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Protein

Protein N-methyltransferase nnt1

Gene

nnt1

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

Functioni

S-adenosyl-L-methionine-dependent protein methyltransferase. Involved in rDNA silencing and in lifespan determination.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei106 – 1061S-adenosyl-L-methionineBy similarity
Binding sitei137 – 1371S-adenosyl-L-methionine; via amide nitrogenBy similarity
Binding sitei162 – 1621S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein N-methyltransferase nnt1By similarity (EC:2.1.1.-By similarity)
Alternative name(s):
Nicotinamide N-methyltransferase-like protein 1By similarity
Gene namesi
Name:nnt1By similarity
ORF Names:SPAC8F11.09cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC8F11.09c.
PomBaseiSPAC8F11.09c. nnt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Protein N-methyltransferase nnt1PRO_0000096899Add
BLAST

Proteomic databases

MaxQBiQ9UT28.

Interactioni

Protein-protein interaction databases

MINTiMINT-4709427.

Structurei

3D structure databases

ProteinModelPortaliQ9UT28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 863S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. NNT1 family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000199189.
InParanoidiQ9UT28.
KOiK17878.
OMAiLVFYTHH.
OrthoDBiEOG7JHMGG.
PhylomeDBiQ9UT28.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Methyltransf_16.
IPR025784. Nicotinamide_N-MeTfrase_put.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51560. SAM_MT_NNT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UT28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNDFEGFG IFEEPEGFRP STPPPKEVLH TRVIVPNGPE EIKLRLVGSH
60 70 80 90 100
SLWAHYLWNS GIELANYIDK NPDTVRAKKV LELGAGAGLP SIVSAFDGAK
110 120 130 140 150
FVVSTDYPDP ALIDNLEHNV KQYAEIASKI SAVGYLWGSN IKEVMSNAGF
160 170 180 190 200
KDNEVFDILL LSDLVFNHTE HSKLIKSCKM AIEGNPNAVV YVFFTHHRPH
210 220 230 240 250
LAKKDMIFFD IAQSEGFQIE KILEEKRTPM FEEDPGAPEI RATVHGYKMT

IPIPV
Length:255
Mass (Da):28,490
Last modified:May 1, 2000 - v1
Checksum:i8E16DB39F6173EA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52170.1.
PIRiT39184.
RefSeqiNP_593958.1. NM_001019385.2.

Genome annotation databases

EnsemblFungiiSPAC8F11.09c.1; SPAC8F11.09c.1:pep; SPAC8F11.09c.
GeneIDi2543599.
KEGGispo:SPAC8F11.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB52170.1.
PIRiT39184.
RefSeqiNP_593958.1. NM_001019385.2.

3D structure databases

ProteinModelPortaliQ9UT28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4709427.

Proteomic databases

MaxQBiQ9UT28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC8F11.09c.1; SPAC8F11.09c.1:pep; SPAC8F11.09c.
GeneIDi2543599.
KEGGispo:SPAC8F11.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC8F11.09c.
PomBaseiSPAC8F11.09c. nnt1.

Phylogenomic databases

HOGENOMiHOG000199189.
InParanoidiQ9UT28.
KOiK17878.
OMAiLVFYTHH.
OrthoDBiEOG7JHMGG.
PhylomeDBiQ9UT28.

Miscellaneous databases

NextBioi20804606.
PROiQ9UT28.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR019410. Methyltransf_16.
IPR025784. Nicotinamide_N-MeTfrase_put.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF10294. Methyltransf_16. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51560. SAM_MT_NNT1. 1 hit.
[Graphical view]
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 nameiNNT1_SCHPO
AccessioniPrimary (citable) accession number: Q9UT28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 78 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.