(data stored in ACNUC7421 zone)

SWISSPROT: Q47SM1_THEFY

ID   Q47SM1_THEFY            Unreviewed;       390 AA.
AC   Q47SM1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=Tfu_0508 {ECO:0000313|EMBL:AAZ54546.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54546.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to
CC       target apoproteins. Can hydrolyze ATP. {ECO:0000256|HAMAP-
CC       Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000256|HAMAP-Rule:MF_02040}.
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DR   EMBL; CP000088; AAZ54546.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0508; -.
DR   EnsemblBacteria; AAZ54546; AAZ54546; Tfu_0508.
DR   KEGG; tfu:Tfu_0508; -.
DR   eggNOG; ENOG4105D1F; Bacteria.
DR   eggNOG; COG0489; LUCA.
DR   HOGENOM; HOG000079915; -.
DR   KO; K03593; -.
DR   OMA; PMLNGII; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02037; MRP-like; 1.
DR   Gene3D; 3.30.300.130; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF117916; SSF117916; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SM1.
DR   SWISS-2DPAGE; Q47SM1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02040,
KW   ECO:0000313|EMBL:AAZ54546.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       19     90       FeS_assembly_P. {ECO:0000259|Pfam:
FT                                PF01883}.
FT   NP_BIND     133    140       ATP. {ECO:0000256|HAMAP-Rule:MF_02040}.
SQ   SEQUENCE   390 AA;  41111 MW;  8B106B262EC1C850 CRC64;
     MGHLGFRTID DMSTTPTTEQ VNAALATVKD PEIHRPITEL DMVKSVEIHD DGTVSVGIYL
     TVAGCPMRGR IEKDVADAVS KVPGVTGVKV TLDVMSDEQR KALQAKLRGG HAEKEIPFAK
     PNSLTKVFAV ASGKGGVGKS SITVNLAAAM AAQGHKVGVV DADIYGHSVP RMLGVSDRPT
     KVEDMILPPT AHGIKVISIG MFTQGNQAVV WRGPMLHRAL QQFLADVYWG DLDVLLMDLP
     PGTGDVAISV AQLLPNAEIL VVTTPQQAAA EVAERAGSIS AQTHQRVAGV IENMSYYQAP
     GSDERVYIFG EGGGQAVCDG LSRTLGTKVP LLGQVPLDVA LREGGDRGVP LVLDAPDSEA
     GKVLRSIAEE LLGKPRGLAG MMLGLSPTRR
//

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