ID A0A3P8RS21_AMPPE Unreviewed; 845 AA.
AC A0A3P8RS21;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000002827.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000002827.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000002827.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Evidence={ECO:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR AlphaFoldDB; A0A3P8RS21; -.
DR STRING; 161767.ENSAPEP00000002827; -.
DR Ensembl; ENSAPET00000002891.1; ENSAPEP00000002827.1; ENSAPEG00000002040.1.
DR GeneTree; ENSGT00940000157013; -.
DR Proteomes; UP000265080; Chromosome 21.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0032392; P:DNA geometric change; IEA:UniProt.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd18015; DEXHc_RecQ1; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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, ECO:0000256|RuleBase:RU364117};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT DOMAIN 114..289
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 313..464
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 645..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..46
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 655..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 95235 MW; 61BBD488DAC088E5 CRC64;
MDGGTTDVQA ELDSVEAELE LVELQIAELL QKQTELTSRK NALLRQVEEA CNAAKPSSSS
SVPSSKSPGA NLVMSEQEMQ RYDGTDFPWS REVEQHLKDS FHLSKFRPLQ LRAINLTMTG
KDLFLVMPTG RGKSLCYQLP AVCSKGFTLV VTPLVSLMED QIMYLKSIEL SAVMLNASSS
KDHAKTVMAG ITDPKGPFKL LYVTPEKIAK SKLLMSRLEK AYNANLLSRI AVDEVHCCSQ
WGHDFRPDYK LLGILKRQFS KVPLLGLTAT ATSSVLKDCE EILCVPKPIT LTASFNRTNL
YYEVRIKDSD DASISDIASL VKSRYKDQSG IVYVFSQKDA ESVAAELQKR DILAYPYHAN
MDPDDKSQVH RRWTYNKIQV VVATVAFGMG IDKPDVRFVI HHTISKSIEN YYQESGRAGR
DDRPADCIVY FGFADIFRIS TMVVMENVGQ QKLLQMVDYC QNVDRCRRSL MAVHFDEVWD
NEGCSQMCDT CRHSKDYTTM DITQHAREVV QIVELATSMD EKLTPLKLVE AWMGKGPAKR
RKMIQTTTLP RRQAEAVVVR LLLQGYLRED FSFTPYTTYF YMKLGRKVPL LKSQTHTLNM
KMRTTGTGAA VDTSAVKANE EEVHMTSVPI VMENSCPLQP KQKLFKEQRN QSRKQDLKPV
NQTDGQTETG KSQLADRHKE EDKRRPIISQ HVVEVDIEIN RVHNIGLSDV QKTPSHPVKP
CSKHKSTTPQ KAKRKLHANV AAGVPSPNPG SSTPASTVPS SPSQASIISD TAAEELCDLR
NYYSKQLKRI NYISHEYLGQ PAETGVLACI REPLKSFRLP RRMTISQTAR SLWTRVSGRR
KLLHR
//
