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A2QN07

- MPKC_ASPNC

UniProt

A2QN07 - MPKC_ASPNC

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Protein

Mitogen-activated protein kinase mpkC

Gene
mpkC, An07g03980
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source By similarity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by tyrosine and threonine phosphorylation By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATP By similarity
Active sitei141 – 1411Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase mpkC (EC:2.7.11.24)
Short name:
MAP kinase C
Gene namesi
Name:mpkC
ORF Names:An07g03980
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 4L

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Mitogen-activated protein kinase mpkCPRO_0000289714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711Phosphothreonine By similarity
Modified residuei173 – 1731Phosphotyrosine By similarity

Post-translational modificationi

Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme By similarity.

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00005558.

Structurei

3D structure databases

ProteinModelPortaliA2QN07.
SMRiA2QN07. Positions 3-341.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 299280Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi171 – 1733TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000233024.
KOiK04441.
OrthoDBiEOG7K3TWD.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2QN07-1 [UniParc]FASTAAdd to Basket

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MAEFLRSQIL GTTFETTNRY SDLQPVGLGA FGLVCSAYDM ITRQPVAIKK    50
MMKPFSNATL AKRTYREVKL LKHLRHENLI GLSDIFISPL EDVYLVTDLL 100
GTDLNRLLTS KPLDGKFVQY FTYQLLRGLK YIHSAGVIHR DLKPSNILIN 150
ENCDLKICDF GLARLQEPQM TGYVSTRYYR APEIMLTWQK YGMQVDIWSA 200
GCIVAEMLRG KPLFPGKDHI NQFFLITDAL GNPPDEVIER ICTKTTLDLV 250
KSLPKRQPAP WATLFPDSDE NAIDLLGEML IFDPDKRISA AKALEHPYLS 300
VYHDPTDEPV AEQMFDWSFS EVAHSIDEWK IMIYTEVVDF HDIGPTEEPV 350
ITEPFLSPDP SLSPEVLDPL GQIQTQSMVT KSAETLDQDI LQYLQI 396
Length:396
Mass (Da):45,038
Last modified:March 6, 2007 - v1
Checksum:iF13BC0AF8E53FF13
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270128 Genomic DNA. Translation: CAK48148.1.
RefSeqiXP_001391480.1. XM_001391443.2.

Genome annotation databases

EnsemblFungiiCADANGAT00005669; CADANGAP00005558; CADANGAG00005669.
GeneIDi4981664.
KEGGiang:ANI_1_492064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270128 Genomic DNA. Translation: CAK48148.1 .
RefSeqi XP_001391480.1. XM_001391443.2.

3D structure databases

ProteinModelPortali A2QN07.
SMRi A2QN07. Positions 3-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00005558.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00005669 ; CADANGAP00005558 ; CADANGAG00005669 .
GeneIDi 4981664.
KEGGi ang:ANI_1_492064.

Phylogenomic databases

HOGENOMi HOG000233024.
KOi K04441.
OrthoDBi EOG7K3TWD.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiMPKC_ASPNC
AccessioniPrimary (citable) accession number: A2QN07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 48 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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