ID A0A2Y9EDR8_PHYMC Unreviewed; 1026 AA.
AC A0A2Y9EDR8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=SMARCAD1 {ECO:0000313|RefSeq:XP_007100308.1,
GN ECO:0000313|RefSeq:XP_007100310.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007100310.1};
RN [1] {ECO:0000313|RefSeq:XP_007100308.1, ECO:0000313|RefSeq:XP_007100310.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007100308.1,
RC ECO:0000313|RefSeq:XP_007100310.1};
RG RefSeq;
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 RefSeq; XP_007100308.1; XM_007100246.4.
DR RefSeq; XP_007100310.1; XM_007100248.4.
DR STRING; 9755.ENSPCTP00005004495; -.
DR GeneID; 102993357; -.
DR CTD; 56916; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000248484; Chromosome 7.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:UP000248484}.
FT DOMAIN 157..199
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 251..294
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 509..677
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 858..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..346
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 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 117197 MW; 0220661A45C9E0BE CRC64;
MNLFNLDRFR FEKRSKIEEA PEATPQPSQP GPSSPISLSA EEENAEGEVS RAGTPDSDIT
EKTEDSSVPE TPENERKASV SYFKNQRGIQ YIDLSSDSED VSPDCSSTAQ EKKFSKDTVI
IVSEPSEDEE SQDLPATAGR NNSDISELED LSELEDLKDA KLQTLKELFP QRSDSDLLKL
IESTSTMDGA IAAALLMFGD AGGGPRKRKL SSSSEPFEED EFNDDQSMKK KRLDQGEESN
ESAESSSNWE KQESIVLRLQ KEFPNFDKEE LREVLKEHEW MYTEALESLK VFAEDQDMQY
ASPSEFPNGK EVSSRSQNYP KNAVKTKLKQ KCSMKPQNGF NKKRKKNVFN PKRVIEDSEY
DSGSDVGSSL DEDYSSGEEV MEDGYKGKIL HFLQDASIGE LTLIPQCSQK KAQKITELRP
FNSWEALFTK MSKTNGLSED LIWHCKTLIQ ERDVVIRLMN KCEDISNKLT KQVTMLTGNG
GGWNIEQPSI LNQSLSLKPY QKVGLNWLAL VHKHGLNGIL ADEMGLGKTI QAIAFLAYLY
QEGNKGPHLI VVPASTIDNW LREVNLWCPT LKVLCYYGSQ EERKQIRYNI HSRYEEYNVI
VTTYNCAISS SDDRSLFRRL KLNYAIFDEG HMLKNMGSIR YQHLMTINAN NRLLLTGTPV
QNNLLELMSL LNFVMPHMFS SSTSEIRRMF SSKTKPADEQ SIYEKERIAH AKQIIKPFIL
RRVKEEVLKQ LPPKKDRIEL CAMSEKQEQL YLGLFNRLKK SINNMEKNTE MCNVMMQLRK
MANHPLLHRQ YYTAEKLKEM SQLMLKEPTH CEANPDLIFE DMEVMTDFEL HVLCKQYRHI
NNFQLDMDLI LDSGKFRVLG CILSELKQKG DRVVLFSQFT MMLDILEVLL KHHQHRYLRL
DGKTQISERI HLIDEFNTDM DIFVFLLSTK AGGLGINLTS ANVVILHDID CNPYNDKQAE
DRCHRVGQTK EVLVIKLIGQ GTIEESMLKI NQQKLKLEQD MTTVDEGDEG SMPADIATLL
KTSMGL
//
