLLAFVKYL TTHRTRRTAI FNINNGEEDG
VNGAHVFLQH PWSRIPDTFL NLEGAAAGGR PLLFRATSTA PVLSFKNKDV FHPHGNVLSA
DAFSRGVINS GTDFTVYNHA REDGPGMEGV DFAFYQGRSK YHTKYDSIPG ARGAKRSLWT
MMETVRGAGM ALLNEDRTHV GSDEPLAPVY FDLFGLVFVV LTQRSLFLFN VFLLIAGPII
IAFLRITYSE RSPAKIADKW GKFWASFVVG LALQFTLALS FIKINPFIVY SHPYLVLGST
LSLAYLTTTF IMNAKSDVSF ADGQKSHMLL QMYIFTWVLL VAATIGLKLL NLGGIYVFSA
WNAFACLGCA VGIIENISPA ARISFTDKDA RSRSPTSNPS EITETSPLVE KSTGPVLPSQ
IIDERPSFAW GIIQLLLVVP IPITLLSHIL LLLVDSLSQT LSDGNNPVIV YGAMGIMSFL
IVIPMSPFTL KIHPWITSLL ALVFVVMTMH NLVAFPFSQD VPLKVYFKQK VLVDIANPDH
GPIQTLTTLV GATQYLEDYI VSELPSSWKS SVLCQGYHSS PRLSICSWES SLSPSPIKSD
STERRTDTWL EATTSRLTPT SALISVKGTN TRVCRLYFDN RRIRSYRVYD VGAHGALVPS
TASTSQSAFP IPKEGLDWMW LWSREWDKTF VVEVAWDADE VHANVTNGLS GRVGCEWAEY
ESATLGLVTM PLTGAIPAYE EVLDYLPSWA VSSKVSGGLV EVFGHFTV
//
