Protein Family Models for Protein (Select 932220576) - Protein Family Models

Links from Protein

Items: 1 to 20 of 31

<< First< Prev

Page of 2

Next >Last >>

Select item 4240291.

tetratricopeptide repeat protein

Date:: 2024-08-14

Family Accession:: NF024806.5
Method:: HMM

Select item 4236382.

tetratricopeptide repeat protein

Date:: 2024-08-14

Family Accession:: NF024823.5
Method:: HMM

Select item 4226463.

tetratricopeptide repeat protein

GO Terms:

Molecular Function:: protein binding (GO:0005515)

Date:: 2024-08-14

Family Accession:: NF024579.5
Method:: HMM

Select item 4225784.

tetratricopeptide repeat protein

Date:: 2024-08-14

Family Accession:: NF025910.5
Method:: HMM

Select item 4224215.

tetratricopeptide repeat protein

This family is found predominantly at the C-terminus of transglutaminase enzyme core regions. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF024824.5
Method:: HMM

Select item 4217626.

tetratricopeptide repeat protein

GO Terms:

Molecular Function:: protein binding (GO:0005515)

Date:: 2024-08-14

Family Accession:: NF024574.5
Method:: HMM

Select item 4217497.

CDC27 family protein

Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes [1, 2]. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20 [3]. [1]. 12049731. The anaphase-promoting complex: proteolysis in mitosis and. beyond.. Peters JM;. Mol Cell. 2002;9:931-943.. [2]. 16896351. The anaphase promoting complex/cyclosome: a machine designed to. destroy.. Peters JM;. Nat Rev Mol Cell Biol. 2006;7:644-656.. [3]. 12956947. TPR subunits of the anaphase-promoting complex mediate binding. to the activator protein CDH1.. Vodermaier HC, Gieffers C, Maurer-Stroh S, Eisenhaber F, Peters. JM;. Curr Biol. 2003;13:1459-1468. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF024299.5
Method:: HMM

Select item 4177198.

tetratricopeptide repeat protein

This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by Pfam:PF00515. [1]. 7667876. Tetratrico peptide repeat interactions: to TPR or not to TPR?. Lamb JR, Tugendreich S, Hieter P;. Trends Biochem Sci 1995;20:257-259.. [2]. 9482716. The structure of the tetratricopeptide repeats of protein. phosphatase 5: implications for TPR-mediated protein-protein. interactions.. Das AK, Cohen PW, Barford D;. EMBO J 1998;17:1192-1199. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF019339.5
Method:: HMM

Select item 4135519.

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

Select item 41190010.

tetratricopeptide repeat protein

GO Terms:

Molecular Function:: protein binding (GO:0005515)

Date:: 2024-08-14

Family Accession:: NF012725.5
Method:: HMM

Select item 40209211.