NUBP1_DANRE
ID NUBP1_DANRE Reviewed; 321 AA.
AC Q6P298; Q561P6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor nubp1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE AltName: Full=Nucleotide-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03038};
DE Short=NBP 1 {ECO:0000255|HAMAP-Rule:MF_03038};
GN Name=nubp1; ORFNames=zgc:92138;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 nubp1-nubp2 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 nubp1 and two labile, bridging clusters
CC between subunits of the nubp1-nubp2 heterotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_03038};
CC -!- SUBUNIT: Heterotetramer of 2 nubp1 and 2 nubp2 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; BC064668; AAH64668.1; -; mRNA.
DR EMBL; BC093447; AAH93447.1; -; mRNA.
DR RefSeq; NP_001017538.1; NM_001017538.2.
DR AlphaFoldDB; Q6P298; -.
DR SMR; Q6P298; -.
DR STRING; 7955.ENSDARP00000129550; -.
DR PaxDb; Q6P298; -.
DR GeneID; 503919; -.
DR KEGG; dre:503919; -.
DR CTD; 4682; -.
DR ZFIN; ZDB-GENE-050417-471; nubp1.
DR eggNOG; KOG3022; Eukaryota.
DR InParanoid; Q6P298; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q6P298; -.
DR TreeFam; TF300755; -.
DR PRO; PR:Q6P298; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..321
FT /note="Cytosolic Fe-S cluster assembly factor nubp1"
FT /id="PRO_0000382592"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
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 26
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 29
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 35
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 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT BINDING 239
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 242
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 CONFLICT 202
FT /note="I -> V (in Ref. 1; AAH64668)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="V -> I (in Ref. 1; AAH64668)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="D -> V (in Ref. 1; AAH93447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 34112 MW; E1F0DA227C85E60C CRC64;
MADVPNDAPE HCPGTSSDQA GKSSACQGCP NQSICASGAT KAPDPAIEEI KQKMTSVKHK
ILVLSGKGGV GKSTFSAHLS HALASDSSKE VALLDVDICG PSIPKIMGLE GEQVHQSGSG
WSPVYVEDNL AVMSIGFLLS SPDDAVIWRG PKKNGMIKQF LRDVDWGEVD YLIVDTPPGT
SDEHLSIVQY LSGAGIDGAV IITTPQEVSL QDVRKEIRFC KKVNLPILGV IENMSGFVCP
KCKNTSQIFP PTTGGAQRMC EELNLPLLGR IPLDPRIGKS CDEGKSFLTE VPDSPAAAAY
QSIVQKIRDY CASHSASDDS C
