DRE2_ARATH
ID DRE2_ARATH Reviewed; 272 AA.
AC Q8L7Z3; F4JWM7; Q8L9M1; Q8RXJ2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Anamorsin homolog {ECO:0000255|HAMAP-Rule:MF_03115};
DE AltName: Full=Fe-S cluster assembly protein DRE2 homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN OrderedLocusNames=At5g18400; ORFNames=F20L16.120;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH ATR3.
RX PubMed=20406405; DOI=10.1111/j.1469-8137.2010.03254.x;
RA Varadarajan J., Guilleminot J., Saint-Jore-Dupas C., Piegu B.,
RA Chaboute M.E., Gomord V., Coolbaugh R.C., Devic M., Delorme V.;
RT "ATR3 encodes a diflavin reductase essential for Arabidopsis embryo
RT development.";
RL New Phytol. 187:67-82(2010).
RN [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=23754812; DOI=10.1098/rstb.2012.0259;
RA Bernard D.G., Netz D.J., Lagny T.J., Pierik A.J., Balk J.;
RT "Requirements of the cytosolic iron-sulfur cluster assembly pathway in
RT Arabidopsis.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 368:20120259-20120259(2013).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein
CC assembly (CIA) machinery. Required for the maturation of
CC extramitochondrial Fe-S proteins. Part of an electron transfer chain
CC functioning in an early step of cytosolic Fe-S biogenesis, facilitating
CC the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S
CC scaffold complex. Electrons are transferred from NADPH via FAD- and
CC FMN-containing diflavin oxidoreductase TAH18/ATR3 (PubMed:23754812).
CC Together with the diflavin oxidoreductase, also required for the
CC assembly of the diferric tyrosyl radical cofactor of ribonucleotide
CC reductase (RNR), probably by providing electrons for reduction during
CC radical cofactor maturation in the catalytic small subunit (By
CC similarity). Required for embryo development (PubMed:23754812).
CC {ECO:0000255|HAMAP-Rule:MF_03115, ECO:0000269|PubMed:23754812}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:23754812};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:23754812};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ATR3
CC (PubMed:20406405). {ECO:0000255|HAMAP-Rule:MF_03115,
CC ECO:0000269|PubMed:20406405}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}.
CC Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L7Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L7Z3-2; Sequence=VSP_042905;
CC -!- DOMAIN: The C-terminal domain binds 2 Fe-S clusters but is otherwise
CC mostly in an intrinsically disordered conformation. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- DOMAIN: The N-terminal domain has structural similarity with S-
CC adenosyl-L-methionine-dependent methyltransferases, but does not bind
CC S-adenosyl-L-methionine. It is required for correct assembly of the 2
CC Fe-S clusters. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- DOMAIN: The twin Cx2C motifs are involved in the recognition by the
CC mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2
CC disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange
CC reactions effectively traps the protein in the mitochondrial
CC intermembrane space. {ECO:0000255|HAMAP-Rule:MF_03115}.
CC -!- SIMILARITY: Belongs to the anamorsin family. {ECO:0000255|HAMAP-
CC Rule:MF_03115}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65895.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC051626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92550.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92551.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92552.1; -; Genomic_DNA.
DR EMBL; AY080855; AAL87328.1; -; mRNA.
DR EMBL; AY123986; AAM74499.1; -; mRNA.
DR EMBL; BT000943; AAN41343.1; -; mRNA.
DR EMBL; BT001035; AAN46789.1; -; mRNA.
DR EMBL; AY088356; AAM65895.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001078602.1; NM_001085133.2. [Q8L7Z3-1]
DR RefSeq; NP_568363.1; NM_121845.3. [Q8L7Z3-1]
DR RefSeq; NP_850844.1; NM_180513.1. [Q8L7Z3-2]
DR AlphaFoldDB; Q8L7Z3; -.
DR SMR; Q8L7Z3; -.
DR BioGRID; 17234; 3.
DR IntAct; Q8L7Z3; 1.
DR STRING; 3702.AT5G18400.2; -.
DR iPTMnet; Q8L7Z3; -.
DR PaxDb; Q8L7Z3; -.
DR PRIDE; Q8L7Z3; -.
DR ProteomicsDB; 242300; -. [Q8L7Z3-1]
DR EnsemblPlants; AT5G18400.1; AT5G18400.1; AT5G18400. [Q8L7Z3-2]
DR EnsemblPlants; AT5G18400.2; AT5G18400.2; AT5G18400. [Q8L7Z3-1]
DR EnsemblPlants; AT5G18400.3; AT5G18400.3; AT5G18400. [Q8L7Z3-1]
DR GeneID; 831958; -.
DR Gramene; AT5G18400.1; AT5G18400.1; AT5G18400. [Q8L7Z3-2]
DR Gramene; AT5G18400.2; AT5G18400.2; AT5G18400. [Q8L7Z3-1]
DR Gramene; AT5G18400.3; AT5G18400.3; AT5G18400. [Q8L7Z3-1]
DR KEGG; ath:AT5G18400; -.
DR Araport; AT5G18400; -.
DR TAIR; locus:2146178; AT5G18400.
DR eggNOG; KOG4020; Eukaryota.
DR InParanoid; Q8L7Z3; -.
DR OMA; NVWKLDD; -.
DR OrthoDB; 1588798at2759; -.
DR PhylomeDB; Q8L7Z3; -.
DR PRO; PR:Q8L7Z3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7Z3; baseline and differential.
DR Genevisible; Q8L7Z3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:TAIR.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IGI:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03115; Anamorsin; 1.
DR InterPro; IPR007785; Anamorsin.
DR InterPro; IPR046408; CIAPIN1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13273; PTHR13273; 1.
DR Pfam; PF05093; CIAPIN1; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Alternative splicing; Cytoplasm; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Reference proteome.
FT CHAIN 1..272
FT /note="Anamorsin homolog"
FT /id="PRO_0000392333"
FT REGION 1..156
FT /note="N-terminal SAM-like domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 157..185
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 195..207
FT /note="Fe-S binding site A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT REGION 233..247
FT /note="Fe-S binding site B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 233..236
FT /note="Cx2C motif 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT MOTIF 244..247
FT /note="Cx2C motif 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 195
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 202
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 205
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 207
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT VAR_SEQ 1..3
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042905"
FT CONFLICT 77
FT /note="I -> K (in Ref. 3; AAL87328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 29436 MW; 1A2CEA44C2BEFDD2 CRC64;
MDSMMNQKTV LAVTDDVVLP VSSVLAIMKE LGKEVIESFD PLIITQASTI NQFPLDASSV
EAVLAISKTS DFPSDKICGE FSRILKPGGT VSVCKVLEGE TGEIQQTIQR RVTLAGFLEP
QCLDLKSIKL STFSLSFGIK AKKPSWKIGS SFALKKPVTN LFKIDLDDDV DLIDEDSLLT
EEDLMKPQLP VASGCETTKK ACKNCVCGRA EIEEKAVKLG LTEDQIENPQ SSCGSCGLGD
AFRCGTCPYK GLPPFKLGEK VTLSQNFLEA DI
