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Database: UniProt
Entry: J5S0H3_SACK1
LinkDB: J5S0H3_SACK1
Original site: J5S0H3_SACK1 
ID   J5S0H3_SACK1            Unreviewed;      1468 AA.
AC   J5S0H3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=CHD1-like protein {ECO:0000313|EMBL:EJT43386.1};
GN   Name=YER164W {ECO:0000313|EMBL:EJT43386.1};
GN   Synonyms=SKDI05G2450 {ECO:0000313|EMBL:CAI4060619.1};
GN   ORFNames=SKDI_05G2450 {ECO:0000313|EMBL:CAI4060619.1}, SKUD_170203
GN   {ECO:0000313|EMBL:EJT43386.1};
OS   Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS   NBRC 1802 / NCYC 2889) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT43386.1, ECO:0000313|Proteomes:UP000002753};
RN   [1] {ECO:0000313|EMBL:EJT43386.1, ECO:0000313|Proteomes:UP000002753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC   {ECO:0000313|EMBL:EJT43386.1};
RX   PubMed=12775844; DOI=10.1126/science.1084337;
RA   Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA   Waterston R., Cohen B.A., Johnston M.;
RT   "Finding functional features in Saccharomyces genomes by phylogenetic
RT   footprinting.";
RL   Science 301:71-76(2003).
RN   [2] {ECO:0000313|EMBL:EJT43386.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43386.1};
RA   Cliften P.F., Johnston M.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000002753}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753};
RX   PubMed=22384314; DOI=10.1534/g3.111.000273;
RA   Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA   Rine J., Johnston M., Hittinger C.T.;
RT   "The awesome power of yeast evolutionary genetics: New genome sequences and
RT   strain resources for the Saccharomyces sensu stricto genus.";
RL   G3 (Bethesda) 1:11-25(2011).
RN   [4] {ECO:0000313|EMBL:EJT43386.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT43386.1};
RA   Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA   Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CAI4060619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4060619.1};
RA   Byrne P K.;
RL   Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; OX365900; CAI4060619.1; -; Genomic_DNA.
DR   EMBL; AACI03000838; EJT43386.1; -; Genomic_DNA.
DR   STRING; 226230.J5S0H3; -.
DR   HOGENOM; CLU_000315_29_2_1; -.
DR   Proteomes; UP000002753; Unassembled WGS sequence.
DR   Proteomes; UP001162087; Chromosome 5.
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; cd18665; CD1_tandem_CHD1_yeast_like; 1.
DR   CDD; cd18664; CD2_tandem_ScCHD1_like; 1.
DR   CDD; cd17993; DEXHc_CHD1_2; 1.
DR   CDD; cd11660; SANT_TRF; 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; IPR009057; Homeobox-like_sf.
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; SSF46689; Homeodomain-like; 1.
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};
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:UP000002753};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          195..257
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          285..350
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          388..562
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          699..860
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          21..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          973..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1218..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1057..1095
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        42..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..85
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1468 AA;  168256 MW;  A6AC90CE8A15265B CRC64;
     MAAKEISTEV LQNPELYGLR RSHRAATHQQ NYFNDSDDDD DEENIKRSRR KRTTTIEDEE
     DNFEDEEDQD VSEEDEVEEN FEEDDNYYGS PVKKSRSKSN SKMKFKSSSK PKYESEKLPI
     VKIPTRFSNR QNKTINYNVD YSDDDLLESG DDYGSEEGLS EESTYEASAN SQLEDFHGID
     IVINHRLKTS LEESKVLERA VPGLNECREN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK
     RLDNYCKQFI IEDQQIRLDP YVTAEDIEVM DMERERRLEE FEEFHVPERI IDSQRSSLED
     GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKQFQN RENSKILPQY SSNYTSQRPR
     FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF
     ARRQNGPHII VVPLSTMPAW LDTFEKWSPD LNCICYMGNQ KSRDTIREYE FYTNPQAKGK
     KTMKFNVLLT TYEYILKDRA ELGGIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI
     TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDAEQE EYIHDLHRRI QPFILRRLKK
     DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN
     HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM
     VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL
     MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE
     YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED
     HVTTPDLGES HLGGEEFLKQ FEVTDYKADV DWDDIIPEDE LKKLQDEEQK RRDEEYVKEQ
     LEMMNRRDNA LKKIKSSVNG DGTATNSDSD DDGTSRSSRR RIRTNDMDSI GEAEVRALYK
     AILKFGDLKE ILDELIADGT LPVKSFEKYG ETYDEMIEKA SECVREEEKN RREALEKLEK
     DASNYRAKLK SGEIKAENQP KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL
     KYLKDLINSN YRDDPLKFNL GNSTPKPVQN WSSDWTKEED EKLLIGVFKY GYGSWTQIRD
     DPFLGITDKI FLNEVQNPAP KKSVSSSDST PAPSKKGKGI TGSSKKVPGA IHLGRRVDYL
     LSFLREGPNA KSPSLELNIK KLPTGPSKKR QRRPANHGKS ATPEIANSES ANGPPGKRMK
     ALPKGPAALL NSSRPSANSP GPSSKPKGSR DGSTRQTSNI SSSSAHEKEY DSMDEEDCRH
     TMSAIRTSLK RLRRGGKGLD RKEWAKILKN ELTTIGNHIE SQKGSSRKID SEKYRKHLWS
     YSANFWPADV KSTKLMAMYD KITESQKK
//
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