ID A0A0N4UAQ1_DRAME Unreviewed; 933 AA.
AC A0A0N4UAQ1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000256|HAMAP-Rule:MF_03038};
GN ORFNames=DME_LOCUS8125 {ECO:0000313|EMBL:VDN58152.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000424201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000424201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN58152.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
CC 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}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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DR EMBL; UYYG01001165; VDN58152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4UAQ1; -.
DR STRING; 318479.A0A0N4UAQ1; -.
DR WBParaSite; DME_0000424201-mRNA-1; DME_0000424201-mRNA-1; DME_0000424201.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
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:0016746; F:acyltransferase activity; IEA:InterPro.
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:0006281; P:DNA repair; IEA:UniProt.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR CDD; cd22325; ERCC1_C-like; 1.
DR CDD; cd00834; KAS_I_II; 1.
DR CDD; cd02037; Mrp_NBP35; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.10130; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR047260; ERCC1-like_central_dom.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR033756; YlxH/NBP35.
DR NCBIfam; TIGR00597; rad10; 1.
DR PANTHER; PTHR23264:SF19; CYTOSOLIC FE-S CLUSTER ASSEMBLY FACTOR NUBP1; 1.
DR PANTHER; PTHR23264; NUCLEOTIDE-BINDING PROTEIN NBP35 YEAST -RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF10609; ParA; 1.
DR Pfam; PF03834; Rad10; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01215; MRP; 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:UP000274756};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 535..930
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT BINDING 222
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 236
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 239
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 245
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 276..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 450
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 453
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 933 AA; 101562 MW; ABD494346C7E4A54 CRC64;
MEFKPEYFSG SMTSGSKLLI NLRRQKGNPL LKYVRNIPFE WADIKADFEA GKEMGILYLS
LKWHKLHPNY IETRMNSDGS GYPIKVLLVL VNVEARFILR ELNLFCYRTG WTLILCYSAE
EAAEYLENIH LSRNKDEHSA IVAILERKKK RMGIADDTEI QQAVNFLCGI RSVTNSDAQR
LIGTFGSIHR IANANLESLL LCPGLGPDSQ MSDIPENANE HCPGTQSENA GKASSCAGCP
NQATCASGEA RSFDPDIALI ADRLGAVKHK ILILSGKGGV GKSLVTANLA RALAMDKSKQ
IAILDVDICG PSQARIMGME DESVHESAEG WSPIYVQDNL AMMSIAFLLQ NRNDAVIWRG
ARKNALIKQF LKDVNWGSID YLLIDTPPGT SDEHISIVQF LLQAGSIDGA ILVTTPQEIS
LLDVRKEISF CRKTGVPILG IIENMASFIC LCCFNSSKLF PSTTGGAKAM CVELCVKLLM
SLPFDPRMAE CADLGEDFFD KCPDSPAVKS FLELASFIIP EISDKEIKFI SLKMVHRVVI
TGIGIVSPFG VGRKILFENL IAGNVSLKYD SMVKTVVGKI PEGTAKNELN LALWRDGERR
QMSRGSLLAL LAADEALKDS KLNETDLKET GVNVGMGIAD LEMIVEVANL IKDGKNRKVT
PFFIPRILTN MPAGHISIRY GLQGPNMSSC TACATGLHAI GDAATFIAIG RAKRMIAGAT
EACINPIAIT GFQRLRALSS TASRPFHRLR DGFILSEGAA IVILERLEDA KKRHALIYAE
IKGYGASSDG FHLTSPTEDG IGAKLSMQRC LEDSHLTPSE IGYINAHATS TPLGDRAEAY
AISELFPNVF VSSIKGHIGH TLAAAGAIET AITAMCIHER IIVGNALLDD TDIMENIQLL
RTSVEWNQKI NALVNSFGFG GPHATLCLSA VQN
//
