ID F9FXV0_FUSOF Unreviewed; 914 AA.
AC F9FXV0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=FOXB_11232 {ECO:0000313|EMBL:EGU78259.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU78259.1};
RN [1] {ECO:0000313|EMBL:EGU78259.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78259.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase
CC activity in the context of the EKC/KEOPS complex and likely plays a
CC supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex
CC also promotes both telomere uncapping and telomere elongation. The
CC complex is required for efficient recruitment of transcriptional
CC coactivators. {ECO:0000256|ARBA:ARBA00003747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least BUD32,
CC CGI121, GON7, KAE1 and PCC1; the whole complex dimerizes.
CC {ECO:0000256|ARBA:ARBA00011534}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU78259.1}.
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; AFQF01002828; EGU78259.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FXV0; -.
DR STRING; 660025.F9FXV0; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00069; Pkinase; 2.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067}; Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 548..912
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 914 AA; 101927 MW; FF7508561E04F4A0 CRC64;
MAPSASSPST QWTHAPVDVA IVGGGLSGLA AAKDLVAAGK SVLVLEARDR VGGKVYDVEV
KDGNGHRVEA GAEFVCKNHT RLLTLANELG IKTFPTYIEG DMLMWIPNQG RLLYDPVKMQ
GMPPLPEEDI AILVDITVQI NEMASEIDVH QPWTHPKAKE WDRLTLSSWL DGFARDGTAR
GDVSLLSAII NVARTGDPET KGRMEMLTNV KNGSLEERIE GGPQNIAIKL AERLGSDTVR
LQAPVRQILQ NDAGYLVVGD SFRVQAQKVI IAIPPTLAGR IVYQPPLPAA RDQLCQRVPM
GSIGKVIAIY KTPFWRDQGL SGEVASLEGV SQSTFDSSPP DASFGAMMGF LEANEMRRLD
DVSEEEIFAA VTEDFVRYFG PKAREVQSWV LQRWDNEEFS RGGHTGLFPP NVWTQFGPAL
TKPVGGFILR LIIAPHRLSI AALGSSFRNN FLVQTFTKSP FNPNYSHSRP LPRIQIMGSE
GSHSPLPTQE QLDDDIAFDY HDLDHAPATS QGTFLQGSNE SLEPLEEYQE GGYHPVHIGD
VLGPSDRYRV IHKLGHGGFG TVWLCRDSLQ ARYIALKVMV SDLRSDEILD FSLAELDQSM
PGAQYIASAL DSFSIEGPNG SHQCLALLPL GPCVSPRLWM RLGTDPATIL RKFAYQSTQA
LDFLHNNQIC HGDFRPSNIL VKLGNVDHLS EDELLSQLGQ PEEVQVQTES GEELPASSPR
YLVQPADISR LGNEFLTEEI CVIDFGESFR FSSPPEDLGI PENYLPPEIL LECPEAIGPA
CDLWALGCTL FEIREQLPLF YMIYDKDELL AEMVRFFGKL PESWWVKWEA REEYFDADGK
WLRDEEDWSL EVALSKPIEI FDAGEKYKEG PKQSLQTPET EQKLLADLLY RLFKYDPRER
LSAEEVLRHE WFRL
//