ID A0A067MZ12_9AGAM Unreviewed; 863 AA.
AC A0A067MZ12;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=BOTBODRAFT_152526 {ECO:0000313|EMBL:KDQ19935.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ19935.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL198018; KDQ19935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067MZ12; -.
DR STRING; 930990.A0A067MZ12; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A0A067MZ12; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000027195; 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:UP000027195};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..312
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 863 AA; 95892 MW; 77E67B9780B29C37 CRC64;
MPSHSHSHSH SGRSRLLPFV SFGLFPVTIL VTVVYAIIFF VAIDSHESPA PYPPGLVKHD
LDLSAAWRDL KVIAEKPHPY NSHHNDVIRD YILSRVSDIA NAYPGKVQVI SDVHSNTTYV
DTYFVYYEGN NILVSVPGSK PDLPAVLFSA HFDSVSTAPG ATDAGMGLVS MIHLVEYFAK
NKHERTAIFN LNNGEEDWLN GAHAFFEHPL SKQVETFLNL EGAGSGGRPI LFRTSNARVA
RSFRDVDNPH GTSASSDVFK RGLIRSDTDY EVYTHRGLKG LDVAFYRARS RYHTKYDSVP
SLNGRASLWA MMDAARVSGN GLLNDLSTAG NEDPAVYFDI LGKAILIFER KTFLIINIVL
LILGPLIVGG VAYLTTKKEK YVWTGAGWGR TPVAYVTGGV VGGLLAALYT WINPFIVYSS
SYPVIISFVA AIYVTIYVVL HTLFYFRPVP YQRVQVNLEH SIIWWIALVV DTKLLHQDDV
TGLYIITILY FGSILAVIVS YLELLQTPHP DKPTNGDVEH SGDEVVDASE RTPLIASRAR
AADCIEEHPA AWYWIPEFIL SVPFPAMLLS QSILITLTAL SQTLSDGSDA DLVYYATCFL
AFMIVIPLGP YIQKTHVLVP LFLAFVFLGT FIYNLTAFPF SNESPLKVFF QQSINLDTGS
NLVYLTGVDG YLQSYDDNII IELPSAHGQT LDCGHDPKKK ELTRCSWEGL FPRVVPQHNL
VDATGDVDYS SWLKVEATRH GSNMASFTIR PQNTRNCRIY FDSPVDSLYV KGGNQEVQEG
YPVPEGGVKE ARLWSRTWDR EFELTVGWVN ATDAFTGRVA CEWAELDGGK IPALDEVLAF
LPNWAVVTKA SDGLVEGWKS FEI
//
