RH3A_MAIZE
ID RH3A_MAIZE Reviewed; 745 AA.
AC A0A1D6GDY8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase 3A, chloroplastic {ECO:0000305};
DE Short=ZmRH3A {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE Flags: Precursor;
GN Name=RH3A {ECO:0000305};
GN ORFNames=ZEAMMB73_Zm00001d012922 {ECO:0000312|EMBL:AQK61830.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
CC -!- FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis
CC in chloroplasts. Binds specific group II introns in chloroplasts and
CC facilitates their splicing. Required for normal development of
CC chloroplasts. {ECO:0000250|UniProtKB:A0A1D6LAB7}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
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DR EMBL; CM000781; AQK61830.1; -; Genomic_DNA.
DR RefSeq; XP_008681151.1; XM_008682929.1.
DR AlphaFoldDB; A0A1D6GDY8; -.
DR SMR; A0A1D6GDY8; -.
DR STRING; 4577.GRMZM2G415491_P01; -.
DR EnsemblPlants; Zm00001eb211400_T001; Zm00001eb211400_P001; Zm00001eb211400.
DR GeneID; 100193526; -.
DR Gramene; Zm00001eb211400_T001; Zm00001eb211400_P001; Zm00001eb211400.
DR eggNOG; KOG0331; Eukaryota.
DR OrthoDB; 1139373at2759; -.
DR BRENDA; 3.6.4.13; 6752.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; A0A1D6GDY8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; ISS:UniProtKB.
DR GO; GO:0000373; P:Group II intron splicing; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Ribosome biogenesis;
KW RNA-binding; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..745
FT /note="DEAD-box ATP-dependent RNA helicase 3A,
FT chloroplastic"
FT /id="PRO_0000441394"
FT DOMAIN 119..295
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 324..469
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 727..744
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 606..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 88..116
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 243..246
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 650..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 745 AA; 80384 MW; 7885203EC936E5BD CRC64;
MASLVTLPAI AFSNPATASG AVRLRAAAFR CWALRRRGWA VAAAVASPNS VLSEHAFKRL
QLGSDDEDEE GPYGSDADEG FQGDEEELAI ARLGLPDELV ATLEKRGITH LFPIQRAVLI
PALGGRDLIA RAKTGTGKTL AFGIPMIKQL MEQDDGRSTR RGRTPRVLVL APTRELAKQV
EKEIKESAPK LGTVCVYGGV SYNVQQNALS RGVDVVVGTP GRIIDLINGG SLQLGEVQYL
VLDEADQMLA VGFEEDVETI LQQLPADRQS MLFSATMPSW VKKLSRRYLN NPLTIDLVGD
QDEKLAEGIK LHAIPLTATS KRTILSDLIT VYAKGGKTIV FTRTKKDADE VSLALTTSIA
SEALHGDISQ HQRERTLNGF RQGKFTVLVA TDVAARGLDI PNVDLIIHYE LPNDPETFVH
RSGRTGRAGK AGTAILMFTS SQKRTVMSLE RDVGCKFEFI SPPSIEEVLE SSAEHVIATL
RGVHPESTQY FLGAAEKLTE ELGPHALASA LAHLSGFSQP PSSRSLISYE QGWVTLQLTR
EPGYGRGFFS PRSVTGFLSD VCSAAADEVG KIYITADENV QGAVFDLPEE IAKDLLTMEV
PPGNTLTKIS KLPALQDDSP ATDSYGRFSN DRGSRNRRSR GGGASRGRGG WDTDSEDRYR
RGGRSLRSDN DSWSDDDWSG GGRKSNRSSS SFGGRSSSYG SRGSPSPSFG VRSSSLGGRE
SSRSFSGACF NCGESGHRAS DCPNK
