SMAL1_XENTR
ID SMAL1_XENTR Reviewed; 942 AA.
AC Q0P4U8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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;
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 MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) 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; BC121897; AAI21898.1; -; mRNA.
DR RefSeq; NP_001072923.1; NM_001079455.1.
DR AlphaFoldDB; Q0P4U8; -.
DR SMR; Q0P4U8; -.
DR STRING; 8364.ENSXETP00000000989; -.
DR PaxDb; Q0P4U8; -.
DR GeneID; 780385; -.
DR KEGG; xtr:780385; -.
DR CTD; 50485; -.
DR Xenbase; XB-GENE-493391; smarcal1.
DR eggNOG; KOG1000; Eukaryota.
DR HOGENOM; CLU_000315_33_1_1; -.
DR InParanoid; Q0P4U8; -.
DR OMA; QEEMPTA; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; Q0P4U8; -.
DR TreeFam; TF106474; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000000465; Expressed in testis and 14 other tissues.
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:0006281; P:DNA repair; IBA:GO_Central.
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..942
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000361535"
FT DOMAIN 228..299
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 331..402
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 448..603
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 719..872
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..29
FT /evidence="ECO:0000255"
FT MOTIF 552..555
FT /note="DESH box"
FT COMPBIAS 28..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 942 AA; 103733 MW; E2C102F15FEFF062 CRC64;
MSVCLTEEQK RKIEENRQRA LARRAERLAA QQNSQTNRSL SAPLNAQIPS GQQGVLPSAQ
SINATGTSRA ANSKYAFQKS PSGGNTAPSV PGAAGNKVQA VGNRSHDSKS LTDPAKDVKG
NYTVPEAQSV PSGPSNAPNP RHLYPAGTTP GQESAKHSNS YSRPEPLTAC DNDTTGPGPL
RSTTTITKFY GAGPGSKPAV PVSNKTVSEG RERGVTGSAA EAVPAKKASG ATRGRCVKHA
ESRFRVEVGY SAELIALFKT IPSKNYDPAT KMWNFGLEDY ASLMSEVQQL QSVELKALEG
MEGVQIAPPP ATGGGTNINA LLAMCNNWQR PSATLRGRCI LVSRSRFEME IGYHAEIIGL
FKQMNTRNYD TKTRKWSFML EDYQKLMESV RNIQQVEVEP LPRPVLQAFA PQFGKTTIIR
EEIPEVDLSQ VDSKLGSNLM PFQRDGVNFA VSREGRLLLA DDMGLGKTIQ AICIAAYYRK
EWPLLVVAPS SVRFTWAEAF QRWLPSIRPE SVNVIVTGRD SQSASLINIV SFDLLGKMDK
QIAATFQVII IDESHFLKNV KTARCKAAMP LLKSAKRVML LSGTPAMSRP AELYTQIAAV
RPSFFPRFHD FGIRYCDAKQ MPWGWDYSGS SNLNELKLLL EESIMIRRLK SEVLSQLPAK
QRKMVVVAPE GITAKTKAAL AAAAKEMAKG FKSKVQEKEA LLLFYNRTAE AKIRSVLEYI
MDLLESGREK FLVFAHHKLV LDHICEELGK KDVPYIRIDG NTSSADRQSL CHKFQMSEKS
CVAVLSITAA NMGLTLSSAD LVVFAELFWN PGVLIQAEDR VHRIGQTSSV NIHYLVAKGT
ADDYLWPMIQ EKIKVLGQAG LSEANFSETT ESTDYFYKDP KQKTIYDLFQ RSFSEEGAET
NADEALLLEA CEEADLGDAV CSPTDYSGNS CKRRKIDEYF AL
