ID A2QD97_ASPNC Unreviewed; 888 AA.
AC A2QD97;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Contig An02c0190, genomic contig {ECO:0000313|EMBL:CAL00629.1};
DE EC=3.4.17.- {ECO:0000313|EMBL:CAL00629.1};
GN ORFNames=An02g06300 {ECO:0000313|EMBL:CAL00629.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAL00629.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAL00629.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; AM270014; CAL00629.1; -; Genomic_DNA.
DR RefSeq; XP_001399767.1; XM_001399730.2.
DR AlphaFoldDB; A2QD97; -.
DR EnsemblFungi; CAL00629; CAL00629; An02g06300.
DR GeneID; 4979120; -.
DR KEGG; ang:An02g06300; -.
DR VEuPathDB; FungiDB:An02g06300; -.
DR HOGENOM; CLU_005688_1_0_1; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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 Carboxypeptidase {ECO:0000313|EMBL:CAL00629.1};
KW Hydrolase {ECO:0000313|EMBL:CAL00629.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:CAL00629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
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; 98952 MW; 6BD85C4CC5CE5E34 CRC64;
MGNDNKFEYE ALPIPSYEEA IGVRPGSSRS HLDSSEEVSD NTERQGLLQR GPQTGARGET
RPHGYHPPTV ESARNSLDDL ESGSGSDRGS LEELQRELAQ MDVEDAGQQT SSQRSRLRSR
FSKRFNDLTR TLSSFNLPFR RYLPRLPDFR FTIHLDEARS GLKHNGCMIL LRVFGLLLVV
TIVYIFFISD LFSMNNRFIM GQSYSAASVE NFVQGHINET SIAENLKKLT AYPHIAGTEG
SFVLAEWVAS EFNKANFDEV EMEEFQVYLN YPQQDGRRVA IIDPPDLTWV 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
//
