ID A0A0V1D5R7_TRIBR Unreviewed; 348 AA.
AC A0A0V1D5R7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha {ECO:0000256|ARBA:ARBA00040965};
DE EC=2.5.1.58 {ECO:0000256|ARBA:ARBA00012702};
DE EC=2.5.1.59 {ECO:0000256|ARBA:ARBA00012700};
DE AltName: Full=CAAX farnesyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00043086};
DE AltName: Full=FTase-alpha {ECO:0000256|ARBA:ARBA00042436};
DE AltName: Full=Ras proteins prenyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00041392};
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00043219};
DE Flags: Fragment;
GN Name=FNTA {ECO:0000313|EMBL:KRY56708.1};
GN ORFNames=T03_2130 {ECO:0000313|EMBL:KRY56708.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY56708.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY56708.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY56708.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000256|ARBA:ARBA00006734}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY56708.1}.
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DR EMBL; JYDI01000040; KRY56708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D5R7; -.
DR STRING; 45882.A0A0V1D5R7; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008318; F:protein prenyltransferase activity; IEA:InterPro.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR InterPro; IPR002088; Prenyl_trans_a.
DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11129:SF1; PROTEIN FARNESYLTRANSFERASE_GERANYLGERANYLTRANSFERASE TYPE-1 SUBUNIT ALPHA; 1.
DR Pfam; PF01239; PPTA; 5.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51147; PFTA; 5.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KRY56708.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY56708.1"
SQ SEQUENCE 348 AA; 41370 MW; 6B5ECF39407A4360 CRC64;
LTELRDITMC PNICGIACFV VLLILSPIDI IFICTMAESL CVFNSSEFKD VQPIYLSEEE
SGVINISCSK KFEDVYAYFR ALFNKQEISE RALKLTEEAA NLNPANYTVW YYRRKILKEL
NKDLKKEVEF CSRMTDETPK NYQIWHHRRL LIEILNDPTG ELEFTQSMLQ EDYKNYHAWQ
HRQWLISHFK LWDNELVYSE EMIKKDARNN SAWNYRYFVI NSTTGFDAQV TEREIQMTLE
NIKKLPHNES AWNYLNGIVE DRGPSSFENV VNFCEYLLSQ KQTSPQLLAF LYTAYLDKFQ
KTEDENFKNK AIKATFVVMI YLQMCDMLLD MDPMRRHFWQ QYKSNVKA
//
