ID Q2UQT8_ASPOR Unreviewed; 573 AA.
AC Q2UQT8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=AO090005001108 {ECO:0000313|EMBL:BAE56077.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE56077.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE56077.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; AP007151; BAE56077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UQT8; -.
DR EnsemblFungi; BAE56077; BAE56077; AO090005001108.
DR VEuPathDB; FungiDB:AO090005001108; -.
DR HOGENOM; CLU_024588_2_1_1; -.
DR OMA; WTLDTDS; -.
DR OrthoDB; 5491171at2759; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR PANTHER; PTHR32494:SF20; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 363..463
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 130..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 63012 MW; E0CB3D238A9D4220 CRC64;
MSSIAGRFPL KLGSIYLVFN VIKNWLIMIH NMRYPPGGLV LPELPCVVVR QQWNPPPDVI
GRRSTSIVQI IAFTGGLPSR FFKKTFLLSY IHKYTMWSIF CLHQALSREG HRFKTPTSCT
SLSAPAAPYS QTLRNNSRQP PDANYQVSRS TTTDYGKRCT KRANGAPLID TANTGMARLT
LTDADASVRR WLDDEVKKLG CTLHVDQMGN MFARQKGRLN SSAPMVAMGS HLDTQPRGGR
YDGILGVMAA LEVLRTMKEN GYQTNYDVGL VNWTNEEGAR FPKSMCSSGV WAGVIPIEQA
WNLQDIHDPN VTLRSELERH GYLGDIPCSP EGFPLGAHFE LHIEQGPILV ETGRSLGVVQ
GGQGYRWLTF TVYGRDAHTG TTPFSARQDP LLAASKMIAS SNEIAKQHGA LASTGVLKIP
SNASTNTVAS QVTFTLDIRH LEDEVVHAVQ KECLESFANI AKQDGKGVSF DWTMDTDSAA
VKFNKDCIDA VRTAADELVG AGQYMDITSG AGHDTVNTSR HCPSTMIFVP CRDGVSHHPE
EYCRPEDCAL GTQALLEAVV NYDQARMKKE ANA
//
