Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O93829

- PGTA_CANAX

UniProt

O93829 - PGTA_CANAX

Protein

Geranylgeranyl transferase type-2 subunit alpha

Gene

BET4

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    GO - Molecular functioni

    1. Rab geranylgeranyltransferase activity Source: UniProtKB
    2. Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    1. protein geranylgeranylation Source: UniProtKB

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geranylgeranyl transferase type-2 subunit alpha (EC:2.5.1.60)
    Alternative name(s):
    GGTase-II-alpha
    Geranylgeranyl transferase type II subunit alpha
    PGGT
    Type II protein geranyl-geranyltransferase subunit alpha
    YPT1/SEC4 proteins geranylgeranyltransferase subunit alpha
    Gene namesi
    Name:BET4
    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 – 371371Geranylgeranyl transferase type-2 subunit alphaPRO_0000119755Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO93829.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati45 – 7935PFTA 1Add
    BLAST
    Repeati92 – 12635PFTA 2Add
    BLAST
    Repeati131 – 16535PFTA 3Add
    BLAST
    Repeati177 – 21135PFTA 4Add
    BLAST
    Repeati242 – 27635PFTA 5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi214 – 2218Poly-Gln

    Sequence similaritiesi

    Contains 5 PFTA repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5536.

    Family and domain databases

    InterProiIPR002088. Prenyl_trans_a.
    [Graphical view]
    PfamiPF01239. PPTA. 4 hits.
    [Graphical view]
    PROSITEiPS51147. PFTA. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O93829-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQHGIKRVKL SEEAKRLKLE KDQIKIKNYR QLTDEIFELR ANENYSDEAL    50
    IKTNELLIIN PEFYTIWNYR REILINNYSS SNDKDDQIYE DILNQDLNFV 100
    LVQLKKFPKC YWIWNHRRWL LFELVKLGKV NWKYEFGVVS KLLDLDQRNF 150
    HGWHYRRFVV KNMELECKND TTLILKINLD EFNYTTLKIQ KDFSNFSAWH 200
    NRTKLIPKIY NLIQQQQQQQ QKDGKIFGDL PGIELFQNPI LLLKNDLEMI 250
    KTGVYMSPED TSVWLYLYWL LTDDLFTNAF KSHQQDYMNI LHEQLQLINE 300
    VNEMEKEDTG QDNVGCLKSM IFINALIQNE NNKPVLTEQV KSCLKQLAKI 350
    DPLRKNKYLD QLAGNAPIFH H 371
    Length:371
    Mass (Da):44,462
    Last modified:May 1, 1999 - v1
    Checksum:i69DC54570B3E9FF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021170 Genomic DNA. Translation: BAA35192.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021170 Genomic DNA. Translation: BAA35192.1 .

    3D structure databases

    ProteinModelPortali O93829.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5536.

    Family and domain databases

    InterProi IPR002088. Prenyl_trans_a.
    [Graphical view ]
    Pfami PF01239. PPTA. 4 hits.
    [Graphical view ]
    PROSITEi PS51147. PFTA. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of BET4 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 nameiPGTA_CANAX
    AccessioniPrimary (citable) accession number: O93829
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 63 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