ID A0A367LAR2_9HYPO Unreviewed; 289 AA.
AC A0A367LAR2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RCI11518.1};
GN ORFNames=L249_7716 {ECO:0000313|EMBL:RCI11518.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI11518.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI11518.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI11518.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
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|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 -!- 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:RCI11518.1}.
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DR EMBL; LKCN02000010; RCI11518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367LAR2; -.
DR STRING; 1330021.A0A367LAR2; -.
DR Proteomes; UP000253664; 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; 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:SF38; 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.
PE 3: Inferred from homology;
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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03039}; Reference proteome {ECO:0000313|Proteomes:UP000253664}.
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03039"
FT BINDING 201
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 204
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 289 AA; 30655 MW; 9B87A0754112779F CRC64;
MATGLDKVKH VVLVLSGKGG VGKSSVTIQL ALSLALSGHS VGILDVDLTG PSIPRMLAVE
ASKVTQVPGG WTPVLVSGAD PTTGVGSLHA MSLGFLLPRR GDAVVWRGPK KTAMIRQFLR
DVIWGETDYL LVDTPPGTSD EHISLVETLH GEARPAQMAG AVVVTTPQAV ATSDVRKELN
FCAKTNTRVL GVVENMSGFV CPHCAECSDI FGSGGGRSMA DQFGVPFLGS VPLDVQLVAL
LEGGQEEEEE EESCNSDRRR LVDKYVDCSL SRFFRPMAAR LAMSVDEHG
//
