ID   A0A3F3PUL1_9EURO        Unreviewed;       888 AA.
AC   A0A3F3PUL1;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Zn-dependent exopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BDQ94DRAFT_67874 {ECO:0000313|EMBL:RDH30518.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH30518.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH30518.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH30518.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; KZ852060; RDH30518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3PUL1; -.
DR   STRING; 1341132.A0A3F3PUL1; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000253729; 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   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        169..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          312..399
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          759..884
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  98938 MW;  2B3931AE99DCEC29 CRC64;
     MGNDNKFEYE ALPIPSYEEA IGVRPGSSRS HLDSSEEVSD NTERQGLLQR GPQTGARGET
     RPHGYHPPTV ESARNSLDDL ESGSGSDRGS LEELQRELAQ MDVEDAGQQT SSQRSRLRSR
     FSKRFNDLTR TLTSFNLPFR RYLPRLPDFR FTIHLDEARS GLKHNGCMIL LRVFGLLLVV
     TIVYIFFISD LFSMNNRFIM GQSYSAASVE NFVQGHINET SIAENLKKLT AYPHIAGTEG
     SFVLAEWVAS EFNKANFDEV EMEEFQVYLN YPQQDGRRVA IIDPPGLTWE ATLEEDNEQT
     LVFHGHSKSG NVTGHLVYAN YGSREDFQYL KDQGVALDGS IALVRYGGSE SDRALKVKAA
     ELAGAAGCII YSDPAEDGFV RGPAFPDGRY MPADGTQRGA VSLMSWVVGD VLSPGFASTP
     DEKVRLKPED SRGLTAIPSI PLAWRDAQRL LQVLKGHGSK VPAKWVGGVP DVNQWWTGDA
     SSPTVNLMNI QDEVERQPIY NVVGRIIGLE QPEKKIIVGN HRDSWCLGSA DPGSGTAVFL
     ELARVFGELL TFGWRPLRTI EFISWDAEEY NLVGSTEHVE KELQALRENA YAYINVDVGV
     SGKEFDAAGS PLFESVIMQI LGRISDPDSN ETLKDIWEKK KKRLGPLGAG SDYVAFQDIA
     GTSSVDFGFI GEPFPYHSCY ENWDWMTKFG DPGFQYHKIL GQFWGLLLLQ LADSPILPFD
     LEAYAAHVGG YISGLENYAK SRNVPIADNT QNAARDTSVT FKPLYEAAAK FKDDASHFQE
     WARVWHDAVW GAGGFENNVV AVQRLAHNTR MAHFETHLLD DRPDGGVPNR TQFKHVIFGP
     ELWSGYDPTL FPAIRDSIDS GNWTLTQEWI DRVSNIISDA SDHLVHKN
//