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NBP35_CHAGB
ID   NBP35_CHAGB             Reviewed;         342 AA.
AC   Q2H317;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000255|HAMAP-Rule:MF_03038};
DE   AltName: Full=Nucleotide-binding protein 35 {ECO:0000255|HAMAP-Rule:MF_03038};
GN   Name=NBP35 {ECO:0000255|HAMAP-Rule:MF_03038}; ORFNames=CHGG_03829;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of extramitochondrial
CC       Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold
CC       complex, mediating the de novo assembly of an Fe-S cluster and its
CC       transfer to target apoproteins. {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
CC       Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC       clusters in the N-termini of NBP35 and two labile, bridging clusters
CC       between subunits of the NBP35-CFD1 heterotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_03038};
CC   -!- SUBUNIT: Heterotetramer of 2 NBP35 and 2 CFD1 chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR   EMBL; CH408032; EAQ87210.1; -; Genomic_DNA.
DR   RefSeq; XP_001223043.1; XM_001223042.1.
DR   AlphaFoldDB; Q2H317; -.
DR   SMR; Q2H317; -.
DR   STRING; 38033.XP_001223043.1; -.
DR   EnsemblFungi; EAQ87210; EAQ87210; CHGG_03829.
DR   GeneID; 4392560; -.
DR   eggNOG; KOG3022; Eukaryota.
DR   HOGENOM; CLU_024839_0_1_1; -.
DR   InParanoid; Q2H317; -.
DR   OMA; QHITFKD; -.
DR   OrthoDB; 1166096at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   HAMAP; MF_03038; NUBP1; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR028601; NUBP1/Nbp35.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264; PTHR23264; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..342
FT                   /note="Cytosolic Fe-S cluster assembly factor NBP35"
FT                   /id="PRO_0000278893"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         47
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         56
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         259
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         262
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
SQ   SEQUENCE   342 AA;  36049 MW;  4E0846FC55517F4F CRC64;
     MGPSLETPEP VEDVLANPLK QKPQLVAPEP EHCPGPESEQ AGTADSCAGC PNQAICASAP
     KGPDPDLPAI TARLAGVKHK ILVLSGKGGV GKSTLTAQLA QALATNPEAT VGVMDTDICG
     PSIPKMLGVE AETIHVSGSG WSPVWAADNL AVMSIQFMLP NRDDAIIWRG PKKNGLIKQF
     LKDVEWGDLD FLLVDTPPGT SDEHLSVNTF LKESRIEGAV VVTTPQEVSL LDVRKEIDFC
     RKAGIRILGL VENMSLFVCP KCTHATEIFQ ATTGGGRALA AEMGIPFLGA VPLDPRLGMA
     CDYGESFFDS FPDSPACLAL KQVVRGLAGQ IGLDPKEVVP EG
 
 
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