ID A0A0S7E567_9EURO Unreviewed; 774 AA.
AC A0A0S7E567;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM43416.1};
GN ORFNames=ALT_003039 {ECO:0000313|EMBL:GIM43416.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM43416.1};
RN [1] {ECO:0000313|EMBL:GIM43416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM43416.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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:GIM43416.1}.
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DR EMBL; BCLY01000016; GIM43416.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7E567; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_8933; -.
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:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 203..279
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 396..585
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 648..774
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 774 AA; 86136 MW; 5FA607FE5BBF1C3B CRC64;
MREKAMAPSE TTPLLVVSVA PQRYRYPHHT LRRACSFSLS LILFVGLILF LIPFSILPRE
HGSLWSYLPG ANPFPYPSWP NSPGLTYEQL QAVLQSTPSA AKAREWSSYY TAGPHLAGKN
LSQALWTREK WQEFGVVDTE IVAYDVYLNY PVDHRLALLK KDGDKTDVTF EASLEEDVLE
EDHTSGLPDR VPTFHGYSAS GNVTAPFVYV NFGTYNDYQD LVDANVSLAG KIAIAKYGRI
FRGLKVKRAQ ELGMVGVILY DDPQEDGDIT EDNGHKPYPE GPARNPSAVQ RGSAQFLSIA
PGDPTTPGYP SKPGCERQDP HNSIPSIPSL PVSYQEVLPF LKALSGHGPK ASDFNKWWQG
GKLGSKGVDY NIGPSPDDVV INLYNEQEYI TTPLWNVIGT IKGAIPDEVV ILGNHRDAWI
AGGAGDPNSG SAVLNEVIRS FGEALKAGWK PLRTIVFASW DGEEYGLLGS TEWVEEMLPW
LSKTTVAYLN VDVAAAGTKL RPTASPLLNN VIYEVTGLVQ SPNQTVEGQT VRDTWDGRIG
TMGSGSDFTA FQDFAGIPSY DLGFNRGPED PVYHYHSNYD SFDWMDRFGD PDWLYHEACT
KIWALAAAKL VETPVLAFNA TDYAMGLSSY LDKIRPAAER LPGHSSFDFV PLDKAIARLQ
KVATKFDAEA AELTSQLDEN LPWWLWWKKV RLYFLIRGVN DKYKVIERKF LYQPGLDGRN
WYKHVVFAPG IWTGYAGATY PGLVESLEAG DLENAEKWRD IIRERIEDAT DLLQ
//
