ID A0A1Y2EKM0_9PEZI Unreviewed; 982 AA.
AC A0A1Y2EKM0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=BCR38DRAFT_479891 {ECO:0000313|EMBL:ORY71395.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY71395.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY71395.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY71395.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY71395.1}.
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DR EMBL; MCFJ01000001; ORY71395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2EKM0; -.
DR STRING; 1141098.A0A1Y2EKM0; -.
DR InParanoid; A0A1Y2EKM0; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000193689; 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|ARBA:ARBA00022723,
KW 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:UP000193689};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..344
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 109639 MW; 01ADA5150F9EF0CF CRC64;
MAVPNPVAFK PFSVTFWTTV IYLALLIPLI IVHETVPSPP HSPTLYSGIN LTDAWSDLAT
LTRAYHPYNS RNNDDVRNWL LFRIGEIVKR NEVDASQVVI FNDTITNVTL THPARLPKTE
QYPGRHPEGA GTYFEGNNIM VYIRGKDDPQ RDWWFDIDGY IRADKVIGKG GVLVNAHFDS
VSSGYGATDD GMGVITILQL INYFTAPGNQ PQRGIVALLN NNEEDGLHGA RVFGYSSLMP
FCHTFLNLEG AGAGGRANLF RATDLEVINA YKGTEHPFGT VMSSDAWSTK AIRSGTDYEV
FKDVYGMRGM DVAFYRPRAR YHTNQDDIRH ASRASLWHML SSSLHTVKGL SGDTGSTFIG
NRRDRNPRKV SNGAGTDGVW FDIFGKGFAM FGLRPMFAWS LTLLIVSPLI LILFTYVLVK
RDKYYFFSSR KSPYEGSVLD SVVLGGRKGM FRFLLAFVVS VALVVGSAYL LRKINPLVIY
SHEYTVWSMM MSLFYFAFWS IMASANFARP SALHRGYVIL WLFIITWALL VVTTVYEDRF
RVAAGYVFVF LHSAVFLSAV ITVCEQFALP TKTAFAQKAH DEHQAHDHMD AVPHADDLIE
HSSMGGGAND VGDDEGNSDE ASETSPLVGG NSRDSTGTTF GTIYRRSISA IKDKSKATED
QRHESFGYEQ EWSKKLPSWV WFLQFLLLGP FLLILFGQAG LELVASVNQT GADGSSLLLP
YLLVAFFTIM TLLPLTPFVH RITHHIPVLL LVVFVATLIY NLVVFPFSAE SRYKVYFRQT
IDLDSGVSTI KYTGIDEYVR QAIAELPSAL GKNVTCESSN PEQAYFVACS YDGSKVSPAV
ARGNYTDWIA LNITRPKAPN QARFKINALE TRTCGLRFNK AISSFQVVGG NSQDDRFGDW
PEGGVKSILL YRREWDKPFT VDVEWDARNA ESGLRGLVYC DWDDATKGKI PAYDEGLQYA
PDWVALTKES WGLLHGSKAF KV
//
