ID A0A427Y6V1_9TREE Unreviewed; 852 AA.
AC A0A427Y6V1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=EHS24_005093 {ECO:0000313|EMBL:RSH86819.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH86819.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH86819.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH86819.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {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:RSH86819.1}.
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DR EMBL; RSCE01000002; RSH86819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427Y6V1; -.
DR STRING; 105984.A0A427Y6V1; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000279236; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:SF54; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1-RELATED; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 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|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000279236};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 375..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..331
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 852 AA; 93810 MW; 0ECD1D44A14895E4 CRC64;
MAPPPGKRAP EPRRERTPWL WLVPLLTIVP FLCSKLHYSL PEPLPPYDAN GRTQPSEEIV
LKHIQALEDI GYRTVGTYEA VLGEKYVEAE ARALKERCDA GGVLDCEVWV QTGAGYHMFS
IMSHDVLKLY SGITNVVLKI SAKNPPSGKA PGKDSVLLGS HIDSTLPSPG AADDGMGVGV
MLDIARVLIE RNEPFDNSVI FMWNGGEETL QDGSHLYSTQ HESANTVKAV INLEAAGTTG
GALLFQATSR EMIEAFWHAP YPRGTVIAND VFSSGIILSD TDFGQFEEYL EGVSGLDMAI
VGHSYYYHTR KDITANIERG SSQHFTTNVM AILDYLLSAE SPLHNDKPWS PPDVVYMSLY
DRIFLHWTME TADKAYAVVA AIAAIFAIAN LSGHGIKAFT VALVGAPLGI VFGLVSANVI
AGVMMLIDRQ MGWFSHEGLC VALYGPAAIF GHLGTQYVLG SLLSPVNRSG LERAHYYAQI
LFLCGTSLLL QSFRIRSAYV FAVLAGVMMI GAVFHQVRRI VWERNSMPFV MAYVCPLVLF
IGFGIEAYTT TLDIFVPLTG RMGKDAPHEI LIASITAICT LTFFPIMVPL FARASRPGQR
GTLAGLAVAF ISVVVLFAGP WWSPYDATHQ KRVAVQYTYN HTTGTPTAHL AFMDLPGNEK
LVNEIHARYG QGTELVPTVL DDYNSDWDTL YPVSSFLITY KWPLEPVEFE WPGIKHKVTR
TQVANGTRIH LSLEHAGLAW PSFAFVAEIS DWKFGIPPPA GKKRHHIKSA TSVDEHELEL
EFTVSDLKEG EKLNIHWSAI DINQMVPGTA SRRGPDMPAS KWLMDMDAWA TEEYNDSLEI
FMAGIVVGVI EA
//
