ID A0A0D1ZEF9_9EURO Unreviewed; 1042 AA.
AC A0A0D1ZEF9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=SWIRM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_00924 {ECO:0000313|EMBL:KIV85198.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV85198.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV85198.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV85198.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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; KN846951; KIV85197.1; -; Genomic_DNA.
DR EMBL; KN846951; KIV85198.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1ZEF9; -.
DR HOGENOM; CLU_004498_1_2_1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000053599; 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 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:UP000053599}.
FT DOMAIN 143..238
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 914..993
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 914..993
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 32..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 116091 MW; 15DB60859CF0DE82 CRC64;
MAAVVAPSNT ARTMGSIMPD VEMSGMPTSN VISHDEPMLD DSDDEFIKME EDDDSVSSTG
PVSLLRSLQV ESENRDSPNS SLTSASVASS IVDQKATTTI KQETKSDSSN SVSPYMFLKA
PTTCRAKSSI PSRLSPSDYA SQCVAAAEAS RLNPYALHED EHKLLQDKLC YSHVSVYLNI
RNGILRLWSR NPSVSVNLEE AIGCIKDERW TRLACFAYEW LLRRGYINFG CVEPPAITKS
AGRGRPKKEN SQQTIVVIGG GMAGLSTARQ LTNLFRHYPD HASPKIIVLE GRDRIGGRIY
SHPLTSMRSS KLAPDQRPTA EMGAHIIVGF ERGNPLDAII RGQLALDYHL LRDLSTLYDI
DGTPVNGVND AMIERLYNDV LDRTGHYRLK HTVKKTAQGD KDLIDAGREP PDEEGLTIKQ
FEEATALGTI DQLLPNKKSR RRGAGHRAAK GDKSSEEVET STETKTQLPA AQAAKEFGFL
LRKTTQMHET LELEDLAVQL NQSLGTVMNA GIDQYQKFLD LKPYALRLLN WHFANLEYAN
AANVDKLSLR GWDQDIGNEF EGEHAQVVGG YQQVPRALWR HPEPLDVRTR KAVKSIKYSA
AGSQGKATVT CEDGHSIEAD KVVFAAPLGV LKAQSIQFDP PLPQWKRDAI RRLGFGLLNK
VILVFERPFW DVNRDMFGLL RAPRDSAGFN QTDYKEGRGQ FYLFWNCIET SGLPVLIALM
AGESAHEAEK VSDEVLVGQC VEQLQNVFGA RNVPQPLESI VTRWGSDRFA RGTYSFVAAE
ARPGDYDLIA APIQNLFFAG EATIATHPAT VHGAYLSGLR AANEVFESMV GSIPIPPTLV
SASTSKKLSS TSIDLTQMDT HMAVGGKRKG DELLPAGTFT RPIKEKDNTL QEAWDAAMWV
RIYDDLGPPP TKPAKANVNS FLLYSGEHWE EVKTRLGEER KKTGKRSKQS ERDQVRVELG
KMWAALTDEE KKPYTDRTNK NREENERLMK EWAVKAADWD KRTWEVKDVW IKEGNSFEEF
CKRKREEDEL MDAADQAKRA KI
//
