ID G0SH86_CHATD Unreviewed; 310 AA. AC G0SH86; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 24-JAN-2024, entry version 45. DE SubName: Full=Cytosolic Fe-S cluster assembling factor cfd1-like protein {ECO:0000313|EMBL:EGS17575.1}; GN ORFNames=CTHT_0069100 {ECO:0000313|EMBL:EGS17575.1}; OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) OS (Thermochaetoides thermophila). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides. OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066}; RN [1] {ECO:0000313|EMBL:EGS17575.1, ECO:0000313|Proteomes:UP000008066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719 RC {ECO:0000313|Proteomes:UP000008066}; RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039; RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P., RA Arumugam M., Bork P., Hurt E.; RT "Insight into structure and assembly of the nuclear pore complex by RT utilizing the genome of a eukaryotic thermophile."; RL Cell 146:277-289(2011). RN [2] {ECO:0007829|PDB:6G2G} RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS). RX PubMed=30201724; DOI=10.1073/pnas.1807762115; RA Stehling O., Jeoung J.H., Freibert S.A., Paul V.D., Banfer S., RA Niggemeyer B., Rosser R., Dobbek H., Lill R.; RT "Function and crystal structure of the dimeric P-loop ATPase CFD1 RT coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 115:E9085-E9094(2018). 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:0000256|HAMAP-Rule:MF_03039}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_03039}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC NUBP2/CFD1 subfamily. {ECO:0000256|HAMAP-Rule:MF_03039}. 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; GL988047; EGS17575.1; -; Genomic_DNA. DR RefSeq; XP_006697193.1; XM_006697130.1. DR PDB; 6G2G; X-ray; 2.57 A; A/B=1-310. DR PDBsum; 6G2G; -. DR AlphaFoldDB; G0SH86; -. DR SMR; G0SH86; -. DR STRING; 759272.G0SH86; -. DR GeneID; 18260948; -. DR KEGG; cthr:CTHT_0069100; -. DR eggNOG; KOG3022; Eukaryota. DR HOGENOM; CLU_024839_0_1_1; -. DR OMA; KTMMIKQ; -. DR OrthoDB; 228512at2759; -. DR Proteomes; UP000008066; 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 CDD; cd02037; Mrp_NBP35; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR HAMAP; MF_03039; NUBP2; 1. DR InterPro; IPR000808; Mrp-like_CS. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR028600; NUBP2/Cfd1_eukaryotes. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033756; YlxH/NBP35. DR PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP2; 1. DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01215; MRP; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6G2G}; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03039}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03039}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03039}; KW Iron {ECO:0000256|HAMAP-Rule:MF_03039}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03039}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03039}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03039}; Reference proteome {ECO:0000313|Proteomes:UP000008066}. FT BINDING 15..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039" FT BINDING 199 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039" FT BINDING 202 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039" SQ SEQUENCE 310 AA; 33239 MW; 0F3BE634AEB4BD6E CRC64; MSLSQVKHII LVLSGKGGVG KSSVTTQLAL SLSQAGYSVG VLDVDLTGPS IPRMFAVEDA KVKQGSGGWL PVVVHEANPS TGIGSLRVMS LGFLLPRRGD AVIWRGPKKT AMVRQFMSDV LWDELDFLLV DTPPGTSDEH ISLAETLLQE ARPGQLSGAI VVTTPQAVAT ADVRKELNFC KKTGIRVLGV VENMSGFVCP NCSECTNIFS SGGGEIMAND FNVRFLGRVP IDPQFLVLIE TGKRPRYPEG TKVNSQDLSF QHLEQVDNAD NPETPNSSLL VDKYRDCSLA PIFRAITADV VVAVEQASGS //