ID A0A165J2J7_9BASI Unreviewed; 661 AA.
AC A0A165J2J7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Copper radical oxidase {ECO:0000313|EMBL:KZT61288.1};
GN ORFNames=CALCODRAFT_491390 {ECO:0000313|EMBL:KZT61288.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT61288.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT61288.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT61288.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV423924; KZT61288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165J2J7; -.
DR STRING; 1353952.A0A165J2J7; -.
DR InParanoid; A0A165J2J7; -.
DR OrthoDB; 2433441at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; Galactose oxidase/kelch, beta-propeller; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR009880; Glyoxal_oxidase_N.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR32208:SF96; GLYOXALOXIDASE 1; 1.
DR PANTHER; PTHR32208; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF07250; Glyoxal_oxid_N; 1.
DR Pfam; PF09118; GO-like_E_set; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..661
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007859752"
FT DOMAIN 103..321
FT /note="Glyoxal oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07250"
FT DOMAIN 486..592
FT /note="Galactose oxidase-like Early set"
FT /evidence="ECO:0000259|Pfam:PF09118"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 69106 MW; D0296F61709D998F CRC64;
MARSSTLLPL LTYALLSTAA PRPQADTTAT YVASASAAGA SPAASSSAST PGQPTRNGTL
NQFEIVGNSG VSAQQMFLGT LNKVYILDKT ENNPNLQVDG FPAWGSEYDL ETDTVRGMFV
LSNTFCAAGA SLGNGSWVNF GGNQAVTWGG LTASSQTGGG PYDDWDGGKA VRLLDPCDDE
TCNWVNLAPM TTRRWYPSVE PLEDGSVIVL GGDEWGGYVN DASQNNPTIE FFPSQGNPIG
LNILNNSLPA NLYPLTWLLP SGNLLIQTNW NTAIFDHKNV VEYALPNIPN AVRTYPGSGA
TAMLPLTPAN NWTATVLFCG GSNLQPDQWV TNWNIAAYPA DQSCVSISPD VGTDWTYDST
LPEGRTLGQF IFLPTGQLFL VNGGGTGTAG YGNDSWAIGH SYADNPVYTP LIYDPSLPAA
ERWTRDGLGS STVARLYHSS AILLPDGSVF VSGSNPNPDY TVGPDVKYPT EYRTERFYPS
YYSSRRPEPV GLPSTISYGG ASFDIQLSAE DLVGSSIANA SCLIIRGGFS THAMNMGQRY
VELASSYTGN ADGSGVLHCA QLPPNPAILA PGPALIFVVV GGVPSVGQMV MVGSGQLGVQ
PTSEASTLPQ SSLPSSTASS SGNGTSSTGS TTGTAASAAL PIAWSSLLVG VAVLLSGMLV
L
//