ID A5DW13_LODEL Unreviewed; 1500 AA.
AC A5DW13;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Chromo domain protein 1 {ECO:0000313|EMBL:EDK43371.1};
GN ORFNames=LELG_01549 {ECO:0000313|EMBL:EDK43371.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43371.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43371.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH981525; EDK43371.1; -; Genomic_DNA.
DR RefSeq; XP_001526721.1; XM_001526671.1.
DR STRING; 379508.A5DW13; -.
DR GeneID; 5234044; -.
DR KEGG; lel:LELG_01549; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; A5DW13; -.
DR OMA; YLWHRNE; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000001996; 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; 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; 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};
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:UP000001996};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 216..291
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 319..384
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 423..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 732..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 20..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..134
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1500 AA; 171641 MW; D5743E6336D43AEB CRC64;
MVKPMVIEEA SLNPELYGLR RSHRERKGPA IVESDSETED FEPRKKRKQV NNDDYYDDDV
DDDDDDLANE DGDEDLGGED DFIDDDDDDD DDFTIGTKLK KKLSNSKKKK PQLHLQRKSG
SVRSRKKKKT SLSTLKSKSK SSTPAYPIQE LRFSTRNSKI VNYNIDDDND DDLLESDDYD
EKNGKANEGG EYDEDDDDEE DGANGDYYYY QQAIEPEIER GIDFVMDHKL NPDNAEVTNE
PKLDYLFKIK WSDASHMHNT WETYKDLKEY KGFRKVDNYI KQFIIYDNEV RNDPLTTKED
IEAMDIERER RRDEQEEYTH VERIVDSQRV EKDDSQTRLE YFVKWKRLYY DECSWEDAEE
IAKIAPEQVK KFQQRLNSKI FPHQSATYSV VNRPKFEKLT KQPIFIKNGE LRDFQLTGLN
WMAFLWSRNE NGILADEMGL GKTVQTVAFL SWLIFSRRQY GPHLVVVPLS TIPAWQETFE
KWAPDVNCVY YLGNGEARKT IREYEWYTTG GSGGGRKPKF NILLTTYEYI LKDRAELGSF
KWQFLAVDEA HRLKNAESSL YESLKSFKCA NKLLITGTPL QNNMKELAAL CDFLMPGKFS
IEQEIDFDTP DEDQELYIKD LQKKINPFIL RRLKKDVETS LPGKTERILR VELSDIQTDY
YKNIITKNYA ALNAGNKGSQ ISLLNVMSEL KKASNHPYLF DGAEERVLSR AGSYSRENVL
KGMVMSSGKM VLLEQLLTRL KKEGHRVLIF SQMVRMLDIL GDYMSIKGYA FQRLDGGIPS
SQRRISIDHF NAPDSKDFAF LLSTRAGGLG INLMTADTVI IFDSDWNPQA DLQAMARAHR
IGQKNQVLVY RFVSKDTVEE QILERARKKM ILEYAIISLG ITDPSAKKNS KAEPSGSELS
QILKFGAGTM FKDNDNQQKL ENLNLDDVLN HAEDHVTTPD LGESNLGSEE FLKQFEVTDY
KADIEWDDII PQEELTKLKD EEKRRADEQF LQQQIAMYSR RTAAVRKLEN GSTNPSDYED
SGEDTKPSGS RRRGTTTRTA MDHQLSEKEI RGIYRSILKW GDLHGKWEQL VEEGTISNKN
PVYIKHAYNE IVSISKKMVK EEETRRAQAL AELERKAKEQ RENSLKDGDS NGNNNQTALW
IAKKKEKKAV LFEYQGVKNI NAELVLNRPL DMKALDAIVP NGDPLKIQLP KQPKAVQSWS
CEWTAKDDSM LLAGVYKFGY GSWIQIRDDP VLGLQNKLFL ETPASSKVAN SSGTNAAASG
SEVAKDGKDG KDGKEAKDTK KVPNAVHLGR RVDYLFTLLR ESDDNNNGSG PAPAPVPKRR
VKRPDALNGK SSKKMKSETP DISVRPIKPK PMNLQLHQHL HQLHKASSKS PKLESSKLHQ
PHSAPTVSTM RLHDLEYESM DEASCKATMH PVSKSLHKLH RGSKGLDKHQ WATVLKEELI
RVGDHIHSEV SKTKQAEEAT TLLKHLWSFA GLYWPSKVPS SKISEMYKRL TTKAKAPKSE
//
