ID A0A1U7SGX5_ALLSI Unreviewed; 1812 AA.
AC A0A1U7SGX5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD1 {ECO:0000313|RefSeq:XP_006035507.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006035507.1};
RN [1] {ECO:0000313|RefSeq:XP_006035507.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_006035507.1; XM_006035445.3.
DR STRING; 38654.A0A1U7SGX5; -.
DR GeneID; 102387554; -.
DR KEGG; asn:102387554; -.
DR CTD; 1105; -.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; A0A1U7SGX5; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000189705; Unplaced.
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 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 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:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 274..366
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 391..454
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 495..665
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 794..945
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1812
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..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1346
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1812 AA; 208654 MW; 9520728EEE4BFB5B CRC64;
MNGHSDEESA RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS
QSESESDASK EKKQVQAKPP KVDGAEFWKS NPSILTVQRS AMLRKQQQQQ QQKAASSDSG
SEEGSSSSDD SVDDSTSETK RKKHKDEDWQ MSGSGSVSGT GSDSESREDR EKSSCEESES
DYEPKNKVKS RKPPSRIKPK SGKKSVGQKK RQLDSSDDDD DDDDEEDDYD KRGSRRQATV
NISYKEAEEA KTDSDDLLEV CGEDVPQPEE DEFETIEKFM DSRTGRKGAT GAATTIYAVE
ADGDPNTGFD KSKEPGEIQY LIKWKGWSHI HNTWETEETL KQQNVKGMKK LDNYKKKDLE
TKRWLKNASP EDVEYYNCQQ ELTDDLHKQY QIVERIIAHS NQKSAAGYPD YYCKWQGLPY
SECSWEDGAL IAKKFQARID EYFSRNQSKT TPFKDCKVLK QRPRFVALKK QPSYIGGHEG
LELRDYQLNG LNWLAHSWCK GNSCILADEM GLGKTIQTIS FLNCLFHEHQ LYGPFLLVVP
LSTLTSWQRE IQIWASQMNA VVYLGDITSR NMIRTHEWMH LQTKRLKFNI LLTTYEILLK
DKSFLGGLNW AFIGVDEAHR LKNDDSLLYK TLIDFKSNHR LLITGTPLQN SLKELWSLLH
FIMPEKFSSW EDFEEEHGKG REVGYASLHK ELEPFLLRRV KKDVEKSLPA KVEQILRMEM
SALQKQYYKW ILTRNYKALS KGSKGSTSGF LNIMMELKKC CNHCYLIKPP DDDEFYNKQE
ALQHLIRSSG KLILLDKLLI RLRERGNRVL IFSQMVRMLD ILAEYLKYRQ FPFQRLDGSI
KGELRKQALD HFNAEGSEDF CFLLSTRAGG LGINLASADT VVIFDSDWNP QNDLQAQARA
HRIGQKKQVN IYRLVTKGSV EEDILERAKK KMVLDHLVIQ RMDTTGKTVL HTGSTPSSST
PFNKEELSAI LKFGAEELFK EPEGEEQEPQ EMDIDEILKR AETRENEPGP LTVGDELLSQ
FKVANFSNMD EDDIELEPER NSRNWEEIIP EVHRRRIEEE ERQKELEEIY MLPRMRNCAK
QISFNGSEGR RSRNRRYSGS DSDSISERKR PKKRGRPRTI PRENIKGFSD AEIRRFIKSY
KKFGGPLERL DAIARDAELV DKSETDLRRL GELVHNGCIK ALKDSSSGQD RAGGRLGKVK
GPTFRISGVQ VNAKLVISHE EELVPLHKSI PSDPEERKRY VIPCHTKAAH FDIDWGKEDD
SNLLIGIYEY GYGSWEMIKM DPDLSLTQKI LPDDPDKKPQ AKQLQTRADY LIKLLNKDLA
RKEAQRLSGA GNSKRRKMRT KKNKVLKSAK MKEEVKSDSS PPASEKSEEE EDDYKDEISS
VKHPNKKIKT EKENEEKSES DIGVKKETEE KRETKEKENK RDLKREKREK EDKKELKEKE
VKEKRENKIK ESTQKEKEVK DEKTNEVKSE SKDKTKKTLL ADTPVHITAS SEPVPISEES
EELDQKTFSV CKERMRPVKA ALKQLDRPEK GLSEREQLEH TRQCLIKIGD HITECLKEYT
NPDQIKQWRK NLWIFVSKFT EFDARKLHKL YKHAIKKRQE SQQHNDQNIG SNVNTHVIRN
PDVERLKENT NHDDSSRDSY SSDRHLSQYH DHHKDRHQGD AYKKSDSRKR PYSAFSNGKD
HRDWDHYKQD NRYYSDSKHR KLDDHRSRDH RSNLEGNLKD SRSHSDHRSH SDHRIHSDHR
STSDYGHHKS SRDYRYHSDW QMDHRASSSG PRSPLDQRSP YGSRSPLGHR SPFEHSSDHK
STPEHTWSSR KT
//
