ID G0SCM4_CHATD Unreviewed; 1109 AA.
AC G0SCM4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=SWM histone demethylase complex-like protein {ECO:0000313|EMBL:EGS19150.1};
GN ORFNames=CTHT_0057750 {ECO:0000313|EMBL:EGS19150.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS19150.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; GL988045; EGS19150.1; -; Genomic_DNA.
DR RefSeq; XP_006696095.1; XM_006696032.1.
DR AlphaFoldDB; G0SCM4; -.
DR STRING; 759272.G0SCM4; -.
DR GeneID; 18259813; -.
DR KEGG; cthr:CTHT_0057750; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_1_2_1; -.
DR OMA; WCAENPF; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000008066; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 1.
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 Methyltransferase {ECO:0000313|EMBL:EGS19150.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transferase {ECO:0000313|EMBL:EGS19150.1}.
FT DOMAIN 226..321
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 958..1034
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 958..1034
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 122049 MW; 4928783AAC2121F9 CRC64;
MRTSGVAAAS STSSSSSSPA ALGKQPVSSS TATCVSPVSS PSDDTESPLP SKSSAAPTTA
LSQRESTNNS EEIAPEIVVW TGQMDSMIVD SPETATPVSP SSGPAAASEE KSVDAIPTSP
SQPTSAPQLS STLTVPQQGE TSEEKRPSVT SSSLSTLSDQ SDLSSVPLSV SSKATTPVDT
DSSREAPAPG APRLTQRATS PRRKWDVRPK VSIPPDLTLS EYALQCVAAA EASRLNPYAL
HQEEYLMLRD HISHAQVTTY LNIRNGILRL WVCNPRIAVT REEAVGCAKD PRWFDVASVC
YDWLVRRGYI NFGCVEIRPS RHKHAENSEL LTKTKEKKKR RTVVVIGAGM AGLGCARQLE
GLFAQYANRF RKMGEEPPEV IVLEARNRVG GRVYSRPFHT RPKHIPEHFK GKRFTAEMGG
MIITGFERGN PINILLRAQL GLSYHYLKPE TILYDSNGKP VDLHRDQLVE NLYNDCLDRV
SEYKYKPPAT KLIEGNKDLI DEGRDSSAET HKTIRQAEEA AAAQPHAAPV SEQNMAPQVN
LVPVSSDRAT GRIHNEPGTP AALNAARKAK LMGWTLKQGV SEDADIDLQA AAIEPGATLG
SVTDKVIMQY KDILDLTAQD FRLMNWHIAN LEYSNATNYH QLSLPGWDID AGNEWEGSHS
MVIGGYQSVP RGLLMIPTPL NLRQKSPVCK ITYTSSSPTG PAIVECEDGY KVEADCVVNT
IPLGVLKHGS VKFEPPLPQW KAEAIERLGF GVLNKVILVY KEPFWDENRD IFGVLRNPPN
RHSTDQKDYA SQRGRFFQWF NVSKSSGLPV LIALMAGDAG YDTEQTCNDD LIAEATDILR
RVYGSRVPYP VEAVITRWAS DKFARGSYSS AGPDMKADDY DTMARPVGNL YFAVLDALIG
PIPVPTPLIL PKDLKRKAPS SSSISSPADI YQARLRTHEA LLHEHLVSRL GPCPTLPPKP
PTNAYMYYSK AHYDEARRRL EAGRRPGKGK PSANEVRVMS SKMWRDASDE DKKPYVEMAE
EAKRKWNETV EKWRKDVEEW EAKAEKERQE WEKTNPPPPQ PSKTEEMLGE GRRTKMRVVE
GMYKEESESE GFGGGTGSGS DVEMGGAWG
//
