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O93830

- PGTB2_CANAX

UniProt

O93830 - PGTB2_CANAX

Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

BET2

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4 By similarity.By similarity

    Catalytic activityi

    Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi249 – 2491ZincBy similarity
    Metal bindingi249 – 2491Zinc; catalyticBy similarity
    Metal bindingi251 – 2511ZincBy similarity
    Metal bindingi251 – 2511Zinc; catalyticBy similarity
    Metal bindingi301 – 3011ZincBy similarity
    Metal bindingi301 – 3011Zinc; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    1. Rab geranylgeranyltransferase activity Source: UniProtKB
    2. Rab GTPase binding Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. protein geranylgeranylation Source: UniProtKB

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geranylgeranyl transferase type-2 subunit beta (EC:2.5.1.60)
    Alternative name(s):
    Geranylgeranyl transferase type II subunit beta
    Short name:
    GGTase-II-beta
    Type II protein geranyl-geranyltransferase subunit beta
    Short name:
    PGGT
    YPT1/SEC4 proteins geranylgeranyltransferase subunit beta
    Gene namesi
    Name:BET2
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    GO - Cellular componenti

    1. Rab-protein geranylgeranyltransferase complex Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341Geranylgeranyl transferase type-2 subunit betaPRO_0000119776Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO93830.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati15 – 5541PFTB 1Add
    BLAST
    Repeati62 – 10443PFTB 2Add
    BLAST
    Repeati122 – 16342PFTB 3Add
    BLAST
    Repeati170 – 21142PFTB 4Add
    BLAST
    Repeati223 – 26442PFTB 5Add
    BLAST
    Repeati271 – 31343PFTB 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 1983Geranylgeranyl diphosphate bindingBy similarity
    Regioni243 – 25513Geranylgeranyl diphosphate bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 6 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5029.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    InterProiIPR001330. Prenyltrans.
    IPR026873. Ptb1.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PANTHERiPTHR11774:SF9. PTHR11774:SF9. 1 hit.
    PfamiPF00432. Prenyltrans. 2 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O93830-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNLPPDEKV ILFDKSKHVQ YIVEQESHRS FEYWLSEHLR MNGLYWGVTA    50
    LITMNELSAL AQQDVIDYIM LCWDDKTGAF GSFPKHDGHI LSTLSALQVL 100
    KIYDQELTVL NDNNESSNGN KRERLIKFIT GLQLPDGSFQ GDKYGEVDTR 150
    FVYTAVSSLS LLNALTDSIA DTASAFIMQC FNFDGGFGLI PGSESHAAQV 200
    FTCVGALAIM NKLDLLDVEN KKVKLIDWLT ERQVLPSGGF NGRPEKLPDV 250
    CYSWWVLSSL SILKRKNWVD LKILENFILT CQDLENGGFS DRPGNQTDVY 300
    HTCFAIAGLS LIDYKKYGFK EIDPVYCMPV EVTSKFVRRS A 341
    Length:341
    Mass (Da):38,460
    Last modified:May 1, 1999 - v1
    Checksum:i24A89E11FF911488
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021171 Genomic DNA. Translation: BAA35193.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021171 Genomic DNA. Translation: BAA35193.1 .

    3D structure databases

    ProteinModelPortali O93830.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5029.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    InterProi IPR001330. Prenyltrans.
    IPR026873. Ptb1.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    PANTHERi PTHR11774:SF9. PTHR11774:SF9. 1 hit.
    Pfami PF00432. Prenyltrans. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of BET2 gene from Candida albicans."
      Ishii N., Aoki Y., Arisawa M.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.

    Entry informationi

    Entry nameiPGTB2_CANAX
    AccessioniPrimary (citable) accession number: O93830
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3