位置:首页 > 蛋白库 > DRE2_ASPCL
DRE2_ASPCL
ID   DRE2_ASPCL              Reviewed;         310 AA.
AC   A1CQP0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
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=ACLA_026830;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW07961.1; 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; DS027059; EAW07961.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001269387.1; XM_001269386.1.
DR   AlphaFoldDB; A1CQP0; -.
DR   STRING; 5057.CADACLAP00001638; -.
DR   EnsemblFungi; EAW07961; EAW07961; ACLA_026830.
DR   GeneID; 4701480; -.
DR   KEGG; act:ACLA_026830; -.
DR   eggNOG; KOG4020; Eukaryota.
DR   OrthoDB; 1588798at2759; -.
DR   Proteomes; UP000006701; 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;
KW   Reference proteome.
FT   CHAIN           1..310
FT                   /note="Fe-S cluster assembly protein dre2"
FT                   /id="PRO_0000392377"
FT   REGION          1..130
FT                   /note="N-terminal SAM-like domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          131..203
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          212..228
FT                   /note="Fe-S binding site A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   REGION          273..287
FT                   /note="Fe-S binding site B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           273..276
FT                   /note="Cx2C motif 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   MOTIF           284..287
FT                   /note="Cx2C motif 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         212
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         223
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03115"
FT   BINDING         226
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         273
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
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         284
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"
SQ   SEQUENCE   310 AA;  33963 MW;  1DA4528ED8B9B190 CRC64;
     MSGRTLLLSP PSLSSQPERL NGILQSYDRK TTDLQMLDRL ILGVVNLPDA AYSRIIILAG
     EEDSISESSK LTTRETFSHI ARSLQKGGYI CSQHEQQGQA FDHNEAVLVG LIPTDNGKFV
     KPDIEDMRAV PLRLGRKKHD KTISSNLAEP VRNHQASPTV AQDQAEDGFR YSSGRNIVTA
     SAHETSDNEI IDEEDLLDGS ELAAPIIQPP ECRPKAGRRR RACKDCTCGL AQKLEEEDAM
     RRHAADKQLG AMKLSHGDLA EVDFTVQGKV GSCGNCSLGD AFRCEGCPFI GLPAFQPGEE
     IRLLNDDIQL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024