ID   SMRCD_XENTR             Reviewed;        1003 AA.
AC   Q5FWR0; F6W182; F7CJC9;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       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   -!- 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; AAMC01061573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01061574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01061575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC089242; AAH89242.1; -; mRNA.
DR   RefSeq; NP_001015697.1; NM_001015697.1.
DR   RefSeq; XP_017948418.1; XM_018092929.1.
DR   RefSeq; XP_017948421.1; XM_018092932.1.
DR   AlphaFoldDB; Q5FWR0; -.
DR   SMR; Q5FWR0; -.
DR   STRING; 8364.ENSXETP00000038323; -.
DR   Ensembl; ENSXETT00000087375; ENSXETP00000064470; ENSXETG00000019214.
DR   GeneID; 548414; -.
DR   KEGG; xtr:548414; -.
DR   CTD; 56916; -.
DR   Xenbase; XB-GENE-492700; smarcad1.
DR   eggNOG; KOG0389; Eukaryota.
DR   InParanoid; Q5FWR0; -.
DR   OrthoDB; 61251at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000019214; Expressed in ovary and 13 other tissues.
DR   ExpressionAtlas; Q5FWR0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   InterPro; IPR009060; UBA-like_sf.
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; SSF46934; SSF46934; 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   2: Evidence at transcript level;
KW   ATP-binding; Chromatin regulator; Chromosome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1003
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily A containing DEAD/H box 1"
FT                   /id="PRO_0000420486"
FT   DOMAIN          221..264
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   DOMAIN          486..654
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          835..997
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          15..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           605..608
FT                   /note="DEGH box"
FT   COMPBIAS        25..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         499..506
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1003 AA;  114788 MW;  9A74272E88E1784F CRC64;
     MSAFNLERFR FDKGKKIDTE FGEKGASSRP STPNSQLEDH VTSIPETPEA KRVNNPSLFK
     KDKGVSFLDS DSENEDHQSK SKFSSTHQQS HPREENGTSD SVTDDSEDDY LAVKRPSAST
     AQVKDGSKYK NLQRLKEIFP KQNNDELLKL IESTSTLDGA VAAGVVLFNK EGSSRKRKLD
     EVPKDSSPVH EGINGQTKKK KKIDRVSSDN DSSLSEDDWE KQEASVKKLQ RHFPDLDKEE
     LREVLQEHDW SFHEALEALK LFAEDETDAL QNAAKKEVSN GKEFSRSNKN DNKSSAKAKA
     NQNSNKAMAQ NGVKKKGKGK KYSENAKRDT RDLESEESAS DAGSCLDEDY SSGDEKLEEE
     YKTKILSFLQ DASLDELYLI PHCSHKKAQK ITELRPFSSW ESLFEKMTKS NGLSEDLIWD
     CQTLIKEREV VMKLMNKCEE ISRTLTKQVT QLTEDGECGW NIEQPSIMSE NLVLKPYQKI
     GLNWLALLHK HKVNMILADE MGLGKTVQAI AFLAHLYVTG DSGPHLVVVP ASTMDNWIRE
     FNQWCPSMNI LLYYGSQEER KHLRYDILNK VVEFNVIVTT YNCAISSAED RSLFRRLKLN
     FAVFDEGHML KNMSAIRYQH LMTLNARSRL LLTGTPVQNN LLELMSLLNF VMPHMFSSST
     SEIKRLFSSK AKSTDEQTIF EKERIAHAKQ IMKPFILRRV KSEVLKQLPP KQDKIKFCQM
     SKKQEQLYSD LLNKLKKSID ATEKNSELCN VMMHLRKMAN HPLLHRQYYT ADRLRTMSKL
     MLKEPTHCDA NPDLIFEDME VMTDFELHRL CNEFTTLSQY KLEKELILDS GKFNILEKLL
     SDIKKKGDRV VLFSQFTMML DIIEVFLRHH QHRYVRLDGK TQISERIHLI DEFNTDMDIF
     IFLLSTKAGG LGINLTSANI VILHDIDCNP YNDKQAEDRC HRVGQTKEVK VIKLIGKGTI
     EESMLKISQQ KLRLEQDMTT NDTGDEGTIP LDMATLLKTS LGL