ID Q2UJ56_ASPOR Unreviewed; 1270 AA.
AC Q2UJ56;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=MATH and UCH domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AO090003001349 {ECO:0000313|EMBL:BAE58409.1};
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:BAE58409.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE58409.1, 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).
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DR EMBL; AP007155; BAE58409.1; -; Genomic_DNA.
DR RefSeq; XP_001820411.1; XM_001820359.1.
DR AlphaFoldDB; Q2UJ56; -.
DR STRING; 510516.Q2UJ56; -.
DR EnsemblFungi; BAE58409; BAE58409; AO090003001349.
DR GeneID; 5992394; -.
DR KEGG; aor:AO090003001349; -.
DR VEuPathDB; FungiDB:AO090003001349; -.
DR HOGENOM; CLU_002789_0_0_1; -.
DR OMA; FHPDLDD; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23084:SF257; MORN REPEAT-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR23084; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE RELATED; 1.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00698; MORN; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 151..345
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 1223..1258
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 142702 MW; 4EDDBFC68CB0F6BA CRC64;
MDTTETSVTV EQLPPVTPDI EPPSTTDTGA TTVALDAPTN DAPESSTDQS NNTVESPLLV
PENNISSQDT SVEEHEPPVR SDISAPPRPP PPEAEHAYWA EMEEDTSVPD EAEMKEIESA
ADGDYSAYEY PYWEKNFHPD LDDPEYRPIE KARLTWKIHG VRGTKEHPNR AKVMRSPPAY
IGGYWWSIKF FPRGNNVGSL SIYIECSPTM PLPDKTLPDS EFKVLRGPAD VDINDRAPDL
NLKFAHTDDS AAWLENYKSQ YPPAANEEKA TSNTWRVSAQ IGVILYNPDE PRTGWMQSSC
HQFNPHNLDW GWTSFHGPWD QIHRRQRGQR QALLRNDTLA FDAYIRIIDD PTRSLWWHAS
DSEPTWDSLG LTGYRPLGDS VINHSAEVAG LATWLHIAPF CKIIQNANIV EHHGNCDVKP
KPLCDALQRF LWQLRSRKNS LQYVDTDIIT STLRNLHEYS GDVCEFWERL RRTLELELAG
TSAVKDLAAL FDSPTPDLLL QETQGSDVVN TIPKDYNSRI CVPADQVKTM REALSNYLDS
KPGRWALPPI LHVELSRQKL DKAARQWRLI YNRVDLDEEL DLSPWLLNGQ RGKYVLYGYI
VHRGRRTSGK FFSILRPGGP GTKWLAFDDG SDNRVECLTR KTALGPHLGL DASQKVDHKT
GHDVAIAVMY IRSDLAPQYL PGPQGPWDAP PAMKEYYERG IHPYAESSDG KVAGDIQVEV
YSAPQYDKLD SLFDTYDLMS QAKAANKVMY LTVPRSTNLI ELRKKIALWA SAGAQDQTGP
EHIRLWQIGH TRDRFGPTLA FSRVSDLRTT LNLPLKTARF WIQVVSDVDA KYFAMADPRE
VDVAQNKPEE AVFEREDSDS SDDQQSVAEV EAGRAGPSGT ASRVDDTAQV VTTETSSEHF
DNNVTENSGE GAAASLETSH PENDIPNGAE NDAVIAAIIA EDIQQMETEQ STDIPQINEV
MNMPRAIEVS TESLTTDDVS APSMEPEPAL PVDHVYYFIQ IFDVDAQALR TVGSFFSQKE
ETIKAAIRKH LQWPVTKDFQ VWQRVDGTTV TTMSSAETFE VFVPDGTCFI VGDKLNKDKR
LKLNQQGLLA NPDQLVRYLW AKSRNHPTKA FTGFKTIEAS FTNEFYSGDL NKGYYHGKGK
HVSDSAATYD GDFVLGKRHG KGFLEYPIGD TYDGDWFENQ CHGQGTFVEK KTGNKYVGGY
KDGKRHGKGI SYWEVADEEM DLCQICYCEE QDALFYDCGH VCACVTCARQ VEICPICRKN
IISVVKIYRT
//
