ID A0A0J9XD92_GEOCN Unreviewed; 1410 AA.
AC A0A0J9XD92;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Similar to Saccharomyces cerevisiae YER164W CHD1 Nucleosome remodeling factor that functions in regulation of transcription elongation {ECO:0000313|EMBL:CDO55496.1};
GN ORFNames=BN980_GECA11s02111g {ECO:0000313|EMBL:CDO55496.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO55496.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO55496.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO55496.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCBN010000011; CDO55496.1; -; Genomic_DNA.
DR STRING; 1173061.A0A0J9XD92; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18664; CD2_tandem_ScCHD1_like; 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; 1.
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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 179..252
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 276..341
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 379..550
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 693..852
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1410 AA; 162080 MW; 351A6DE3BEA19E61 CRC64;
MTTRTSSEYY ENPSLYGLRR STRAHNPPER FVVEEASRSK YADYSSDSDS TSTQKTKKKP
KTRKPKIKDD DFYEDYNDNV KSASEVEEED EEDDDEAYAS SKRARLKELA KSKKRRKLGS
NSEEESSGVY TPPTRFSTRN NKVINYNIDH QDDDADLMET DDENGVDYNI QYESEQPADS
IDLVVDHRQI EGLLGRDPKN DIEYLIKWQS SSHLHKTWEL YENIKYRKGI KKVDNYIRNF
VNPENLYLSD PAKYQEEYEA FSIELDKRRE EYRVFTIVER IIAQKRVSAD DGSTHMEYYV
KWKGLTYHLC TWEDAELIAK QAPAQVDHFQ NRLSSQIAPY QSTNYGSNRP KFEKLTSQPS
FIKGGELRDF QLTGLNWMAF LWSRNENGIL ADEMGLGKTV QTVAFLSWLV YARKQNGPFL
VVVPLSTISA WQETLELWAP DLNCIVYNGN DESRKIIRQF EFYANNNTKR PKFNVLLTTY
EYAIRDKTEL GSLKWQFLAV DEAHRLKNPE SSLTISLGEF RITNRLLITG TPLQNNIKEL
ITLIKFLKGG QVNPALQAFE EIDLDNQQDS RNQEELIRQL HKSLQPFILR RLKKDVEKSL
PSKSERILRV EMSDMQTEYY RNIISRNYEA LNAGSSGSSQ MSLLNIMVEL KKVSNHPYLF
PTAEERYIES NGNNRARDVI LKGMIMNSGK MVLLDKLLTR LKRDGHRVLI FSQMVRMLDI
LADYMAIKGY QYQRLDGTVA SYTRKTLIDH YNAPGSQDFV FLLSTRAGGL GINLMTADTV
ILFDSDWNPQ ADLQAMARAH RIGQKNHVMV YRFVSKDTVE EEILERAKRK MVLEYAVISM
GITNKKVTND LEKDASSAEL SAILKFGAGN MFKKNNNQKK LEEMNLDDVL NHAEDHVSAE
DTLAQSHLGG DEFVKQFEVT DFKADVEWDD IIPAEELEKI KAEDQKRKDE EFLQEQLHLY
GKRKAALKAS GQPVSDDESG NDDDQPKSRS RPKPRRKDDA LDSTTLSERE VRQLYKAILR
YGDLSKMWDK LFQDGSLTNR NRELVQKTYN DLIATARSEV DAEMQRRAST AKVSDGTPVP
RRKEKKAILF EFGGVKSINA EQLLQRPVDM EVLRKTVPSE NQSAFRINRN VKPVHGWTCE
WGTKEDSMLL VGVKKYGYGA WTNIRDDPIL GMGDKMFLEE HRVEKKQQRE EGDKAAGPKM
PGSVHLCRRV DYLVSVLQEE DVEPTKRSRN RRKETSRPDS ANDRTQSPLP TSSSPSSTQT
PNHRANSIGP KTAKRSPSAV GNSANSGITP SKSTNHNKEE SQDPEEEAVE YESMDERECK
AQLHPVRHSL RTLKKGNKGL DRDEFLSILK RELITVGTFI DEQVQEAKDG VDKEKLRKHL
WSFAGYFWPR RVPSKKIMAM YKKMKGSASA
//
