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O94609

- UBA1_SCHPO

UniProt

O94609 - UBA1_SCHPO

Protein

Ubiquitin-activating enzyme E1 1

Gene

ptr3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei593 – 5931Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi437 – 46630ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: PomBase
    2. magnesium ion binding Source: PomBase
    3. protein binding Source: PomBase
    4. ubiquitin activating enzyme activity Source: PomBase

    GO - Biological processi

    1. mRNA export from nucleus Source: PomBase
    2. protein ubiquitination Source: PomBase

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-activating enzyme E1 1
    Alternative name(s):
    Poly(A)+ RNA transport protein 3
    Gene namesi
    Name:ptr3
    ORF Names:SPBC1604.21c, SPBC211.09
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC1604.21c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. nucleus Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10121012Ubiquitin-activating enzyme E1 1PRO_0000194976Add
    BLAST

    Proteomic databases

    MaxQBiO94609.
    PaxDbiO94609.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi277267. 1 interaction.
    DIPiDIP-48686N.
    MINTiMINT-4685507.
    STRINGi4896.SPBC1604.21c-1.

    Structurei

    Secondary structure

    1
    1012
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2711
    Helixi29 – 368
    Beta strandi39 – 435
    Helixi47 – 5913
    Beta strandi62 – 676
    Helixi74 – 785
    Helixi85 – 873
    Helixi92 – 10110
    Beta strandi109 – 1113
    Helixi118 – 1225
    Beta strandi124 – 1285
    Helixi133 – 14513
    Beta strandi149 – 1568
    Beta strandi159 – 1657
    Beta strandi170 – 1767
    Beta strandi182 – 1898
    Beta strandi193 – 1975
    Beta strandi209 – 2146
    Helixi221 – 2233
    Beta strandi233 – 2386
    Beta strandi247 – 2515
    Beta strandi253 – 2575
    Beta strandi261 – 2633
    Helixi268 – 2714
    Beta strandi272 – 2743
    Helixi282 – 2843
    Helixi287 – 30418
    Turni305 – 3073
    Helixi315 – 33117
    Helixi340 – 3489
    Turni349 – 3513
    Helixi355 – 37218
    Beta strandi382 – 3876
    Helixi389 – 3913
    Beta strandi394 – 3963
    Helixi400 – 4034
    Helixi411 – 4177
    Helixi419 – 4268
    Beta strandi429 – 4335
    Helixi437 – 44913
    Turni450 – 4523
    Beta strandi454 – 4563
    Beta strandi458 – 4625
    Helixi469 – 4713
    Turni472 – 4743
    Helixi480 – 4823
    Helixi487 – 49812
    Helixi500 – 5023
    Beta strandi505 – 5095
    Helixi515 – 5173
    Turni518 – 5203
    Helixi523 – 5275
    Beta strandi530 – 5345
    Helixi539 – 55214
    Beta strandi556 – 5627
    Beta strandi565 – 5717
    Turni573 – 5753
    Helixi579 – 5813
    Helixi592 – 5976
    Helixi602 – 61716
    Helixi619 – 6279
    Helixi633 – 6375
    Turni638 – 6403
    Helixi644 – 65512
    Turni656 – 6583
    Helixi663 – 67816
    Helixi680 – 6889
    Beta strandi698 – 7025
    Helixi719 – 73517
    Helixi744 – 7529
    Helixi788 – 7925
    Helixi797 – 7993
    Helixi819 – 83315
    Helixi841 – 8488
    Helixi856 – 87419
    Helixi880 – 8823
    Beta strandi885 – 8895
    Helixi890 – 8923
    Beta strandi894 – 8985
    Beta strandi905 – 9084
    Beta strandi911 – 9144
    Turni915 – 9173
    Beta strandi919 – 9246
    Helixi927 – 93610
    Beta strandi941 – 9477
    Beta strandi950 – 9545
    Helixi959 – 9635
    Turni964 – 9674
    Helixi970 – 9778
    Beta strandi988 – 9969
    Beta strandi1007 – 10115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4II2X-ray2.20A13-1012[»]
    4II3X-ray2.90A/C13-1012[»]
    ProteinModelPortaliO94609.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000167329.
    KOiK03178.
    OMAiKFHPVKQ.
    OrthoDBiEOG7FZ07P.
    PhylomeDBiO94609.

    Family and domain databases

    Gene3Di1.10.3240.10. 2 hits.
    3.40.50.720. 4 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SMARTiSM00985. UBA_e1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    TIGRFAMsiTIGR01408. Ube1. 1 hit.
    PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O94609-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNNMNIDQT DQNTIDEGLY SRQLYVLGHE AMKQMSQSNV LIIGCKGLGV     50
    EIAKNVCLAG VKSVTLYDPQ PTRIEDLSSQ YFLTEDDIGV PRAKVTVSKL 100
    AELNQYVPVS VVDELSTEYL KNFKCVVVTE TSLTKQLEIN DFTHKNHIAY 150
    IAADSRGLFG SIFCDFGENF ICTDTDGNEP LTGMIASITD DGVVTMLEET 200
    RHGLENGDFV KFTEVKGMPG LNDGTPRKVE VKGPYTFSIG SVKDLGSAGY 250
    NGVFTQVKVP TKISFKSLRE SLKDPEYVYP DFGKMMRPPQ YHIAFQALSA 300
    FADAHEGSLP RPRNDIDAAE FFEFCKKIAS TLQFDVELDE KLIKEISYQA 350
    RGDLVAMSAF LGGAVAQEVL KATTSKFYPL KQYFYFDSLE SLPSSVTISE 400
    ETCKPRGCRY DGQIAVFGSE FQEKIASLST FLVGAGAIGC EMLKNWAMMG 450
    VATGESGHIS VTDMDSIEKS NLNRQFLFRP RDVGKLKSEC ASTAVSIMNP 500
    SLTGKITSYQ ERVGPESEGI FGDEFFEKLS LVTNALDNVE ARMYVDRRCV 550
    FFEKPLLESG TLGTKGNTQV VVPHLTESYG SSQDPPEKSF PICTLKNFPN 600
    RIEHTIAWAR DLFEGLFKQP IDNVNMYLSS PNFLETSLKT SSNPREVLEN 650
    IRDYLVTEKP LSFEECIMWA RLQFDKFFNN NIQQLLFNFP KDSVTSTGQP 700
    FWSGPKRAPT PLSFDIHNRE HFDFIVAAAS LYAFNYGLKS ETDPAIYERV 750
    LAGYNPPPFA PKSGIKIQVN ENEEAPETAA NKDKQELKSI ADSLPPPSSL 800
    VGFRLTPAEF EKDDDSNHHI DFITAASNLR AMNYDITPAD RFKTKFVAGK 850
    IVPAMCTSTA VVSGLVCLEL VKLVDGKKKI EEYKNGFFNL AIGLFTFSDP 900
    IASPKMKVNG KEIDKIWDRY NLPDCTLQEL IDYFQKEEGL EVTMLSSGVS 950
    LLYANFQPPK KLAERLPLKI SELVEQITKK KLEPFRKHLV LEICCDDANG 1000
    EDVEVPFICI KL 1012
    Length:1,012
    Mass (Da):112,949
    Last modified:May 1, 1999 - v1
    Checksum:iAB5207808ACC6C2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87259 Genomic DNA. Translation: BAA75198.1.
    CU329671 Genomic DNA. Translation: CAA22354.1.
    PIRiT50344.
    T52000.
    RefSeqiXP_001713148.1. XM_001713096.2.

    Genome annotation databases

    EnsemblFungiiSPBC1604.21c.1; SPBC1604.21c.1:pep; SPBC1604.21c.
    GeneIDi2540744.
    KEGGispo:SPBC1604.21c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87259 Genomic DNA. Translation: BAA75198.1 .
    CU329671 Genomic DNA. Translation: CAA22354.1 .
    PIRi T50344.
    T52000.
    RefSeqi XP_001713148.1. XM_001713096.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4II2 X-ray 2.20 A 13-1012 [» ]
    4II3 X-ray 2.90 A/C 13-1012 [» ]
    ProteinModelPortali O94609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277267. 1 interaction.
    DIPi DIP-48686N.
    MINTi MINT-4685507.
    STRINGi 4896.SPBC1604.21c-1.

    Proteomic databases

    MaxQBi O94609.
    PaxDbi O94609.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC1604.21c.1 ; SPBC1604.21c.1:pep ; SPBC1604.21c .
    GeneIDi 2540744.
    KEGGi spo:SPBC1604.21c.

    Organism-specific databases

    PomBasei SPBC1604.21c.

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000167329.
    KOi K03178.
    OMAi KFHPVKQ.
    OrthoDBi EOG7FZ07P.
    PhylomeDBi O94609.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 20801866.
    PROi O94609.

    Family and domain databases

    Gene3Di 1.10.3240.10. 2 hits.
    3.40.50.720. 4 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SMARTi SM00985. UBA_e1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    TIGRFAMsi TIGR01408. Ube1. 1 hit.
    PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and molecular characterization of mRNA transport mutants in Schizosaccharomyces pombe."
      Azad A.K., Tani T., Shiki N., Tsuneyoshi S., Urushiyama S., Ohshima Y.
      Mol. Biol. Cell 8:825-841(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "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.

    Entry informationi

    Entry nameiUBA1_SCHPO
    AccessioniPrimary (citable) accession number: O94609
    Secondary accession number(s): Q9P7R2, Q9USY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 119 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3