ID G1LTR2_AILME Unreviewed; 1812 AA.
AC G1LTR2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD5 {ECO:0000313|Ensembl:ENSAMEP00000010459.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000010459.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000010459.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000010459.2}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR STRING; 9646.ENSAMEP00000010459; -.
DR Ensembl; ENSAMET00000010914.2; ENSAMEP00000010459.2; ENSAMEG00000009880.2.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000159249; -.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; G1LTR2; -.
DR TreeFam; TF106448; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IEA:Ensembl.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18057; DEXHc_CHD5; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR028727; DEXHc_CHD5.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF6; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 5; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 206..253
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 279..326
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 360..417
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 455..488
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 575..759
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 891..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 91..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1812 AA; 206497 MW; 97D8FBF7F1437AC3 CRC64;
MAEWGLDDVE YLFSEADYHT LTNYKAFSQF LRPLIAKKNP KIPMSKMMTV LGAKWREFSA
NNPFKGSSAA AAAAAVAAAV ETVTIAPPLA VSPQQAPQPV PIRKAKTKEG KGPGVRKKIK
GSKDAKKKGK GRKVAGLKFR FGGISNKRKK GSSSEEDERE ESDFDSASIH SSSVRSEGST
ALGKKSKRRR KKKRIDDGDG YETDHQDYCE VCQQGGEIIL CDTCPRAYHL VCLDPELEKA
PEGKWSCPHC EKEGIQWEPK DDDDEEEEGG CEEEEDDHME FCRVCKDGGE LLCCDACPSS
YHLHCLNPPL PEIPNGEWLC PRCTCPPLKG KVQRILHWRW TEPPAPFMVG LPGSDVEPGV
PPPKPLEGIP EREFFVKWAG LSYWHCSWVK ELQLELYHTV MYRNYQRKND MDEPPPFDYG
SGDEDGKSEK RKNKDPLYAK MEERFYRYGI KPEWMMIHRI LNHSFDKKGD VHYLIKWKDL
PYDQCTWEID DIDIPYYDNL KQAYWGHREL MLGEDARLPK RLVKKGKKLK DDKQEKPPDT
PIVDPTVKFD KQPWYIDSTG GTLHPYQLEG LNWLRFSWAQ GTDTILADEM GLGKTVQTIV
FLYSLYKEGH SKGPYLVSAP LSTIINWERE FEMWAPDFYV VTYTGDKESR SVIRENEFAF
EDNAIRSGKK VFRMKKEVQI KFHVLLTSYE LITIDQAILG SIEWACLVVD EAHRLKNNQS
KFFRVLNSYK IDYKLLLTGT PLQNNLEELF HLLNFLTPER FNNLEGFLEE FADISKEDQI
KKLHDLLGPH MLRRLKADVF KNMPAKTELI VRVELSQMQK KYYKFILTRN FEALNSKGGG
NQVSLLNIMM DLKKCCNHPY LFPVAAVEAP VLPNGSYDGS SLVKSSGKLM LLQKMLKKLR
DEGHRVLIFS QMTKMLDLLE DFLEYEGYKY ERIDGGITGG LRQEAIDRFN APGAQQFCFL
LSTRAGGLGI NLATADTVII YDSDWNPHND IQAFSRAHRI GQNKKVMIYR FVTRASVEER
ITQVAKRKMM LTHLVVRPGL GSKSGSMTKQ ELDDILKFGT EELFKDDVEG MMSQGQRPVT
PIPDVQSSKG GALAASAKKK HGSTPPGDNK DVEDSSVIHY DDAAISKLLD RNQDATDDTE
LQNMNEYLSS FKVAQYVVRE EDGVEEVERE IIKQEENVDP DYWEKLLRHH YEQQQEDLAR
NLGKGKRVRK QVNYNDASQE DQEWQDELSD NQSEYSIGSE DEDEDFEERP EGQSGRRQSR
RQLKSDRDKP LPPLLARVGG NIEVLGFNAR QRKAFLNAIM RWGMPPQDAF NSHWLVRDLR
GKSEKEFRAY VSLFMRHLCE PGADGAETFA DGVPREGLSR QHVLTRIGVM SLVRKKVQEF
EHVNGKYSTP DLIPEGPEGK KPSEVISSDP NTPVPASPAH LLPAPLGLPD KMEAQLGYMD
EKELGVQKPK KPPEIQALPT ALDRVEGEDK QESSDGKEQP EETEKAPPSP EQLPREEVLP
EKEKILDKLE LSLIHSRGDG SGFRPDDTKV EEKEPFETQQ NGDKEEDEEG KKEDKNGKFK
FMFNIADGGF TELHTLWQNE ERAAVSSGKI YDIWHRRHDY WLLAGIVTHG YARWQDIQND
PRYMILNEPF KSEIHKGNYL EMKNKFLARR FKLLEQALVI EEQLRRAAYL NMTQDPSHPA
MALNARLAEV ECLAESHQHL SKESLAGNKP ANAVLHKVLN QLEELLSDMK ADVTRLPSML
SRIPPVAARL QMSERSILSR LTNRAGDPTI QQGAFGNSQM YNNNFGPNFR GPGPGGIVNY
NQMPLGPYVT DI
//
