ID SMRCD_BOVIN Reviewed; 1028 AA.
AC E1B7X9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1;
DE EC=3.6.4.12;
GN Name=SMARCAD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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. Required for the
CC restoration of heterochromatin organization after replication. Acts at
CC replication sites to facilitate the maintenance of heterochromatin by
CC directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation
CC (H3K9me3) and restoration of silencing (By similarity). {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 -!- SUBUNIT: Binds to DNA preferentially in the vicinity of transcriptional
CC start sites. Interacts with MSH2 and TRIM28. Part of a complex composed
CC of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PCNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Colocalizes with PCNA at replication forks during S phase.
CC Recruited to double-strand breaks (DSBs) sites of DNA damage (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; DAAA02016925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02016926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1B7X9; -.
DR SMR; E1B7X9; -.
DR STRING; 9913.ENSBTAP00000045084; -.
DR PaxDb; 9913-ENSBTAP00000045084; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; E1B7X9; -.
DR TreeFam; TF105768; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0051304; P:chromosome separation; ISS:UniProtKB.
DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
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; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1028
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A containing DEAD/H box 1"
FT /id="PRO_0000416933"
FT DOMAIN 158..200
FT /note="CUE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 253..296
FT /note="CUE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 511..679
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 860..1012
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 13..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 630..633
FT /note="DEGH box"
FT /evidence="ECO:0000250"
FT MOTIF 723..740
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1007..1010
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 44..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 523..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 899..906
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 726
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
FT CROSSLNK 998
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L7"
SQ SEQUENCE 1028 AA; 117573 MW; F6187DAB8C917A30 CRC64;
MNLFNLDRFR FEKRNKIEEA PEATPQPSQP GPSSPISLSA EEENAEGEVS RAGTPDSDVT
EKTEDSSVPE TPENDRKASI SYFKNQRGIQ YIDLSSDSED VVSPNCSSTV QEKKFNKDTV
IIVSEPSEDE ESQGLPTMAT RNNNDITNLK NLSFFPNYSD NLSTVRQTRY SENLSSDLLK
LIDSTSTMDG AIAAALLMFG DAEGGGPRKR KLSSSSEPFE EDEFNDDQSM KKKRLDHGEE
SNESAESSTN WEKQESIVLK LQKEFPNFDK EELREVLKEH EWMYTEALES LKVFAEDQDM
QYASPSEFPN GKEVSSRSQN YPKNAAKTKL KQKCSMKPQN GFNKKRKKNV FNPKRVIEDS
EYDSGSDVGS SLDEDYSSGE EVMEDGYKGK ILHFLQDASI GELTLIPQCS QKKAQKITEL
RPFNSWEALF TKMSKTNGLS EDLIWHCKTL IQERDVVIKL MNKCEDISNK LTKQVTMLTG
NGGGWNTEQP SILNQSLSLK PYQKVGLNWL ALVHKHGLNG ILADEMGLGK TIQAIAFLAY
LYQEGNKGPH LIVVPASTID NWLREVNLWC PTLKVLCYYG SQEERKQIRY NIHSRYEEYN
VIVTTYNCAI SSSDDRSLFR RLKLNYAIFD EGHMLKNMGS IRYQHLMTIN ANNRLLLTGT
PVQNNLLELM SLLNFVMPHM FSSSTSEIRR MFSSKTKPAD EQSIYEKERI AHAKQIIKPF
ILRRVKEEVL KQLPPKKDRI ELCAMSEKQE QLYMNLFNRL KKSINNMEKN TEMCNVMMQL
RKMANHPLLH RQYYTAEKLK EMSQLMLKEP THCEANPDLI FEDMEVMTDF ELHVLCKQYR
HINNFQLDMD LILDSGKFRV LGCILSELKQ KGDRVVLFSQ FTMMLDILEV LLKHHQHRYL
RLDGKTQISE RIHLIDEFNT DMDIFVFLLS TKAGGLGINL TSANVVILHD IDCNPYNDKQ
AEDRCHRVGQ TKEVLVIKLI GQGTIEESML KINQQKLKLE QDMTTVDEGD EGSMPADIAT
LLKTSMGL
//
