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NARF_CAEEL
ID   NARF_CAEEL              Reviewed;         457 AA.
AC   Q9N392;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 5.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable cytosolic Fe-S cluster assembly factor oxy-4;
GN   Name=oxy-4; ORFNames=Y54H5A.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-373.
RX   PubMed=19335616; DOI=10.1111/j.1365-2443.2009.01282.x;
RA   Fujii M., Adachi N., Shikatani K., Ayusawa D.;
RT   "[FeFe]-hydrogenase-like gene is involved in the regulation of sensitivity
RT   to oxygen in yeast and nematode.";
RL   Genes Cells 14:457-468(2009).
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly machinery. Required for maturation of extramitochondrial Fe/S
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Arrest at the L2-L3 stage in 90% oxygen.
CC       {ECO:0000269|PubMed:19335616}.
CC   -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
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DR   EMBL; FO081201; CCD69851.1; -; Genomic_DNA.
DR   RefSeq; NP_498092.4; NM_065691.5.
DR   AlphaFoldDB; Q9N392; -.
DR   SMR; Q9N392; -.
DR   BioGRID; 40933; 2.
DR   IntAct; Q9N392; 1.
DR   STRING; 6239.Y54H5A.4; -.
DR   EPD; Q9N392; -.
DR   PaxDb; Q9N392; -.
DR   PeptideAtlas; Q9N392; -.
DR   EnsemblMetazoa; Y54H5A.4.1; Y54H5A.4.1; WBGene00021902.
DR   GeneID; 175702; -.
DR   KEGG; cel:CELE_Y54H5A.4; -.
DR   UCSC; Y54H5A.4.1; c. elegans.
DR   CTD; 175702; -.
DR   WormBase; Y54H5A.4; CE29883; WBGene00021902; oxy-4.
DR   eggNOG; KOG2439; Eukaryota.
DR   GeneTree; ENSGT00940000153514; -.
DR   HOGENOM; CLU_018240_0_0_1; -.
DR   InParanoid; Q9N392; -.
DR   OMA; PHEQRAW; -.
DR   OrthoDB; 705416at2759; -.
DR   PhylomeDB; Q9N392; -.
DR   PRO; PR:Q9N392; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00021902; Expressed in germ line (C elegans) and 4 other tissues.
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: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   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..457
FT                   /note="Probable cytosolic Fe-S cluster assembly factor oxy-
FT                   4"
FT                   /id="PRO_0000383695"
FT   REGION          38..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         25
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         176
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         232
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         380
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         384
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         373
FT                   /note="D->N: In allele qa5001; increased sensitivity to
FT                   oxygen."
FT                   /evidence="ECO:0000269|PubMed:19335616"
SQ   SEQUENCE   457 AA;  50824 MW;  571C63FA6CD381EA CRC64;
     MEDSGFSGVV RLSNVSDFIA PNLDCIIPLE TRTVEKKKEE SQVNIRTKKP KDKESSKTEE
     KKSVKISLAD CLACSGCITS AETVLVEEQS FGRVYEGIQN SKLSVVTVSP QAITSIAVKI
     GKSTNEVAKI IASFFRRLGV KYVIDSSFAR KFAHSLIYEE LSTTPSTSRP LLSSACPGFV
     CYAEKSHGEL LIPKISKIRS PQAISGAIIK GFLAKREGLS PCDVFHAAVM PCFDKKLEAS
     REQFKVDGTD VRETDCVIST AELLEEIIKL ENDEAGDVEN RSEEEQWLSA LSKGSVIGDD
     GGASGGYADR IVRDFVLENG GGIVKTSKLN KNMFSTTVES EAGEILLRVA KVYGFRNVQN
     LVRKMKTKKE KTDYVEIMAC PGGCANGGGQ IRYETMDERE EKLIKVEALY EDLPRQDDEE
     TWIKVREEWE KLDKNYRNLL FTDYRPVETN VAQVLKW
 
 
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