ID A0A1L9RZS8_ASPWE Unreviewed; 1071 AA.
AC A0A1L9RZS8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=SWIRM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPWEDRAFT_99436 {ECO:0000313|EMBL:OJJ40432.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ40432.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; KV878209; OJJ40432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9RZS8; -.
DR STRING; 1073089.A0A1L9RZS8; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_99436; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000184383; 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; PF04433; SWIRM; 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:UP000184383}.
FT DOMAIN 145..240
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 924..1004
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 924..1004
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 118126 MW; F1E65F3C6B3D594D CRC64;
MLQFKHYLPN GNSKNGGTHF SLLPPSQNAP RVSQFQNVPP EYPVNNGSRG STDVIDGGSQ
TTDGLSRDLD TDTNHGTPND STTSTSLMSA PSQKKSRSPS TVINVSSSSL SSFVKTVDGN
FDYSQYRPRS SIPSRLSAAV YAQQCITAAY ASRLNPFALH KKEQEALQDY MCHLHVTVYL
NIRNGILRLW TRNPMVSVNK EEALGCAKDY RWMNLASFAY EWLIRNGYIN FGCVEIPMAL
IPPKRARRKD GPVIVVIGAG MSGLGCARHL EGLFNQYRDT STSPRVVVLE GRRRIGGRVY
SHPLRSLQSP NLAPGLVPKA EMGAQIIVGF DRGNPLDQII RGQLALQYHL LRDISTIYDI
DGSPVDEVRD AMDERLYNDV LDRSGFYRHK SVIVPTAEGD RELINSGRDL TTSDGVTVRQ
YEEARAAGTI GQLLPSKRVR RGVGHKTADI KATAAPLADL GPIEENPAVL ACQAMGWNLN
QGVSANESIN LEPIAIASRA QTLGAVLDDG VKQYQRMLPL APKDMRLLNW HFANLEYANA
VNIGKLSLSG WDQDMGNEFE GEHSQVIGGY QQVPYGLWSL PTKLDVRTNK IVSKIAYDPS
GNGKQKTVVH CEDGDSIVAD KVVFTGSLGT LKHQSIKFEP PLPDWKAGAI ERLGFGVMNK
VILVFDQPFW DVERDMFGLL REPKNRDSMV QEDYSANRGR FYLFWNCLKT TGLPVLIALM
AGDAAHQAER TPDAEIIAEV TSQLRNVFKH VAVPDPLETI VTRWATDRFT RGSYSYVAAE
ALPGDYDLMA KPIGNLHFAG EATCGTHPAT VHGAYLSGLR AASEVIDTIL GPIEIPEPLV
PEKGKTTELS TPITAGQKRK EPSSATISTA ATAPAPTPID SSELAAQARS NNSFPTDTAL
REAYDQAMWA AIHAELGPPE PRPAKTGLNP FLLYQKDFWG KARIQCDEAR QASSKNPKAK
AARDEIRQAL GLMWRRASEE EKRPYIEQTE VNRQTNAEVW ERWKRTIAEW EKNTYKVKDR
WCAANPFESW QPTSSPASKR PNRTSTNGNA AAINVPIGVT TNGHTELKQI I
//
