SMAL1_DANRE
ID SMAL1_DANRE Reviewed; 807 AA.
AC B2ZFP3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1;
DE EC=3.6.4.-;
DE AltName: Full=HepA-related protein;
DE AltName: Full=Sucrose nonfermenting protein 2-like 1;
GN Name=smarcal1; Synonyms=harp; ORFNames=si:ch211-239d11.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C., Gu S., Yu P., Yu F., Feng C., Gao N., Qin-Zang Y., Du J.;
RT "Deficiency of smarcal1 causes developmental defects through the inhibition
RT of cell proliferation in zebrafish.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent annealing helicase that catalyzes the rewinding
CC of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are
CC stably bound by replication protein A (RPA). Acts throughout the genome
CC to reanneal stably unwound DNA, performing the opposite reaction of
CC many enzymes, such as helicases and polymerases, that unwind DNA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00800}.
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DR EMBL; EU655703; ACD03327.1; -; mRNA.
DR RefSeq; NP_001120938.1; NM_001127466.1.
DR AlphaFoldDB; B2ZFP3; -.
DR SMR; B2ZFP3; -.
DR STRING; 7955.ENSDARP00000106260; -.
DR PaxDb; B2ZFP3; -.
DR PeptideAtlas; B2ZFP3; -.
DR PRIDE; B2ZFP3; -.
DR GeneID; 560412; -.
DR KEGG; dre:560412; -.
DR CTD; 50485; -.
DR ZFIN; ZDB-GENE-041210-303; smarcal1.
DR eggNOG; KOG1000; Eukaryota.
DR InParanoid; B2ZFP3; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; B2ZFP3; -.
DR PRO; PR:B2ZFP3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0048589; P:developmental growth; IMP:ZFIN.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:ZFIN.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030101; HARP(SMARCAL1).
DR InterPro; IPR010003; HARP_dom.
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 PANTHER; PTHR45766:SF3; PTHR45766:SF3; 2.
DR Pfam; PF07443; HARP; 2.
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; PS51467; HARP; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..807
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000361533"
FT DOMAIN 127..198
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 231..302
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 348..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 620..773
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..33
FT /evidence="ECO:0000255"
FT MOTIF 453..456
FT /note="DESH box"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 807 AA; 89896 MW; EB65E571C4CB674E CRC64;
MSVSLTPEQQ RRIEENRKKA LARRAERQAQ IADPGPAQNK HTQSGTTGGP AKNNQHFASD
RGQSGAPTRQ TQLIDINAAC TKTAPPTSIT AASTASSFYG QAGKPSTGEK RPPKPPEPAA
NIPAKKPAVY LRGRCVSHSE NRFRVEVGYH ADLILVFKSI PSKNYDPATK MWNFSLEDYQ
MLMEQVAHLP SISLKPLEGM EGLNISASTC RPKDAAAMAA LMRLCQGWQK PGATIKGKCV
LVSRSRLEVD IGYQADVIGI FKQMPSKSYD MKTRKWTFLL EDYGKLMADL NELPTVETEP
LPHAVLQSFS SQFEKTQSQA PVPPEADLSH IDPQLTRSLM PFQRDGVNFA VSREGRLLLA
DDMGLGKTVQ AICIAAYYRS EWPLLVVAPS SVRFTWAEAF RRWLPSVKPD SINVVVKGKD
SLRSGLINII SYDLLNKMDK QPPSSPFNVI IMDESHFLKN MKTARCRAAL PLLKTAKRVI
LLSGTPAMSR PAELYTQIQA VRPALFPRFH DFGTRYCDAK QLPWGWDYSS SSNLTELKLL
LEESLMLRRL KSEVLSQLPA KQRKVVTVTT DGINSRTKAA LNAAARELAK GYHNKSQEKE
ALLVFFNHTA EAKIRAIMEY ISDMLECGRE KFLVFAHHKL VLDSITKELG EKSISFIRID
GSTPSAERQL LCERFQASQQ SCVAVLSITA ANMGLTLHSA ALVVFAELFW NPGVLIQAED
RVHRIGQTSN VDIHYLVAKG TADDYLWPMI QAKMNVLEQV GLSESNISEN AESASFHSRD
RQQLTITEMF QRSFDEDEML ALMDQDP
