ID   ARIP4_XENTR             Reviewed;        1396 AA.
AC   A4IHD2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Helicase ARIP4;
DE            EC=3.6.4.12;
DE   AltName: Full=Androgen receptor-interacting protein 4;
DE   AltName: Full=RAD54-like protein 2;
GN   Name=rad54l2; Synonyms=arip4;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA helicase that modulates androgen receptor (AR)-dependent
CC       transactivation in a promoter-dependent manner. {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}.
CC   -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to be important
CC       for the association with nuclear receptors. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR   EMBL; BC135473; AAI35474.1; -; mRNA.
DR   RefSeq; NP_001076824.1; NM_001083355.1.
DR   RefSeq; XP_012816701.1; XM_012961247.2.
DR   RefSeq; XP_012816702.1; XM_012961248.2.
DR   RefSeq; XP_012816703.1; XM_012961249.2.
DR   AlphaFoldDB; A4IHD2; -.
DR   SMR; A4IHD2; -.
DR   STRING; 8364.ENSXETP00000009619; -.
DR   PaxDb; A4IHD2; -.
DR   GeneID; 733747; -.
DR   KEGG; xtr:733747; -.
DR   CTD; 23132; -.
DR   Xenbase; XB-GENE-5829376; rad54l2.
DR   eggNOG; KOG1016; Eukaryota.
DR   InParanoid; A4IHD2; -.
DR   OrthoDB; 815681at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000070; Expressed in 4-cell stage embryo and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd18069; DEXHc_ARIP4; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044574; ARIP4-like.
DR   InterPro; IPR044573; ARIP4_DEXHc.
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; PTHR45797; PTHR45797; 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; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1396
FT                   /note="Helicase ARIP4"
FT                   /id="PRO_0000315783"
FT   DOMAIN          290..510
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          717..891
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1194..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           461..464
FT                   /note="DEAH box"
FT   MOTIF           549..553
FT                   /note="LXXLL motif 1"
FT   MOTIF           1273..1277
FT                   /note="LXXLL motif 2"
FT   COMPBIAS        10..49
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         303..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1396 AA;  156367 MW;  79566FD319FAA98B CRC64;
     MSDASISGSE PELDPEDMEE EEEDDEDDDE EEEEEEDEED NDGDDEDDKQ DINEKSQNAA
     LGEDSPEQGE EGWKRSTTSG QSGQESDEAK KKRLQKPANL RRNIRKLLRE DQLESVTKTA
     QQEELERRKR LEQQRKDYPL PLTLPPVSLD FLQEEIELRA ADVSQLVKSQ EIICLDSSSG
     ESDDEGKVKS HSIKDEIIEL SSGEEDNLQI SDNADSTNEV DGDITTENSG SHVNDALNQA
     DHLGRVLVNI NHPPNEKDIF LAPQLARAVK SHQIGGIRFL YDNLVESLER FSGSSGFGCI
     LAHSMGLGKT LQVISFLDVL FQHTSAKTVL AIVPVNTLQN WLAEFNMWLP PPESLPKDHN
     QELVQPRAFK VHTMNDEHKT TAARAKVVND WATDGGVLLM GYEMYRLLSL KKSFTAGRKK
     KSKKAAGPVI IDLDEEDRQQ EMLKGIEKAL SRPGPDVVIC DEGHRIKNCH ASTSQALKNI
     RSRRRVVLTG YPLQNNLIEY WCMVDFVRPD FLGTRQEFSN MFERPILNGQ CVDSTPQDKR
     LMRYRSHVLH SLLEGFVQRR GHTVLKAQLP FKEEHVILVR LSKIQRDLYT EFMNRFRDAG
     NSGWLGLNPL KAFCVCCKIW NHPDVLYEAL QKENLANEQD LDVEDLGTNN RCNAQSGKIK
     VEPNSLGALM GETAHTKQLQ GIVLNPSHEK ANQVVTYEWA KEILSDYIPG QLQNSPKMVL
     LFHLIEESMR MGDKILVFSQ SLSTLSIMEE FLAKRKMPIP AGSDGQEGHT WIRNVNYYRL
     DGSTSASERE RLINQFNDPS NEKVWLFLLS TRAGCLGVNL IGANRVVVFD ASWNPCHDAQ
     AVCRVYRYGQ RKPCYIYRLV SDFTLEKKIY DRQITKQGMS DRVVDDLNPE VNFTRREVEN
     LLHFVEEEPD ASRQHLDSSS FHEAVLQKAC LQYPHLITKE PFQHESLLLD RKEQKLTLAE
     KKAAKRGYEE EKRASVPYTR PSYTQYYPAP DHNLGNIPAF SQRHWRPLMK GDDRPVASVR
     PLQSTPIPML PRHVSVNHPG SASASVHPYN FPVNYLQRAG VLVQKVVTTT DIVIPGMTTS
     TDVQARISAG ESIHVIRGTK GTYIRTSDGR IFAIRASGKQ KSGEVRRQAT SGAQGSSAPY
     LSNGRHSTSS PSQQDSEDPP RPLSPDSPEI LNELQKYADA AAARGSHTAP QLQNLGLHHQ
     GINPAPKLQP RKRKDPQDQS SHWPSNKRNP YSQLSYPNTG GFGVTPSTMN HNLVRSSNPV
     FMGPGGGSSH FQLPSLLSDP QTGLPLVQDS LLTHSSGTSS APSVPPHYLL PRGFPLPFSQ
     SLLPQTRMFA PYPSQILNRG LPTNNPASTF PGYLSSHSNY QASPGTSSRP LPSGETELGS
     CEEDGRDDDV VEVTGE