ID A0A212FNT3_DANPL Unreviewed; 974 AA.
AC A0A212FNT3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000256|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03065};
GN Name=LOC116767650 {ECO:0000313|RefSeq:XP_032513964.1};
GN ORFNames=KGM_205937 {ECO:0000313|EMBL:OWR55404.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR55404.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR55404.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR55404.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
RN [2] {ECO:0000313|EMBL:OWR55404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR55404.1};
RA Zhan S., Reppert S.M.;
RT "MonarchBase: the monarch butterfly genome database.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_032513964.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: ATP-dependent DNA helicase implicated in DNA repair and the
CC maintenance of genomic stability. Acts as an anti-recombinase to
CC counteract toxic recombination and limit crossover during meiosis.
CC Regulates meiotic recombination and crossover homeostasis by physically
CC dissociating strand invasion events and thereby promotes noncrossover
CC repair by meiotic synthesis dependent strand annealing (SDSA) as well
CC as disassembly of D loop recombination intermediates.
CC {ECO:0000256|HAMAP-Rule:MF_03065}.
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|HAMAP-Rule:MF_03065};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03065}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03065}.
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DR EMBL; AGBW02004392; OWR55404.1; -; Genomic_DNA.
DR RefSeq; XP_032513964.1; XM_032658073.1.
DR STRING; 278856.A0A212FNT3; -.
DR EnsemblMetazoa; XM_032658073.1; XP_032513964.1; LOC116767650.
DR KEGG; dpl:KGM_205937; -.
DR eggNOG; KOG1132; Eukaryota.
DR OrthoDB; 124793at2759; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR Proteomes; UP000596680; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd17970; DEAHc_FancJ; 1.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 1.20.1160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_03065; RTEL1; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030845; RTEL1.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03065};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03065};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03065};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03065};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03065};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03065};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT DOMAIN 7..300
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03065"
SQ SEQUENCE 974 AA; 109945 MW; 621569161B4AE016 CRC64;
MSEIMIYGIP VTFPFEPYEV QKSYMEKVIE SLQNNTNAVL ESPTGTGKTL SLLCSSLAWL
LVKKAQLQMN AQLGNFSEHS GYSNALRDNL KSNAGKSKDN TSWGMPKIIY SSRTHSQLTQ
AMQELKRSSY RHVKAAVLGS RDQMCIHPEV SKETNNMNKV HMCQLKVKSR TCHFYNNVES
KKDDRSVKGD DILDIEDLVS VGKKLKCCPY YLSKELKQDA DIIFMPYNYL LDPKSRRANG
VELMNNIIIL DEAHNVEKMC EESASLQIRT TDVALCIDEI TYIMKSFADG EDLDVTLDPN
QPKDFTCDDL CTLKEMMLAF EKAVDEIQVG SEGSTFPGGY IFELLSKAEI TDRNQMSVIG
LIENLIQYLS TASSSPFTRK GVGLQKIVDL LNVVFSGTTV AYKERVKLCY KVHVQVEDKK
NNKKTDSWGA LKASNTKSAE RVLSYWCFSP GFGMKQLLEQ NVRSIILTSG TLAPLKPLIS
ELGIPIGVQL ENPHIVKSNQ IHVKIIGQGP DSETLNSNYQ NRNNPKYISS LGRTILSFSR
VIPDGLLVFF PSYPIMTKCQ EMWQAEGIWS SINSIKPIFV EPQRKDTFNS IINDYYSKIR
DPNSRGACFM AVCRGKVSEG LDFADMNGRA VIITGLPFPP LKDPRIILKK KYLEELRVNQ
KEYLSGDEWY SLEASRAVNQ AIGRVIRHQN DYGAILLCDT RFNNPKLKNQ LSAWLRDHIV
VSNKFGLTVS EICRFFKNAE ASLPTPKLKP LLPHESNTNF KESGAPSLTG VSFPVTNSRT
VNKAKTINTV SQYPNSNEVY ADFSIDFYKN AQASTYVNEF KPKATKDLFS ALDGSSSTRG
TSESLVTINK RPSQDIPILA ASKKKKLKIK SFGFEENLHN GGTSELPKER MAPTSLIDFV
KEIKTLLEPD EYKKFQLSIS TYKKEGDYDV FLKMLSELLE NSRLFYLFKG MKRFLKDDHK
QAFDEYCDNV KFPS
//
