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Protein

Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrial

Gene

SPAC3A11.07

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the oxidation of NADH.By similarity

Catalytic activityi

NADH + ubiquinone = NAD+ + ubiquinol.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi93 – 12331FADBy similarityAdd
BLAST
Nucleotide bindingi255 – 29137NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, Ubiquinone

Names & Taxonomyi

Protein namesi
Recommended name:
Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrial (EC:1.6.5.9)
Gene namesi
ORF Names:SPAC3A11.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3A11.07.
PomBaseiSPAC3A11.07.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionSequence analysisAdd
BLAST
Chaini38 – 551514Probable NADH-ubiquinone oxidoreductase C3A11.07, mitochondrialPRO_0000337257Add
BLAST

Proteomic databases

MaxQBiO14121.

Interactioni

Protein-protein interaction databases

BioGridi279551. 20 interactions.
MINTiMINT-4670647.

Structurei

3D structure databases

ProteinModelPortaliO14121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NADH dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000182501.
InParanoidiO14121.
KOiK17871.
OMAiRIRNRIM.
OrthoDBiEOG7034S6.
PhylomeDBiO14121.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14121-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFSRSILRG MPKAGIPKSP LALSASRNLR LANSVRFASD AASSPKSTTS
60 70 80 90 100
KWKILKRTTL GLFATAVVLY GANVYRFRHP DPHQPLPDPS KKTLVVLGAG
110 120 130 140 150
WGATSILRTI DTSLFNVIVV SPRNYFLFTS LLPSTATGSV HTRSIVQPIR
160 170 180 190 200
YMLRHKSCYV KFYEAECTDV DADKKVIHIK KTTTDGVDLE QEIKYDYLVC
210 220 230 240 250
SHGAETQTFN IPGIAEYGCF LKEIWDAQKI RARILHCLEQ AQFKDLPAET
260 270 280 290 300
RRRYVHTVVV GGGPTGMEFA GEMADFIEDD LKSWYPELAD DFAVTLVEAL
310 320 330 340 350
PSVLPMFSAK LRDYTQSLFD SSHIKIRTNT ALKKVTAENI HVEVKNPDGS
360 370 380 390 400
KQEEVIPYGL LVWAGGNRAR PLTKKLMEGS EEQNNRRGLV VDEYLKLKGY
410 420 430 440 450
KDIFALGDCT HTAYAPTAQV ASQQGAYLGQ LFNKLGSLNF EKPSEDRHIA
460 470 480 490 500
LGDEMDSSTL ISLANEKHAS TKVFLPFKYS HQGSLAYVGH EKAIADIEVP
510 520 530 540 550
WFGKQLHASG ALAFYFWRSV YLSELYSLRN RTNVTLDWIR VKLFGRDISS

L
Length:551
Mass (Da):61,675
Last modified:January 1, 1998 - v1
Checksum:iFED02DB71DEB9281
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16382.1.
PIRiT11629.
RefSeqiNP_594196.1. NM_001019620.2.

Genome annotation databases

EnsemblFungiiSPAC3A11.07.1; SPAC3A11.07.1:pep; SPAC3A11.07.
GeneIDi2543119.
KEGGispo:SPAC3A11.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16382.1.
PIRiT11629.
RefSeqiNP_594196.1. NM_001019620.2.

3D structure databases

ProteinModelPortaliO14121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279551. 20 interactions.
MINTiMINT-4670647.

Proteomic databases

MaxQBiO14121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3A11.07.1; SPAC3A11.07.1:pep; SPAC3A11.07.
GeneIDi2543119.
KEGGispo:SPAC3A11.07.

Organism-specific databases

EuPathDBiFungiDB:SPAC3A11.07.
PomBaseiSPAC3A11.07.

Phylogenomic databases

HOGENOMiHOG000182501.
InParanoidiO14121.
KOiK17871.
OMAiRIRNRIM.
OrthoDBiEOG7034S6.
PhylomeDBiO14121.

Miscellaneous databases

NextBioi20804146.
PROiO14121.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNDH1_SCHPO
AccessioniPrimary (citable) accession number: O14121
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 1, 1998
Last modified: January 20, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.