ID I7ZRQ0_ASPO3 Unreviewed; 1519 AA.
AC I7ZRQ0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Chromodomain-helicase DNA-binding protein {ECO:0000313|EMBL:EIT74689.1};
GN ORFNames=Ao3042_09265 {ECO:0000313|EMBL:EIT74689.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT74689.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT74689.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT74689.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) 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:EIT74689.1}.
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DR EMBL; AKHY01000187; EIT74689.1; -; Genomic_DNA.
DR HOGENOM; CLU_000315_29_2_1; -.
DR Proteomes; UP000002812; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 DNA-binding {ECO:0000313|EMBL:EIT74689.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EIT74689.1};
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 267..339
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 367..427
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 465..636
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 767..925
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1519 AA; 172728 MW; 0CA2F2EDB846FBF8 CRC64;
MPRSTSMVIP STSEPSTVMA FANGHPASPA SDTVSFGNEP LASDGDSNMF DSVDNHVVSD
SSPDPDAADE SFNADSPDAE GYEDDSAMED NAKDSSQSSS ENSSSSESGR GTKRKSSSVN
ESDYIRQNPD LYGLRRSGRA RTTRQVAQSL SDSDSDAVAP RSKRRRPVAS QQTSKRPSRS
ATQSSFSEDS ETSESEYGGS RSRTSKTKRR RQQASASAPS HAEVRFSTRN AARVSTYNED
DDDSMFEDDP DELMQNYWVN AVEDDRPAVD IVLNHRLKAG VDSSNTDLDR HDFEFYIKWQ
GKSHYHATWE TAESLANCRS TRRLDNYIRK VLYEDIRLRQ DEDVAPEDRE KWNLDRERDV
DAIEDYKQVE RVIATREGDE GTEYLVKWKR LFYDSCTWEN EELVSEIAQC EIDRFLNRSS
RPPVSDKSES NPASRKSFEA IKGTPSFLRN GELKEFQVKG VNFMAFNWVK NRNVVLADEM
GLGKTVQTVS FINWLRHVRR QQGPFVVVVP LSTMPSWAET FDNWTPDLNY VVYNGNEAAR
TVLREHELMI DGNPRRPKFN VLLTTYEYVL LDSSFLSQFK WQFMAIDEAH RLKNRESQLY
AKLLEFRSPA RLLITGTPIQ NNLAELSALL DFLNPGLVDI DADMDLNAEA ASQKLAELTK
AIQPFMLRRT KSKVESDLPP KVEKIIRVEL SDVQLEYYKN ILTKNYAALN DGAKGQKQSL
LNIMMELKKA SNHPFMFPNA EAKILDGSTR REDVLRAMIT SSGKMMLLDQ LLAKLKRDGH
RVLIFSQMVK MLDLLGEYME FRGYTYQRLD GTIPAASRRL AIEHYNAPGS SDFAFILSTR
AGGLGINLMT ADTVVLFDSD WNPQADLQAM ARAHRIGQTR PVSVYRLVSK DTVEEEVIER
ARNKLLLEFI TIQRGVTDKE ASEIQNKMAR NGISITEPNS TEDISRILKR RGQRMFEQTG
NQEKLEQLDI DSVLANAELH QTEQAEDIQA DGGEEFLKAF DYVDIKVDDL TWDDIIPKEQ
LEEIKAEEKK KADERYLAEV IEQNRPRKRN VPGDERDSRE ERKAKRQARA QVSLDDGDES
DSNTQLDPKR PLIEKEYRHL LRAFLRYGDI DDREEDVIRE ARLLDRDRET VKGALREITE
KASSLVREDI EKMEALEHAG KMPTKKEKKA VLFDLHGVKR LNAYTIVERP VEMRILKEAT
NAVSDFKNFR VPEATKAADY SCPWGAREDG MLCIGIIRHG YGAWAQIRDD PDLALGDKFF
LEEHRVERKN ERLNAEDKST KSPGAVHLVR RADYLLSVLK DKVTNGSSVN AKRAVENHHR
NNRKGSRPHA SASVSASPAP SIPRKGHREM DRSRHRSHTH GARDSVERHH TPNYDSRPRS
FHESERARHR TSDASSEDVR RRKNSENGYS AGKEDVARLF FKPIREDLRK VSAVTKENYP
NKAERASELR NLLRKIGEFI DGTLKGQSSV HSLETRLWHF VADNHWPNKE AGGAKLQEMY
RKLMAAQKVA AAAPASNGS
//
