ID A0A0P7BFK7_9HYPO Unreviewed; 524 AA.
AC A0A0P7BFK7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
GN ORFNames=AK830_g7736 {ECO:0000313|EMBL:KPM38806.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM38806.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM38806.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM38806.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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:KPM38806.1}.
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DR EMBL; LKCW01000123; KPM38806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BFK7; -.
DR STRING; 78410.A0A0P7BFK7; -.
DR OrthoDB; 20949at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
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 Prenyltransferase {ECO:0000256|ARBA:ARBA00022602};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022602}.
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 59425 MW; ED607DDF52D69F47 CRC64;
MPPKSKGSSK APHPEPKGST PLSHTASEPP LPPQTVSQRT QERFFRTNPC EKRRQDVGLA
SLTPAEKKSY THARLILPVA DRRVPLSNKA EREFWKHVAK EGLPARRLAP GYAWGTDRSG
RDIGTYSPDE LEQRTLKHAR LTALQIRHRQ FLAARDGSRA RDVSPEDLQD EKKRRQAMAA
LKRDLYGEVT GTLAKDPDWD DVLPIPQDEP EGALSQIAYP DDYAEAVSYL RAVMAANECS
PRCLRLTEHV ISMNPAHYTV WLYRFKIISV LKLSIPDEIT WLNQVALANL KNYQIWNHRQ
LLIDYYYPEI EEDTATIRAL GRSETAFITT MLDEDAKNYH VWSYRQYLVG KLFMWTASEL
GSTQNLIEDD VRNNSAWSHR FYLVFSDPTA STAGSIPTEH DPKVPDATVD REIAYAQEKI
AIAPQNQSPW NYLLGVLAKS GRKLATVQDF AEQYVSAIGE EGEEVRSSHA LDLLAKVYHE
QDDTEKAALC LKRLSEKWDP VREGYWKYRA AQLEGVAAPA QTAE
//
