ID A0A1E1KXX6_9HELO Unreviewed; 1062 AA.
AC A0A1E1KXX6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Related to VPS33-vacuolar sorting protein {ECO:0000313|EMBL:CZT03080.1};
GN ORFNames=RCO7_06088 {ECO:0000313|EMBL:CZT03080.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT03080.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT03080.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT03080.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; FJUW01000026; CZT03080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1KXX6; -.
DR STRING; 914237.A0A1E1KXX6; -.
DR InParanoid; A0A1E1KXX6; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000178129; 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; 3.90.660.10; -; 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:UP000178129}.
FT DOMAIN 183..278
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 930..1006
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 930..1006
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 93..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 118878 MW; 322D288DE5AAF741 CRC64;
MDTHMAQHDD LHLMGLQELD SHLSIFESSN MEMESSAGTP ESTSNYGDTI NVSDQLNSII
VKSTDEVYLP SAQYGSRARP TDPKLNALQA EHSIKSTSDG SLHLRPESAR DSMVSSMNTD
IDDGSSALSS ISSKATSPTG FDAHSKETHK SASQLAKRRE KFDIRPKVSI PTDLTPSEYA
RQCIAAAESS RLNPYSLHIE EHAMLRKHIS HQQVTTYLNI RNGILRLWTR NPMIGVMRDE
AVGCAKDVRW FDAASVCYEW LVRRGYINYG CLEHIEAKRV NKKPRAPKRT RRTIAVLGAG
MSGLGCARQL EGLFSQFEER FIAMGEDPPR VIVLEGRDRI GGRVYSKAMK SKPKYPTLSY
GSRHTAEMGG MIITGFDRGN PLNIIVRGQL ALPYHALKPD TTIYDAIGRP VDINRDQFAE
KLFNYILDRV SEYKFKLPTH PVIDGDKDLL DAGRDNSSEG SKTISEVEDS SNSSTSSSKN
TSRAPSEQMV PVSSDRLTGR AHLEPGIPAV HTAAFKAQEI GWQLRDGVGI EQDLDLENVV
NSKYATLGLV FDEAIRQYTR IIEFAPLDLQ LINWHVANLE YSNAVTCNKL SLGGWDLDTG
NEWEGKHTMV TGGYQQVPRG LLNCPEPLTV RKGRKVRRVS YKPDTNDSPS LIECEDGEEI
EADYIVSSIP LGVLKQQNIQ FEPALPDWKM GPIQRIGYGV LNKVVLVYEK AFWDESRDIF
GTLRNPANRF SLEQSEYFTQ RGRFFQWFNV TNTTGLPTLL ALMAGDAAFS TESTPNDFLI
AEATKVLRCV FGASVPLPVE AIVTRWGHDQ FSYGSYSYTG PNFRPDDYDV MAKPIGNLFF
AGEHTCGTHP ATVHGAYISG LRAASEVLES MIGPIDIPEP LVLPNSSSMK RKSDSIRSPK
DPKQARLEKY EAEVWDAIYV KLGDRPWKPA NNYANPYRMY SKDKWEEAKK KCETGRRPGK
GKPIPNEVKK MVTKMWKEAS DEEKQPYNDR AEVQKKAYAD ALADYNLKAG QWDKDALAYR
EIYELEHPSI PTPEEFASPS RDRRAKRGVN GYAEDSDDEV DV
//
