ID A0A2N3N1S7_9PEZI Unreviewed; 1150 AA.
AC A0A2N3N1S7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HMG box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=jhhlp_007121 {ECO:0000313|EMBL:PKS06373.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS06373.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS06373.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS06373.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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:PKS06373.1}.
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DR EMBL; NLAX01001034; PKS06373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3N1S7; -.
DR STRING; 41688.A0A2N3N1S7; -.
DR VEuPathDB; FungiDB:jhhlp_007121; -.
DR InParanoid; A0A2N3N1S7; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000233524; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR CDD; cd00084; HMG-box_SF; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
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; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_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; 2.
DR Pfam; PF09011; HMG_box_2; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524}.
FT DOMAIN 326..386
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 1010..1088
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1010..1088
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 125947 MW; 836DACDB403A4A2C CRC64;
MGRSSRVRRS QEYRSTKVLA PQRTSPRSKN GLKAQPASTT QAQDTQLATP SSPSSSESHT
EIAQEIVVWT EVKSPGWFAT LIWAGACPFT LDRRALTRDR MNGMSIPPTA HIPAINLELT
GDVMGSSLSA LSESSDLSSV PSVVSSRATT PVEADEPTDD TPVPKFSQES SSPSLSASPL
TDNGHFQPVS TAAPSISALS ESAVVEPRPK STSPPSSTYT ATAVKRVPSE SPTPTPITTE
TFPTPQPSTP SLPVFVPTVL PQSQGLERPV FNVRPKSSIP TDLSPAEYAS QCIEGAENSR
LNPFILHTGE YEILRNHLSY VQVTTYLNIR NGILRLWIRN PRVAVTREEA VGCAGARWAN
VASVCYDWLV RNGYINYGCL EFPSLAPKGN ITKKKKKQKT IVVIGAGLAG LGCARQLEGL
FKQYSDRLDE VGEVAPRVIL LEGRGRVGGR VYSRPFQTKP PNVSPRVERC TAEMGGMIIT
GFIGNPLNIL VRAQLGLPYH ALNSRTTIFD YDGQAVEDDR DLRAEGLYND CLDRVIEYKY
KLDPPKIVKG NRELIMEARD ACNDGQKTIS QKEDEEHPTL SPQSLAKPPS APKAKATAAE
AARSIGWTLR PGISETDNLD LVTPTSAPGA TLGSVVDSCI AQYKKIVDLT EQDFRLLNWH
VANLEYSNAT NMHNLSLGGW DIDAGNEWVG KHTMIVGGYQ RVARGLLHCP SPLDIRMKAP
VRKINYQPTQ PSSRATVVCQ DGSSIEADIV VSTIPLGVLK HGDVEFNPPL PEWKMGPIQR
LGFGVLNKVI LVYKQPFWDL TRHIFGVLRC PENPQSVEQS DYRSQRGRFF QFLDVTATSG
LPCLVALMAG DAAVDTENSS DDELVQEATE VLRKIFGHDV PLPVEVTVAR WARDRFARGS
YSSSGPDMLP TDYDTMAKPV GNLYFAGEHT IGTHPATVHG AFMSGLRAAG EVLHSLIGDI
DVPTPLLIPK ESQTLKRKTL EEPKDPLDIY EEQVYCHIIS KIGPRPAPPE KVSANAYRLY
CTTNQDAARE KCQAGIRPGK RKGKAGPNEV RHMLSKMWKQ ATPDEKKPFE NMAAELKNAY
ALKAAAFERL APQWDEKAAA VRAEYVKEHP FVEPGMEGSD DAVVGEDGHV VKQRRKKQVS
YVENSEEGSE
//
