ID C0NRV3_AJECG Unreviewed; 693 AA.
AC C0NRV3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=N-acetylated-alpha-linked acidic dipeptidase {ECO:0000313|EMBL:EEH05619.1};
GN ORFNames=HCBG_05883 {ECO:0000313|EMBL:EEH05619.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05619.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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; GG663370; EEH05619.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NRV3; -.
DR STRING; 447093.C0NRV3; -.
DR VEuPathDB; FungiDB:I7I50_06134; -.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; C0NRV3; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
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: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 Hydrolase {ECO:0000256|ARBA:ARBA00023049};
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:UP000001631};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..693
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002899767"
FT DOMAIN 164..236
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 349..463
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 579..691
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 252..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 75198 MW; F238CFA7AC7142E2 CRC64;
MQLLALSLLA ASASVVDACV SDHLMDRSFD MRQLDLAKRS SKPPPALTEQ ESILVNSFDN
NTISDWLYYY THGLHIAGTN KTMAQWTADR WTEFGVPSSL AEYYVYLNYP VSSSLSLTLA
DGTVWNAELD EDVLAADDTT SYPNRVPIFH GYSASGDAKA EFVYVGRGQQ VDFDRLVELG
VDLKGKIAMA RYGGPFRGLK VKNAQDYGML GCVIFTDPGD DGNVTEANGY VAYPDGPARQ
PSSVQRGSVL FLSTAPGDPT TPGYPSKEDS PRADTSPVVP KIPSIPISYA NAQKILGALD
GQGQSADAVN RTKWVGGLDV QYSSGPAPGV ELSLSNVMRD EVAPIYNPIG IINGTKEDEV
IVVGNHWDAW IIGGAVDPNS GSAVMVELAK ALGKLQESGW KPKRTIVLAS WDGEEYGLLG
STEWVEEYVN WLKETCVAYV NIDSAVSGPH PGLSGTPGLH QLSIELMKKI SWPYKGDESL
TMYDMWLAGS KGQVNVGSSG GSGDPVYHYH SNYDSFHWVD TYGDPGFVFH KAMGQYLALL
TYHLASDDII PFEVNNYGPE LAKYLASLRK VIDASGLTVD LSRLEAAMEV LNKAAKATTE
LRDQAIKTGD ERLIDLVNAK FRDFERGFVS QGGLPNREFY KHLIWAPGLD TGYAPTTFPG
ITEAVQGGDQ ALAQEFVERT SNAIYIAAGI LTP
//
