ID A0A395I4Q0_ASPHC Unreviewed; 773 AA.
AC A0A395I4Q0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Putative galactose oxidase {ECO:0000313|EMBL:RAL14726.1};
GN ORFNames=BO97DRAFT_465338 {ECO:0000313|EMBL:RAL14726.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL14726.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL14726.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL14726.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824274; RAL14726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395I4Q0; -.
DR STRING; 1450537.A0A395I4Q0; -.
DR VEuPathDB; FungiDB:BO97DRAFT_465338; -.
DR OrthoDB; 2433441at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; Galactose oxidase/kelch, beta-propeller; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR32208:SF68; GALACTOSE OXIDASE; 1.
DR PANTHER; PTHR32208; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF09118; GO-like_E_set; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..773
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017383827"
FT DOMAIN 93..195
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 773 AA; 85070 MW; 7D899B5DB502FD58 CRC64;
MKFRFVAGVL LGAAAVDAFK PAEYSYESSE ADEIEIAKQS TGIVKYQSPP PDSHLIPKTN
SENSDENWEV VCSSQKKAYQ CEYAIDDRMD RYWHSDSSTD EPSWIHIDLQ KEYYVSGLTM
LPRLDGDGSE GQIGEHRIHL SPDGLNWTEV AYGTWGSNRS PKMSAFVPTL ARFVKLTAET
ASHPHSQTRN GPISIVNMAV YAYNEDTFPE AKPSKGGVWG PTLDLPIVPV SAAVEQHGNI
IMWSAWADDQ FFASPGGKTL TTTMNRSGII TQSEVSETKH DMFCPGTSMD IDGNIVVSGG
ADSGRTSVYN GTAWLKGPAM QTRRGYQSST TLSDGRIFVI GGSWSGGDKV EKNGEVYYPG
PNAHWEMRSN AKVAPMMTDD RLGAWRADNH GWLFGWKKAS VFQAGPSVMM HWYDVDAKDR
KGRVRGSWQE AGERGEDHDS MSGSAVMYDA TRGKVLTFGG QRHYDGSYGS KNAHIITLGD
PYQEPKVEVA GKGPKGELEG GMHYKRVFHT SVVLPDGKVF ITGGQSWGKP FHEGDINFTP
ELYDPTTDTF TELTRNNIKR VYHSISMLLP DGRVLNGGGG LCGNCTANHY DAEIYSPPYL
FTPNGAEARR PQIISIPDGF RVTVGEQIKI KTDDFIESAS LVRVGTTTHT VNTDQRRIPL
DTLKSVGHLQ YSAKLPDDAG IILPGWYMLF VMDAKGTPSV AKMVKVELPS TPSYEANVIP
VEEEDGEQRS GHSHVGVTVD CDDDDEVMGI MSIMFASASK FWRNWRAALV SQP
//