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DRE2_ASPFN
ID   DRE2_ASPFN              Reviewed;         313 AA.
AC   B8NL00;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Fe-S cluster assembly protein dre2 {ECO:0000255|HAMAP-Rule:MF_03115};
DE   AltName: Full=Anamorsin homolog {ECO:0000255|HAMAP-Rule:MF_03115};
GN   Name=dre2 {ECO:0000255|HAMAP-Rule:MF_03115}; ORFNames=AFLA_095840;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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 scaffold complex
CC       cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the
CC       FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for
CC       the 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 rnr2.
CC       {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03115};
CC   -!- SUBUNIT: Monomer. Interacts with tah18. Interacts with mia40.
CC       {ECO:0000255|HAMAP-Rule:MF_03115}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03115}.
CC       Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03115}.
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}.
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DR   EMBL; EQ963480; EED49502.1; -; Genomic_DNA.
DR   RefSeq; XP_002381403.1; XM_002381362.1.
DR   AlphaFoldDB; B8NL00; -.
DR   STRING; 5059.CADAFLAP00009268; -.
DR   EnsemblFungi; EED49502; EED49502; AFLA_095840.
DR   VEuPathDB; FungiDB:AFLA_095840; -.
DR   eggNOG; KOG4020; Eukaryota.
DR   HOGENOM; CLU_067152_1_0_1; -.
DR   OMA; KRPINIP; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03115; Anamorsin; 1.
DR   InterPro; IPR007785; Anamorsin.
DR   InterPro; IPR046408; CIAPIN1.
DR   InterPro; IPR031838; Dre2_N.
DR   PANTHER; PTHR13273; PTHR13273; 1.
DR   Pfam; PF05093; CIAPIN1; 1.
DR   Pfam; PF16803; DRE2_N; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion.
FT   CHAIN           1..313
FT                   /note="Fe-S cluster assembly protein dre2"
FT                   /id="PRO_0000392378"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          20..145
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          146..203
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          151..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..230
FT                   /note="Fe-S binding site A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          276..290
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           276..279
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           287..290
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   COMPBIAS        160..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         228
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         230
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         276
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         279
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         287
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         290
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
SQ   SEQUENCE   313 AA;  33761 MW;  03CFB8B0522F4C08 CRC64;
     MSITIDTSVD IDLPTPPQSN GSQKRNLLLA PPSVAAHEEK LRDVFSTFDR SSTDLQMLDR
     LSAGFVSLPP NTYDLVLVLT DAQSDEAVRL LTRDVYTALV PAMKAGARLQ LQQGSLGASE
     GLEAILAGLV EKDGGFEKPV QEAAVPLKLG GRKKKDKTNG VNGVQNGVAT NGASTNGVGM
     FDPAQNNDDE LIDEDALLSD DDLKRPLPRP QNCVPETAKK RRRPCKDCTC GLASQLEEED
     RAREAKAAQD LNILKLNTDD LNDELDFTVQ GKTSSCNSCS LGDAFRCSSC PYIGLPPFKP
     GEEVKIMNDM VQL
 
 
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