ID Q8X0H3_NEUCS Unreviewed; 649 AA.
AC Q8X0H3;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE SubName: Full=Uncharacterized protein B13O8.030 {ECO:0000313|EMBL:CAD21336.1};
GN Name=B13O8.030 {ECO:0000313|EMBL:CAD21336.1};
GN ORFNames=GE21DRAFT_7529 {ECO:0000313|EMBL:KHE88270.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAD21336.1};
RN [1] {ECO:0000313|EMBL:CAD21336.1}
RP NUCLEOTIDE SEQUENCE.
RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA Nyakatura G., Mewes H.W., Mannhaupt G.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD21336.1}
RP NUCLEOTIDE SEQUENCE.
RA German Neurospora genome project;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KHE88270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73 {ECO:0000313|EMBL:KHE88270.1};
RG DOE Joint Genome Institute;
RA Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.;
RT "Draft genome sequence of Neurospora crassa strain FGSC 73.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AL670008; CAD21336.1; -; Genomic_DNA.
DR EMBL; KN389636; KHE88270.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:NCU01106; -.
DR eggNOG; ENOG502QWMG; Eukaryota.
DR HOGENOM; CLU_004498_8_1_1; -.
DR OMA; AMRIPEI; -.
DR OrthoDB; 4889at2759; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.1620; -; 1.
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:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 95..567
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 619..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 72319 MW; 4ED489DBA1D699B6 CRC64;
MAQLQTDIPR DINFLLPGGG DSLRIAYAKH LLSKFLTEEH AKQHGWSKAE SRPLKHIFSP
IPSSLDDLKK RDGLFSDDPN SAVFKGKICI VGAGVAGLFT ALMLKIGGIY NFDVVEASDR
VGGRLYTHWF SDKESPDSEH DYYDIGAMRI PEINTMQSAL DLIKYLELDD KLVDYNYVEP
TKEDIVPHTW WYKSEKPDCK KFDDAIASVV QSFTQAPGKA FEEYMSGNND YYSTRAWLML
QADPKLTYEE TAMSEASETS TGLFDQAFIE TIFDYCDFAA ARNVEWKRLE GGMSQVADRM
KELIEKPDWP VKGAPAIKVT TSRPVTVMSE TADRSAISVT TTCPKGQSPS TTDYSAVFST
TAMAPLRRID IEGLHLPDKI LTGIRSLSYD RATKVAIKFA SPWWTLVGGV SSTDLPISKV
VYPSWNDGPD KPAVLMVSYS WAQDATRMGA LVPDYTKTLP SKDDEVVSVC LNALVKLFSK
ADPQTMAANV PKPITLDFLR SQYVTHHAFA WSHDPWQGGA FALFGPGQFK DVYPDFHKAY
CNGKFFMSGE ALSTHHAWIS GAVDSAYMSF VLFTTVYKLK EPMVKVKESN LVGARGENPE
EIDEFLLRWA AKLSEGVEVE GDQNRGSEHR NYGPGEEKGG LDDDWCDCC
//