ID W9XJJ6_9EURO Unreviewed; 973 AA.
AC W9XJJ6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=A1O3_09747 {ECO:0000313|EMBL:EXJ77520.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ77520.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ77520.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ77520.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ77520.1}.
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DR EMBL; AMGY01000010; EXJ77520.1; -; Genomic_DNA.
DR RefSeq; XP_007738030.1; XM_007739840.1.
DR AlphaFoldDB; W9XJJ6; -.
DR STRING; 1182542.W9XJJ6; -.
DR GeneID; 19173830; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000019478; 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:UP000019478};
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..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 160..336
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 567..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 108139 MW; 58AB2EEA05AF5DBB CRC64;
MAWLSNPFAF TRWPVTILTS ILYLAVLIPL LIVHTGVPSP PKSETPIHGI NLTEAWLDLQ
LLTSSYHPYN SRRNDEVHAW LLQRINSLLE ENTGASLLPT ETVSKAYVFD DTVSNSTFSS
PGISPSSGIS VYFEGTNLIV YIPGIDDDAT TWWLDPNGKP SKRNAVLVNA HYDSVSTGFG
STDDGVGVVC ILQLVKYFST PGNKPQNGVV LLLNNGEEDF LNGANVFGQH PMSKVVSTFL
NLEGAGAGGR AALFRSTDEA VTKAYAHSKY PFGSSVSADG FNRGLVRSQT DYVIFNGKLG
YRGLDVAFIG PRARYHTDQD DSRHTGKASL WHMLSGAVAT SRALTSASLT TNLEPGHTPG
SPSLWFDLFG RTFAILKAHT FFALSVTLLV VGPILLLLTL ALLYRVDKFY LWSGSRPYHM
PNGDDEIRLY GWRGFFRFPL ILLAACATPI ALAFLQVKEN QHIAHSSEWA VWSMMISSFV
FVAWFFCRAA DFSRPSSLTR AYGFSWIWAG WWTFLVVATV FEEHFHLLGT YFVLIYAATV
WFATWLSYLE LFSLPKKSVY CRGKFGEDHA SSRSRSTSRP PHASASGQED NAEQSENEED
EPTERSSLLR SRGRSTFKGY HPESDEPSPA APVKDDQGDT YEEQEWSQSQ WTWLWVLQVI
VLVPINLILV GQLALLTTEA LHQTGQDGSS TFLVYIMIAV CTILLFSPVV PILHRFTWHV
PIFLLLVLAA TMIYNLTAFP FSPGNRLKLF FQQQIDLDAG NNSVSLQGVP PYVRHAIANL
PSSTGQELAC IKTGPSDNLE KCSWSGIAPN VVNPPKSLLE KQYKSWLNFN VTRVNVSDSD
NRARFILYGR NTRSCKITFD QPISAFQVEG QAPRDKRFTP VPEGGSQEIR LWSRTWDRAW
TVDVSWDNPS ADDDSKSKAS TTPLQGKVVC SWSDANQVGV IPAFDEAKHY VPSWVAITKA
GDGLVEGYKK FQV
//
