






| 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 |
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0.0 | [632..1835] | [1..1203] |
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0.0 | [1..1835] | [1..1835] |
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0.0 | [12..1832] | [4..1830] |
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0.0 | [632..1834] | [1..1213] |
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0.0 | [633..1074] | [3..446] |
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0.0 | [632..1074] | [1..445] |
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0.0 | [633..1072] | [3..444] |
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0.0 | [633..1072] | [3..444] |
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0.0 | [622..1170] | [1..579] |
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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
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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
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| 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):![]() |
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Region A: Residues: [736-762] |
1 11 21 31 41 51
| | | | | |
1 PSGDIIRGLG LKHSARQIAQ KAGVPLV
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Region B: Residues: [833-858] |
1 11 21 31 41 51
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1 IENARHVEVQ LMGDGFGKAI ALGERD
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Region C: Residues: [872-963] |
1 11 21 31 41 51
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1 TPAPNLPEKT RLALRKAAES LGSLLNYKCA GTVEFIYDEK KDEFYFLEVN TRLQVEHPIT 60
61 EMVTGLDLVE WMIRIAANDA PDFDSTKVEV NG
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| 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):![]() |
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Region A: Residues: [763-832] |
1 11 21 31 41 51
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1 PGSLLITSVE EAKKVAAELE YPVMVKSTAG GGGIGLQKVD SEEDIEHIFE TVKHQGETFF 60
61 GDAGVFLERF
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Region B: Residues: [859-871] |
1 11 21 31 41 51
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1 CSLQRRNQKV IEE
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Region C: Residues: [964-1094] |
1 11 21 31 41 51
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1 VSMEARLYAE NPLKNFRPSP GLLVDVKFPD WARVDTWVKK GTNISPEYDP TLAKIIVHGK 60
61 DRDDAISKLN QALEETKVYG CITNIDYLKS IITSDFFAKA KVSTNILNSY QYEPTAIEIT 120
121 LPGAHTSIQD Y
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| 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):![]() |
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Region A: Residues: [1095-1417] |
1 11 21 31 41 51
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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
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| 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 |
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Region A: Residues: [1418-1655] |
1 11 21 31 41 51
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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
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| 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.
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Region A: Residues: [1656-1751] |
1 11 21 31 41 51
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1 LAASSEVPWL MNPFDQVEFY PVSEEDLDKM TEDCDNGVYK VNIEKSVFDH QEYLRWINAN 60
61 KDSITAFQEG QLGERAEEFA KLIQNANSEL KESVTV
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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 |
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Region A: Residues: [1752-1835] |
1 11 21 31 41 51
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1 KPDEEEDFPE GAEIVYSEYS GRFWKSIASV GDVIEAGQGL LIIEAMKAEM IISAPKSGKI 60
61 IKICHGNGDM VDSGDIVAVI ETLA
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| Detection Method: | |
| Confidence: | 46.09691 |
| Match: | 1dczA_ |
| Description: | Biotin carboxyl carrier domain of transcarboxylase (TC 1.3S) |
Matching Structure (courtesy of the PDB):![]() |
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