ID A0A093X6P1_9PEZI Unreviewed; 682 AA.
AC A0A093X6P1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
DE Flags: Fragment;
GN ORFNames=V490_07737 {ECO:0000313|EMBL:KFX88283.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX88283.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX88283.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX88283.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFX88283.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJS01002320; KFX88283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X6P1; -.
DR STRING; 1437433.A0A093X6P1; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000029320; 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:UP000029320};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 605..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 226..401
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 657..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 682
FT /evidence="ECO:0000313|EMBL:KFX88283.1"
SQ SEQUENCE 682 AA; 74695 MW; 9000EC5CC9CA8B3E CRC64;
MAHVLRDLVS SPVSVMLITV IVYLAIAIPL LVIHEVVPPA PSDDALPSGL NISEAWLDLA
ELTKAYHPYA SRRNDEVHDW LLKRVEGILE SNGVQWSSEN SHIPISPQQI AGAEAGGEEV
TGKVAAAPFP GFIGVETNVQ TQEEETNEAD ELRKRDASPL VTIFNDLQSN VTCSGLGAIG
ADGKGRLPGQ SVYFEGTNVI VYIRGTEDEE GEWWKSSLHL RNTHGQGGIL VNAHYDSVST
GFGATDDGVG VVTILQLIRY FTTTGRQPKK GIVALFNNGE EDFLNGARAY TQHPMSLFTH
TFLNLEGAGA GGRAVLFRST DTEVTRAYAK SSHPFGSVVG GDGFKQGMIR SQTDYVVFED
ILGLRGLDVS FWNPRARYHT NQDDARHTSR DSVWHMLSTS VSTVEALSSD TSGTFNSPRG
DNAWGKVKNG KGSDGVWFDL FGKGFAVFNL RTLFAWSLTF LIACPLAIIL IIYLLIREDK
FYLFSSSVPS EGGSEEADVS LNGWRGAFRW PLTLIATSAL TVGSGLLIVK INPLIIYSSQ
YAVWTMALSL NFFVFWFIMR GANFVRPSAS HRTYAYFWMF IVGWIVLVAV TVLEDRFKIA
SGYFFVFYEI AIFFALAISL LELFALPTKA QFAANVHAQD EAVENINALP DSDTLIAPTE
DEHAEPESAA AADEAEEAEP TE
//
