TWIH_ARATH
ID TWIH_ARATH Reviewed; 709 AA.
AC B5X582; Q8GUI8; Q9SA83;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Twinkle homolog protein, chloroplastic/mitochondrial;
DE AltName: Full=DNA helicase;
DE EC=3.6.4.12;
DE AltName: Full=DNA primase;
DE EC=2.7.7.-;
DE Flags: Precursor;
GN OrderedLocusNames=At1g30680; ORFNames=T5I8.13;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19036033; DOI=10.1111/j.1365-313x.2008.03745.x;
RA Carrie C., Kuehn K., Murcha M.W., Duncan O., Small I.D., O'Toole N.,
RA Whelan J.;
RT "Approaches to defining dual-targeted proteins in Arabidopsis.";
RL Plant J. 57:1128-1139(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23452619; DOI=10.1186/1471-2229-13-36;
RA Diray-Arce J., Liu B., Cupp J.D., Hunt T., Nielsen B.L.;
RT "The Arabidopsis At1g30680 gene encodes a homologue to the phage T7 gp4
RT protein that has both DNA primase and DNA helicase activities.";
RL BMC Plant Biol. 13:36-36(2013).
CC -!- FUNCTION: Has both DNA primase and DNA helicase activities and may be
CC involved in organelle DNA replication. Capable of producing RNA primers
CC of 9 to 18 bases from a single-stranded DNA template.
CC {ECO:0000269|PubMed:23452619}.
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:0000269|PubMed:23452619};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:23452619}. Mitochondrion
CC {ECO:0000269|PubMed:19036033, ECO:0000305|PubMed:23452619}.
CC -!- TISSUE SPECIFICITY: Expressed in young leaves and shoot apex tissues.
CC Detected in developing tissues such as cotyledons, sepals, pistils and
CC inflorescences. Nearly undetectable in mature leaves.
CC {ECO:0000269|PubMed:23452619}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007060; AAD25755.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31259.1; -; Genomic_DNA.
DR EMBL; BT002484; AAO00844.1; -; mRNA.
DR EMBL; BT046201; ACI49800.1; -; mRNA.
DR PIR; C86432; C86432.
DR RefSeq; NP_849735.1; NM_179404.3.
DR AlphaFoldDB; B5X582; -.
DR SMR; B5X582; -.
DR STRING; 3702.AT1G30680.1; -.
DR PaxDb; B5X582; -.
DR PRIDE; B5X582; -.
DR ProteomicsDB; 234636; -.
DR EnsemblPlants; AT1G30680.1; AT1G30680.1; AT1G30680.
DR GeneID; 839948; -.
DR Gramene; AT1G30680.1; AT1G30680.1; AT1G30680.
DR KEGG; ath:AT1G30680; -.
DR Araport; AT1G30680; -.
DR TAIR; locus:2204584; AT1G30680.
DR eggNOG; ENOG502QPXS; Eukaryota.
DR HOGENOM; CLU_020382_0_0_1; -.
DR InParanoid; B5X582; -.
DR OMA; DDEHYKD; -.
DR OrthoDB; 212176at2759; -.
DR PhylomeDB; B5X582; -.
DR BRENDA; 3.6.4.12; 399.
DR PRO; PR:B5X582; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B5X582; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0003896; F:DNA primase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0009260; P:ribonucleotide biosynthetic process; IDA:TAIR.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; PTHR12873; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Nucleotidyltransferase; Plastid; Primosome; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..709
FT /note="Twinkle homolog protein,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000422119"
FT DOMAIN 280..385
FT /note="Toprim"
FT DOMAIN 430..698
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT CONFLICT 552
FT /note="D -> N (in Ref. 3; AAO00844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 80403 MW; 793B687467EEAC1D CRC64;
MRFLLRLPQI HFRKLSCSMS VLMGSKQFLE FCLLPSFASY PSSPSYSSSR QVSSVSRRFR
PVLASRPVSK NSPYYQRTNG LSSYNSIPRV PTPVDTEVEA DKRVVLSRLV TLRRKLAEQG
VDAENCPPGQ HSGLICPTCE GGNSGEKSLS LFIAPDGSSA TWNCFRGKCG LKGGVRADGG
LASADPIEKV ERKITVEGIE LEPLCDEIQD YFAARAISRK TLERNRVMQK RIGDEIVIAF
TYWQRGELVS CKYRSLTKMF FQERKTRRIL YGLDDIEKTS EVIIVEGEID KLAMEEAGFL
NCVSVPDGAP AKVSSKEIPS EDKDTKYKFL WNCNDYLKKA SRIVIATDGD GPGQAMAEEI
ARRLGKERCW RVKWPKKSED EHFKDANEVL MSKGPHLLKE AILDAEPYPI LGLFSFKDFF
DEIDAYYDRT HGHEYGVSTG WKNLDNLYSV VPGELTVVTG IPNSGKSEWI DAMLCNLNHS
VGWKFALCSM ENKVRDHARK LLEKHIKKPF FDADYGRSVQ RMSVEEKDEG KKWLNDTFYP
IRCEMDSLPS IDWVLERAKA AVLRYGIRGL VIDPYNELDH QRTPRQTETE YVSQMLTKIK
RFSQHHSCHV WFVAHPKQLQ HWDGGAPNLY DISGSAHFIN KCDNGIIVHR NRDENAGPLD
LVQIGVRKVR NKVAGQIGDA YLCYDRTTGS YSDSPVTPGM PERRSPKRY
