ID   A0A0A2W062_BEABA        Unreviewed;       832 AA.
AC   A0A0A2W062;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Vacuolar protein sorting-associated protein 70 {ECO:0000313|EMBL:KGQ12007.1};
GN   ORFNames=BBAD15_g2261 {ECO:0000313|EMBL:KGQ12007.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12007.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ12007.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12007.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) 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:KGQ12007.1}.
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DR   EMBL; ANFO01000154; KGQ12007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W062; -.
DR   STRING; 1245745.A0A0A2W062; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_005688_2_0_1; -.
DR   Proteomes; UP000030106; 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: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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          216..293
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          411..596
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          707..832
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          283..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..336
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   832 AA;  92196 MW;  23950C5F6712891C CRC64;
     MAAHAHHHYH HAESTPLIHA SRTAALADQR RRRENRTCRR FFLIAVSCIA LWGLFSFFFH
     ALFVWPYHYH RSHDGRHSAS DRDGGGVLTY DQLKAILLDT PDSEKAREWS KYYTAGAHLA
     GKNFSQLANT RHGQADWTRQ KWESWGVSSS IAAYDVYINY PVDHSLSLLE KAKGHPGAWD
     VAFKASLTED VLDEDPTSGS PDRIPTFHGY SASGNVTGQF VYVNYGTYAD YEDLVRAGVD
     LRGKIAVAKY GGIFRGLKIK RAQELGVIGV LIYSDPGDDG ELTEENGYKA YPHGPARQPS
     SVQRGSVEFL STRPGDPTTP GYPSKPGAPR APPNDVIPEI PSIPISYVDA LPILKALNGH
     GPNASDFGNP WTRNLGLVHK GVKYNVGPSP AHLALNLYNE QEYVTTPQWD VIGIVNGTVP
     NEVIIIGNHR DAWIVGGAGD PNSGSAILNE VVRSVGVALE AGWQPHRTIV FASWDGEEYG
     LIGSTEWVEE YLPWIDDANV AYINVDVGAA GPVFQASAAP LLNQVLRDAT RLVPSANQTV
     PGQTIGDVWD GRISTMGSGS DFTAFQDYAG VPCIDMGFKG GPRDPVYHYH SNYDSFAWME
     SFGDPGFRYH RSMAQLLGVL VAELVDNLVI PFQATEYADA LGTYLDQVEN KLRHYDYRDG
     DDNNNHHAAI DFASMDDETL FLERGRVGSF HAKDDVVTVN ADAFWTSLRD MRLSLARFRI
     VAGELDEQAE HAREVLDRGL PWWNIVGKIR LGVTILLVNH KYKELERYFL FEGGLDGRSW
     FKHVVFAPGL WTGYAAVYPG LMESIDAKDY SNGLKWSGII NKCIRRATKS LQ
//