ID A0A1L9TDQ1_9EURO Unreviewed; 1150 AA.
AC A0A1L9TDQ1;
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=ASPSYDRAFT_1061168 {ECO:0000313|EMBL:OJJ57560.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ57560.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
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; KV878588; OJJ57560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9TDQ1; -.
DR STRING; 1036612.A0A1L9TDQ1; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_1061168; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000184356; 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:0008152; P:metabolic process; 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; 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:UP000184356}.
FT DOMAIN 170..265
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 936..1016
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 936..1016
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 100..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 126085 MW; A1046F56476CCB0F CRC64;
MMDVTASMAA RPPAGYSSQA SVFRQYIPSN SIGSNGYSSK QPLPLQPNGA RFEYGMTNPY
SPQNHVLAAG PQEPRNVPND INSGNKNMDY LTYKLVTETN ASTPNDSTTT SFPSASSNGK
STPPSTIVNF NTSSASTASI RSDESPDYSK YRPRSSIPPR LPAPIYAQQC VVAAYSSRLN
PYALHRKEQE ALQDYLCHLH VTVYLNIRNG ILRLWTRNPM VSVTKEEALG CAKDYRWMNL
ASFAYEWLVR NGYINFGCVE IPPSLALPKK GRRREGPVIV IIGAGMAGLG CARQLEGFFN
HYHDSYSSPR VILLEGRRRI GGRIYSHPLR SLQSSTLPAG LVPKAEMGAQ IVVGFEHGNP
LDQIIRGQLA LSYHLLRDLS TIYDVDGSPV DEVRDATAES LYNDVLDRSG AYRHKSVITP
TAEGDRELID SGRDITTSDG VTIKQYEEAR AAGTIGLLLP AKRLRRGVGH KTADIKSAAA
PAADPEQPEE NPATVACQAM GWELNEGFTP NQTVNLDSVA RASRTQNLGN AMDEGVRQYQ
EMLPLTPKDM RLLNWHFANL EYANATNIGN LSLSGWDQDM GNEFYGPHSQ VVGGYQRVPY
GLWQHPTKLD VRTNKIVSRI TYDAAENHKT VVQCEDGDSI AADIVVYTGS LGTLKHRSVQ
FSPPLPEWKL GAIDRLGFGV MNKVILTFEQ PFWDTERDMF GLLREPNNRE SMIQEDYAAN
RGRFYLFWNC MKTTGLPVLI ALMAGDAAHQ AERTSDAEII AEVMSQLRNV FKLVAVPDPL
ETIITRWASD KFTRGTYSYV AADALPEDYD LMAKPIGNLY FAGEATCGTH PATVHGAYLS
GLRAASEIID SILGPIPIPN PLVPEKNKTT NPSFSNGTPL GTPHIPLDTG TPKIPIQQQP
HPPTSNYSES ASRASYDQAM LAAIYTETGP PVPRPARTGL NPFLLYQKDF WPKARAECDA
THQFETSNPS AKAPRDAVRA ALGLMWRQAP EEIKRPYLEQ AEVNRQTNAE IAAKWKRDNA
EWEKKSAAAK KRWREENPFE RWLAMEAGEP PSKKANNSSS VASSSLKRDE AGAPMATATA
TSSGLPSHLA GTGMHNGAVN GAGNIANTPT TLTITNGIAS APVTNTFPFS NTQPTSLPRP
TNQPNHVTSH
//
