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ISCA1_CHICK
ID   ISCA1_CHICK             Reviewed;         129 AA.
AC   Q5ZJ74;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial;
DE   AltName: Full=HESB-like domain-containing protein 2;
DE   AltName: Full=Iron-sulfur assembly protein IscA;
DE   Flags: Precursor;
GN   Name=ISCA1; Synonyms=HBLD2; ORFNames=RCJMB04_20e4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC       functioning late in the iron-sulfur cluster assembly pathway. Probably
CC       involved in the binding of an intermediate of Fe/S cluster assembly.
CC       {ECO:0000250|UniProtKB:Q9BUE6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR   EMBL; AJ720560; CAG32219.1; -; mRNA.
DR   RefSeq; NP_001258865.1; NM_001271936.1.
DR   AlphaFoldDB; Q5ZJ74; -.
DR   SMR; Q5ZJ74; -.
DR   STRING; 9031.ENSGALP00000020553; -.
DR   PaxDb; Q5ZJ74; -.
DR   GeneID; 427463; -.
DR   KEGG; gga:427463; -.
DR   CTD; 81689; -.
DR   VEuPathDB; HostDB:geneid_427463; -.
DR   eggNOG; KOG1120; Eukaryota.
DR   HOGENOM; CLU_069054_4_0_1; -.
DR   InParanoid; Q5ZJ74; -.
DR   OrthoDB; 1187554at2759; -.
DR   PhylomeDB; Q5ZJ74; -.
DR   TreeFam; TF314956; -.
DR   PRO; PR:Q5ZJ74; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 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; IBA:GO_Central.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR   Gene3D; 2.60.300.12; -; 1.
DR   InterPro; IPR000361; FeS_biogenesis.
DR   InterPro; IPR016092; FeS_cluster_insertion.
DR   InterPro; IPR017870; FeS_cluster_insertion_CS.
DR   InterPro; IPR035903; HesB-like_dom_sf.
DR   Pfam; PF01521; Fe-S_biosyn; 1.
DR   SUPFAM; SSF89360; SSF89360; 1.
DR   TIGRFAMs; TIGR00049; TIGR00049; 1.
DR   PROSITE; PS01152; HESB; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron-sulfur; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..129
FT                   /note="Iron-sulfur cluster assembly 1 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000042738"
FT   BINDING         57
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ   SEQUENCE   129 AA;  14125 MW;  B37AD1FD1A626A9B CRC64;
     MASSVVRATV RAVSKRKIQA TRAALTLTPS AVQKIKQLLK DQPEHVGVKV GVRTRGCNGL
     SYTLEYTKSK GDSDEEVVQD GVRVFIEKKA QLTLLGTEMD YVEDKLSSEF VFNNPNIKGT
     CGCGESFNI
 
 
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