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Entry: I3M455_ICTTR
LinkDB: I3M455_ICTTR
Original site: I3M455_ICTTR 
ID   I3M455_ICTTR            Unreviewed;      1712 AA.
AC   I3M455;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=CHD1 {ECO:0000313|Ensembl:ENSSTOP00000003939.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003939.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000003939.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AGTP01043259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01043260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005326193.1; XM_005326136.2.
DR   STRING; 43179.ENSSTOP00000003939; -.
DR   Ensembl; ENSSTOT00000004392.3; ENSSTOP00000003939.3; ENSSTOG00000004336.3.
DR   GeneID; 101967387; -.
DR   CTD; 1105; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000156579; -.
DR   HOGENOM; CLU_000315_8_0_1; -.
DR   InParanoid; I3M455; -.
DR   OrthoDB; 5482994at2759; -.
DR   TreeFam; TF313461; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; IEA:Ensembl.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
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; IPR040793; CDH1_2_SANT_HL1.
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:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF18375; CDH1_2_SANT_HL1; 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; 2.
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   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          272..364
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          389..452
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          493..663
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          792..943
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1080..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1347..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1505..1589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1601..1712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..207
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1347..1388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1509..1524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1526..1589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1601..1668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1669..1690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1693..1712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1712 AA;  197145 MW;  1DFD25D263786A1E CRC64;
     MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSASESGS
     QSESESDTSR ENKVQAKPPK VDGTEFWKSS PSILAVQRSA MLKKQQQQQQ QQQQQHPASS
     NSGSEEDSSS SEDSDDSSSE VKRKKHKDED WQMSGSGSPS QSGSDSESEE RDKSSCDETE
     SDYEPQNKVK SRKPQNRSKS KNGKKIIGQK KRQIDSSDDD DDEDYDNDKR SSRRQATVNV
     SYKEDEEMKT DSDDLLEVCG EDVPQPEEEE FETIEKFMDC RIGRKGATGA TTTIYAVEAD
     GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD NYKKKDQETK
     RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ KSAAGYPDYY CKWQGLPYSE
     CSWEDGALIS KKFQACIDEY FSRNQSKTTP FKDCKVLKQR PRFVALKKQP SYIGGHEGLE
     LRDYQLNGLN WLAHSWCKGN SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS
     TLTSWQREIQ TWASQMNAVV YLGDINSRNM IRTHEWMHPQ TKRLKFNILL TTYEILLKDK
     AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL KELWSLLHFI
     MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK DVEKSLPAKV EQILRMEMSA
     LQKQYYKWIL TRNYKALSKG SKGSTSGFLN IMMELKKCCN HCYLIKPPDN NEFYNKQEAL
     QHLIRSSGKL ILLDKLLIRL RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG
     ELRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR
     IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT GSAPSSSTPF
     NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE THENEPGPLT VGDELLSQFK
     VANFSNMDED DIELEPERNS KNWEEIIPED QRRRLEEEER QKELEEIYML PRMRNCAKQI
     SFNGSEGRRS RSRRYSGSDS DSISERKRPK KRGRPRTIPR ENIKGFNDAE IRRFIKSYKK
     FGGPLERLDA IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP
     TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD IDWGKEDDSN
     LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK QLQTRADYLI KLLSRDLAKK
     EALRLSGAGG LKRRKIRAKK NKAIKSMKLK EEIKSDSSPL PSEKSDEEDD KLGESKSESK
     ERSKKSSVSD APVHITASGE PVPISEESEE LDQKTFSICK ERMRPVKAAL KQLDRPEKGL
     SEREQLEHTR QCLIKIGDHI TECLKEYTNP EQIKQWRKNL WIFVSKFTEF DARKLHKLYK
     HAIKKRQESQ QNNDQNSNSS AHMIRNPDVE RLKENTNHDD SSRDSYSSDR HLSQYHDHHK
     DRHQGDSYKK RDSRKRPYSS FSNGKDHREW DHYKQDSRYY SDREKHRKLD DHRSRDHRSN
     LEGSLKDRSH SDHRSHSDHR LHSDHRSSSE YIHHKSSRDY RYHSDWQMDH RASSSGPRSP
     LDQRSPYGSR SPFEHSVEHK STPEHTWSSR KT
//
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