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Database: UniProt
Entry: A0A0F0IDY7_ASPPU
LinkDB: A0A0F0IDY7_ASPPU
Original site: A0A0F0IDY7_ASPPU 
ID   A0A0F0IDY7_ASPPU        Unreviewed;       887 AA.
AC   A0A0F0IDY7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=M28 Zn-peptidase Transferrin Receptor-like family protein {ECO:0000313|EMBL:KJK64922.1};
GN   ORFNames=P875_00010794 {ECO:0000313|EMBL:KJK64922.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64922.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64922.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-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:KJK64922.1}.
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DR   EMBL; JZEE01000380; KJK64922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IDY7; -.
DR   STRING; 1403190.A0A0F0IDY7; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000313|EMBL:KJK64922.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          310..395
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          499..682
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          759..884
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  99352 MW;  B10C53FDB93DB085 CRC64;
     MGNDSKFEYE ALPIPSYEEA VGARPSSSRS NLGPEANDES ERQGLLHNVD DVTARESARP
     RPHGYQPPTV ESVRDSLDGL DSTGADSERG SLEELQRELH EMDVEDGDQQ SSQRSRLLRS
     RFSKRISSLT RSLSAIHLPI RRFLPSFRFT IDLNGARTNM RTHGCMIMLR LFGLFLVVLV
     VYIFFVSDLF NMNSRFIMGQ SYSAASVENF VQGHVNETNI AENLKRVTNF THMAGTEGSY
     ALAEWVKQEF KIAGLDDIEM EEFQVYLNYP RDDGRRVAIV DPPDLSWEAT LEETNEEMPV
     FHGHSKAGNV TGPIVYANYG SREDFQYLAD QGVTVEGSIA LVRYYGSESD RALKIKAAEL
     AGAVGCIIYS DPSEDGFVRG PAYPDGRFMP EDGVQRGGVS LMSWVVGDVL SPGFASTPDE
     KKRLKPEESQ GLTSIPSLPI AWRDAQRLLQ VIKGHGSQVP AKWVGGVPNV DQWWTGDGTS
     PKVNLMNLQD EEERQPIYNV LGRIIGLEQP EKKIIVGNHR DSWCLGSADP GSGTAVFLEV
     VRVFGELRTF GWRPLRTIEF VSWDAEEYNL IGSTEHVEKE LEKLREHAYA YMNVDVGVSG
     SEFEASGCPL FERVVTQILG RISDPVANET LKEIWEKKQK KLGPLGAGSD YVAFQDIAGT
     SSVDFGFVGE PYPYHSCYEN WDWMVRFGDP GFQYHKILAQ FWGLLILQFA DTPVLPFDLE
     VYADHIASYV IDLEKYAKSQ NVPIAHDASS GKSNREVTVT FKPLYDAAAK VKDDAAQFQQ
     WARVWHDTVL GTGGFENNVI AAQRMDHNAR MARFDTHLLD DRVDGGVPNR TQFKHVLFGP
     ELWSGYDATF FPAIRDSIDS RNWTLTQEWV DRVSDILSTA GDKLLHG
//
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