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Database: UniProt
Entry: F9FXV0_FUSOF
LinkDB: F9FXV0_FUSOF
Original site: F9FXV0_FUSOF 
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}.
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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
//
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