RTEL1_ARATH
ID RTEL1_ARATH Reviewed; 1040 AA.
AC F4HQE2; Q9CA97; Q9SSD8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000303|PubMed:21081662, ECO:0000303|PubMed:25516598};
DE EC=3.6.4.12 {ECO:0000305};
GN Name=RTEL1 {ECO:0000303|PubMed:21081662, ECO:0000303|PubMed:25516598};
GN OrderedLocusNames=At1g79950 {ECO:0000312|Araport:AT1G79950};
GN ORFNames=F18B13.3 {ECO:0000312|EMBL:AAD55463.1},
GN F19K16.9 {ECO:0000312|EMBL:AAG52242.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP REVIEW, AND IDENTIFICATION.
RX PubMed=21081662; DOI=10.1093/jxb/erq357;
RA Knoll A., Puchta H.;
RT "The role of DNA helicases and their interaction partners in genome
RT stability and meiotic recombination in plants.";
RL J. Exp. Bot. 62:1565-1579(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25516598; DOI=10.1105/tpc.114.132472;
RA Recker J., Knoll A., Puchta H.;
RT "The Arabidopsis thaliana homolog of the helicase RTEL1 plays multiple
RT roles in preserving genome stability.";
RL Plant Cell 26:4889-4902(2014).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25595823; DOI=10.1105/tpc.114.134312;
RA Hu Z., Cools T., Kalhorzadeh P., Heyman J., De Veylder L.;
RT "Deficiency of the Arabidopsis helicase RTEL1 triggers a SOG1-dependent
RT replication checkpoint in response to DNA cross-links.";
RL Plant Cell 27:149-161(2015).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27760121; DOI=10.1371/journal.pgen.1006394;
RA Roehrig S., Schroepfer S., Knoll A., Puchta H.;
RT "The RTR complex partner RMI2 and the DNA helicase RTEL1 are both
RT independently involved in preserving the stability of 45S rDNA repeats in
RT Arabidopsis thaliana.";
RL PLoS Genet. 12:E1006394-E1006394(2016).
CC -!- FUNCTION: ATP-dependent DNA helicase implicated in DNA replication, DNA
CC repair and the maintenance of genomic stability. Acts as an anti-
CC recombinase to counteract toxic recombination and limit crossover
CC during meiosis. Regulates meiotic recombination and crossover
CC homeostasis by physically dissociating strand invasion events and
CC thereby promotes noncrossover repair by meiotic synthesis dependent
CC strand annealing (SDSA) as well as disassembly of D loop recombination
CC intermediates (PubMed:25516598, PubMed:25595823). Also plays a role in
CC preserving the stability of 45S rDNA repeats (PubMed:27760121).
CC {ECO:0000269|PubMed:25516598, ECO:0000269|PubMed:25595823,
CC ECO:0000269|PubMed:27760121}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the
CC interaction with PCNA and localization to replication foci.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased homologous recombination and
CC replication defects (PubMed:25516598, PubMed:25595823). Growth
CC inhibition due to defective cell proliferation. Hypersensitivity to DNA
CC cross-link agents (PubMed:25595823). Loss of 45S rDNA repeats
CC (PubMed:27760121). {ECO:0000269|PubMed:25516598,
CC ECO:0000269|PubMed:25595823, ECO:0000269|PubMed:27760121}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55463.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52242.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009322; AAD55463.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011717; AAG52242.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36333.1; -; Genomic_DNA.
DR PIR; G96830; G96830.
DR RefSeq; NP_178113.3; NM_106644.4.
DR AlphaFoldDB; F4HQE2; -.
DR SMR; F4HQE2; -.
DR STRING; 3702.AT1G79950.1; -.
DR iPTMnet; F4HQE2; -.
DR PaxDb; F4HQE2; -.
DR PRIDE; F4HQE2; -.
DR ProteomicsDB; 228028; -.
DR EnsemblPlants; AT1G79950.1; AT1G79950.1; AT1G79950.
DR GeneID; 844335; -.
DR Gramene; AT1G79950.1; AT1G79950.1; AT1G79950.
DR KEGG; ath:AT1G79950; -.
DR Araport; AT1G79950; -.
DR TAIR; locus:2016209; AT1G79950.
DR eggNOG; KOG1132; Eukaryota.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; F4HQE2; -.
DR OrthoDB; 186062at2759; -.
DR PRO; PR:F4HQE2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQE2; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:UniProtKB.
DR GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IMP:UniProtKB.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IMP:UniProtKB.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0000725; P:recombinational repair; IMP:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0000723; P:telomere maintenance; IMP:TAIR.
DR GO; GO:0090657; P:telomeric loop disassembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
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; IPR036600; PAH_sf.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 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; SSF47762; SSF47762; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1040
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000442765"
FT DOMAIN 52..355
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 289..292
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 992..999
FT /note="PIP-box; degenerate"
FT /evidence="ECO:0000305|PubMed:25595823"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1040 AA; 116632 MW; D9D49FFC069DB261 CRC64;
MGFTVVSRSG SPTRRENQKR RVCFRLLLRL LRRGFVVLSA ESDPKMPNYS IRGINVEFPF
EAYQSQIIYM DRVIESLQNK CHALLESPTG TGKTLCLLCA TLAWRKSLGS FSTRKDRKNS
AIPWSDSDEP LSQSGGGGGG AFPTIVYASR THSQLRQVIK ELKRSSYRPK MVVLGSREQL
CVNEEVNSLR GKALTNACQY LCKKRGKRQC NHFNRLPDYL KHNPHIGDEP VDIEDLVNIG
KDSGPCPYYI TRELHKDVDI IFAPYNYLIS NGYRKFLKVN WTNSVLIFDE AHNLESLCAD
SASFDLPSVL LSACISEAQE CVQLAAARRD SLNDVSINPE NFAILKGLLL KLQELISKVP
IPKRDEGFTK PGPYIYEMLK SLNITHETAP KLIGTVEEAA VFLEEEKQRT ATNAGSKLEI
IADMLKLIFR ENGSNHADVY RVHVQELEQN STDVMKGKVS RTLSWWCFSP GITMLDIAQK
GVGSIILTSG TLSPMDSLAQ ELKLDFPIRL ENPHVISSNQ LWAGVVSTGP SGYVLNSSYR
NRDVPEYKQE LGNAIVNFSR VVPEGLLIFF PSYYLMDSCI TFWKNGCYRN SMTVWERICK
LKKPVIEPKD SSLFPAAMRD FSEKLQDRAT SGVVFFAVCR GKVSEGLDFA DGAGRAVVIT
GLPYARVTDP RVKLKREFLD EQSQLADVKL PRSTLLSGSM WYSQEAARAV NQAIGRVIRH
RHDYGAIIFC DDRFEQPSQQ SKISLWIRPN VKCYSRYGEV ISDLARFFRT ERSNFPARLV
TEQENNIVST LLPVESIEDN PTPAFGNSNL KNVGVAQNEL SRLEAFPPAN RASPLERDGN
NVKRNGLTIL KHTGKIPRIV KGDVMQGCSS RKAKLVELSD DEETPVERRC EVVDLESDNC
ETQTCVTEVL ASSTCLNTMG LKKKRKVPES QGSASSSVLT AKGNGGGDKK EASASAFLSQ
VKEKLNTEEY KKFIGYMQAL KKKEIKLANV MQSIVQLFCG SERDHLLMGF KDFVPVKYRP
AYEECIKTRK RQSIIFGNSN
