ID A0A371H1Z0_MUCPR Unreviewed; 715 AA.
AC A0A371H1Z0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000256|HAMAP-Rule:MF_03038};
GN Name=NBP35 {ECO:0000256|HAMAP-Rule:MF_03038,
GN ECO:0000313|EMBL:RDX96838.1};
GN ORFNames=CR513_20460 {ECO:0000313|EMBL:RDX96838.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX96838.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDX96838.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDX96838.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-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. Functions as Fe-S scaffold, mediating the de novo
CC assembly of an Fe-S cluster and its transfer to target apoproteins.
CC Essential for embryo development. {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 3 [4Fe-4S] clusters per homodimer. Contains two stable
CC clusters in the N-termini and one labile, bridging cluster between
CC subunits of the homodimer. {ECO:0000256|HAMAP-Rule:MF_03038};
CC -!- SUBUNIT: Homodimer and homotetramer. Predominantly homodimeric.
CC {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03038}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362088}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362088}.
CC -!- MISCELLANEOUS: Although plant and algal NBP35 proteins lack the
CC characteristic CXXC motif in the C-terminus, thought to be required for
CC Fe-S cluster binding, they can bind a [4Fe-4S] cluster in the C-
CC terminus. Also, in this linage, no CFD1 partner protein homolog as
CC found in other eukaryotes can be found. {ECO:0000256|HAMAP-
CC 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 ZIP transporter (TC 2.A.5) family.
CC {ECO:0000256|RuleBase:RU362088}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362088}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDX96838.1}.
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DR EMBL; QJKJ01003803; RDX96838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371H1Z0; -.
DR STRING; 157652.A0A371H1Z0; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
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; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR004698; Zn/Fe_permease_fun/pln.
DR NCBIfam; TIGR00820; zip; 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; PF10609; ParA; 1.
DR Pfam; PF02535; Zip; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Ion transport {ECO:0000256|RuleBase:RU362088};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03038};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03038};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362088};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362088};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362088}; Transport {ECO:0000256|RuleBase:RU362088}.
FT TRANSMEM 394..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT TRANSMEM 430..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT TRANSMEM 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT TRANSMEM 622..644
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT TRANSMEM 664..683
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT TRANSMEM 695..714
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362088"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..552
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 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
SQ SEQUENCE 715 AA; 77146 MW; 126EA183E2AA7DDB CRC64;
MGNGDIPENA NEHCPGPQSE SAGKSDACEG CPNQQICATA PKGPDPDLVA IAERMATVKH
KILVLSGKGG VGKSTFSAQL AFALAARDFQ VGLLDVDICG PSIPKMLGLE GQEIHQSNLG
WSPVYVESNL GVMSIGFMLP HPDEAVIWRG PRKNGLIKQF LKDVYWGELD FLIVDAPPGT
SDEHISIVQC LDATGVDGAI IVTTPQQVSL IDVRKEVNFC KKVGVKVLGV VENMSGLCQP
ITDFKFLKLT DNGEQKDVTE WVWEYMREKA PEMLNLLACS EVFDSSGGGA VKMCNEMGIP
FLGKVPLDPQ LCKAAEGGTS CFADKDCVAS ASALKKIIEQ LIETNEWSML DLRPLRRLHH
VFSESFLQTV RESVTSSNCK SAELEQCRDE SVALVLKLVA MASILVAGFG GVAIPLVGKS
RRFLRTDGDV FAAAKAFAAG VILATGFVHM LRDSWDALSD PCLGSRAWSK FPFTGFFAMM
SALFTLLVDF LATEYYQRRE NRGRVERGKV VDGGYQALET GIEEVKDVGQ VSEGEGRHSH
SHAHAHSHHR DGVESTVRHV VVSQVLELGI VSHSMIIGLS LGVSQSPCTM RPLIVALTFH
QFFEGFALGG CISQAQFKTL SATIMACFFS LTTPLGVAIG AAIASNFNPH SPGALITEGI
LDSLSAGILV YMALVDLIAA DFLTKKMRSN FRLQIICYFL LLLGAGLMSS LALWA
//
