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NUP1B_XENLA
ID   NUP1B_XENLA             Reviewed;         315 AA.
AC   Q5I050;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor nubp1-B {ECO:0000255|HAMAP-Rule:MF_03038};
DE   AltName: Full=Nucleotide-binding protein 1-B {ECO:0000255|HAMAP-Rule:MF_03038};
DE            Short=NBP 1-B {ECO:0000255|HAMAP-Rule:MF_03038};
GN   Name=nubp1-B;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC       assembly (CIA) machinery. Required for maturation of extramitochondrial
CC       Fe-S proteins. The nubp1-nubp2 heterotetramer forms a Fe-S scaffold
CC       complex, mediating the de novo assembly of an Fe-S cluster and its
CC       transfer to target apoproteins. {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03038};
CC       Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC       clusters in the N-termini of nubp1 and two labile, bridging clusters
CC       between subunits of the nubp1-nubp2 heterotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_03038};
CC   -!- SUBUNIT: Heterotetramer of 2 nubp1 and 2 nubp2 chains.
CC       {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038}.
CC   -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC       NUBP1/NBP35 subfamily. {ECO:0000255|HAMAP-Rule:MF_03038}.
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DR   EMBL; BC088708; AAH88708.1; -; mRNA.
DR   RefSeq; NP_001088915.1; NM_001095446.1.
DR   AlphaFoldDB; Q5I050; -.
DR   SMR; Q5I050; -.
DR   DNASU; 496286; -.
DR   GeneID; 496286; -.
DR   KEGG; xla:496286; -.
DR   CTD; 496286; -.
DR   Xenbase; XB-GENE-6252195; nubp1.S.
DR   OMA; EMDCQVG; -.
DR   OrthoDB; 1166096at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 496286; Expressed in testis and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_02040; Mrp_NBP35; 1.
DR   HAMAP; MF_03038; NUBP1; 1.
DR   InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR   InterPro; IPR000808; Mrp_CS.
DR   InterPro; IPR028601; NUBP1/Nbp35.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033756; YlxH/NBP35.
DR   PANTHER; PTHR23264; PTHR23264; 1.
DR   Pfam; PF10609; ParA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01215; MRP; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..315
FT                   /note="Cytosolic Fe-S cluster assembly factor nubp1-B"
FT                   /id="PRO_0000382594"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         35
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         239
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
FT   BINDING         242
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03038"
SQ   SEQUENCE   315 AA;  33704 MW;  4FF321470DE5E9E1 CRC64;
     MADIPENAPQ HCPGTGSTEA GKSSACQGCP NQSICASAAT SAPDPAIEEI KEKMSLVKHK
     ILVLSGKGGV GKSTFSAHLA HGLAQDEGKE VALLDVDICG PSIPRMMGLE GEQVHQSGSG
     WSPVYVEDNL AVMSVGFLLS SPDDAVIWRG PKKNGMIKQF LRDVDWGEVD YLIVDTPPGT
     SDEHLSVVQY LSAAGIDGAV IVTTPQEVSL QDVRKEINFC RKVKLPIIGV VENMSGFICP
     KCENESQIFP PTTGGAEKMC TDLNVSLLGK VPLDPNIGKS CDTGKSFFTE IPDSPATLSY
     RIIIQRIQDY CEKKK
 
 
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