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NAR1_ASPFU
ID   NAR1_ASPFU              Reviewed;         597 AA.
AC   Q4WQ87;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor nar1;
DE   AltName: Full=Nuclear architecture-related protein 1;
GN   Name=nar1; ORFNames=AFUA_4G11960;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000005; EAL89597.1; -; Genomic_DNA.
DR   RefSeq; XP_751635.1; XM_746542.1.
DR   AlphaFoldDB; Q4WQ87; -.
DR   SMR; Q4WQ87; -.
DR   STRING; 746128.CADAFUBP00006715; -.
DR   EnsemblFungi; EAL89597; EAL89597; AFUA_4G11960.
DR   GeneID; 3509141; -.
DR   KEGG; afm:AFUA_4G11960; -.
DR   VEuPathDB; FungiDB:Afu4g11960; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   HOGENOM; CLU_018240_0_1_1; -.
DR   InParanoid; Q4WQ87; -.
DR   OMA; PHEQRAW; -.
DR   OrthoDB; 705416at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0097361; C:CIA complex; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; 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; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..597
FT                   /note="Cytosolic Fe-S cluster assembly factor nar1"
FT                   /id="PRO_0000383716"
FT   REGION          25..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..445
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         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         67
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         208
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         263
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         464
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         468
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   597 AA;  64361 MW;  22ED1664E70A8D3E CRC64;
     MSAILSADDL NDFISPGVAC IKPVESLPQK ESQSENPYEV TKEDKVQPEN LPPAQISLTD
     CLACSGCVTS AEAVLISLQS HTEVLNTLDS YPELPLGSTS YQRGTQKVGS ADSDGRIFVA
     SVSPQVRASL AATYGITERE AKYMIDQFLM GPHGLRAGGK HGNGFTWVVD TNVMREAVLA
     LTADEVTSSL LSTGSGSLPK SPILSSACPG WICYAEKTHP FILPHLSRLK SPQALSGTFL
     KSVLSKALGV PPSQIWHLAI MPCFDKKLEA SREELTDIAW ASTFTQSQTT PVRDVDCVIT
     TRELLTLATA RGLSLPNLPL KPLPASCLTP FPDQALESFL FSKSSSGQTV ESGTSGGYLH
     HVLQIFQARN PGSKIVTQRG RNADVVEYVL MSSGDEPLFR AARYYGFRNI QNLVRKLKPA
     RVSRLPGAKP QAVSSSANRR QPMSRNAAPA GTGADYAYVE VMACPGGCTN GGGQIRIEDA
     REAVPNALKE TSTETPVAAP KPTPHEQRAW LARVDEAYYS ADSDSEGSVT TEPVSVLSRD
     NQIHEFLNYW SEKVDIPLSR LAYTSYREVE SDVGKTKNAP NETARVVELA GKIGGGW
 
 
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