Protein: | MET10 |
Organism: | Saccharomyces cerevisiae |
Length: | 1035 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 MET10.
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..1035] | [1..1035] |
|
0.0 | [1..1035] | [1..1035] |
|
0.0 | [17..637] | [4..673] |
|
0.0 | [16..637] | [2..674] |
|
0.0 | [16..701] | [4..765] |
|
0.0 | [15..637] | [2..674] |
Region A: Residues: [1-373] |
1 11 21 31 41 51 | | | | | | 1 MPVEFATNPF GEAKNATSLP KYGTPVTAIS SVLFNNVDSI FAYKSFSQPD LLHQDLKKWS 60 61 EKRGNESRGK PFFQELDIRS GAGLAPLGFS HGLKNTTAIV APGFSLPYFI NSLKTVSHDG 120 121 KFLLNVGALN YDNATGSVTN DYVTALDAAS KLKYGVVTPI SANEVQSVAL LALAIATFSN 180 181 NSGAINLFDG LNYSKTVLPL VESVPEASIL AKLSKVIAPD AAFDDVLDKF NELTGLRLHN 240 241 FQYFGAQDAE TVFITYGSLE SELFNSAISG NNSKIGLINV RVPLPFNVAK FVTHVPSTTK 300 301 QIVVIGQTLD GSSPSFLRSQ VSAALFYHGR TSISVSEYIY QPDFIWSPKA VKSIVSSFIP 360 361 EFTYNADSSF GEG |
Detection Method: | ![]() |
Confidence: | 231.9897 |
Match: | 1b0pA_ |
Description: | Pyruvate-ferredoxin oxidoreductase, PFOR, domain I; Pyruvate-ferredoxin oxidoreductase, PFOR, domains VI; Pyruvate-ferredoxin oxidoreductase, PFOR, domain II; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; Pyruvate-ferredoxin oxidoreductase, PFOR, domain V |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
oxidoreductase activity, acting on sulfur group of donors | 2.53979678006253 | bayes_pls_golite062009 |
oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor | 1.31432587516415 | bayes_pls_golite062009 |
pyruvate dehydrogenase activity | 1.05771099058484 | bayes_pls_golite062009 |
pyruvate dehydrogenase (acetyl-transferring) activity | 0.91689889002022 | bayes_pls_golite062009 |
catalytic activity | 0.488483980994331 | bayes_pls_golite062009 |
binding | 0.284953915352797 | bayes_pls_golite062009 |
oxidoreductase activity, acting on NADH or NADPH | 0.240775137189639 | bayes_pls_golite062009 |
acetolactate synthase activity | 0.201869061877972 | bayes_pls_golite062009 |
Region A: Residues: [374-643] |
1 11 21 31 41 51 | | | | | | 1 FIYWASDKSI NIDVASKLVK ALSLEDGKFV SLRTKFDNLA NAGTFQAQFV TSKEQIPVSN 60 61 IDSTKLSVVE DVSLLKHLDV AATVAEQGSI ALVSQKAVKD LDLNSVESYV KNLGIPESFL 120 121 ISIAKKNIKL FIIDGETTND ESKLSLFIQA VFWKLAFGLD VAECTNRIWK SIDSGADISA 180 181 ASISEFLTGA FKNFLSEVPL ALYTKFSEIN IEKKEDEEEP AALPIFVNET SFLPNNSTIE 240 241 EIPLPETSEI SDIAKKLSFK EAYEVENKLR |
Detection Method: | ![]() |
Confidence: | 231.9897 |
Match: | 1b0pA_ |
Description: | Pyruvate-ferredoxin oxidoreductase, PFOR, domain I; Pyruvate-ferredoxin oxidoreductase, PFOR, domains VI; Pyruvate-ferredoxin oxidoreductase, PFOR, domain II; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; Pyruvate-ferredoxin oxidoreductase, PFOR, domain V |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
sulfite reductase (NADPH) activity | 8.084406223553 | bayes_pls_golite062009 |
oxidoreductase activity, acting on sulfur group of donors, NAD or NADP as acceptor | 4.30314846685644 | bayes_pls_golite062009 |
oxidoreductase activity, acting on sulfur group of donors | 4.06091555929351 | bayes_pls_golite062009 |
catalytic activity | 1.45374095556065 | bayes_pls_golite062009 |
transferase activity, transferring alkyl or aryl (other than methyl) groups | 1.198269073975 | bayes_pls_golite062009 |
oxidoreductase activity | 0.812246071526761 | bayes_pls_golite062009 |
transferase activity | 0.708491789248912 | bayes_pls_golite062009 |
oxidoreductase activity, acting on NADH or NADPH | 0.637241226597849 | bayes_pls_golite062009 |
binding | 0.568113451649995 | bayes_pls_golite062009 |
Region A: Residues: [644-694] |
1 11 21 31 41 51 | | | | | | 1 PDLPVKNFVV KVKENRRVTP ADYDRYIFHI EFDISGTGMT YDIGEALGIH A |
Region B: Residues: [816-839] |
1 11 21 31 41 51 | | | | | | 1 RREYSIASSQ KVHPNEVHLL IVVV |
Region C: Residues: [852-873] |
1 11 21 31 41 51 | | | | | | 1 QASKYISDLA VGSELVVSVK PS |
Detection Method: | ![]() |
Confidence: | 618.54902 |
Match: | 1amoA_ |
Description: | NADPH-cytochrome p450 reductase; NADPH-cytochrome p450 reductase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [695-815] |
1 11 21 31 41 51 | | | | | | 1 RNNESLVKEF LTFYGLNESD VVLVPNKDNH HLLETRTVLQ AFVENLDIFG KPPKRFYESL 60 61 IPYASNEEEK KKLEDLVTPA GAVDLKRFQD VEYYTYADIF ELFPSVRPSL EELVTIIEPL 120 121 K |
Region B: Residues: [840-851] |
1 11 21 31 41 51 | | | | | | 1 DWVDNKGRKR YG |
Region C: Residues: [874-1035] |
1 11 21 31 41 51 | | | | | | 1 VMKLPPSPKQ PVIMSGLGTG LAPFKAIVEE KLWQKQQGYE IGEVFLYLGS RHKREEYLYG 60 61 ELWEAYKDAG IITHIGAAFS RDQPQKIYIQ DRIKENLDEL KTAMIDNKGS FYLCGPTWPV 120 121 PDITQALQDI LAKDAEERGI KVDLDAAIEE LKEASRYILE VY |
Detection Method: | ![]() |
Confidence: | 618.54902 |
Match: | 1amoA_ |
Description: | NADPH-cytochrome p450 reductase; NADPH-cytochrome p450 reductase, N-terminal domain |
Matching Structure (courtesy of the PDB):![]() |