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Database: UniProt
Entry: E1B7X9
LinkDB: E1B7X9
Original site: E1B7X9 
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   16-OCT-2019, entry version 57.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.,
RA   Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
RA   Marcais G., 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
CC       and heterochromatin organization. Promotes DNA end resection of
CC       double-strand breaks (DSBs) following DNA damage: probably acts by
CC       weakening histone DNA interactions in nucleosomes flanking DSBs.
CC       Required for the restoration of heterochromatin organization after
CC       replication. Acts at replication sites to facilitate the
CC       maintenance of heterochromatin by directing H3 and H4 histones
CC       deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration
CC       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
CC       transcriptional start sites. Interacts with MSH2 and TRIM28. Part
CC       of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts
CC       with PCNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Colocalizes with PCNA at replication forks
CC       during S phase. Recruited to double-strand breaks (DSBs) sites of
CC       DNA damage (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; DAAA02016925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02016926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; E1B7X9; -.
DR   STRING; 9913.ENSBTAP00000045084; -.
DR   PaxDb; E1B7X9; -.
DR   PRIDE; E1B7X9; -.
DR   eggNOG; KOG0389; Eukaryota.
DR   eggNOG; ENOG410XNUT; LUCA.
DR   InParanoid; E1B7X9; -.
DR   OMA; FPDQDKE; -.
DR   OrthoDB; 61251at2759; -.
DR   TreeFam; TF105768; -.
DR   Proteomes; UP000009136; Unplaced.
DR   Bgee; ENSBTAG00000017061; Expressed in 10 organ(s), highest expression level in spleen.
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: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:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0051304; P:chromosome separation; ISS:UniProtKB.
DR   GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR   GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10810; -; 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; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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;
KW   Complete proteome; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN         1   1028       SWI/SNF-related matrix-associated actin-
FT                                dependent regulator of chromatin
FT                                subfamily A containing DEAD/H box 1.
FT                                /FTId=PRO_0000416933.
FT   DOMAIN      158    200       CUE 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00468}.
FT   DOMAIN      253    296       CUE 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00468}.
FT   DOMAIN      511    679       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      860   1012       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     523    531       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   NP_BIND     899    906       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       630    633       DEGH box. {ECO:0000250}.
FT   MOTIF       723    740       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF      1007   1010       DEAD box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES      54     54       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES      57     57       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES      71     71       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     124    124       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     127    127       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     132    132       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     153    153       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     213    213       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     216    216       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     241    241       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     244    244       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   MOD_RES     304    304       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK     77     77       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK     84     84       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK    337    337       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK    473    473       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK    726    726       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H4L7}.
FT   CROSSLNK    998    998       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {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
//
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