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NAR1_EMENI
ID   NAR1_EMENI              Reviewed;         590 AA.
AC   Q5B748; C8V443;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor nar1;
DE   AltName: Full=Nuclear architecture-related protein 1;
GN   Name=nar1; ORFNames=AN3632;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA59840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AACD01000061; EAA59840.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BN001302; CBF75735.1; -; Genomic_DNA.
DR   RefSeq; XP_661236.1; XM_656144.1.
DR   AlphaFoldDB; Q5B748; -.
DR   STRING; 162425.CADANIAP00005108; -.
DR   EnsemblFungi; CBF75735; CBF75735; ANIA_03632.
DR   EnsemblFungi; EAA59840; EAA59840; AN3632.2.
DR   GeneID; 2873057; -.
DR   KEGG; ani:AN3632.2; -.
DR   VEuPathDB; FungiDB:AN3632; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   HOGENOM; CLU_018240_0_1_1; -.
DR   InParanoid; Q5B748; -.
DR   OMA; PHEQRAW; -.
DR   OrthoDB; 705416at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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: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; Reference proteome.
FT   CHAIN           1..590
FT                   /note="Cytosolic Fe-S cluster assembly factor nar1"
FT                   /id="PRO_0000383728"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
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         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         204
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         259
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         461
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         465
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   590 AA;  63750 MW;  8017455063117EAA CRC64;
     MSAILSADDL NDFISPGVAC IKPVESLPQK QSNENPYEVT TEDKVQPENP PPAQISLTDC
     LACSGCVTSA EAVLISLQSH NEVLNTLDAQ PEIRLVSGEN GTVIEDSGRT RDEGRIFVAS
     VSPQVRASLA ATYGVSEKEA NHIIHQFLSG PNGLRAGGKH GSGFSWVVDT NSLREAVLVL
     TADEVSESLT GSSAPKRPIL SSACPGWICY AEKTHPFILP HLSRLKSPQA LTGTFLKTVI
     SKKLGVPASR IWHLSIMPCF DKKLEASREE LTDAAWNRLS SGEPNTPVRD VDCVITSREL
     LSLASSRGIS LPNLPRKSLP QSLRLPFPDP ALNVFLFSEK SFSRQTSASG TSGGYLHNVL
     LSFQARNPGS EIVTQRGRNA DVVDYTLMSP EGEPILKAAR YYGFRNIQNL VRKLKPARVS
     RLPGAKVATG QTAGGRRQPI SRNGASAGSS MDYAYVEVMA CPGGCTNGGG QIRIGDAREF
     NAQHDASVTS ETSKPLPHEQ RSWLARVDEA YYSADSDMDD AVEDVRTVSV TDNEDRVHKT
     LQHWSAITDI PLEKLAYTTY REVESDVGKP SAPNDTSRVV ELAGKIGGGW
 
 
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