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Items: 3

1.

Protein prenyltransferase alpha subunit repeat

Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognise a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognises a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family [2]. [1]. 9843427. Crystal structure of farnesyl protein transferase complexed with. a CaaX peptide and farnesyl diphosphate analogue.. Strickland CL, Windsor WT, Syto R, Wang L, Bond R, Wu Z,. Schwartz J, Le HV, Beese LS, Weber PC;. Biochemistry 1998;37:16601-16611.. [2]. 12702202. Protein prenyltransferases.. Maurer-Stroh S, Washietl S, Eisenhaber F;. Genome Biol 2003;4:212.. [3]. 11812124. The crystal structures of phosphopantetheine adenylyltransferase. with bound substrates reveal the enzyme's catalytic mechanism.. Izard T;. J Mol Biol. 2002;315:487-495.. [4]. 18713740. Structure of protein geranylgeranyltransferase-I from the human. pathogen Candida albicans complexed with a lipid substrate.. Hast MA, Beese LS;. J Biol Chem. 2008;283:31933-31940. (from Pfam)

GO Terms:
Molecular Function:
protein prenyltransferase activity (GO:0008318)
Biological Process:
protein prenylation (GO:0018342)
Date:
2024-08-14
Family Accession:
NF013409.5
Method:
HMM
2.

protein farnesyltransferase subunit beta

protein farnesyltransferase subunit beta is an essential subunit of the farnesyltransferase complex that catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X

Date:
2021-05-07
Family Accession:
10121010
Method:
Sparcle
3.

squalene synthase

This HMM describes farnesyl-diphosphate farnesyltransferase, also known as squalene synthase, as found in eukaryotes. This family is related to phytoene synthases. Tentatively identified archaeal homologs (excluded from this model) lack the C-terminal predicted transmembrane region universally conserved among members of this family.

Date:
2019-09-10
Family Accession:
TIGR01559.1
Method:
HMM
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