SMRCD_CAEEL
ID SMRCD_CAEEL Reviewed; 989 AA.
AC G5EDG2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 homolog;
DE EC=3.6.4.12;
GN ORFNames=M03C11.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: DNA helicase that possesses intrinsic ATP-dependent
CC nucleosome-remodeling activity and is both required for DNA repair and
CC heterochromatin organization. Promotes DNA end resection of double-
CC strand breaks (DSBs) following DNA damage: probably acts by weakening
CC histone DNA interactions in nucleosomes flanking DSBs (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; Z49128; CAA88960.2; -; Genomic_DNA.
DR EMBL; AL021171; CAA88960.2; JOINED; Genomic_DNA.
DR PIR; T23046; T23046.
DR RefSeq; NP_499301.2; NM_066900.5.
DR AlphaFoldDB; G5EDG2; -.
DR SMR; G5EDG2; -.
DR BioGRID; 41654; 9.
DR STRING; 6239.M03C11.8; -.
DR EPD; G5EDG2; -.
DR PaxDb; G5EDG2; -.
DR PeptideAtlas; G5EDG2; -.
DR PRIDE; G5EDG2; -.
DR EnsemblMetazoa; M03C11.8.1; M03C11.8.1; WBGene00010845.
DR GeneID; 176462; -.
DR KEGG; cel:CELE_M03C11.8; -.
DR CTD; 176462; -.
DR WormBase; M03C11.8; CE34059; WBGene00010845; -.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_4_1; -.
DR InParanoid; G5EDG2; -.
DR OMA; TIENWIG; -.
DR OrthoDB; 132523at2759; -.
DR PhylomeDB; G5EDG2; -.
DR PRO; PR:G5EDG2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010845; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR000330; SNF2_N.
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; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..989
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1
FT homolog"
FT /id="PRO_0000420487"
FT DOMAIN 406..574
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 757..912
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 525..528
FT /note="DEGH box"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 989 AA; 113046 MW; 5FDE10D1C492035A CRC64;
MSTTSDFQTG ERVRVAHQGN PQSSSLQADM DAKKALLSQN LNNGHLTARP PRTTGPGIKY
GEKKPKKQKG SDDDDEDYVD ETMPSEDEED FDNNEEDEDD DDYEEEGPRK RKAPSKKKLV
YPRENYRRED SETPEPEMKR IRTLSDSSDD EWMTKPRLNG SESPIGNVMR TQMAKRSAAS
KRKIVIDDES EDDFINDEEI SEKGSGKGSE KEESEGSGKD SETEEVTMKQ GQSLKAAMAK
AQKEQKKKAE SDEDWEEDED DMNADGDETP SDDSDIEERR AKRGETKNQK ECREFFNKAK
KEDLLQQARI NDKIADFVLA NRPFEIYGAM VAKMKGVTRG TNAIEAYMEF LEKRGILSRI
LDDCKDHAHT VTKDFERCTE GPLQLPLLKE GCTLHDYQLI GVKWLIMMYN KDLNAILGDE
MGLGKTIQIV AFLSYLKQIG KTGPHLIVVP SSTIENWIGE FHKWCPSIQL LTYYGSQDER
KHLRHRVKKQ KDHIDVILTT YNMVTSKSDD KKFFKNFSLN YVIYDEGHML KNCDSERYRG
LMKVKGKKKI LLTGTPLQNN LIELISLMYF VLSKVFNKYC EDITHLLQHF KQLGPALDTK
NKALYQQDRI EEAKAILQPY ILRRLKNQVL GSLPSKSEQI IEVEMKKPQK QLYDNIVEAL
QQSEESGDSY GSLMRLRQAA NHPLLRRSEY TDQKLDKIAK MLCLREKAYA DKKWQHVSED
LAWLSDIKIH QLCERFRCTS KFLLNEQLAL KSGKCEQLDV MLPEIQKKGD KVLIFSQFTS
MLDILEVYLN IRGYSYKRLD GQTPVLDRQE MINEFNLSKD LFVFLLSTRA GGLGINLTSA
NHIIIHDIDF NPYNDKQAED RCHRMGQEKP VHVTRLVSKG TVEVGMLALA KKKLQLEKQV
TDGVKGQLDE DALRELKEEE GGEQCGGRDL SKLLSSAISG RYDDVEDDSG DSKNGIDAEE
AAKKEDEAVK EPVEKEQQKE EESQPSTSA
