ID W1QD04_OGAPD Unreviewed; 1384 AA.
AC W1QD04;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative ATP-dependent chromodomain helicase {ECO:0000313|EMBL:ESW98470.1};
DE EC=3.6.1.- {ECO:0000313|EMBL:ESW98470.1};
GN ORFNames=HPODL_04097 {ECO:0000313|EMBL:ESW98470.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW98470.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESW98470.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) 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:ESW98470.1}.
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DR EMBL; AEOI02000008; ESW98470.1; -; Genomic_DNA.
DR RefSeq; XP_013934353.1; XM_014078878.1.
DR STRING; 871575.W1QD04; -.
DR GeneID; 25773528; -.
DR KEGG; opa:HPODL_04097; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000008673; Chromosome V.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17993; DEXHc_CHD1_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ESW98470.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ESW98470.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 179..242
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 270..335
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 373..544
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 679..840
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 19..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 918..947
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1032..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 39..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 158202 MW; 157BE48D938EF692 CRC64;
MSTDIRSEIE SNPELYGLRR SGRARSKPLG VAEFSDEEDE DYTAKKKTRQ KRAYSDDEAA
LDDDMLDSDD SEYGGKKKRG RPRKKKQPAY KSSEQFPGFT ELRLSNRSNR AVNYALDADD
DEFLESEDED GEAYGEYYSA EPEEVAPEEG IDQVLDHRVI GEESDVSDDD DTKFEEHKKR
VQDVLANGDP KTDFEYMIKW TNTSHLHNTW ETYDAIKSRN VKGMKKVDNY INLYIINDRE
IRKDPFVTRE DIEQMELENE TRRENLQEYK KVERIVDSER VTLETGESDL RYLVKWKRLN
YDECTWESGS EIAPLAPQEV TKFQNRQNSK ILPGLSASYG SNRPRFEKLT SQPLFIKNGE
LRDFQLTGLN WMAFLWSRNE NGILADEMGL GKTVQTVSFL SWLIYARRQN GPHLVVVPLS
TVPAWQETFD KWAPDVNVIY YMGNTKSRKA IRDYEFYVGG NRKKVKFNVL LTTYEYILKD
RAELGSFKWQ YLAVDEAHRL KNAESSLYES LSEFKVANRL LITGTPLQNN LKELAALCNF
LMPGKFQIDQ EIDFDTPNAE AEGYIKALQA EIKPFILRRL KKDVETSLPG KTERILRVEL
SDIQTEYYKN ILTKNYGALN QGPRGSQISL LNIMAELKKA SNHPYLFDGV EEHVLAKVGS
HSRENILKGL IMSSGKMVLL DQLLNKLHRD GHRVLIFSQM VRILDIIGDY LQLKGHSFQR
LDGTISSHKR RLAIDHFNAE GSKDFVFLLS TRAGGLGINL MTADTVIIFD SDWNPQADLQ
AMARAHRIGQ KNHVMVYRFV SKDTVEEQVL ERARRKMILE YAIISLGITD NNKSKTKAEP
TSGELSEILK FGASNMFKSN DNQKKLENLD LEDVLNHAED HVTTPDLGES NLGGEEFLKQ
FEVTDYKADV DWDDIIPEDE LKKIKEEEEK RKEEAFLQEQ IEMASRRRLA AVKKPEYDEQ
DDDEGPSRRQ KKLDMNNLTE SQIRNVYKAI LRYGDISERL EELVADGTLP NKNIKILDQC
QREIMETSSR LVAEYEAKRA EELKELEAKA MEEKEQLAKL PPRADGQPHP TPAMQLYSAR
KRDKKAILFD YKGVKNMNAE VVLNRPQELK LLQSVIPADD PMKFKLTKEP KPVNGWSCKW
TIKQDTMLLI GVYKFGYGAW TQIRDDPILG LQNMMYLETP PAGASKEEKE KMSKRIPASI
HLVRRTDYLL GFLKEIQSNA GSHPEPKEPK KNSRPKKTAK KSSTPDVESK SGTPKPAGSG
ASSPTSSQPT LYQVMKNNKS SSPEAQKQKK PASSGAKSEH DLLKPVDKDL KIWESKGKGL
DKAEWGSKLK SSLISIGNQI EKVSKNDAKL NGKLWAMAQK SWPNAGVSSE LIKKMYLKKV
GQHK
//
