ID   NAR1_ASPFN              Reviewed;         562 AA.
AC   B8N122;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor nar1;
DE   AltName: Full=Nuclear architecture-related protein 1;
GN   Name=nar1; ORFNames=AFLA_027970;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Component of the cytosolic Fe/S protein assembly machinery.
CC       Required for maturation of extramitochondrial Fe/S proteins. May play a
CC       role in the transfer of pre-assembled Fe/S clusters to target
CC       apoproteins (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
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DR   EMBL; EQ963473; EED55525.1; -; Genomic_DNA.
DR   RefSeq; XP_002374307.1; XM_002374266.1.
DR   AlphaFoldDB; B8N122; -.
DR   STRING; 5059.CADAFLAP00002172; -.
DR   EnsemblFungi; EED55525; EED55525; AFLA_027970.
DR   VEuPathDB; FungiDB:AFLA_027970; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   HOGENOM; CLU_018240_0_1_1; -.
DR   OMA; PHEQRAW; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR   InterPro; IPR009016; Fe_hydrogenase.
DR   InterPro; IPR004108; Fe_hydrogenase_lsu_C.
DR   Pfam; PF02906; Fe_hyd_lg_C; 1.
DR   SUPFAM; SSF53920; SSF53920; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT   CHAIN           1..562
FT                   /note="Cytosolic Fe-S cluster assembly factor nar1"
FT                   /id="PRO_0000383715"
FT   REGION          28..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         214
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         269
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         475
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         479
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   562 AA;  60371 MW;  5FA411FD1E3945D1 CRC64;
     MSAILSADDL NDFISPGVAC IKPVETLPKN ESSNSQNPYE VTTEDKVQPE NLPPAQISLT
     DCLACSGCVT SAEAVLISLQ SHAEVLNTLD AYPELPLTQN HNGPYTGSSD ALDGESRIFV
     ASVSPQVRAS LAATYGISEK EATYMIDQFL SGPHGLRAGG KHGSGFSWVV DTNVMRDAIL
     VLTADEVSET LKEPSARAIS KDTLPKRPVL SSACPGWICY AEKTHPFVLP HLSRLKSPQA
     LTGTFLKTVL SKALGVPPSR VWHLAIMPCF DKKLEASREE LTDVSWSPLD GGVPLTESNK
     PVRDVDCVIT TRELLTLASS RGISLPTLPL KSLAPSYTPH FPDETLNAFL FRKQNGSEQS
     MEAGTSGGYL HHVLKTFQAK NPGSEIVTQR GRNADVVEYS LMSPGGEPLM KAARYYGFRN
     IQNLVRKLKP ARVSRLPGAR VPAASAGGNR RQPISRNSAS AGSGTDYAYV EVMACPGGCT
     NGGGQIRIED AREASTSTQS VTAVENPSKP TPHEQRAWLA RVDEAYFSAE SDAEAKWTVR
     HSPSPSLRGR LGSMKLSSIG LT