Protein: | DAP2_YEAST |
Organism: | Saccharomyces cerevisiae S288c |
Length: | 818 amino acids |
Reference: | Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for DAP2_YEAST.
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..818] | [1..818] |
|
0.0 | [6..815] | [12..788] |
|
0.0 | [6..815] | [12..788] |
|
0.0 | [6..815] | [12..788] |
|
0.0 | [6..815] | [12..788] |
Region A: Residues: [1-257] |
1 11 21 31 41 51 | | | | | | 1 MEGGEEEVER IPDELFDTKK KHLLDKLIRV GIILVLLIWG TVLLLKSIPH HSNTPDYQEP 60 61 NSNYTNDGKL KVSFSVVRNN TFQPKYHELQ WISDNKIESN DLGLYVTFMN DSYVVKSVYD 120 121 DSYNSVLLEG KTFIHNGQNL TVESITASPD LKRLLIRTNS VQNWRHSTFG SYFVYDKSSS 180 181 SFEEIGNEVA LAIWSPNSND IAYVQDNNIY IYSAISKKTI RAVTNDGSSF LFNGKPDWVY 240 241 EEEVFEDDKA AWWSPTG |
Detection Method: | ![]() |
Confidence: | 35.09691 |
Match: | 1erjA_ |
Description: | Tup1, C-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
hydrolase activity | 4.09944423676394 | bayes_pls_golite062009 |
peptidase activity | 2.49064988313037 | bayes_pls_golite062009 |
peptidase activity, acting on L-amino acid peptides | 2.10044305272656 | bayes_pls_golite062009 |
catalytic activity | 1.39629727416851 | bayes_pls_golite062009 |
palmitoyl-(protein) hydrolase activity | 1.01438408843885 | bayes_pls_golite062009 |
binding | 0.549512873906854 | bayes_pls_golite062009 |
heparin binding | 0.437236652275566 | bayes_pls_golite062009 |
endopeptidase activity | 0.43631945855397 | bayes_pls_golite062009 |
hydrolase activity, acting on ester bonds | 0.282381128231187 | bayes_pls_golite062009 |
Region A: Residues: [258-353] |
1 11 21 31 41 51 | | | | | | 1 DYLAFLKIDE SEVGEFIIPY YVQDEKDIYP EMRSIKYPKS GTPNPHAELW VYSMKDGTSF 60 61 HPRISGNKKD GSLLITEVTW VGNGNVLVKT TDRSSD |
Region B: Residues: [365-555] |
1 11 21 31 41 51 | | | | | | 1 KTSNVVRNES SNGGWWEITH NTLFIPANET FDRPHNGYVD ILPIGGYNHL AYFENSNSSH 60 61 YKTLTEGKWE VVNGPLAFDS MENRLYFIST RKSSTERHVY YIDLRSPNEI IEVTDTSEDG 120 121 VYDVSFSSGR RFGLLTYKGP KVPYQKIVDF HSRKAEKCDK GNVLGKSLYH LEKNEVLTKI 180 181 LEDYAVPRKS F |
Detection Method: | ![]() |
Confidence: | 83.0 |
Match: | 1qfsA_ |
Description: | Prolyl oligopeptidase, N-terminal domain; Prolyl oligopeptidase, C-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [354-364] |
1 11 21 31 41 51 | | | | | | 1 ILTVFLIDTI A |
Region B: Residues: [556-818] |
1 11 21 31 41 51 | | | | | | 1 RELNLGKDEF GKDILVNSYE ILPNDFDETL SDHYPVFFFA YGGPNSQQVV KTFSVGFNEV 60 61 VASQLNAIVV VVDGRGTGFK GQDFRSLVRD RLGDYEARDQ ISAASLYGSL TFVDPQKISL 120 121 FGWSYGGYLT LKTLEKDGGR HFKYGMSVAP VTDWRFYDSV YTERYMHTPQ ENFDGYVESS 180 181 VHNVTALAQA NRFLLMHGTG DDNVHFQNSL KFLDLLDLNG VENYDVHVFP DSDHSIRYHN 240 241 ANVIVFDKLL DWAKRAFDGQ FVK |
Detection Method: | ![]() |
Confidence: | 83.0 |
Match: | 1qfsA_ |
Description: | Prolyl oligopeptidase, N-terminal domain; Prolyl oligopeptidase, C-terminal domain |
Matching Structure (courtesy of the PDB):![]() |