ID   C9SIQ4_VERA1            Unreviewed;       989 AA.
AC   C9SIQ4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Lysine-specific histone demethylase {ECO:0000313|EMBL:EEY18827.1};
GN   ORFNames=VDBG_04936 {ECO:0000313|EMBL:EEY18827.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995}.
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DR   EMBL; DS985218; EEY18827.1; -; Genomic_DNA.
DR   RefSeq; XP_003005330.1; XM_003005284.1.
DR   AlphaFoldDB; C9SIQ4; -.
DR   STRING; 526221.C9SIQ4; -.
DR   GeneID; 9536745; -.
DR   KEGG; val:VDBG_04936; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_1_2_1; -.
DR   OrthoDB; 5402444at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-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   Pfam; PF04433; SWIRM; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:EEY18827.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Transferase {ECO:0000313|EMBL:EEY18827.1}.
FT   DOMAIN          199..293
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   REGION          94..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..983
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  108479 MW;  DC8C4FA4D9F53CB6 CRC64;
     MRTSPRSRDK LGIGSGKELF TPSGFLNSHM LHSSPLSKTA KTSFSISPLR DLTSSASSQI
     SLEAMSEIAS EIVVHGEDMD VDDSMNDTSM ATSAVASPAE FSGNEGMAEP SPHRDILQTN
     RNSLESPMSH TSEQSELSSL LSSVSSKATT PVDLNAAQEP DLSSARYSQP RQVPRRTYDI
     EPKSSVPAGL DDITYAAECI RAVEASRLDP FSLHQGEYQL LRQHITHNQV TTYLNVRNGI
     VRLWYHNPRV PVTREQAIGC ASVRWFDVAS VCYDWLVRNG FINFGCVEFP TVDEEKEGEP
     PATKQKTIVV IGGGMSGLGC ARQLENLAKQ YKDQFRELGE LPPKVVVLEG RTRVGGRVYS
     RAFTTKPTLS VPGFPGERYT AEMGGMIITG FERGNPINVL LRGQLGLHYR ALRPETTIYD
     SNGRPVDPLR DDLVEKLYND CLDRVSEYKH HNQPSKLVRG NHDYIEHGRD SGTDGSKTIA
     ESEEAAAALP HAAPVSQQNV PERVNRVPVS ADKLTGRIHT EPGTPATSKA SEKAKEMGWT
     LKNNIAPEAN IDLDDAAARS DATLGSVLDE AIGQYRNLVD LTAQDHRLIN WHVANLEYSN
     ATSLHNLSLG NWDIDAGNEW EGKHTMVAGG YQTVPRGLAL CPTPLDLKTN APVQKIKYSS
     EGGLKRSLVE CEDGTIVEAD YVVSTIPLGV LKQGSVEFDP PLPGWKTDVI ERIGFGVLNK
     VILVYDKPFW DTERHIFGVL RDAPNRHSLA QSDYASQRGR FFQWFNVTQT TGLPCLVALM
     AGVAGFDTER ESNEDLVKEA TGILRGVFGR KVPFPVEAVI TRWGSDKFSR GSYSSSGPGM
     HPHDYDVMAK PVDNLYFAGE HTIGTHPATV HGAYMSGLRA ASEVFDALLG PIDIPSPLVL
     SKSSMWRAAS AEERKPFEET PSRAKAAHAL AVQEYNDGSV RWDEAAINLR AEYEEEHDLA
     GSATLTADGK HRRTSKPVDY AEDDESVSE
//