Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
blastp_kegg | ssl:SS1G_09546 | 1 | 298 | 298 | n/a | 100.00 | 298 | 100.00 | 0.00 | 1e-177 | hypothetical protein |
bfu:BC1G_14083 | 8 | 262 | 255 | n/a | 21.48 | 1187 | 89.41 | 6.27 | 1e-138 | nitrilase |
aor:AO090102000347 | 8 | 276 | 269 | Gaps:18 | 97.55 | 286 | 53.41 | 19.35 | 2e-83 | hypothetical protein |
act:ACLA_002910 | 10 | 276 | 267 | Gaps:11 | 90.34 | 290 | 55.34 | 18.32 | 6e-82 | hydrolase carbon-nitrogen family putative |
afm:AFUA_5G02350 | 10 | 276 | 267 | Gaps:17 | 83.49 | 321 | 55.97 | 15.67 | 2e-79 | hydrolase carbon-nitrogen family |
pcs:Pc21g15050 | 8 | 276 | 269 | Gaps:11 | 90.72 | 291 | 52.27 | 20.45 | 6e-79 | Pc21g15050 |
nfi:NFIA_039740 | 10 | 276 | 267 | Gaps:17 | 87.87 | 305 | 54.85 | 16.42 | 1e-78 | hydrolase carbon-nitrogen family putative |
ani:AN8024.2 | 7 | 276 | 270 | Gaps:26 | 91.75 | 303 | 50.72 | 17.99 | 3e-77 | hypothetical protein |
pno:SNOG_08320 | 8 | 267 | 260 | Gaps:41 | 95.35 | 301 | 53.31 | 11.85 | 1e-76 | hypothetical protein |
nfi:NFIA_007720 | 4 | 289 | 286 | Gaps:27 | 94.21 | 311 | 50.17 | 13.99 | 5e-73 | hydrolase carbon-nitrogen family protein |
blastp_uniprot_sprot | sp|O31664|MTNU_BACSU | 1 | 267 | 267 | Gaps:24 | 93.82 | 259 | 32.10 | 16.46 | 3e-17 | UPF0012 hydrolase mtnU OS Bacillus subtilis GN mtnU PE 3 SV 1 |
sp|Q9NQR4|NIT2_HUMAN | 10 | 259 | 250 | Gaps:29 | 85.87 | 276 | 29.11 | 20.25 | 2e-15 | Omega-amidase NIT2 OS Homo sapiens GN NIT2 PE 1 SV 1 |
sp|P49954|NIT3_YEAST | 10 | 260 | 251 | Gaps:25 | 84.54 | 291 | 28.46 | 20.33 | 3e-14 | Probable hydrolase NIT3 OS Saccharomyces cerevisiae GN NIT3 PE 1 SV 1 |
sp|O59829|YCU9_SCHPO | 64 | 252 | 189 | Gaps:22 | 62.87 | 272 | 31.58 | 22.22 | 1e-13 | Probable nitrilase C965.09 OS Schizosaccharomyces pombe GN SPCC965.09 PE 2 SV 1 |
sp|Q9JHW2|NIT2_MOUSE | 10 | 259 | 250 | Gaps:35 | 85.87 | 276 | 27.85 | 21.10 | 1e-13 | Omega-amidase NIT2 OS Mus musculus GN Nit2 PE 1 SV 1 |
sp|Q6INI7|NIT2B_XENLA | 10 | 264 | 255 | Gaps:35 | 87.68 | 276 | 26.86 | 21.90 | 1e-12 | Omega-amidase NIT2-B OS Xenopus laevis GN nit2b PE 2 SV 1 |
sp|Q5R4L6|NIT2_PONAB | 10 | 259 | 250 | Gaps:36 | 85.82 | 275 | 27.97 | 20.34 | 1e-12 | Omega-amidase NIT2 OS Pongo abelii GN NIT2 PE 3 SV 1 |
sp|Q6IR61|NIT2A_XENLA | 10 | 259 | 250 | Gaps:39 | 85.87 | 276 | 27.85 | 21.94 | 2e-12 | Omega-amidase NIT2-A OS Xenopus laevis GN nit2a PE 2 SV 1 |
sp|Q28IE5|NIT2_XENTR | 10 | 264 | 255 | Gaps:35 | 87.68 | 276 | 26.03 | 21.49 | 2e-12 | Omega-amidase NIT2 OS Xenopus tropicalis GN nit2 PE 2 SV 1 |
sp|P55175|Y601_SYNY3 | 10 | 259 | 250 | Gaps:36 | 88.97 | 272 | 27.27 | 21.07 | 2e-12 | UPF0012 hydrolase sll0601 OS Synechocystis sp. (strain PCC 6803) GN sll0601 PE 3 SV 1 |
blastp_pdb | 1f89_B | 10 | 260 | 251 | Gaps:25 | 84.54 | 291 | 28.46 | 20.33 | 5e-15 | mol:protein length:291 32.5 KDA PROTEIN YLR351C |
1f89_A | 10 | 260 | 251 | Gaps:25 | 84.54 | 291 | 28.46 | 20.33 | 5e-15 | mol:protein length:291 32.5 KDA PROTEIN YLR351C |
2w1v_B | 10 | 259 | 250 | Gaps:35 | 85.87 | 276 | 27.85 | 21.10 | 2e-14 | mol:protein length:276 NITRILASE HOMOLOG 2 |
2w1v_A | 10 | 259 | 250 | Gaps:35 | 85.87 | 276 | 27.85 | 21.10 | 2e-14 | mol:protein length:276 NITRILASE HOMOLOG 2 |
1j31_D | 8 | 253 | 246 | Gaps:29 | 85.11 | 262 | 30.49 | 16.59 | 5e-13 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_C | 8 | 253 | 246 | Gaps:29 | 85.11 | 262 | 30.49 | 16.59 | 5e-13 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_B | 8 | 253 | 246 | Gaps:29 | 85.11 | 262 | 30.49 | 16.59 | 5e-13 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_A | 8 | 253 | 246 | Gaps:29 | 85.11 | 262 | 30.49 | 16.59 | 5e-13 | mol:protein length:262 Hypothetical protein PH0642 |
3hkx_A | 17 | 252 | 236 | Gaps:33 | 77.39 | 283 | 29.68 | 18.26 | 2e-12 | mol:protein length:283 Amidase |
3iw3_B | 8 | 254 | 247 | Gaps:29 | 85.50 | 262 | 29.02 | 17.41 | 2e-11 | mol:protein length:262 Nitrilase |
rpsblast_cdd | gnl|CDD|143587 | 8 | 266 | 259 | Gaps:23 | 94.07 | 253 | 34.87 | 15.55 | 1e-50 | cd07197 nitrilase Nitrilase superfamily including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes. This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds it includes nitrilases cyanide dihydratases aliphatic amidases N-terminal amidases beta-ureidopropionases biotinidases pantotheinase N-carbamyl-D-amino acid amidohydrolases the glutaminase domain of glutamine-dependent NAD+ synthetase apolipoprotein N-acyltransferases and N-carbamoylputrescine amidohydrolases among others. These enzymes depend on a Glu-Lys-Cys catalytic triad and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. These oligomers include dimers tetramers hexamers octamers tetradecamers octadecamers as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism in detoxifying small molecules in the synthesis of signaling molecules and in the post-translational modification of proteins. They are used industrially as biocatalysts in the fine chemical and pharmaceutical industry in cyanide remediation and in the treatment of toxic effluent. This superfamily has been classified previously in the literature based on global and structure-based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative the plasmid-borne TraB family has not been included in the hierarchy. |
gnl|CDD|143605 | 10 | 260 | 251 | Gaps:26 | 91.37 | 255 | 30.90 | 16.74 | 1e-32 | cd07581 nitrilase_3 Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. |
gnl|CDD|30737 | 8 | 266 | 259 | Gaps:27 | 89.05 | 274 | 32.79 | 16.80 | 2e-31 | COG0388 COG0388 Predicted amidohydrolase [General function prediction only]. |
gnl|CDD|143607 | 8 | 257 | 250 | Gaps:34 | 90.12 | 253 | 33.33 | 20.18 | 2e-28 | cd07583 nitrilase_5 Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. |
gnl|CDD|143596 | 10 | 267 | 258 | Gaps:57 | 91.70 | 265 | 32.51 | 15.23 | 1e-26 | cd07572 nit Nit1 Nit 2 and related proteins and the Nit1-like domain of NitFhit (class 10 nitrilases). This subgroup includes mammalian Nit1 and Nit2 the Nit1-like domain of the invertebrate NitFhit and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13) this subgroup corresponds to class 10. |
gnl|CDD|143600 | 7 | 261 | 255 | Gaps:33 | 91.34 | 254 | 30.17 | 16.81 | 5e-26 | cd07576 R-amidase_like Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases). Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13) class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer. |
gnl|CDD|143608 | 3 | 252 | 250 | Gaps:44 | 89.92 | 258 | 33.19 | 12.93 | 6e-26 | cd07584 nitrilase_6 Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. |
gnl|CDD|143598 | 12 | 273 | 262 | Gaps:33 | 91.79 | 280 | 31.91 | 14.79 | 3e-25 | cd07574 nitrilase_Rim1_like Uncharacterized subgroup of the nitrilase superfamily some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases). Some members of this subgroup are implicated in post-translational modification as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13) this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. |
gnl|CDD|144405 | 10 | 165 | 156 | Gaps:9 | 90.12 | 172 | 29.68 | 20.65 | 2e-22 | pfam00795 CN_hydrolase Carbon-nitrogen hydrolase. This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1 Aliphatic amidase EC:3.5.1.4 Biotidinase EC:3.5.1.12 Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad and are multimeric alpha-beta-beta-alpha sandwich proteins. |
gnl|CDD|143604 | 8 | 176 | 169 | Gaps:6 | 61.57 | 268 | 33.94 | 16.97 | 8e-22 | cd07580 nitrilase_2 Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer. |
rpsblast_kog | gnl|CDD|36025 | 10 | 256 | 247 | Gaps:36 | 81.69 | 295 | 28.63 | 17.84 | 6e-18 | KOG0807 KOG0807 KOG0807 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |
gnl|CDD|36024 | 4 | 263 | 260 | Gaps:46 | 86.58 | 298 | 21.71 | 15.50 | 1e-16 | KOG0806 KOG0806 KOG0806 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |
gnl|CDD|36023 | 12 | 165 | 154 | Gaps:21 | 49.55 | 337 | 26.35 | 16.17 | 1e-07 | KOG0805 KOG0805 KOG0805 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |