Protein: | DUR1,2 |
Organism: | Saccharomyces cerevisiae |
Length: | 1835 amino acids |
Reference: | Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for DUR1,2.
Description | E-value | Query Range |
Subject Range |
|
0.0 | [632..1835] | [1..1203] |
|
0.0 | [1..1835] | [1..1835] |
|
0.0 | [12..1832] | [4..1830] |
|
0.0 | [632..1834] | [1..1213] |
|
0.0 | [633..1074] | [3..446] |
|
0.0 | [632..1074] | [1..445] |
|
0.0 | [633..1072] | [3..444] |
|
0.0 | [633..1072] | [3..444] |
|
0.0 | [622..1170] | [1..579] |
Region A: Residues: [1-483] |
1 11 21 31 41 51 | | | | | | 1 MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN AWISLISKEN 60 61 LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA CPSFAYEPSK DSKVVELLRN 120 121 AGAIIVGKTN LDQFATGLVG TRSPYGKTPC AFSKEHVSGG SSAGSASVVA RGIVPIALGT 180 181 DTAGSGRVPA ALNNLIGLKP TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP 240 241 DPDNDEYSRP YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI 300 301 DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK KYSAVDCFSF 360 361 EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV LVNSRQGTWT NFVNLADLAA 420 421 LAVPAGFRDD GLPNGITLIG KKFTDYALLE LANRYFQNIF PNGSRTYGTF TSSSVKPAND 480 481 QLV |
Detection Method: | ![]() |
Confidence: | 194.980454 |
Match: | 1gr8A_ |
Description: | No description for 1gr8A_ was found. |
Term | Confidence | Notes |
ligase activity | 7.63077869457441 | bayes_pls_golite062009 |
glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | 7.42914157198604 | bayes_pls_golite062009 |
binding | 1.24905380693412 | bayes_pls_golite062009 |
hydrolase activity | 1.16287375250451 | bayes_pls_golite062009 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 1.02750000262516 | bayes_pls_golite062009 |
ligase activity, forming carbon-nitrogen bonds | 0.977723384067654 | bayes_pls_golite062009 |
catalytic activity | 0.906509857495572 | bayes_pls_golite062009 |
carbon-nitrogen ligase activity, with glutamine as amido-N-donor | 0.461750895886233 | bayes_pls_golite062009 |
protein binding | 0.276132955069873 | bayes_pls_golite062009 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 0.0166505316914077 | bayes_pls_golite062009 |
Region A: Residues: [484-604] |
1 11 21 31 41 51 | | | | | | 1 GPDYDPSTSI KLAVVGAHLK GLPLHWQLEK VNATYLCTTK TSKAYQLFAL PKNGPVLKPG 60 61 LRRVQDSNGS QIELEVYSVP KELFGAFISM VPEPLGIGSV ELESGEWIKS FICEESGYKA 120 121 K |
Shown below is our most confident de novo (Rosetta) prediction for this domain.
Click here to view all matches.
Found no confident structure predictions for this domain.
Term | Confidence | Notes |
structural molecule activity | 1.24470630176758 | bayes_pls_golite062009 |
Region A: Residues: [605-735] |
1 11 21 31 41 51 | | | | | | 1 GTVDITKYGG FRAYFEMLKK KESQKKKLFD TVLIANRGEI AVRIIKTLKK LGIRSVAVYS 60 61 DPDKYSQHVT DADVSVPLHG TTAAQTYLDM NKIIDAAKQT NAQAIIPGYG FLSENADFSD 120 121 ACTSAGITFV G |
Detection Method: | ![]() |
Confidence: | 1882.218487 |
Match: | 1bncA_ |
Description: | Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2 |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [736-762] |
1 11 21 31 41 51 | | | | | | 1 PSGDIIRGLG LKHSARQIAQ KAGVPLV |
Region B: Residues: [833-858] |
1 11 21 31 41 51 | | | | | | 1 IENARHVEVQ LMGDGFGKAI ALGERD |
Region C: Residues: [872-963] |
1 11 21 31 41 51 | | | | | | 1 TPAPNLPEKT RLALRKAAES LGSLLNYKCA GTVEFIYDEK KDEFYFLEVN TRLQVEHPIT 60 61 EMVTGLDLVE WMIRIAANDA PDFDSTKVEV NG |
Detection Method: | ![]() |
Confidence: | 1882.218487 |
Match: | 1bncA_ |
Description: | Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2 |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [763-832] |
1 11 21 31 41 51 | | | | | | 1 PGSLLITSVE EAKKVAAELE YPVMVKSTAG GGGIGLQKVD SEEDIEHIFE TVKHQGETFF 60 61 GDAGVFLERF |
Region B: Residues: [859-871] |
1 11 21 31 41 51 | | | | | | 1 CSLQRRNQKV IEE |
Region C: Residues: [964-1094] |
1 11 21 31 41 51 | | | | | | 1 VSMEARLYAE NPLKNFRPSP GLLVDVKFPD WARVDTWVKK GTNISPEYDP TLAKIIVHGK 60 61 DRDDAISKLN QALEETKVYG CITNIDYLKS IITSDFFAKA KVSTNILNSY QYEPTAIEIT 120 121 LPGAHTSIQD Y |
Detection Method: | ![]() |
Confidence: | 1882.218487 |
Match: | 1bncA_ |
Description: | Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), C-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase, (BC), N-domain; Biotin carboxylase subunit of acetyl-CoA carboxylase (BC), domain 2 |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [1095-1417] |
1 11 21 31 41 51 | | | | | | 1 PGRVGYWRIG VPPSGPMDAY SFRLANRIVG NDYRTPAIEV TLTGPSIVFH CETVIAITGG 60 61 TALCTLDGQE IPQHKPVEVK RGSTLSIGKL TSGCRAYLGI RGGIDVPKYL GSYSTFTLGN 120 121 VGGYNGRVLK LGDVLFLPSN EENKSVECLP QNIPQSLIPQ ISETKEWRIG VTCGPHGSPD 180 181 FFKPESIEEF FSEKWKVHYN SNRFGVRLIG PKPKWARSNG GEGGMHPSNT HDYVYSLGAI 240 241 NFTGDEPVII TCDGPSLGGF VCQAVVPEAE LWKVGQVKPG DSIQFVPLSY ESSRSLKESQ 300 301 DVAIKSLDGT KLRRLDSVSI LPS |
Detection Method: | ![]() |
Confidence: | 190.244125 |
Match: | PF02626 |
Description: | Allophanate hydrolase subunit 2 |
Shown below is our most confident prediction for this domain.
Click here to view all matches.
Found no confident structure predictions for this domain.
Term | Confidence | Notes |
ligase activity | 6.81588178611521 | bayes_pls_golite062009 |
peptidyl-prolyl cis-trans isomerase activity | 1.05326644345172 | bayes_pls_golite062009 |
binding | 1.03084911722464 | bayes_pls_golite062009 |
cis-trans isomerase activity | 0.985752998974367 | bayes_pls_golite062009 |
catalytic activity | 0.748655649755714 | bayes_pls_golite062009 |
nucleic acid binding | 0.438324825951616 | bayes_pls_golite062009 |
protein binding | 0.130251391659493 | bayes_pls_golite062009 |
Region A: Residues: [1418-1655] |
1 11 21 31 41 51 | | | | | | 1 FETPILAQME KVNELSPKVV YRQAGDRYVL VEYGDNEMNF NISYRIECLI SLVKKNKTIG 60 61 IVEMSQGVRS VLIEFDGYKV TQKELLKVLV AYETEIQFDE NWKITSNIIR LPMAFEDSKT 120 121 LACVQRYQET IRSSAPWLPN NVDFIANVNG ISRNEVYDML YSARFMVLGL GDVFLGSPCA 180 181 VPLDPRHRFL GSKYNPSRTY TERGAVGIGG MYMCIYAANS PGGYQLVGRT IPIWDKLC |
Detection Method: | ![]() |
Confidence: | 3.008774 |
Match: | PF02682 |
Description: | Allophanate hydrolase subunit 1 |
Shown below is our most confident prediction for this domain.
Click here to view all matches.
Found no confident structure predictions for this domain.
Region A: Residues: [1656-1751] |
1 11 21 31 41 51 | | | | | | 1 LAASSEVPWL MNPFDQVEFY PVSEEDLDKM TEDCDNGVYK VNIEKSVFDH QEYLRWINAN 60 61 KDSITAFQEG QLGERAEEFA KLIQNANSEL KESVTV |
Shown below is our most confident de novo (Rosetta) prediction for this domain.
Click here to view all matches.
MCM Score |
SCOP Match |
SCOP Description | ||
View | Download | 0.810 | c.58.1 | Aminoacid dehydrogenase-like, N-terminal domain |
Region A: Residues: [1752-1835] |
1 11 21 31 41 51 | | | | | | 1 KPDEEEDFPE GAEIVYSEYS GRFWKSIASV GDVIEAGQGL LIIEAMKAEM IISAPKSGKI 60 61 IKICHGNGDM VDSGDIVAVI ETLA |
Detection Method: | ![]() |
Confidence: | 46.09691 |
Match: | 1dczA_ |
Description: | Biotin carboxyl carrier domain of transcarboxylase (TC 1.3S) |
Matching Structure (courtesy of the PDB):![]() |