SMAL1_XENLA
ID SMAL1_XENLA Reviewed; 960 AA.
AC Q498E7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) 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; BC100245; AAI00246.1; -; mRNA.
DR RefSeq; NP_001089668.1; NM_001096199.1.
DR AlphaFoldDB; Q498E7; -.
DR SMR; Q498E7; -.
DR MaxQB; Q498E7; -.
DR DNASU; 734728; -.
DR GeneID; 734728; -.
DR KEGG; xla:734728; -.
DR CTD; 734728; -.
DR Xenbase; XB-GENE-866253; smarcal1.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 734728; Expressed in testis and 19 other tissues.
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; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IEA:InterPro.
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..960
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000361534"
FT DOMAIN 246..317
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 349..420
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 466..621
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 737..890
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 81..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..41
FT /evidence="ECO:0000255"
FT MOTIF 570..573
FT /note="DESH box"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 960 AA; 106531 MW; 47EF94297D05E6CD CRC64;
MSVCLTEEQK RKIEENRQRA LARRAERLAA QQNTLKQTNN SHSTLFNIQK STVEQGALFS
GQRTNVTAAC MAPLQQGSNN KYAFQKTSSG GSAASSLPGT AENKPQAGGN GPCDYKVPAD
PAQDFTSSKN LTGKYVAPKA HCVSSVPSFN DTPNPRQLNP ACTTQEQEKP KNSSYSYSRP
DSDTACDKFT AGPGPGPIRN TTAISKFYGA NPGIKPALPV SNKTVSEVRD RGVTGSSVEA
VPVKKASSST RGRCVKHMEG RFRVEVGYSA ELIALFKTIP SKAYDPATKM WNFGLEDYAS
LMSEVQRVQS VELKALEGME GVQIAPPPTS GSGTNINALL AMCNNWQRPN ATLRGRCILI
SRSRFEMEIG YHTEIIGLFK QMNTRNYDTK TRKWSFMLED YQKLMESVRN IQQVEVEPLP
RPVLQAFAPQ FEKTTISLAE IEDVDLSHVD SKLIGNLMPF QRDGVNFAIS REGRLLLADD
MGLGKTIQAI CIAAYYRKEW PLLVVAPSSV RFTWAEAFHR WLPSLNPESV NVIVTGRDSQ
SANLINIISF DLLGKMDKQI AANFKVIIID ESHFLKNVKT ARCKAAMPLL KSAKRVMLLS
GTPAMSRPAE LYTQIAAVRP TFFPRFHDFG IRYCDAKQMP WGWDYSGSSN LNELKLLLEE
SIMIRRLKSE VLSQLPAKQR KMVVVAPEGI TAKTKAALAA AAKEMAKGFK SKVQEKEALL
LFYNRTAEAK IRSVLEYIID LLESGREKFL VFAHHKLVLD NICEELGKKE VPYIRIDGNT
SSADRQSLCH KFQFSEKSCV AVLSITAANM GLTLSSADLV VFAELFWNPG VLIQAEDRVH
RIGQTSSVNI HYLVAKGTAD DYLWPMIQEK IKVLGQAGLS EANFSETTES TDYFYKDPKQ
KTIYDLFQRS FSEQGAENDS DEALLLEACE EVDLGESTCG PTDYSGNACK RRKIDDYFAL
