NIFU1_ARATH
ID NIFU1_ARATH Reviewed; 231 AA.
AC Q93W77; Q9SYJ1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=NifU-like protein 1, chloroplastic;
DE Short=AtCNfu1;
DE Short=AtCnfU-IVb;
DE Flags: Precursor;
GN Name=NIFU1; Synonyms=CNFU1, NFU1; OrderedLocusNames=At4g01940;
GN ORFNames=T7B11.20;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12553879; DOI=10.1042/bj20021946;
RA Leon S., Touraine B., Ribot C., Briat J.-F., Lobreaux S.;
RT "Iron-sulphur cluster assembly in plants: distinct NFU proteins in
RT mitochondria and plastids from Arabidopsis thaliana.";
RL Biochem. J. 371:823-830(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15031412; DOI=10.1105/tpc.020511;
RA Yabe T., Morimoto K., Kikuchi S., Nishio K., Terashima I., Nakai M.;
RT "The Arabidopsis chloroplastic NifU-like protein CnfU, which can act as an
RT iron-sulfur cluster scaffold protein, is required for biogenesis of
RT ferredoxin and photosystem I.";
RL Plant Cell 16:993-1007(2004).
CC -!- FUNCTION: Molecular scaffold for [Fe-S] cluster assembly of
CC chloroplastic iron-sulfur proteins. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12553879, ECO:0000269|PubMed:15031412}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in floral stalks and
CC siliques. Expressed in leaves, cauline leaves, flower stalks and
CC flowers (at protein level). {ECO:0000269|PubMed:12553879,
CC ECO:0000269|PubMed:15031412}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22656.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80687.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ512933; CAD55558.1; -; mRNA.
DR EMBL; AC007138; AAD22656.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161493; CAB80687.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82103.1; -; Genomic_DNA.
DR EMBL; AY039552; AAK62607.1; -; mRNA.
DR EMBL; AY050363; AAK91380.1; -; mRNA.
DR EMBL; AY102161; AAM26728.1; -; mRNA.
DR PIR; H85024; H85024.
DR RefSeq; NP_567219.1; NM_116425.3.
DR AlphaFoldDB; Q93W77; -.
DR SMR; Q93W77; -.
DR STRING; 3702.AT4G01940.1; -.
DR PaxDb; Q93W77; -.
DR PRIDE; Q93W77; -.
DR ProteomicsDB; 249384; -.
DR EnsemblPlants; AT4G01940.1; AT4G01940.1; AT4G01940.
DR GeneID; 828196; -.
DR Gramene; AT4G01940.1; AT4G01940.1; AT4G01940.
DR KEGG; ath:AT4G01940; -.
DR Araport; AT4G01940; -.
DR TAIR; locus:2141400; AT4G01940.
DR eggNOG; KOG2358; Eukaryota.
DR HOGENOM; CLU_080894_1_0_1; -.
DR InParanoid; Q93W77; -.
DR OMA; EGGDCHV; -.
DR OrthoDB; 1536051at2759; -.
DR PhylomeDB; Q93W77; -.
DR PRO; PR:Q93W77; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93W77; baseline and differential.
DR Genevisible; Q93W77; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR Gene3D; 3.30.300.130; -; 2.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF01106; NifU; 1.
DR SUPFAM; SSF117916; SSF117916; 2.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..231
FT /note="NifU-like protein 1, chloroplastic"
FT /id="PRO_0000247612"
FT DISULFID 126
FT /note="Interchain (with C-129)"
FT /evidence="ECO:0000250"
FT DISULFID 129
FT /note="Interchain (with C-126)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 231 AA; 24768 MW; 4791ED25C75E91DE CRC64;
MMASLATSIS GSFRILVKSS STRNGFPVIS DQNPSFVLFA NKRRHISRTA IFHRSAISGS
SQGEKISPLA SGVSSGLYSA QTFDLTPQNV DLVLEDVRPF LISDGGNVDV VSVEDGVVSL
KLQGACTSCP SSSTTMTMGI ERVLKEKFGD ALKDIRQVFD EEVKQITVEA VNAHLDILRP
AIKNYGGSVE VLSVEGEDCV VKYVGPESIG MGIQAAIKEK FKDISNVTFT S
