ID A0A0D2E8V3_9EURO Unreviewed; 985 AA.
AC A0A0D2E8V3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, 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=PV06_05340 {ECO:0000313|EMBL:KIW44324.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44324.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW44324.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44324.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
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; KN847335; KIW44324.1; -; Genomic_DNA.
DR RefSeq; XP_016264540.1; XM_016406334.1.
DR AlphaFoldDB; A0A0D2E8V3; -.
DR STRING; 215243.A0A0D2E8V3; -.
DR GeneID; 27357414; -.
DR VEuPathDB; FungiDB:PV06_05340; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000053342; 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:UP000053342};
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 381..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 655..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..339
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 563..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 108825 MW; AD32FDAC1096E1CE CRC64;
MARLSNPVAF TRWPVTILTT AVYLAITITL IIVHTGVPTP PSSATPLHGI NLTEAWDDLQ
LLTSSRHPYN THANDKVHDW LLARITSILE ENVESPSGTS ARPPSVYVFE DNTSNLTYSS
GGISGVGGTS VYFEGTNVIV YIPGIEDDLS QWWLEPNGKP SSRNAVLVNA HYDSVSTGFG
STDDGVGVIC VLQLLKYFST PDNKPKNGVV LLLNNGEEDF LNGANVFGQH PMSKVVSNFL
NLEGAGAGGR AALFRSTDDA VTKAYAHSKY PFGSSTSADG FERGLIRSQT DYVVFNGKLG
LRGLDVAFIG PRARYHTDQD DSRHTGRASL WHMLSAAVAT TESLTSTSLE TNLEPGNTPG
HRALWFDMFG RAFAVLRAHT FFALSVTLLV AGPVILLITL ILLYRFDKFY LFSGSREYHM
PDGEDKVSLY GWRGFFRFPM ILLVACAAPI ALAYLLFKEN QYIAHSSEWA VWSMMISSFV
FVAWFLCRTA DFGRPSSLTR VYGLSWMWLA WWVFLVVATV FEEHLHLVGV YFVLIYTATL
FLATWLAYLE LFSLPKKSTY CRGKVGDDSS TAPSRSSSGA RYGTSAPGQE ETGEDGGNDE
GEPTERSSLL RSRGRSTFKG YRPEGTEPSP SAKSKDDKSS QPEEQEWSKS QWTSLWLLQM
LVVVPINLII VGQLGLLTAE GLHQTGQDGS SMFLVYIMMA VATILMFSPV VPILHRFTWH
IPIFLLLVLI GTLSYNLVAF PFSADNRLKL FFVQQVDLDT GDNLASLAGA TPFVRYAVAE
LPSAPDRSLD CISYGPDNNL ERCSWPGIPP NVANPTSSVP PEKRYKSWLS FNATRINNSD
SNNEARFVIY GKNTRACKIV FDSPISAFHV EGQAPRDKRF TPVPESGSTE VRLWSRTWDR
AWTVNVSWAD SASGKEGDDD DDDQDGHKLA RNETNMTGRV VCLWSDVNQV GLIPAFDEAV
HYTPDWVAIT KASDGLVEGY KNFKV
//
