位置:首页 > 蛋白库 > NAR1_VANPO
NAR1_VANPO
ID   NAR1_VANPO              Reviewed;         524 AA.
AC   A7TQP0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Cytosolic Fe-S cluster assembly factor NAR1;
DE   AltName: Full=Nuclear architecture-related protein 1;
GN   Name=NAR1; ORFNames=Kpol_1015p11;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Component of the cytosolic Fe/S protein assembly machinery.
CC       Required for maturation of extramitochondrial Fe/S proteins. May play a
CC       role in the transfer of pre-assembled Fe/S clusters to target
CC       apoproteins (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NARF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480461; EDO15421.1; -; Genomic_DNA.
DR   RefSeq; XP_001643279.1; XM_001643229.1.
DR   AlphaFoldDB; A7TQP0; -.
DR   SMR; A7TQP0; -.
DR   STRING; 436907.A7TQP0; -.
DR   PRIDE; A7TQP0; -.
DR   EnsemblFungi; EDO15421; EDO15421; Kpol_1015p11.
DR   GeneID; 5543496; -.
DR   KEGG; vpo:Kpol_1015p11; -.
DR   eggNOG; KOG2439; Eukaryota.
DR   HOGENOM; CLU_018240_0_1_1; -.
DR   InParanoid; A7TQP0; -.
DR   OMA; PHEQRAW; -.
DR   OrthoDB; 705416at2759; -.
DR   PhylomeDB; A7TQP0; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   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   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..524
FT                   /note="Cytosolic Fe-S cluster assembly factor NAR1"
FT                   /id="PRO_0000383741"
FT   REGION          362..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         52
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         158
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         206
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         408
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         412
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   524 AA;  59390 MW;  89048D9E741B33A9 CRC64;
     MSALLREEDL NDFITPEVAC IKPVSSKPSN GVDGELSVGK EPEKVEISLA DCLACVGCIT
     SSEEILLSRQ NQDVFVKEWN EKKTEGYILS VSIAPQCRVS LSQYFGMGVL KFDQMFIRYL
     QEVWGARYVV GIQEGREESI KLMNEVADKG ERKICSACPG FLMYCEKKQQ DLLPLLIDVK
     SPMEITGHLL KDGNKEKMYH LSIMPCFDKK LESMRPESIG LVDCVITPKE LVNLITPEQV
     DKYFATTKET IGMLEWEDAI QRVTPKWMNI DTSFKTNEGS SSGGFAWQYI LHRRFQMSDN
     DNDNAYKIET VRGRNLDVTE FRLIDEEGKI LVRSTQVFGF RNIQNLRRLV KDVKPRKLKR
     FIRKRPTANG NDNSISLSSS INNQDNNNTK VEEPVDFCKS DFLEVMACPR GCIAGGGNLK
     NGIKNGPDQD SDPNQDLNTV YMTSIPMTSI EPRHNLTLPS SQENVIVGVI SHDLDDSNTI
     IKLQEEQKYG NKYKRKLYNP SSISETHNGD SKNTIEQPVQ FTTW
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025