ID A0A1J9P3D4_9EURO Unreviewed; 844 AA.
AC A0A1J9P3D4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptide hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ78_08582 {ECO:0000313|EMBL:OJD10386.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD10386.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD10386.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD10386.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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:OJD10386.1}.
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DR EMBL; LGRN01000821; OJD10386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9P3D4; -.
DR STRING; 1447872.A0A1J9P3D4; -.
DR VEuPathDB; FungiDB:AJ78_08582; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000182235; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF71; CARBOXYPEPTIDASE TRE2, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10650)-RELATED; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..398
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 501..684
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 770..833
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94510 MW; 30201518ED947BC4 CRC64;
MSDEKSKYEF LPIPTYEEAT SSRPSSSQSR LGPEETSDDA ERQGLLSRSS EGQGPRYPGN
YQPPTVESER SSLDFLPSSN GSSARGSTDE LRRELEQMDM EEPDETSASS LSQSSFSKRF
THLRRTLSSI HLPLWKYVPK FNFNPRFLSD LRLRVEHHHC IIILRMIALF FVVTIIYFLI
VSDVVGFVRP INMGQMYEPE SVRIYVQNHI NESHIAENLR RMTAFPHVAG TEGNYVLAQL
VEERFKSALL DSVSMEQFDV YLNYPKEDGR RIAIVDPPEL AWEAKIEEEQ AYRGSPNNQY
PVFHGHSKSG NVTGPLIYVN YGSREDFKKL ADMGVNLEGA IVLVRYYGTQ SDRALKIKAA
ELAGAAGCII YSDPAEDGIV LGPEWPKGRY MPSDGVQRGG VSMKSWVIGD VLSPGFASTP
GEKKRISPEE STALPKIPSI PIAWRDAQPL LKALRGHGKK VPKEWVGGVP EIDEWWSGDP
TSPKVNLANA QEELERHPIF NVIGRIVGIE QSEKKIVVGS HRDAWCFGAA DPGSGTAVFL
EVVRVFGLLR AHGWRPLRTI EFASWDGEEY NLIGSTEHVE NDVDELRRNG FAYLNVDVAV
SGNKFRASAS PVFEPVLLRV LERTSDPRTH QTLRSLWDQQ RSKLEGLGAG GDYVAFQDIA
GMSSIDFGFT GGPYPYHSCY DTFEWMTKFG DPGFKYHQVL GQIWALLILE LSDSPMLPFD
MQAYASAVTK YVSDLEQYSK SKHVPLLRAR GPDETSNNNH KVPNSGTNVV NMQPLHDAAK
EFRESAATFH QWGNNWNESL TSSGGYESNV MAIKRMSYNS HMTYFDTNLL DLGEDGGYLA
AKEN
//
