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ISCAP_ARATH
ID   ISCAP_ARATH             Reviewed;         180 AA.
AC   Q9XIK3; Q6NM99;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Iron-sulfur assembly protein IscA, chloroplastic;
DE   AltName: Full=Plastid SufA-like protein;
DE   AltName: Full=Protein scaffold protein AtCpIscA;
DE   Flags: Precursor;
GN   Name=ISCA; OrderedLocusNames=At1g10500; ORFNames=T10O24.11;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=15888686; DOI=10.1104/pp.104.058602;
RA   Abdel-Ghany S.E., Ye H., Garifullina G.F., Zhang L., Pilon-Smits E.A.H.,
RA   Pilon M.;
RT   "Iron-sulfur cluster biogenesis in chloroplasts. Involvement of the
RT   scaffold protein CpIscA.";
RL   Plant Physiol. 138:161-172(2005).
RN   [2]
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   [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;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the assembly of chloroplastic iron-sulfur
CC       proteins. Is able to transfer iron-sulfur clusters to apo-ferredoxin.
CC       {ECO:0000269|PubMed:15888686}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per dimer. The dimer may bind additional iron
CC       ions. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; may form tetramers and higher multimers.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:15888686}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous with higher expression level in green,
CC       photosynthetic tissues. {ECO:0000269|PubMed:15888686}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. Ycf83 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD39571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY971959; AAY40769.1; -; mRNA.
DR   EMBL; AC007067; AAD39571.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28586.1; -; Genomic_DNA.
DR   EMBL; BT010894; AAR24672.1; -; mRNA.
DR   EMBL; BT011763; AAS65934.1; -; mRNA.
DR   PIR; F86238; F86238.
DR   RefSeq; NP_172520.1; NM_100924.3.
DR   AlphaFoldDB; Q9XIK3; -.
DR   SMR; Q9XIK3; -.
DR   STRING; 3702.AT1G10500.1; -.
DR   PaxDb; Q9XIK3; -.
DR   PRIDE; Q9XIK3; -.
DR   ProteomicsDB; 247134; -.
DR   EnsemblPlants; AT1G10500.1; AT1G10500.1; AT1G10500.
DR   GeneID; 837590; -.
DR   Gramene; AT1G10500.1; AT1G10500.1; AT1G10500.
DR   KEGG; ath:AT1G10500; -.
DR   Araport; AT1G10500; -.
DR   TAIR; locus:2194594; AT1G10500.
DR   eggNOG; KOG1120; Eukaryota.
DR   HOGENOM; CLU_069054_3_0_1; -.
DR   InParanoid; Q9XIK3; -.
DR   OMA; FSAITTH; -.
DR   OrthoDB; 1360948at2759; -.
DR   PhylomeDB; Q9XIK3; -.
DR   PRO; PR:Q9XIK3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XIK3; baseline and differential.
DR   Genevisible; Q9XIK3; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:TAIR.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
DR   Gene3D; 2.60.300.12; -; 1.
DR   InterPro; IPR000361; FeS_biogenesis.
DR   InterPro; IPR016092; FeS_cluster_insertion.
DR   InterPro; IPR017870; FeS_cluster_insertion_CS.
DR   InterPro; IPR035903; HesB-like_dom_sf.
DR   InterPro; IPR031108; ISCA_plant_cyanobact.
DR   PANTHER; PTHR47265; PTHR47265; 1.
DR   Pfam; PF01521; Fe-S_biosyn; 1.
DR   SUPFAM; SSF89360; SSF89360; 1.
DR   TIGRFAMs; TIGR00049; TIGR00049; 1.
DR   PROSITE; PS01152; HESB; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..180
FT                   /note="Iron-sulfur assembly protein IscA, chloroplastic"
FT                   /id="PRO_0000077033"
FT   BINDING         104
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         170
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         172
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ   SEQUENCE   180 AA;  19337 MW;  FAF5D859F06B7AFF CRC64;
     MAFATGITTS SNPTFLGLKI SNTSLRSVVS CNSISFPSLS YVNLNLNRRN RLSVRSASVP
     AAPAMEGLKP AISLSENALK HLSKMRSERG EDLCLRIGVK QGGCSGMSYT MDFENRANAR
     PDDSTIEYQG FTIVCDPKSM LFLFGMQLDY SDALIGGGFS FSNPNATQTC GCGKSFAAEM
 
 
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