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Conserved domains on  [gi|68565067|sp|Q8VC97|]
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RecName: Full=Beta-ureidopropionase; AltName: Full=Beta-alanine synthase; AltName: Full=N-carbamoyl-beta-alanine amidohydrolase

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 10166108)

carbon-nitrogen hydrolase family protein similar to nitrilase, which is involved in the reduction of organic nitrogen compounds and ammonia production, breaks carbon-nitrogen bonds and depends on a Glu-Lys-Cys catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
9-371 0e+00

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This subgroup includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. 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 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


:

Pssm-ID: 143611 [Multi-domain]  Cd Length: 363  Bit Score: 790.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   9 LEQCLEKHLPPDDLAQVKRILYGKQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRIPLPTSAP 88
Cdd:cd07587   1 LEDLLEKHLPPEELKEVKRILYGEEVKPLELPESALDLAKENDFELKGYKFEAAPEQTRPPRIVRVGLIQNKIVLPTTAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  89 VAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILE 168
Cdd:cd07587  81 IAEQREAIHDRIKKIIEAAAMAGVNIICFQEAWTMPFAFCTREKLPWCEFAESAEDGPTTKFCQELAKKYNMVIVSPILE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 169 RDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSIN 248
Cdd:cd07587 161 RDEEHGDTIWNTAVVISNSGNVLGKSRKNHIPRVGDFNESTYYMEGNTGHPVFETQFGKIAVNICYGRHHPLNWLMYGLN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 249 GAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAAPDGSRTP 328
Cdd:cd07587 241 GAEIVFNPSATVGALSEPMWPIEARNAAIANSYFTVGINRVGTEVFPNEFTSGDGKPAHKDFGHFYGSSYVAAPDGSRTP 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 68565067 329 GLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAE 371
Cdd:cd07587 321 GLSRTRDGLLVAELDLNLCRQVKDKWGFRMTARYEMYADFLAK 363
 
Name Accession Description Interval E-value
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
9-371 0e+00

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This subgroup includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. 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 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143611 [Multi-domain]  Cd Length: 363  Bit Score: 790.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   9 LEQCLEKHLPPDDLAQVKRILYGKQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRIPLPTSAP 88
Cdd:cd07587   1 LEDLLEKHLPPEELKEVKRILYGEEVKPLELPESALDLAKENDFELKGYKFEAAPEQTRPPRIVRVGLIQNKIVLPTTAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  89 VAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILE 168
Cdd:cd07587  81 IAEQREAIHDRIKKIIEAAAMAGVNIICFQEAWTMPFAFCTREKLPWCEFAESAEDGPTTKFCQELAKKYNMVIVSPILE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 169 RDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSIN 248
Cdd:cd07587 161 RDEEHGDTIWNTAVVISNSGNVLGKSRKNHIPRVGDFNESTYYMEGNTGHPVFETQFGKIAVNICYGRHHPLNWLMYGLN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 249 GAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAAPDGSRTP 328
Cdd:cd07587 241 GAEIVFNPSATVGALSEPMWPIEARNAAIANSYFTVGINRVGTEVFPNEFTSGDGKPAHKDFGHFYGSSYVAAPDGSRTP 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 68565067 329 GLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAE 371
Cdd:cd07587 321 GLSRTRDGLLVAELDLNLCRQVKDKWGFRMTARYEMYADFLAK 363
PLN00202 PLN00202
beta-ureidopropionase
6-392 0e+00

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 591.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067    6 WQSLEQCLEKHLPPDDLAQVKRILYG----KQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRI 81
Cdd:PLN00202  17 YESLHRLLSANLPPELFQEVSRLLLGlncgRPVEMIALPEAAKALSKAHDFDLQAFRFTADKEQLRAPRVVRVGLIQNSI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   82 PLPTSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLpWTEFAESAeDGLTTRFCQKLAKKHNMV 161
Cdd:PLN00202  97 ALPTTAPFADQKRAIMDKVKPMIDAAGAAGVNILCLQEAWTMPFAFCTREKR-WCEFAEPV-DGESTKFLQELARKYNMV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  162 VVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLN 241
Cdd:PLN00202 175 IVSPILERDVNHGETLWNTAVVIGNNGNIIGKHRKNHIPRVGDFNESTYYMEGNTGHPVFETAFGKIAVNICYGRHHPLN 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  242 WLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAA 321
Cdd:PLN00202 255 WLAFGLNGAEIVFNPSATVGDLSEPMWPIEARNAAIANSYFVGSINRVGTEVFPNPFTSGDGKPQHKDFGHFYGSSHFSA 334
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68565067  322 PDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAEAVKPNYSPNIVKEDLVLAPSS 392
Cdd:PLN00202 335 PDASCTPSLSRYKDGLLISDMDLNLCRQLKDKWGFRMTARYEMYADFFAEYLKPDFKPQVISDPLLHKKSL 405
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
73-350 7.68e-66

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.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 209.90  E-value: 7.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067    73 RVGLVQNRIPlptsapvAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFctreklpWTEFAESAE--DGLTTRF 150
Cdd:pfam00795   1 RVALVQLPQG-------FWDLEANLQKALELIEEAARYGADLIVLPELFITGYPC-------WAHFLEAAEvgDGETLAG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   151 CQKLAKKHNMVVVSPILERdREHGGVLWNTAVVISNSGLVMGKTRKNH---IPRVGDFNESTYYMEGNlGHPVFQTQFGR 227
Cdd:pfam00795  67 LAALARKNGIAIVIGLIER-WLTGGRLYNTAVLLDPDGKLVGKYRKLHlfpEPRPPGFRERVLFEPGD-GGTVFDTPLGK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   228 IAVNICYGRHHPLNWLMYSINGAEIIFNPSA---TIGELSESLWPIEARNAAIANHCFTCALNRVGqehfpneftsgdgk 304
Cdd:pfam00795 145 IGAAICYEIRFPELLRALALKGAEILINPSArapFPGSLGPPQWLLLARARALENGCFVIAANQVG-------------- 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 68565067   305 kAHHDLGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQI 350
Cdd:pfam00795 211 -GEEDAPWPYGHSMIIDPDGRILAGAGEWEEGVLIADIDLALVRAW 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
72-365 1.88e-50

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 170.43  E-value: 1.88e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQnriplptSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFctrEKLPWTEFAESAeDGLTTRFC 151
Cdd:COG0388   2 MRIALAQ-------LNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPP---EDDDLLELAEPL-DGPALAAL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 152 QKLAKKHNMVVVSPILERDreHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGhPVFQTQFGRIAVN 231
Cdd:COG0388  71 AELARELGIAVVVGLPERD--EGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFDEKRYFTPGDEL-VVFDTDGGRIGVL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 232 ICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGqehfpneftsgdgkkaHHDLG 311
Cdd:COG0388 148 ICYDLWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAANQVG----------------GEDGL 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 68565067 312 YFYGSSYVAAPDGSRTpGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMY 365
Cdd:COG0388 212 VFDGGSMIVDPDGEVL-AEAGDEEGLLVADIDLDRLREARRRFPVLRDRRPDLY 264
 
Name Accession Description Interval E-value
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
9-371 0e+00

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This subgroup includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. 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 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143611 [Multi-domain]  Cd Length: 363  Bit Score: 790.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   9 LEQCLEKHLPPDDLAQVKRILYGKQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRIPLPTSAP 88
Cdd:cd07587   1 LEDLLEKHLPPEELKEVKRILYGEEVKPLELPESALDLAKENDFELKGYKFEAAPEQTRPPRIVRVGLIQNKIVLPTTAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  89 VAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILE 168
Cdd:cd07587  81 IAEQREAIHDRIKKIIEAAAMAGVNIICFQEAWTMPFAFCTREKLPWCEFAESAEDGPTTKFCQELAKKYNMVIVSPILE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 169 RDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSIN 248
Cdd:cd07587 161 RDEEHGDTIWNTAVVISNSGNVLGKSRKNHIPRVGDFNESTYYMEGNTGHPVFETQFGKIAVNICYGRHHPLNWLMYGLN 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 249 GAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAAPDGSRTP 328
Cdd:cd07587 241 GAEIVFNPSATVGALSEPMWPIEARNAAIANSYFTVGINRVGTEVFPNEFTSGDGKPAHKDFGHFYGSSYVAAPDGSRTP 320
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 68565067 329 GLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAE 371
Cdd:cd07587 321 GLSRTRDGLLVAELDLNLCRQVKDKWGFRMTARYEMYADFLAK 363
PLN00202 PLN00202
beta-ureidopropionase
6-392 0e+00

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 591.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067    6 WQSLEQCLEKHLPPDDLAQVKRILYG----KQTRNLDLPREALKAASERNFELKGYAFGAAKEQQRCPQIVRVGLVQNRI 81
Cdd:PLN00202  17 YESLHRLLSANLPPELFQEVSRLLLGlncgRPVEMIALPEAAKALSKAHDFDLQAFRFTADKEQLRAPRVVRVGLIQNSI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   82 PLPTSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLpWTEFAESAeDGLTTRFCQKLAKKHNMV 161
Cdd:PLN00202  97 ALPTTAPFADQKRAIMDKVKPMIDAAGAAGVNILCLQEAWTMPFAFCTREKR-WCEFAEPV-DGESTKFLQELARKYNMV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  162 VVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLN 241
Cdd:PLN00202 175 IVSPILERDVNHGETLWNTAVVIGNNGNIIGKHRKNHIPRVGDFNESTYYMEGNTGHPVFETAFGKIAVNICYGRHHPLN 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  242 WLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSGDGKKAHHDLGYFYGSSYVAA 321
Cdd:PLN00202 255 WLAFGLNGAEIVFNPSATVGDLSEPMWPIEARNAAIANSYFVGSINRVGTEVFPNPFTSGDGKPQHKDFGHFYGSSHFSA 334
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68565067  322 PDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYARELAEAVKPNYSPNIVKEDLVLAPSS 392
Cdd:PLN00202 335 PDASCTPSLSRYKDGLLISDMDLNLCRQLKDKWGFRMTARYEMYADFFAEYLKPDFKPQVISDPLLHKKSL 405
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
70-366 5.61e-132

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family 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 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 379.92  E-value: 5.61e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  70 QIVRVGLVQNRIPLPTSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPfAFCTREKLPWTEFAESAEDGLTTR 149
Cdd:cd07568   2 RIVRVGLIQASNVIPTDAPIEKQKEAMIQKHVTMIREAAEAGAQIVCLQEIFYGP-YFCAEQDTKWYEFAEEIPNGPTTK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 150 FCQKLAKKHNMVVVSPILERdrEHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIA 229
Cdd:cd07568  81 RFAALAKEYNMVLILPIYEK--EQGGTLYNTAAVIDADGTYLGKYRKNHIPHVGGFWEKFYFRPGNLGYPVFDTAFGKIG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 230 VNICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQEHFPNeftsgdgkkahhd 309
Cdd:cd07568 159 VYICYDRHFPEGWRALGLNGAEIVFNPSATVAGLSEYLWKLEQPAAAVANGYFVGAINRVGTEAPWN------------- 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 68565067 310 LGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMYA 366
Cdd:cd07568 226 IGEFYGSSYFVDPRGQFVASASRDKDELLVAELDLDLIREVRDTWQFYRDRRPETYG 282
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
73-350 7.68e-66

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.


Pssm-ID: 425873 [Multi-domain]  Cd Length: 257  Bit Score: 209.90  E-value: 7.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067    73 RVGLVQNRIPlptsapvAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFctreklpWTEFAESAE--DGLTTRF 150
Cdd:pfam00795   1 RVALVQLPQG-------FWDLEANLQKALELIEEAARYGADLIVLPELFITGYPC-------WAHFLEAAEvgDGETLAG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   151 CQKLAKKHNMVVVSPILERdREHGGVLWNTAVVISNSGLVMGKTRKNH---IPRVGDFNESTYYMEGNlGHPVFQTQFGR 227
Cdd:pfam00795  67 LAALARKNGIAIVIGLIER-WLTGGRLYNTAVLLDPDGKLVGKYRKLHlfpEPRPPGFRERVLFEPGD-GGTVFDTPLGK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   228 IAVNICYGRHHPLNWLMYSINGAEIIFNPSA---TIGELSESLWPIEARNAAIANHCFTCALNRVGqehfpneftsgdgk 304
Cdd:pfam00795 145 IGAAICYEIRFPELLRALALKGAEILINPSArapFPGSLGPPQWLLLARARALENGCFVIAANQVG-------------- 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 68565067   305 kAHHDLGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQI 350
Cdd:pfam00795 211 -GEEDAPWPYGHSMIIDPDGRILAGAGEWEEGVLIADIDLALVRAW 255
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
72-365 1.86e-55

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.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 183.92  E-value: 1.86e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQNRIplptSAPVAEQVSalhKSIEEIAEvAAMCGVNIICFQEAWNMPFaFCTREKLPWTEFAESAEDGLTTRFC 151
Cdd:cd07573   1 VTVALVQMAC----SEDPEANLA---KAEELVRE-AAAQGAQIVCLQELFETPY-FCQEEDEDYFDLAEPPIPGPTTARF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 152 QKLAKKHNMVVVSPILERDREhgGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVN 231
Cdd:cd07573  72 QALAKELGVVIPVSLFEKRGN--GLYYNSAVVIDADGSLLGVYRKMHIPDDPGYYEKFYFTPGDTGFKVFDTRYGRIGVL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 232 ICYGRHHPLNWLMYSINGAEIIFNPSAtIGEL---------SESLWPIEARNAAIANHCFTCALNRVGQEHFPNEFTSgd 302
Cdd:cd07573 150 ICWDQWFPEAARLMALQGAEILFYPTA-IGSEpqeppegldQRDAWQRVQRGHAIANGVPVAAVNRVGVEGDPGSGIT-- 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68565067 303 gkkahhdlgyFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMY 365
Cdd:cd07573 227 ----------FYGSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWPFFRDRRPDLY 279
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
74-356 1.38e-53

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.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 178.29  E-value: 1.38e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  74 VGLVQnriplptSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREklpWTEFAESAEDGLTTRFCQK 153
Cdd:cd07197   1 IAAVQ-------LAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAK---EDLDLAEELDGPTLEALAE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 154 LAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGLVMGKTRKNHIPrvgDFNESTYYMEGNlGHPVFQTQFGRIAVNIC 233
Cdd:cd07197  71 LAKELGIYIVAGIAEKD---GDKLYNTAVVIDPDGEIIGKYRKIHLF---DFGERRYFSPGD-EFPVFDTPGGKIGLLIC 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 234 YGRHHPLNWLMYSINGAEIIFNPSATIGELSESlWPIEARNAAIANHCFTCALNRVGQEHFpneftsgdgkkahhdlGYF 313
Cdd:cd07197 144 YDLRFPELARELALKGADIILVPAAWPTARREH-WELLLRARAIENGVYVVAANRVGEEGG----------------LEF 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 68565067 314 YGSSYVAAPDGSRTPGLSRNqDGLLVTELNLNLCQQINDFWTF 356
Cdd:cd07197 207 AGGSMIVDPDGEVLAEASEE-EGILVAELDLDELREARKRWSY 248
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
72-365 1.88e-50

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 170.43  E-value: 1.88e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQnriplptSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFctrEKLPWTEFAESAeDGLTTRFC 151
Cdd:COG0388   2 MRIALAQ-------LNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPP---EDDDLLELAEPL-DGPALAAL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 152 QKLAKKHNMVVVSPILERDreHGGVLWNTAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGhPVFQTQFGRIAVN 231
Cdd:COG0388  71 AELARELGIAVVVGLPERD--EGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFDEKRYFTPGDEL-VVFDTDGGRIGVL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 232 ICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGqehfpneftsgdgkkaHHDLG 311
Cdd:COG0388 148 ICYDLWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAANQVG----------------GEDGL 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 68565067 312 YFYGSSYVAAPDGSRTpGLSRNQDGLLVTELNLNLCQQINDFWTFKMTGRLEMY 365
Cdd:COG0388 212 VFDGGSMIVDPDGEVL-AEAGDEEGLLVADIDLDRLREARRRFPVLRDRRPDLY 264
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
96-345 1.09e-31

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.


Pssm-ID: 143608  Cd Length: 258  Bit Score: 120.55  E-value: 1.09e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  96 LHKSIEEIAEVAAMcGVNIICFQEAWNMPFAFcTREKLPWTEFAESAeDGLTTRFCQKLAKKHNMVVVSPILERDrEHGG 175
Cdd:cd07584  18 LKKAAELCKEAAAE-GADLICFPELATTGYRP-DLLGPKLWELSEPI-DGPTVRLFSELAKELGVYIVCGFVEKG-GVPG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 176 VLWNTAVVISNSGLVMGKTRKNHIprVGDfnESTYYMEGNLgHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFN 255
Cdd:cd07584  94 KVYNSAVVIDPEGESLGVYRKIHL--WGL--EKQYFREGEQ-YPVFDTPFGKIGVMICYDMGFPEVARILTLKGAEVIFC 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 256 PSATiGELSESLWPIEARNAAIANHCFTCALNRVGQEhfpneftsgdgkkahHDLGYFyGSSYVAAPDGSRTPGLSRNQD 335
Cdd:cd07584 169 PSAW-REQDADIWDINLPARALENTVFVAAVNRVGNE---------------GDLVLF-GKSKILNPRGQVLAEASEEAE 231
                       250
                ....*....|
gi 68565067 336 GLLVTELNLN 345
Cdd:cd07584 232 EILYAEIDLD 241
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
73-353 1.33e-29

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. 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 was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 115.09  E-value: 1.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  73 RVGLVQNRiplPTSAPVAEQVSALHKSIEEIAevaamcgVNIICFQEAWNMPFAFCTREKLpwTEFAESAEDGLTTRFCQ 152
Cdd:cd07577   1 KVGYVQFN---PKFGEVEKNLKKVESLIKGVE-------ADLIVLPELFNTGYAFTSKEEV--ASLAESIPDGPTTRFLQ 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 153 KLAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGlVMGKTRKNHIprvgdFNESTYYME-GNLGHPVFQTQFGRIAVN 231
Cdd:cd07577  69 ELARETGAYIVAGLPERD---GDKFYNSAVVVGPEG-YIGIYRKTHL-----FYEEKLFFEpGDTGFRVFDIGDIRIGVM 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 232 ICYGRHHPLNWLMYSINGAEIIFNPSatigELSESLWP--IEARnaAIANHCFTCALNRVGQEHFPNEFTSgdgkkahhd 309
Cdd:cd07577 140 ICFDWYFPEAARTLALKGADIIAHPA----NLVLPYCPkaMPIR--ALENRVFTITANRIGTEERGGETLR--------- 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 68565067 310 lgyFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLCQQ--INDF 353
Cdd:cd07577 205 ---FIGKSQITSPKGEVLARAPEDGEEVLVAEIDPRLARDkrINEE 247
PLN02747 PLN02747
N-carbamolyputrescine amidase
101-365 1.11e-27

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 110.63  E-value: 1.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  101 EEIAEVAAMCGVNIICFQEAWNMPFaFCTREKLPWTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILErdrEHGGVLWNT 180
Cdd:PLN02747  28 ERLVREAHAKGANIILIQELFEGYY-FCQAQREDFFQRAKPYEGHPTIARMQKLAKELGVVIPVSFFE---EANNAHYNS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  181 AVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSAtI 260
Cdd:PLN02747 104 IAIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFDTKFAKIGVAICWDQWFPEAARAMVLQGAEVLLYPTA-I 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  261 GEL-------SESLWPIEARNAAIANHCFTCALNRVGQEHFPNEftsgDGKKAHHdlgyFYGSSYVAAPDGSRTPGLSRN 333
Cdd:PLN02747 183 GSEpqdpgldSRDHWKRVMQGHAGANLVPLVASNRIGTEILETE----HGPSKIT----FYGGSFIAGPTGEIVAEADDK 254
                        250       260       270
                 ....*....|....*....|....*....|..
gi 68565067  334 QDGLLVTELNLNLCQQINDFWTFKMTGRLEMY 365
Cdd:PLN02747 255 AEAVLVAEFDLDQIKSKRASWGVFRDRRPDLY 286
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
96-344 1.31e-25

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.


Pssm-ID: 143604  Cd Length: 268  Bit Score: 104.35  E-value: 1.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  96 LHKSIEEIAEvAAMCGVNIICFQEAWNMPFAFCTREKLpwTEFAESAEDGLTTRFCQKLAKKHNMVVVSPILERDrehGG 175
Cdd:cd07580  18 LARSIELIRE-AADAGANLVVLPELANTGYVFESRDEA--FALAEEVPDGASTRAWAELAAELGLYIVAGFAERD---GD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 176 VLWNTAVVISNSGlVMGKTRKNHIPRvgdfNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFN 255
Cdd:cd07580  92 RLYNSAVLVGPDG-VIGTYRKAHLWN----EEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWFPETFRLLALQGADIVCV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 256 PS--ATIGELSESLWPIE---ARNAAIANHCFTCALNRVGQEHfpneftsGDGkkahhdlgyFYGSSYVAAPDG-SRTPG 329
Cdd:cd07580 167 PTnwVPMPRPPEGGPPMAnilAMAAAHSNGLFIACADRVGTER-------GQP---------FIGQSLIVGPDGwPLAGP 230
                       250
                ....*....|....*
gi 68565067 330 LSRNQDGLLVTELNL 344
Cdd:cd07580 231 ASGDEEEILLADIDL 245
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
73-346 8.75e-25

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.


Pssm-ID: 143607  Cd Length: 253  Bit Score: 101.85  E-value: 8.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  73 RVGLVQNRIplptsapVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAfctreklpWTEFAESAE--DGLTTRF 150
Cdd:cd07583   1 KIALIQLDI-------VWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGYF--------LDDLYELADedGGETVSF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 151 CQKLAKKHNMVVV--SpILERDREHggvLWNTAVVISNSGLVMGKTRKNHipRVGDFNESTYYMEGNlGHPVFQTQFGRI 228
Cdd:cd07583  66 LSELAKKHGVNIVagS-VAEKEGGK---LYNTAYVIDPDGELIATYRKIH--LFGLMGEDKYLTAGD-ELEVFELDGGKV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 229 AVNICY-------GRHHPLnwlmysiNGAEIIFNPSAtigelseslWP---IE-------ARnaAIANHCFTCALNRVGq 291
Cdd:cd07583 139 GLFICYdlrfpelFRKLAL-------EGAEILFVPAE---------WPaarIEhwrtllrAR--AIENQAFVVACNRVG- 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 68565067 292 ehfpnefTSGDGKkahhdlgyFYGSSYVAAPDGSRTPGLSrNQDGLLVTELNLNL 346
Cdd:cd07583 200 -------TDGGNE--------FGGHSMVIDPWGEVLAEAG-EEEEILTAEIDLEE 238
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
73-350 4.89e-20

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.


Pssm-ID: 143596  Cd Length: 265  Bit Score: 88.64  E-value: 4.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  73 RVGLVQnripLPTSAPVAEQVSALHKSIEEiaevAAMCGVNIICFQEAWNMPFAfcTREKLpwTEFAESAEDGLTTRFCQ 152
Cdd:cd07572   1 RVALIQ----MTSTADKEANLARAKELIEE----AAAQGAKLVVLPECFNYPGG--TDAFK--LALAEEEGDGPTLQALS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 153 KLAKKHNMVVVSP-ILERDREHGGVlWNTAVVISNSGLVMGKTRKNH-----IPRVGDFNESTYYMEGNlGHPVFQTQFG 226
Cdd:cd07572  69 ELAKEHGIWLVGGsIPERDDDDGKV-YNTSLVFDPDGELVARYRKIHlfdvdVPGGISYRESDTLTPGD-EVVVVDTPFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 227 RIAVNICYG-RHHPLnWLMYSINGAEIIFNPSA---TIGELSeslWPIEARNAAIANHCFTCALNRVGqehfpneftsgd 302
Cdd:cd07572 147 KIGLGICYDlRFPEL-ARALARQGADILTVPAAftmTTGPAH---WELLLRARAIENQCYVVAAAQAG------------ 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 68565067 303 gkkaHHDLGYF-YGSSYVAAPDG---SRTPglsrNQDGLLVTELNLNLCQQI 350
Cdd:cd07572 211 ----DHEAGREtYGHSMIVDPWGevlAEAG----EGEGVVVAEIDLDRLEEV 254
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
72-347 5.05e-20

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of 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 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 89.47  E-value: 5.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQnriplptSAPVAEQVSA-LHKSIEEIAEVAAMcGVNIICFQEAWnMP----FAFC-----TREklPWTEFAES 141
Cdd:cd07564   1 VKVAAVQ-------AAPVFLDLAAtVEKACRLIEEAAAN-GAQLVVFPEAF-IPgypyWIWFgapaeGRE--LFARYYEN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 142 A--EDGLTTRFCQKLAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGLVMGKTRK---NHIprvgdfnESTYYMEGNl 216
Cdd:cd07564  70 SveVDGPELERLAEAARENGIYVVLGVSERD---GGTLYNTQLLIDPDGELLGKHRKlkpTHA-------ERLVWGQGD- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 217 GH--PVFQTQFGRIAVNICYGRHHPLN-WLMYSINgaEIIF---NPSATIGELSESLWPIEARNAAIANHCFT-CALNRV 289
Cdd:cd07564 139 GSglRVVDTPIGRLGALICWENYMPLArYALYAQG--EQIHvapWPDFSPYYLSREAWLAASRHYALEGRCFVlSACQVV 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 68565067 290 GQEHFPNEFTSGDGKKAHHDLGyfYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNLC 347
Cdd:cd07564 217 TEEDIPADCEDDEEADPLEVLG--GGGSAIVGPDGEVLAGPLPDEEGILYADIDLDDI 272
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
99-295 2.87e-19

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.


Pssm-ID: 143609  Cd Length: 261  Bit Score: 86.60  E-value: 2.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  99 SIEEIAEVAAMCGVNIICFQEAwNMPfAFCTREKLPwteFAESAEDGLTTRFCQKLAKKHNMVVVSPILERDrehGGVLW 178
Cdd:cd07585  20 VIARWTRKAAAQGAELVCFPEM-CIT-GYTHVRALS---REAEVPDGPSTQALSDLARRYGLTILAGLIEKA---GDRPY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 179 NTAVVISNSGLVmGKTRKNHIPRVgdfnESTYYMEGNlGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSA 258
Cdd:cd07585  92 NTYLVCLPDGLV-HRYRKLHLFRR----EHPYIAAGD-EYPVFATPGVRFGILICYDNHFPENVRATALLGAEILFAPHA 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 68565067 259 TIGELSES---LWPIEARNAAIANHCFTCALNRVG---QEHFP 295
Cdd:cd07585 166 TPGTTSPKgreWWMRWLPARAYDNGVFVAACNGVGrdgGEVFP 208
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
102-361 9.01e-16

First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the first of those two domains. 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.


Pssm-ID: 143602  Cd Length: 258  Bit Score: 76.42  E-value: 9.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 102 EIAEVAAMCGVNIICFQEAWNMPFAFCTREKLpwTEFAESAEDGLTTRFCQkLAKKHNMVVVSPILERDrEHGGVLWNTA 181
Cdd:cd07578  24 ALCEEAARAGARLIVTPEMATTGYCWYDRAEI--APFVEPIPGPTTARFAE-LAREHDCYIVVGLPEVD-SRSGIYYNSA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 182 VVISNSGLVmGKTRKNHiPRVGdfnESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIG 261
Cdd:cd07578 100 VLIGPSGVI-GRHRKTH-PYIS---EPKWAADGDLGHQVFDTEIGRIALLICMDIHFFETARLLALGGADVICHISNWLA 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 262 ELSESLWPIearNAAIANHCFTCALNRVGQEHFPNeftsgdgkkahhdlgyFYGSSYVAAPDGSRTPGLSrNQDGLLVTE 341
Cdd:cd07578 175 ERTPAPYWI---NRAFENGCYLIESNRWGLERGVQ----------------FSGGSCIIEPDGTIQASID-SGDGVALGE 234
                       250       260
                ....*....|....*....|
gi 68565067 342 LNLNLCQQINDFWTFKMTGR 361
Cdd:cd07578 235 IDLDRARHRQFPGELVFTAR 254
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
72-344 3.34e-15

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.


Pssm-ID: 143598  Cd Length: 280  Bit Score: 75.32  E-value: 3.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQNRIPLPTSAPvaeqvsALHKSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLTTRFC 151
Cdd:cd07574   1 VRVAAAQYPLRRYASFE------EFAAKVEYWVAEAAGYGADLLVFPEYFTMELLSLLPEAIDGLDEAIRALAALTPDYV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 152 ---QKLAKKHNMVVVS---PILERDRehggvLWNTAVVISNSGLVmGKTRKNHIPRvgdFNESTYYMEGnlGHP--VFQT 223
Cdd:cd07574  75 alfSELARKYGINIIAgsmPVREDGR-----LYNRAYLFGPDGTI-GHQDKLHMTP---FEREEWGISG--GDKlkVFDT 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 224 QFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSAT----------IGelseslwpIEARnaAIANHCFTCALNRVGQ-E 292
Cdd:cd07574 144 DLGKIGILICYDSEFPELARALAEAGADLLLVPSCTdtragywrvrIG--------AQAR--ALENQCYVVQSGTVGNaP 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68565067 293 HFPNEFTsgdgkkahhdlgyFYGSSYVAAP-------DG--SRTPGlsrNQDGLLVTELNL 344
Cdd:cd07574 214 WSPAVDV-------------NYGQAAVYTPcdfgfpeDGilAEGEP---NTEGWLIADLDL 258
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
152-325 1.76e-14

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.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 73.09  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 152 QKLAKKH-NMVVVSPILERDREhgGVLWNTAVVISNsGLVMGKTRKNHIPRVGDFNESTYYMEGN-LGHpvFQTQFGRIA 229
Cdd:cd07586  65 QALAEASgGICVVFGFVEEGRD--GRFYNSAAYLED-GRVVHVHRKVYLPTYGLFEEGRYFAPGShLRA--FDTRFGRAG 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 230 VNICYGRHHP-LNWLMySINGAEIIFNPSATIGEL------SESLWPIEARNAAIANHCFTCALNRVGQEhfpneftsgd 302
Cdd:cd07586 140 VLICEDAWHPsLPYLL-ALDGADVIFIPANSPARGvggdfdNEENWETLLKFYAMMNGVYVVFANRVGVE---------- 208
                       170       180
                ....*....|....*....|...
gi 68565067 303 gkkahhDLGYFYGSSYVAAPDGS 325
Cdd:cd07586 209 ------DGVYFWGGSRVVDPDGE 225
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
73-325 5.57e-14

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.


Pssm-ID: 143600  Cd Length: 254  Bit Score: 71.07  E-value: 5.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  73 RVGLVQnriplptSAPVAEQVSALHKSIEEIAEVAAMCGVNIICFQEAWnmPFAFCTREKLPWteFAESAEDGLTTRFCQ 152
Cdd:cd07576   1 RLALYQ-------GPARDGDVAANLARLDEAAARAAAAGADLLVFPELF--LTGYNIGDAVAR--LAEPADGPALQALRA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 153 kLAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGLVMGKTRKNHIPrvGDFnESTYYMEGNlGHPVFQTQFGRIAVNI 232
Cdd:cd07576  70 -IARRHGIAIVVGYPERA---GGAVYNAAVLIDEDGTVLANYRKTHLF--GDS-ERAAFTPGD-RFPVVELRGLRVGLLI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 233 CYGRHHPLNWLMYSINGAEIIFNPSATI---GELSESLWPieARnaAIANHCFTCALNRVGQEhfpNEFTsgdgkkahhd 309
Cdd:cd07576 142 CYDVEFPELVRALALAGADLVLVPTALMepyGFVARTLVP--AR--AFENQIFVAYANRCGAE---DGLT---------- 204
                       250
                ....*....|....*.
gi 68565067 310 lgyFYGSSYVAAPDGS 325
Cdd:cd07576 205 ---YVGLSSIAGPDGT 217
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
72-346 1.33e-13

aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of short-chain aliphatic amides to form ammonia and the corresponding organic acid. This group includes Pseudomonas aeruginosa (Pa) AmiE, the amidase from Geobacillus pallidus RAPc8 (RAPc8 amidase), and Helicobacter pylori (Hp) AmiE and AmiF. PaAimE and HpAmiE hydrolyze various very short aliphatic amides, including propionamide, acetamide and acrylamide. HpAmiF is a formamidase which specifically hydrolyzes formamide. These proteins 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 2. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. HpAmiE , HpAmiF, and RAPc8 amidase, and PaAimE appear to be homohexameric enzymes, trimer of dimers.


Pssm-ID: 143589  Cd Length: 291  Bit Score: 70.78  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  72 VRVGLVQNRIP-LPTSAPVAEQVSALHKSIEEIAevAAMCGVNIICFQEAWNMPFAFCTREklpWTEFAESAEDGLTTRF 150
Cdd:cd07565   1 VGVAVVQYKVPvLHTKEEVLENAERIADMVEGTK--RGLPGMDLIVFPEYSTQGLMYDKWT---MDETACTVPGPETDIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 151 CQKlAKKHNMVVVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNH--IPRVGdfnestyYMEGNLGHPVFQTQFG-R 227
Cdd:cd07565  76 AEA-CKEAKVWGVFSIMERNPDHGKNPYNTAIIIDDQGEIVLKYRKLHpwVPIEP-------WYPGDLGTPVCEGPKGsK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 228 IAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESlWPIEARNAAIANHCFTCALNRVGqehFPNEFtsgdgkkah 307
Cdd:cd07565 148 IALIICHDGMYPEIARECAYKGAELIIRIQGYMYPAKDQ-WIITNKANAWCNLMYTASVNLAG---FDGVF--------- 214
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 68565067 308 hdlgYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLNL 346
Cdd:cd07565 215 ----SYFGESMIVNFDGRTLGEGGREPDEIVTAELSPSL 249
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
100-344 1.52e-12

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.


Pssm-ID: 143605  Cd Length: 255  Bit Score: 66.83  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 100 IEEIAEVAAMCGVNIICFQEAwnMPFAFcTREKLPWTEFAESaEDGLTTRFCQKLAKKHNMVVVSPILERDreHGGVLWN 179
Cdd:cd07581  19 VRRLLAEAAAAGADLVVFPEY--TMARF-GDGLDDYARVAEP-LDGPFVSALARLARELGITVVAGMFEPA--GDGRVYN 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 180 TAVVISNSGLVMGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFG-RIAVNICYGRHHPLNWLMYSINGAEIIFNPSA 258
Cdd:cd07581  93 TLVVVGPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVVFVVGGvKVGLATCYDLRFPELARALALAGADVIVVPAA 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 259 TI-GELSESLWPIEARNAAIANHCFTCALNRVGqehfpneftsgdgkkahhdlGYFYGSSYVAAPDGSRTPGLsRNQDGL 337
Cdd:cd07581 173 WVaGPGKEEHWETLLRARALENTVYVAAAGQAG--------------------PRGIGRSMVVDPLGVVLADL-GEREGL 231

                ....*..
gi 68565067 338 LVTELNL 344
Cdd:cd07581 232 LVADIDP 238
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
144-321 1.94e-12

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.


Pssm-ID: 143606  Cd Length: 294  Bit Score: 67.37  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 144 DGLTTRFCQKLAKKHNMVVVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNHIPrvgdfnestYYMEGNLGH----- 218
Cdd:cd07582  75 PGPETEALGEKAKELNVYIAANAYERDPDFPGLYFNTAFIIDPSGEIILRYRKMNSL---------AAEGSPSPHdvwde 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 219 -------------PVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWPIEARNAAIANHCFTCA 285
Cdd:cd07582 146 yievygygldalfPVADTEIGNLGCLACEEGLYPEVARGLAMNGAEVLLRSSSEVPSVELDPWEIANRARALENLAYVVS 225
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 68565067 286 LNRVGQEHFPNEFTSGDGKK----------AHHdlGYFYGSSYVAA 321
Cdd:cd07582 226 ANSGGIYGSPYPADSFGGGSmivdykgrvlAEA--GYGPGSMVAGA 269
PLN02798 PLN02798
nitrilase
101-346 8.09e-12

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 65.15  E-value: 8.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  101 EEIAEVAAMCGVNIICFQEAwnmpFAFCTREKLPWTEFAESAEDGLTTRFCQkLAKKHNM-VVVSPILERDREHGGvLWN 179
Cdd:PLN02798  32 SRLAKEAAAAGAKLLFLPEC----FSFIGDKDGESLAIAEPLDGPIMQRYRS-LARESGLwLSLGGFQEKGPDDSH-LYN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  180 TAVVISNSGLVMGKTRKNHIPRVgDFNESTYYMEGNLGHP-----VFQTQFGRIAVNICYGRHHP-----LNWLMysinG 249
Cdd:PLN02798 106 THVLIDDSGEIRSSYRKIHLFDV-DVPGGPVLKESSFTAPgktivAVDSPVGRLGLTVCYDLRFPelyqqLRFEH----G 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  250 AEIIFNPSATIGELSESLWPIEARNAAIANHCFTCALNRVGQehfpneftsgdgkkaHHDLGYFYGSSYVAAPDGS---R 326
Cdd:PLN02798 181 AQVLLVPSAFTKPTGEAHWEVLLRARAIETQCYVIAAAQAGK---------------HNEKRESYGHALIIDPWGTvvaR 245
                        250       260
                 ....*....|....*....|
gi 68565067  327 TPglSRNQDGLLVTELNLNL 346
Cdd:PLN02798 246 LP--DRLSTGIAVADIDLSL 263
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
171-367 1.52e-10

N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. 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 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.


Pssm-ID: 143593  Cd Length: 302  Bit Score: 61.56  E-value: 1.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 171 REHGGVL--WNTAVVISNSGLVMGKTRKNHIPRVGDFN--------ESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPL 240
Cdd:cd07569  99 TEDGGVKrrFNTSILVDKSGKIVGKYRKVHLPGHKEPEpyrpfqhlEKRYFEPGDLGFPVFRVPGGIMGMCICNDRRWPE 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 241 NWLMYSINGAEII--------FNPSAT-IGELSE--SLWPIEArnAAIANHCFTCALNRVGQEhfpneftsgDGkkahHD 309
Cdd:cd07569 179 TWRVMGLQGVELVllgyntptHNPPAPeHDHLRLfhNLLSMQA--GAYQNGTWVVAAAKAGME---------DG----CD 243
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68565067 310 LgyfYGSSYVAAPDG---SRTPGLsrnQDGLLVTELNLNLCQQI-NDFWTFKMTGRLEMYAR 367
Cdd:cd07569 244 L---IGGSCIVAPTGeivAQATTL---EDEVIVADCDLDLCREGrETVFNFARHRRPEHYGL 299
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
138-325 2.28e-09

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain 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 classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 57.48  E-value: 2.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 138 FAESAEDGLTtRFCQKLAKKhNMVVV--SPIlerdrEHGGVLWNTAVVISNsGLVMGKTRKNHIPRVGDFNESTYYMEGN 215
Cdd:cd07570  57 FLEAAEEALE-ELAAATADL-DIAVVvgLPL-----RHDGKLYNAAAVLQN-GKILGVVPKQLLPNYGVFDEKRYFTPGD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 216 LGHPVFQTQFgRIAVNIC------YGrhhPLNWLmySINGAEIIFNPSA---TIG--ELSESLwpieARNAAIANHCFTC 284
Cdd:cd07570 129 KPDVLFFKGL-RIGVEICedlwvpDP---PSAEL--ALAGADLILNLSAspfHLGkqDYRREL----VSSRSARTGLPYV 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 68565067 285 ALNRVGqehfpneftSGDgkkahhDLgYFYGSSYVAAPDGS 325
Cdd:cd07570 199 YVNQVG---------GQD------DL-VFDGGSFIADNDGE 223
PLN02504 PLN02504
nitrilase
153-345 1.02e-07

nitrilase


Pssm-ID: 178120  Cd Length: 346  Bit Score: 53.23  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  153 KLAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGLVMGKTRK---NHIPRV--GDFNESTYymegnlghPVFQTQFGR 227
Cdd:PLN02504 112 AMAGKYKVYLVMGVIERD---GYTLYCTVLFFDPQGQYLGKHRKlmpTALERLiwGFGDGSTI--------PVYDTPIGK 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  228 IAVNICYGRHHPL-NWLMYSiNGAEIIFNPSATIGElsesLWPIEARNAAIANHCFTCALNRVGQEH---FPNEFT-SGD 302
Cdd:PLN02504 181 IGAVICWENRMPLlRTAMYA-KGIEIYCAPTADSRE----TWQASMRHIALEGGCFVLSANQFCRRKdypPPPEYLfSGT 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 68565067  303 GKKAHHDLGYFYGSSYVAAPDGSRTPGLSRNQDGLLVTELNLN 345
Cdd:PLN02504 256 EEDLTPDSIVCAGGSVIISPSGTVLAGPNYEGEGLITADLDLG 298
PRK13981 PRK13981
NAD synthetase; Provisional
138-290 1.44e-05

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 47.07  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  138 FAESAEDGLTtRFCQKLAKKHNMVVVSPILErdrehGGVLWNTAVVISNsGLVMGKTRKNHIPRVGDFNESTYYMEGNLG 217
Cdd:PRK13981  58 FLAACEAALE-RLAAATAGGPAVLVGHPWRE-----GGKLYNAAALLDG-GEVLATYRKQDLPNYGVFDEKRYFAPGPEP 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  218 HPVfqtQFG--RIAVNICYGRHHPLNWLMYSINGAEIIFNPSA---TIG--ELSESLwpieARNAAIANHCFTCALNRVG 290
Cdd:PRK13981 131 GVV---ELKgvRIGVPICEDIWNPEPAETLAEAGAELLLVPNAspyHRGkpDLREAV----LRARVRETGLPLVYLNQVG 203
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
142-269 2.43e-05

Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the second of those two domains. 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.


Pssm-ID: 143603  Cd Length: 279  Bit Score: 45.63  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 142 AEDGLTTRFCQKLAKKHNMVVVSPILERDrehGGVLWNTAVVISNSGLVmGKTRKNHIPRvgdfNESTYYMEGNlGHPVF 221
Cdd:cd07579  54 SDTGPAVSALRRLARRLRLYLVAGFAEAD---GDGLYNSAVLVGPEGLV-GTYRKTHLIE----PERSWATPGD-TWPVY 124
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 68565067 222 QTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGELSESLWP 269
Cdd:cd07579 125 DLPLGRVGLLIGHDALFPEAGRVLALRGCDLLACPAAIAIPFVGAHAG 172
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
82-226 2.85e-05

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. 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 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143591  Cd Length: 299  Bit Score: 45.31  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  82 PLPTSAPVAEQVSALH-KSIEEIAEVAAMCGVNIICFQEAWNMPFAFCTREKLPWTEFAESAEDGLT----------TRF 150
Cdd:cd07567  10 PILSPDPDALQIMEKNlDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEVNWNpcldpdrfdyTEV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067 151 CQKL---AKKHNMVVVSPILER---DR------EHGGVLWNTAVVISNSGLVMGKTRKNHIprvgdFNE----STYYMEg 214
Cdd:cd07567  90 LQRLscaARENSIYVVANLGEKqpcDSsdphcpPDGRYQYNTNVVFDRDGTLIARYRKYNL-----FGEpgfdVPPEPE- 163
                       170
                ....*....|..
gi 68565067 215 nlgHPVFQTQFG 226
Cdd:cd07567 164 ---IVTFDTDFG 172
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
138-198 1.83e-04

Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. 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 3.


Pssm-ID: 143590  Cd Length: 295  Bit Score: 43.10  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68565067 138 FAESAEDGLTTRFCQKLAKKHNMVVVSPILERDREHGGVLWNTAVVISNSGLVMGKTRKNH 198
Cdd:cd07566  61 YLEPTTSGPSFEWAREVAKKFNCHVVIGYPEKVDESSPKLYNSALVVDPEGEVVFNYRKSF 121
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
72-254 1.13e-03

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 41.02  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067   72 VRVGLVQNRIP-----LPtsapvAEQVSALHKSIEEIAEVAAmcGVNIICFQEAwNMPFafctreklpwteFAESAEDGL 146
Cdd:PRK00302 220 LKVALVQGNIPqslkwDP-----AGLEATLQKYLDLSRPALG--PADLIIWPET-AIPF------------LLEDLPQAF 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68565067  147 TTRFCQKLAKKHNMVVVSPILERDREHGGVLWNTAVVISNSGlVMGKTRKNH-------IP--------------RVGDF 205
Cdd:PRK00302 280 LKALDDLAREKGSALITGAPRAENKQGRYDYYNSIYVLGPYG-ILNRYDKHHlvpfgeyVPlesllrplapffnlPMGDF 358
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 68565067  206 NEstyymeGNLGHPVFQTQFGRIAVNICYgrhhplnwlmysingaEIIF 254
Cdd:PRK00302 359 SR------GPYVQPPLLAKGLKLAPLICY----------------EIIF 385
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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