ID A0A0S7E0R2_9EURO Unreviewed; 963 AA.
AC A0A0S7E0R2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=ALT_002827 {ECO:0000313|EMBL:GIM43211.1}, CNMCM8060_005125
GN {ECO:0000313|EMBL:KAF4183098.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM43211.1};
RN [1] {ECO:0000313|EMBL:GIM43211.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM43211.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4183098.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4183098.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4183098.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4183098.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:GIM43211.1}.
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DR EMBL; BCLY01000016; GIM43211.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000002; KAF4183098.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7E0R2; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_8725; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000713487; 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 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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..339
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 579..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 106551 MW; D53EEF1119EB1B77 CRC64;
MARPSLSRSN PLGFTPWPVT VITAVVYLAL VVPLLVLHHV VPSAPSSSPN GLNLTEAWTD
LQVLTKGFHP YNSHRNDEVH EWLLKRIHEL IDSAPPASEY ESVDEEKPDT FVFDDTQSNL
TFSGRGSGLG VYFESTNIMV YIRGWEEDKE RWWEDPHGRP AGKGGVLVNA HYDSVSTGYG
ATDDGVGVVS CLQLIKYFTT PGHVPRRGLV VLFNNGEEDF LNGARVYSQH PISQLPHTFL
NLEGAGAGGR ATLFRSSDAE VTKPYMRAPH PFGSVLSANG FEAGLISSQT DYVVFEGDLG
LRGLDVAFME PRARYHTDQD DARHTSLDSV WHMLSAAVAT TNGLVSDASG RFEGLPREDG
RIASGSGPRG VWFDMFGSTF VVFELHTLFA LSVTLLVVAP LVLLMTSIAL ARADKMYLFR
SSASPEDSDG SEAVPLHGVR GFFRFPFLLV IPTGVTVGLA YLVTKFNPYI IHSSEYAVWS
MMVSAWVFSA WFVSRVADFA RPSAFHRVYT LTWLFLVEWV LLVISTVYEN KYGLAGGYFV
FFAFAGTALA TWISYLELFA LPRKSEYATQ LALPSRRASS HGSRLGTASG EDVEDGEDED
DDGTAAEATE TTSLLRGQRT TFANYVRVTG DYLRDDDDEP RQPNLYGHEQ AWSIHLPKWV
WVLQFLVTAP VVLIFAGPLA LLLTSALRQT GQDGSSSLFI YIAIAALTTL LFMPLLPFIH
RYTHHIPLFL LCVFAGTLIY NLVAFPFSPA NRLKLFFIQE VDLDTGVNRA SLSGAYPFVH
DVASSLPSAA GQNITCDLDL LRPKCSWQGI PPQVVQPQPR PQFQSEASKM KDWLSYNITR
SDTGPKAQFS ISGRNTRACK LVFDRPVVSF TVADSAYDPR FPHVSPDGTK EIRLWSREWG
HTWTVEVEHD GEGLRGRVVC LWSDGNTAGV IPALDEVRQY VPVWVGVSKL SDGLVEGSRR
FEI
//