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APBC_PYRHO
ID   APBC_PYRHO              Reviewed;         295 AA.
AC   O58667;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040};
GN   OrderedLocusNames=PH0949;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target
CC       apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       {ECO:0000255|HAMAP-Rule:MF_02040}.
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DR   EMBL; BA000001; BAA30046.1; -; Genomic_DNA.
DR   PIR; H71085; H71085.
DR   RefSeq; WP_010885042.1; NC_000961.1.
DR   AlphaFoldDB; O58667; -.
DR   SMR; O58667; -.
DR   STRING; 70601.3257363; -.
DR   EnsemblBacteria; BAA30046; BAA30046; BAA30046.
DR   GeneID; 1443277; -.
DR   KEGG; pho:PH0949; -.
DR   eggNOG; arCOG00585; Archaea.
DR   OMA; NMAYFTP; -.
DR   OrthoDB; 32313at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR044304; NUBPL-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR42961; PTHR42961; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..295
FT                   /note="Iron-sulfur cluster carrier protein"
FT                   /id="PRO_0000184956"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02040"
SQ   SEQUENCE   295 AA;  32033 MW;  ECB9CC105ADE84A8 CRC64;
     MTIKTPTVKV PGLGTDPLEQ RIKEKEKKWK YKIAVLSGKG GVGKSTVAVN LTAALAKMGY
     FVGILDADIH GPNVAKMLGV DKEEVYAEKF DDGHFEMIPP TTDFMGQVTP IKVMSMGMMV
     PEDQPVIWRG PLVTKAIKQL LGDVKWGSLD FMIIDFPPGT GDEILTVVQS IKLDAAIIVT
     TPQEVALLDT GKAVNMMKKM EVPYVAVVEN MSYLICPHCG NKIDIFGEGG GEKLAQKEGV
     DFLGKIPIDL KAREASDLGI PIVLYEDTPA AKAFMELAEK LVNKLKEIKG DGGKE
 
 
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