ID A0A058ZFL0_FONAL Unreviewed; 359 AA.
AC A0A058ZFL0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000256|HAMAP-Rule:MF_03038};
GN ORFNames=H696_00320 {ECO:0000313|EMBL:KCV72741.1};
OS Fonticula alba (Slime mold).
OC Eukaryota; Rotosphaerida; Fonticulaceae; Fonticula.
OX NCBI_TaxID=691883 {ECO:0000313|EMBL:KCV72741.1};
RN [1] {ECO:0000313|EMBL:KCV72741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38817 {ECO:0000313|EMBL:KCV72741.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Brown M., Walker B., Young S.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fonticula alba ATCC 38817.";
RL Submitted (APR-2013) 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:0000256|HAMAP-Rule:MF_03038}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03038};
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
CC {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily. {ECO:0000256|HAMAP-Rule:MF_03038}.
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DR EMBL; KB932201; KCV72741.1; -; Genomic_DNA.
DR RefSeq; XP_009492442.1; XM_009494167.1.
DR AlphaFoldDB; A0A058ZFL0; -.
DR STRING; 691883.A0A058ZFL0; -.
DR EnsemblProtists; KCV72741; KCV72741; H696_00320.
DR GeneID; 20525045; -.
DR eggNOG; KOG3022; Eukaryota.
DR OMA; KTMMIKQ; -.
DR OrthoDB; 228512at2759; -.
DR Proteomes; UP000030693; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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_03038; NUBP1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP1; 1.
DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR Pfam; PF10609; ParA; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03038};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03038};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03038};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03038}; Reference proteome {ECO:0000313|Proteomes:UP000030693}.
FT DOMAIN 61..275
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 285
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:0000256|HAMAP-Rule:MF_03038"
FT BINDING 288
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:0000256|HAMAP-Rule:MF_03038"
SQ SEQUENCE 359 AA; 37574 MW; 911FF62816FF4688 CRC64;
MSTAELSAPP PQDCPGTSSE AAGKMDACAG CPNQRICASS PPQPAVDPDA AAIAERMLPV
RHRVLVLSGK GGVGKSTVSS QLAWMLSRGG FDADPNAGDD AAGGDDDMDL DPDPEADAWD
VGLVDIDITG PSAPRLLGAG AERLQRTASG LSPVFVSDTL FAVSVGFMLE RSDDAVIWRG
PKKNGLIKQF LRDVDYQPTD VLLVDTPPGT SDEHISIVQL LKQANEITAQ HPEAAATHAG
SKFGAVIVTT PQEVALADVR RELNFCRRVG LPVLGIIENM AGFVCPGCSI NTDIFPATTG
GARSLAQDFD VPFLGSIPID PRVAKACDEG RPIADACPTS PATIAMRRIA NKLKEVLES
//