位置:首页 > 蛋白库 > NDUV1_SCHPO
NDUV1_SCHPO
ID   NDUV1_SCHPO             Reviewed;         452 AA.
AC   O94500;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial {ECO:0000305};
DE            EC=1.6.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=SPBC18E5.10 {ECO:0000312|PomBase:SPBC18E5.10};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255};
CC       Note=Binds 1 FMN. {ECO:0000255};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was previously considered as a subunit of the NADH
CC       dehydrogenase of the mitochondrial respiratory chain complex I. Due to
CC       lack of 38 of the other 40 subunits that are present in that complex in
CC       mammals, this attribution is unlikely. {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; CU329671; CAA22670.1; -; Genomic_DNA.
DR   PIR; T39761; T39761.
DR   RefSeq; NP_595857.1; NM_001021761.2.
DR   AlphaFoldDB; O94500; -.
DR   SMR; O94500; -.
DR   STRING; 4896.SPBC18E5.10.1; -.
DR   MaxQB; O94500; -.
DR   PaxDb; O94500; -.
DR   EnsemblFungi; SPBC18E5.10.1; SPBC18E5.10.1:pep; SPBC18E5.10.
DR   GeneID; 2540740; -.
DR   KEGG; spo:SPBC18E5.10; -.
DR   PomBase; SPBC18E5.10; -.
DR   VEuPathDB; FungiDB:SPBC18E5.10; -.
DR   eggNOG; KOG2658; Eukaryota.
DR   HOGENOM; CLU_014881_1_0_1; -.
DR   InParanoid; O94500; -.
DR   OMA; CDDVIMD; -.
DR   PhylomeDB; O94500; -.
DR   PRO; PR:O94500; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1440.230; -; 1.
DR   Gene3D; 3.40.50.11540; -; 1.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF140490; SSF140490; 1.
DR   SUPFAM; SSF142019; SSF142019; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..452
FT                   /note="NADH-ubiquinone oxidoreductase 51 kDa subunit
FT                   homolog SPBC18E5.10, mitochondrial"
FT                   /id="PRO_0000317309"
FT   BINDING         80..89
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         198..245
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255"
FT   BINDING         377
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         380
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         383
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         424
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  50095 MW;  6C199251A7598374 CRC64;
     MLSRGHCCKL KHSFNGLRNV ALKRLVGSKA GYRMFPNLIE KRIRRIDDAL ADGEYENLSE
     ILKYDPLNII ELVQESELRG RGRYGFPTGE KMLSLYKATS SERGRKEKPV VIVNAAENDI
     GSFKDRLLLR HEPHKIIEGA IIAARAVEAS ACYLFIRKDY YEETVMMQKC IIQAYAKKLL
     GKNLLGTSIG LELLIHPGAG SYITGEESAL IQSLQGEFPV PDIPINNTIT SGLFGLPTLV
     LNVETVSNLP AIIKKGPKFF ISMGRPNNRG TKLFSISGEV NEPNVIEACM SIPLKDLIEN
     YAGGVRGGWN KLVGIFPGGP CSGILNKNQC EQVTMDFDSL KALDSSLGTG SVIVLNDHDQ
     IFESLLNFAK FYSTNTCHTC PVCRDGVEDV IETLKGLKDG HAHLSQLKDM FSKFNMPSSS
     KVFCGFGDSM RHQIHSIQRN FPDQITFRTK VT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024