ID A0A0L1ITV9_ASPNO Unreviewed; 1512 AA.
AC A0A0L1ITV9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Chromodomain helicase (Chd1) {ECO:0000313|EMBL:KNG82919.1};
GN ORFNames=ANOM_008297 {ECO:0000313|EMBL:KNG82919.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG82919.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG82919.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG82919.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG82919.1}.
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DR EMBL; JNOM01000305; KNG82919.1; -; Genomic_DNA.
DR RefSeq; XP_015403842.1; XM_015553553.1.
DR STRING; 1509407.A0A0L1ITV9; -.
DR GeneID; 26810101; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KNG82919.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 260..332
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 360..420
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 458..629
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 760..918
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 171952 MW; 4CED5DFEF9B7BAB1 CRC64;
MVIPPTSEPS TMMAFANGHP ASPASDTASF RNEPLASDGD SNMFDSVDNH VVSDSSPDPD
AADESFNADS PDAEGYEDDS AMEDNAKDSS QSSSENSSSE FGRGTKRKSS SVNESDYIRQ
NPDLYGLRRS GRARTTRQVA QSLSDSDSDA VAPRSKRRRP VASQPPSKRP SRSATQSSFS
EDSETSESEY GGSRARTSKA KRRRQQASAS EPSHAEVRFS TRNAARVSTY NEDDDDSMFE
EDPDDLMQNY WVNAVEDDRP AVDVVLNHRL KAGVDSSNTD LDRHDFEFYI KWQGKSHYHA
TWETAESIAN CRSTRRLDNY IRKVLYEDIR LRQDEDVAPE DREKWNLDRE RDVDAIEDYK
QVERVIATRD GDEGAEYLVK WKRLFYDSCT WENEELVSEI AQCEIDRFLD RSSRPPVSDK
SETNPASRKS FEAIKGTPSF LRNGELKEFQ VKGVNFMAFN WVKNRNVVLA DEMGLGKTVQ
TVSFINWLRH VRRQQGPFVV VVPLSTMPSW AETFDNWTPD LNYVVYNGNE AARTVLREHE
LMIDGNPRRP KFNVLLTTYE YVLLDSSFLS QFKWQFMAID EAHRLKNRES QLYAKLLEFR
SPARLLITGT PIQNNLAELS ALLDFLNPGM VEIDADMDLN AEAASHKLAE LTKAIQPFML
RRTKSKVESD LPPKVEKIIR VELSDVQLEY YKNILTKNYA ALNDGAKGQK QSLLNIMMEL
KKASNHPFMF PNAEAKILDG STRREDVLRA MITSSGKMML LDQLLAKLKR DGHRVLIFSQ
MVKMLDLLGE YMEFRGYTYQ RLDGTIPAAS RRLAIEHYNA PGSSDFAFIL STRAGGLGIN
LMTADTVVLF DSDWNPQADL QAMARAHRIG QTRPVSVYRL VSKDTVEEEV IERARNKLLL
EFITIQRGVT DKEASEIQNK MARNGISITE PNSTEDISRI LKRRGQRMFE QTGNQEKLEQ
LDIDSVLANA ELHQTEQAEE IQADGGEEFL KAFDYVDIKV DDLTWDDIIP KEQLEEIKAE
EKKKADERYL AEVIEQNRPR KRNVPGDGRD SREERKAKRQ ARAQVALDDG DESDSNTQLD
PKRPLIEKEY RHLLRAFLRY GDIDDREEDV IREARLLDRD RETVKAALRE ITEKASSLVR
EDVEKMEALE HAGKMPTKKE KKAVLFDLHG VKRLNAYTIV ERPAEMRILK EATNALSDFR
NFRVPEATKA ADYSCPWGAR EDGMLCIGII RHGYGAWAQI RDDPDLGLGD KFFLEEHRVE
RKNERLNAED KSTKSPGAVH LVRRADYLLS VLKDKVTNGA SVNAKRAVEN HHRNNRKGSR
PHASTSVSAS PAPSISRKGH REMDRSRHRS HTHGARDSVE RHHTPNYDSR PRSIHESERA
RHRTSDASSE DVRRRKNSEN GYSAGKEDVA RLFFKPIRED LRKVSAVTKE NYPSKAERAS
ELRNLLRKIG EFIDGTLKGQ GSVHALETRL WHFVADNHWP NKEAGGAKLQ EMYRKLMAAQ
KVAAAAPASN GS
//
