Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
blastp_kegg | bfu:BC1G_08982 | 1 | 2346 | 2346 | n/a | 99.03 | 2369 | 94.67 | 0.00 | 0.0 | hypothetical protein |
ssl:SS1G_10280 | 289 | 2346 | 2058 | Gaps:21 | 97.96 | 2106 | 78.19 | 7.03 | 0.0 | hypothetical protein |
pan:PODANSg7976 | 1586 | 2208 | 623 | Gaps:10 | 37.65 | 1676 | 58.64 | 15.06 | 0.0 | hypothetical protein |
fgr:FG10094.1 | 1584 | 2233 | 650 | Gaps:13 | 49.70 | 1314 | 51.61 | 15.93 | 0.0 | hypothetical protein |
pno:SNOG_14179 | 1612 | 2202 | 591 | Gaps:16 | 65.68 | 912 | 49.92 | 17.86 | 1e-168 | hypothetical protein |
mgr:MGG_13812 | 1586 | 2211 | 626 | Gaps:95 | 59.02 | 937 | 52.26 | 17.72 | 1e-160 | MG04497.4 MG04498.4 hypothetical protein |
ssl:SS1G_10281 | 1 | 282 | 282 | n/a | 94.63 | 298 | 90.43 | 1.77 | 1e-150 | hypothetical protein |
afm:AFUA_6G13230 | 1 | 282 | 282 | n/a | 96.58 | 292 | 72.34 | 11.35 | 1e-123 | nitrilase family protein (Nit3) |
act:ACLA_086490 | 1 | 282 | 282 | n/a | 96.58 | 292 | 71.63 | 10.99 | 1e-121 | nitrilase family protein (Nit3) putative |
nfi:NFIA_059160 | 1 | 282 | 282 | n/a | 96.58 | 292 | 71.63 | 10.99 | 1e-121 | nitrilase family protein (Nit3) putative |
blastp_uniprot_sprot | sp|Q10166|YAUB_SCHPO | 7 | 282 | 276 | Gaps:9 | 82.92 | 322 | 57.30 | 14.23 | 3e-86 | UPF0012 hydrolase C26A3.11 OS Schizosaccharomyces pombe GN SPAC26A3.11 PE 2 SV 1 |
sp|P49954|NIT3_YEAST | 2 | 282 | 281 | Gaps:8 | 95.88 | 291 | 51.25 | 14.70 | 1e-75 | Probable hydrolase NIT3 OS Saccharomyces cerevisiae GN NIT3 PE 1 SV 1 |
sp|Q497B0|NIT2_RAT | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 54.41 | 11.88 | 1e-73 | Omega-amidase NIT2 OS Rattus norvegicus GN Nit2 PE 1 SV 1 |
sp|Q9JHW2|NIT2_MOUSE | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 54.79 | 11.49 | 3e-73 | Omega-amidase NIT2 OS Mus musculus GN Nit2 PE 1 SV 1 |
sp|Q2T9R6|NIT2_BOVIN | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 53.26 | 14.18 | 9e-73 | Omega-amidase NIT2 OS Bos taurus GN NIT2 PE 2 SV 1 |
sp|Q4VBV9|NIT2_DANRE | 10 | 281 | 272 | Gaps:11 | 94.22 | 277 | 53.26 | 13.03 | 3e-72 | Omega-amidase NIT2 OS Danio rerio GN nit2 PE 2 SV 1 |
sp|Q6INI7|NIT2B_XENLA | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 53.26 | 12.64 | 4e-72 | Omega-amidase NIT2-B OS Xenopus laevis GN nit2b PE 2 SV 1 |
sp|Q28IE5|NIT2_XENTR | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 52.11 | 14.56 | 7e-72 | Omega-amidase NIT2 OS Xenopus tropicalis GN nit2 PE 2 SV 1 |
sp|Q9NQR4|NIT2_HUMAN | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 52.49 | 14.94 | 3e-71 | Omega-amidase NIT2 OS Homo sapiens GN NIT2 PE 1 SV 1 |
sp|Q6IR61|NIT2A_XENLA | 10 | 276 | 267 | Gaps:11 | 92.75 | 276 | 53.12 | 11.72 | 4e-70 | Omega-amidase NIT2-A OS Xenopus laevis GN nit2a PE 2 SV 1 |
blastp_pdb | 1f89_B | 2 | 282 | 281 | Gaps:8 | 95.88 | 291 | 51.25 | 14.70 | 2e-76 | mol:protein length:291 32.5 KDA PROTEIN YLR351C |
1f89_A | 2 | 282 | 281 | Gaps:8 | 95.88 | 291 | 51.25 | 14.70 | 2e-76 | mol:protein length:291 32.5 KDA PROTEIN YLR351C |
2w1v_B | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 54.79 | 11.49 | 5e-74 | mol:protein length:276 NITRILASE HOMOLOG 2 |
2w1v_A | 10 | 281 | 272 | Gaps:11 | 94.57 | 276 | 54.79 | 11.49 | 5e-74 | mol:protein length:276 NITRILASE HOMOLOG 2 |
1ems_B | 11 | 281 | 271 | Gaps:10 | 60.23 | 440 | 30.57 | 17.36 | 1e-28 | mol:protein length:440 NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN |
1ems_A | 11 | 281 | 271 | Gaps:10 | 60.23 | 440 | 30.57 | 17.36 | 1e-28 | mol:protein length:440 NIT-FRAGILE HISTIDINE TRIAD FUSION PROTEIN |
1j31_D | 9 | 243 | 235 | Gaps:25 | 81.68 | 262 | 29.44 | 20.56 | 7e-12 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_C | 9 | 243 | 235 | Gaps:25 | 81.68 | 262 | 29.44 | 20.56 | 7e-12 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_B | 9 | 243 | 235 | Gaps:25 | 81.68 | 262 | 29.44 | 20.56 | 7e-12 | mol:protein length:262 Hypothetical protein PH0642 |
1j31_A | 9 | 243 | 235 | Gaps:25 | 81.68 | 262 | 29.44 | 20.56 | 7e-12 | mol:protein length:262 Hypothetical protein PH0642 |
rpsblast_cdd | gnl|CDD|143596 | 10 | 281 | 272 | Gaps:7 | 100.00 | 265 | 49.81 | 16.60 | 1e-115 | 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|143607 | 10 | 281 | 272 | Gaps:37 | 100.00 | 253 | 39.53 | 15.81 | 1e-57 | 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|143587 | 11 | 281 | 271 | Gaps:20 | 100.00 | 253 | 39.13 | 14.62 | 3e-57 | 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|30737 | 7 | 281 | 275 | Gaps:18 | 95.99 | 274 | 34.22 | 20.91 | 2e-53 | COG0388 COG0388 Predicted amidohydrolase [General function prediction only]. |
gnl|CDD|143605 | 11 | 281 | 271 | Gaps:30 | 100.00 | 255 | 36.47 | 19.22 | 2e-49 | 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|166439 | 7 | 281 | 275 | Gaps:11 | 95.07 | 284 | 33.70 | 20.74 | 2e-42 | PLN02798 PLN02798 nitrilase. |
gnl|CDD|143597 | 9 | 281 | 273 | Gaps:42 | 96.83 | 284 | 33.45 | 16.00 | 3e-41 | cd07573 CPA N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases). CPA (EC 3.5.1.53 also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA also known as nitrilase-like 1 (NLP1) and Pseudomonas aeruginosa AguB. 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) this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes the basic building block of which is a homodimer P. aeruginosa AugB is a homohexamer Arabidopsis thaliana NLP1 is a homooctomer. |
gnl|CDD|144405 | 10 | 194 | 185 | Gaps:17 | 100.00 | 172 | 37.79 | 12.21 | 2e-34 | 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|143608 | 10 | 281 | 272 | Gaps:19 | 99.61 | 258 | 35.41 | 15.56 | 3e-33 | 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|143600 | 10 | 281 | 272 | Gaps:24 | 99.21 | 254 | 32.14 | 15.08 | 8e-32 | 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. |
rpsblast_kog | gnl|CDD|36024 | 1 | 282 | 282 | Gaps:16 | 96.64 | 298 | 39.24 | 16.32 | 2e-75 | KOG0806 KOG0806 KOG0806 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |
gnl|CDD|36025 | 7 | 281 | 275 | Gaps:12 | 91.86 | 295 | 32.47 | 19.56 | 4e-45 | KOG0807 KOG0807 KOG0807 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |
gnl|CDD|35476 | 1617 | 2136 | 520 | Gaps:93 | 83.88 | 521 | 17.39 | 18.76 | 3e-15 | KOG0255 KOG0255 KOG0255 Synaptic vesicle transporter SVOP and related transporters (major facilitator superfamily) [General function prediction only]. |
gnl|CDD|36023 | 9 | 271 | 263 | Gaps:61 | 83.09 | 337 | 26.79 | 16.43 | 6e-14 | KOG0805 KOG0805 KOG0805 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |
gnl|CDD|36026 | 10 | 219 | 210 | Gaps:14 | 52.71 | 387 | 25.00 | 17.16 | 1e-06 | KOG0808 KOG0808 KOG0808 Carbon-nitrogen hydrolase [Amino acid transport and metabolism]. |