ID Q2HDT7_CHAGB Unreviewed; 1010 AA.
AC Q2HDT7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=SWIRM domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHGG_01617 {ECO:0000313|EMBL:EAQ93382.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ93382.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; CH408029; EAQ93382.1; -; Genomic_DNA.
DR RefSeq; XP_001220838.1; XM_001220837.1.
DR AlphaFoldDB; Q2HDT7; -.
DR STRING; 306901.Q2HDT7; -.
DR GeneID; 4386237; -.
DR VEuPathDB; FungiDB:CHGG_01617; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR InParanoid; Q2HDT7; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000001056; 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 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:UP000001056}.
FT DOMAIN 129..224
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 892..968
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 892..968
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 110616 MW; 4B3B8C50EDDBCDF7 CRC64;
MEVDSPESAA PTTPPTPTVE GKTATPVPIS ETTHPPAALS NPIRTETPGK ESSLSSLSSM
SDQYDLSSSV PSGSSKATTP IDGDSSREAL AAGVPRSSQS IDSPRRKWDV RPKVSIPPDL
PLSEYAMQCV AAAEASRLNP YSLHQEEYLM LRDHISHAQV TTYLNIRNGI LRLWVRNPQI
PVTREEAVGC AKDSRWFDVA DVCYDWLVRR GYINFGCVEV RSSRKHAKQN DSSQRKQKTV
VVIGAGMSGL GCARQLEGLI AQYGKKFRSL GEEPPRVVVL EGRDRIGGRV YSRAFKSRPK
QTPDLFEGKR YTAEMGGMII TGFERGNPLN ILLRGQLGLA YHILRPETTL YDPNGKPVDL
HRDQLVENLY NDCLDRVSEY KFKQPASKLI EANRDLIDEG KDSSAETHKT IRQMEESAAA
QPYAAPVSEQ NIAPRVNLVP VSTDRATGKI HTEPGTPGAL KAAHKAKMIG WTLKQGVSDD
ADLDIETATK EPGATLGSVT DKVIAQYKDL LDLTAQDFRL MNWHIANLEY SNATNYRQLS
LQGWDIDAGN EWEGGHSMVV GGYQSVPRGL MHLPTSLNVK QKSPVSNITY TSGGTTGPAT
VTCEDGSIVE ADFVVSTIPL GVLKHGNVKF EPPLPSWKSD AIDRLGFGVL NKVILVYKEP
FWDEDRDIFG VLRSPTIRHS LDQKDYASQR GRFFQWFNVT KTSGLPVLIA LMAGDAGFDT
EQTCNDDLVA EATSILRSVY GSRVPHPIEA VVTRWASDKF ARGSYSSAGP DMKADDYDTM
ARPIGNLFFA GEHTCGTHPA TVHGAYLSGL RAASEVLDAM IGPIHVPTPL ILPRDHGTKR
KASSLLEGTG HPNNPNTNTT NKDSAQARLE AYEARLWEHI TTQLGPRPLP PAKPATNAYI
FYSKAHYDDA RARLEAARRP GKGKPSANEV RVMNAKMWRD ASDEVRRPFL EAAEEQKRAH
AAALEAHKAA AAAWDAMAIV VRRNWVAENP EEGEGSGAGG GGFEDVKNEF
//
