ID G1LGZ7_AILME Unreviewed; 1029 AA.
AC G1LGZ7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=SMARCAD1 {ECO:0000313|Ensembl:ENSAMEP00000006188.2};
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:ENSAMEP00000006188.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000006188.2, 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:ENSAMEP00000006188.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR AlphaFoldDB; G1LGZ7; -.
DR STRING; 9646.ENSAMEP00000006188; -.
DR Ensembl; ENSAMET00000006442.2; ENSAMEP00000006188.2; ENSAMEG00000005844.2.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; G1LGZ7; -.
DR OrthoDB; 5482994at2759; -.
DR TreeFam; TF105768; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0051304; P:chromosome separation; IEA:Ensembl.
DR GO; GO:0000729; P:DNA double-strand break processing; IEA:Ensembl.
DR GO; GO:0000018; P:regulation of DNA recombination; IEA:Ensembl.
DR CDD; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR003892; CUE.
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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51140; CUE; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912}.
FT DOMAIN 158..200
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 252..295
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 510..678
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 861..1013
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 14..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 117557 MW; D8D60BD55675EDCC CRC64;
MNLFNLDRFR FEKRSKIEEV PEATPQPSQP GPSSPISLSA EEENAEGEGS RAGTPDSDIT
EKTEDSSVPE TTENERKASI SYFKNQRGIQ YIDLSSDSED IVSPNCSSTV QEKKFNKDTV
IIVSEPSEDE ESQGLPTMAG RNTDDISELE DLSELEDLKD AKLQTLKELF PQRSDNDLLK
LIESTSTMDG AIAAALLMFG DAGGGPRKRK LSSSSEPYEE DEFNDDQSIK KKRLDHGEES
NESAESSNNW EKQESIVLKL QKEFPNFDKQ ELREVLKEHE WMYTEALESL KVFAEDQDMQ
YASQSEFPNG KEASSRSQNY PKNAAKTKLK QKCSMKPQNG FNKKRKKNVF NPKRVIEDSE
YDSGSDVGSS LDEDYSSGEE VMEDGYKGKI LHFLQDASIG ELTLIPQCSQ KKAQKITELR
PFNSWEALFT KMSKTNGLSE DLIWHCKTLI QERDVVIRLM NKCEDISNKL TKQVTMLTGN
GGGWNIEQPS ILNQSLSLKP YQKVGLNWLA LVHKHGLNGI LADEMGLGKT IQAIAFLAYL
YQEGNKGPHL IVVPASTIDN WLREVNLWCP TLKVLCYYGS QEERKQIRYN IHSKYEEYNV
IVTTYNCAIS SSDDRSLFRR LKLNYAIFDE GHMLKNMGSI RYQHLMTINA NNRLLLTGTP
VQNNLLELMS LLNFVMPHMF SSSTSEIRRM FSSKTKSADE QSIYEKERIA HAKQIIKPFI
LRRVKEEVLK QLPPKKDQIE LCAMSEKQEQ LYLGLFNRLK KSINNMVTEK NTEMCNVMMQ
LRKMANHPLL HRQYYTAEKL KEMSQLMLKE PTHCEANPDL IFEDMEVMTD FELHVLCKQY
RHINNFQLDM DLILDSGKFR VLGCILSELK QKGDRVVLFS QFTMMLDILE VLLKHHQHRY
LRLDGKTQIS ERIHLIDEFN TDMDIFVFLL STKAGGLGIN LTSANVVILH DIDCNPYNDK
QAEDRCHRVG QTKEVLVIKL ISQGTIEESM LKINQQKLKL EQDMTTVDEG DEGSMPADIA
TLLKTSMGL
//
