ID M3CFB3_SPHMS Unreviewed; 538 AA.
AC M3CFB3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Amine oxidase {ECO:0000313|EMBL:EMF12503.1};
GN ORFNames=SEPMUDRAFT_149157 {ECO:0000313|EMBL:EMF12503.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12503.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF12503.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF12503.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456264; EMF12503.1; -; Genomic_DNA.
DR RefSeq; XP_016760624.1; XM_016905378.1.
DR AlphaFoldDB; M3CFB3; -.
DR STRING; 692275.M3CFB3; -.
DR GeneID; 27902515; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_10_1_1; -.
DR OMA; RMWTELW; -.
DR OrthoDB; 2949649at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF404; POLYAMINE OXIDASE FMS1; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 77..522
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 17..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 59424 MW; 37D45BB7A692D773 CRC64;
MSACQNNMAH LYHQTTHICA SPPKKPSNRG SGLGEDSISV SPSTTLQAET PAAVDKLAPR
TGAEGKKVKL VVLGAGISGL RAASCLQRHG VDVVILEARN RIGGRIHTTR NEAGAPRDIG
AAWLHETSQN KLVKLISKLK LDYYYDDGLP LYYTEQGRAG AQFKAKKVAD EAADHMQWWY
ETHPDAPDQT ASDFVNSFVD KHELITEDER LWAPQAFKEV ELWIGTTIET ASARHLSYFV
TERNLYMKGG YDNVVKWVAD SLLPDTVHLN KTVDHISWSE DGSCTLEYHD ASGNVAVMEA
DAVISTLPLG ALRRNLVTFD PPLPDDMQLA LSKFSYGALG KIFFEFADVF WSKDNDQFMF
YPTPPALEED SYSTSPSSSS SNEPDNILNY ATVTINLWIM TGGKELCVQI AEPLTQRIEA
MTDKQAIYKF FEPLFKLLRT EPYKTLPRLI NVETTHWTQD PLAGYGSYSA DKVGDEPELL
LNALENHKGS RLQFAGEHCT MVANGCVHGA FATGEKAAKN ILNTFGIAYD GGDMVSID
//
