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MER3_ARATH
ID   MER3_ARATH              Reviewed;        1133 AA.
AC   Q5D892; A0A1I9LN52; Q9LVW8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=DExH-box ATP-dependent RNA helicase DExH17 {ECO:0000305};
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent DNA helicase homolog MER3 {ECO:0000305};
DE            EC=3.6.4.12;
DE   AltName: Full=Protein ROCK-N-ROLLERS {ECO:0000303|PubMed:16045469};
GN   Name=MER3 {ECO:0000303|PubMed:15854901};
GN   Synonyms=RCK {ECO:0000303|PubMed:16045469};
GN   OrderedLocusNames=At3g27730 {ECO:0000312|Araport:AT3G27730};
GN   ORFNames=MGF10.14 {ECO:0000312|EMBL:BAB02697.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15854901; DOI=10.1016/j.cub.2005.02.056;
RA   Mercier R., Jolivet S., Vezon D., Huppe E., Chelysheva L., Giovanni M.,
RA   Nogue F., Doutriaux M.-P., Horlow C., Grelon M., Mezard C.;
RT   "Two meiotic crossover classes cohabit in Arabidopsis: one is dependent on
RT   MER3, whereas the other one is not.";
RL   Curr. Biol. 15:692-701(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16045469; DOI=10.1111/j.1365-313x.2005.02461.x;
RA   Chen C., Zhang W., Timofejeva L., Gerardin Y., Ma H.;
RT   "The Arabidopsis ROCK-N-ROLLERS gene encodes a homolog of the yeast ATP-
RT   dependent DNA helicase MER3 and is required for normal meiotic crossover
RT   formation.";
RL   Plant J. 43:321-334(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [4]
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   [5]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT   in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT   sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: DNA helicase required for crossover formation, complete
CC       synapsis of homologous chromosomes and bivalent formation during
CC       meiosis. Is specific to recombination events resulting in interference-
CC       sensitive crossovers (class I meiotic crossover).
CC       {ECO:0000269|PubMed:15854901, ECO:0000269|PubMed:16045469}.
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=3.6.4.13;
CC         Evidence={ECO:0000305};
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   -!- TISSUE SPECIFICITY: Expressed in meiocytes during meiosis.
CC       {ECO:0000269|PubMed:15854901, ECO:0000269|PubMed:16045469}.
CC   -!- DISRUPTION PHENOTYPE: Low levels of fertility due to a significant
CC       decrease of meiotic crossovers. {ECO:0000269|PubMed:15854901,
CC       ECO:0000269|PubMed:16045469}.
CC   -!- SIMILARITY: Belongs to the DExH box helicase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02697.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY822649; AAX14498.1; -; mRNA.
DR   EMBL; AY960701; AAX58606.1; -; mRNA.
DR   EMBL; AB018114; BAB02697.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77357.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64007.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64010.1; -; Genomic_DNA.
DR   RefSeq; NP_001326060.1; NM_001338909.1.
DR   RefSeq; NP_001326063.1; NM_001338910.1.
DR   RefSeq; NP_189410.2; NM_113689.2.
DR   AlphaFoldDB; Q5D892; -.
DR   SMR; Q5D892; -.
DR   STRING; 3702.AT3G27730.1; -.
DR   PaxDb; Q5D892; -.
DR   PRIDE; Q5D892; -.
DR   EnsemblPlants; AT3G27730.1; AT3G27730.1; AT3G27730.
DR   EnsemblPlants; AT3G27730.6; AT3G27730.6; AT3G27730.
DR   EnsemblPlants; AT3G27730.7; AT3G27730.7; AT3G27730.
DR   GeneID; 822395; -.
DR   Gramene; AT3G27730.1; AT3G27730.1; AT3G27730.
DR   Gramene; AT3G27730.6; AT3G27730.6; AT3G27730.
DR   Gramene; AT3G27730.7; AT3G27730.7; AT3G27730.
DR   KEGG; ath:AT3G27730; -.
DR   Araport; AT3G27730; -.
DR   TAIR; locus:2089144; AT3G27730.
DR   eggNOG; KOG0952; Eukaryota.
DR   HOGENOM; CLU_000335_0_2_1; -.
DR   InParanoid; Q5D892; -.
DR   PhylomeDB; Q5D892; -.
DR   PRO; PR:Q5D892; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q5D892; baseline and differential.
DR   Genevisible; Q5D892; AT.
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:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:TAIR.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:TAIR.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 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; Meiosis; Nucleotide-binding;
KW   Nucleus; Reference proteome; RNA-binding; rRNA-binding.
FT   CHAIN           1..1133
FT                   /note="DExH-box ATP-dependent RNA helicase DExH17"
FT                   /id="PRO_0000432116"
FT   DOMAIN          34..229
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          263..460
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          536..847
FT                   /note="SEC63"
FT                   /evidence="ECO:0000255"
FT   REGION          878..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           165..168
FT                   /note="DEVH box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        889..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1133 AA;  128290 MW;  07583DBD0D5BAB4B CRC64;
     MDTHTLKSVS DLPGNFRSAF SFRYFNSLQS ECFPLCFHSD INMIISAPTG SGKTVLFELC
     ILRLFSKSIS KEGSFLHAKG ALKTVYISPS KALVQEKLRD WNQKFNSWGI SCLELTGDNE
     TYSTKNIQDA DIILTTPEKF DAVSRYRVTS GGLGFFSDIA LVLIDEVHLL NDPRGAALEA
     IVSRLKILSS NHELRSSTLA SVRLLAVSAT IPNIEDLAEW LKVPTAGIKR FGEEMRPVKL
     TTKVFGYAAA KNDFLFEKRL QNYIYDILMQ YSKGKSALVF CSTRKGAQEA AQKLAQTAMT
     YGYSNPFIKS REQLERLREA SPMCSDKQMQ SYILQGVGYH NGGLCQKDRS LVEGLFLNGD
     IQVICTTNTL AHGINLPAHT VVIKSTQHFN KEKGHYMEYD RSTLLQMSGR AGRPPFDDTG
     MVIIMTRRET VHLYENLLNG CEVVESQLLP CLIEHLTAEI VQLTISDITR AIEWMKCSYL
     YVRMKKNPEN YAIKKGIPKD RVEKHLQELC LQKINELSQY QMIWTDTDGF VLKPEEPGRL
     MTKYYLKFET MKYIINTPTS YSLDEALHIV CHAEEISWIQ LRRNEKKTLN DVNADKEGRL
     RFHINDNKGK RKKRIQTREE KLFVLANDWL TGDPSVHDLS MTQDANSICS NGSRIARCMK
     EYFIYKKNYK GTLSSTLLAK SLYQKLWDDS PYLLKQLPGI GMVTAKALHS MGVRSFEALA
     EADPRRIEIV TGRKYPFGNT IKESLSSLPP KVEIKVEEVD CQKQGISKLA VTLSRVSQPL
     QSTKRHYADL IVGSEEENLI HFHEKIRMED FSSPYSVTVL LERPHQQTKV TVKADLIFEE
     YIGIDLHETL LLKKANNNKV NYKSENRMPQ YYPPMASACI ADDDNPVTSG PSNRKDKKDD
     MPSFKLIDDD SEEEKEPYVT MEEDDCVIIN EHTVFDHIRE KAKCFPSLNP LNPTSSPASG
     KSILKRKSLV ENNSPELDPL FQYDSVFDLP TNTKDIKQSA QQITSPGYAS FAEKTETERP
     FSDETIFNYI RKRSKNSPAL ATSKIENPIT ISSQEGRNAE ISPYRTYGLL VSPATKIPRI
     TSDAPSEILS FDISMVKRSD TSLEQTKGFC STLAGKSNVS DSFLGFKSIF SFL
 
 
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