ID A1D352_NEOFI Unreviewed; 1523 AA.
AC A1D352;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Chromodomain helicase (Chd1), putative {ECO:0000313|EMBL:EAW22845.1};
GN ORFNames=NFIA_015380 {ECO:0000313|EMBL:EAW22845.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22845.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS027688; EAW22845.1; -; Genomic_DNA.
DR RefSeq; XP_001264742.1; XM_001264741.1.
DR STRING; 331117.A1D352; -.
DR EnsemblFungi; EAW22845; EAW22845; NFIA_015380.
DR GeneID; 4591735; -.
DR KEGG; nfi:NFIA_015380; -.
DR VEuPathDB; FungiDB:NFIA_015380; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000006702; 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; IPR041150; Cdh1_DBD.
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; PF18196; Cdh1_DBD_1; 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:EAW22845.1};
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:UP000006702};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 262..335
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 363..423
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 461..632
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 763..921
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 16..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 173009 MW; 81E9555BE9E3C016 CRC64;
MVIPSPPDNI ANMALSNGLS PSLTSNSPAV NGELADNNAG YNLSEQSNNF TSSESSPDAE
MEDESYHSGS PDAEAVGSYS ATDSSEKGSS PSSIGNSSSS EIKRGIKRKS SSLSESDFIR
QNPDLYGLRR SGRARTTRQV VQSTSSESES VVRVSRTKRR RPVASQRSSK RPSPPASQSS
YSAESDDDEY GGPSRTSKAK RRRMLQPASN KEPSHAEIRF STRTASRRVS NYNEDDDDDM
FLDEPDEVMD NYQANTVEDD RPAVDVVLNH RPKEGVSPGD NDVDEHSFEF YIKWQEKSHY
HATWETYKSL IDNCRGTRRV DNYIRKVLSE ELRMNHDGDA LPEEREKWNL DRERDVEAIE
DYKQVERVIA MRDGDEGTEY LVKWKRLFYD SCTWESESLV SEIAQREVDR FLDRSSHPPS
SDKTEMNPAT RKPFEPIKGT PSFLQNGELK DFQVKGVNFM AFNWVKNRNV VLADEMGLGK
TVQTVAFIAW LRHVRRQQGP FIVVVPLSTM PSWAETFDNW SPDLNYVVYN GNEAARTMLK
DYELMIDGNP RRAKFNVLLT TYEYVLQDST FLSQFKWQFM AVDEAHRLKN RDSQLYQKLL
EFRSPARLLI TGTPIQNNLA ELSALMDFLN PGVIDVDVDM DLNAEAASQK LAALTNAIQP
YMLRRTKSKV ESDLPPKTEK IIRVELSDVQ LEYYKNILTK NYAALNDGAQ GQKQSLLNIM
MELKKASNHP FMFPNAEAKI LEGSTRREDV LRALITSSGK MMLLDQLLAK LKRDGHRVLI
FSQMVKMLDL LGDYMESRGY SYQRLDGTIP AASRRLAIEH FNAPGSSDFC FLLSTRAGGL
GINLMTADTV ILFDSDWNPQ ADLQAMARAH RIGQTRPVSV YRLVSKDTVE EEVIERARNK
LLLEFITIQR GVTDKEASEI QNKMARSGIN VSEPNSTEDI SRILKRRGQK MFEQTGNQQK
LEQLDIDSVL ANAELHQTEQ AEGIQADGGE EFLKAFDFVD IKVDDLTWDD IIPKDQLDEI
KAEEKRKADE RYLAEQIEMS RPRKRNVPAD GQDTREERKA KRRARAQVTV DEGNSSDESR
PHLDPKRPLN HKEIRHLYRA LVRYGDINER TEEFLREARL MDRDRETIVA VLREMSDMAA
KLIREDDAKM EALEKAGKMV TKKERKAVLF DFKGANRLNA HHIVDRPRDL RILRQVTSSV
ADVKSFRIPE ATKAADYSCS WGAREDGMLC VGVARHGWGA WTQIRDDPEL GLGDKLFLEE
HRVEKKNERA NADDKTTKTP GAVHLVRRVE YLLSVLRDKL TNGTNVSARR AVENHHRNHR
STARTNVSAS VSASPAPSIA RKGHREADRS RHRSQTHGAR DSVERNHTPG RDSRPKSGQE
NDRRRKLSDA SSEDIRRRKP SERKSSDNGN SDEMLRLLFK PILSSLERVS GLTRDSMTSK
ARRASELRNL LGYIGGFIRK TLKGENYMPS LEIRLWEYVA INYWPNKEAG GRQLQTMYQK
IVAANNATTN KDGSASTPYS ARD
//
