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Conserved domains on  [gi|488811876|ref|WP_002724282|]
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MULTISPECIES: N-carbamoyl-D-amino-acid hydrolase [Cereibacter]

Protein Classification

N-carbamoyl-D-amino-acid hydrolase( domain architecture ID 10166051)

N-carbamoyl-D-amino-acid hydrolase catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-298 0e+00

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: 519.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   1 MRKMIVGGAQMGPIQQADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMDRWFESEMPNGATQPL 80
Cdd:cd07569    1 SRQVILAAAQMGPIARAETRESVVARLIALLEEAASRGAQLVVFPELALTTFFPRWYFPDEAELDSFFETEMPNPETQPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  81 FDLAREMGMAFTFGFAELTPDG---HHFNTSILTDAQANIVGTYRKVHLPGHVEFDPERTHQHLEKRYFEPGDLGFNVWR 157
Cdd:cd07569   81 FDRAKELGIGFYLGYAELTEDGgvkRRFNTSILVDKSGKIVGKYRKVHLPGHKEPEPYRPFQHLEKRYFEPGDLGFPVFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 158 NEGVVMGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNSQKGaEGLRQRLFHSDLSMQAGAYQNSTYVVGVAKAGTE 237
Cdd:cd07569  161 VPGGIMGMCICNDRRWPETWRVMGLQGVELVLLGYNTPTHNPPAP-EHDHLRLFHNLLSMQAGAYQNGTWVVAAAKAGME 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488811876 238 DGHHLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKATVFDFARHRRIEHYQRI 298
Cdd:cd07569  240 DGCDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDLCREGRETVFNFARHRRPEHYGLI 300
 
Name Accession Description Interval E-value
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-298 0e+00

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: 519.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   1 MRKMIVGGAQMGPIQQADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMDRWFESEMPNGATQPL 80
Cdd:cd07569    1 SRQVILAAAQMGPIARAETRESVVARLIALLEEAASRGAQLVVFPELALTTFFPRWYFPDEAELDSFFETEMPNPETQPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  81 FDLAREMGMAFTFGFAELTPDG---HHFNTSILTDAQANIVGTYRKVHLPGHVEFDPERTHQHLEKRYFEPGDLGFNVWR 157
Cdd:cd07569   81 FDRAKELGIGFYLGYAELTEDGgvkRRFNTSILVDKSGKIVGKYRKVHLPGHKEPEPYRPFQHLEKRYFEPGDLGFPVFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 158 NEGVVMGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNSQKGaEGLRQRLFHSDLSMQAGAYQNSTYVVGVAKAGTE 237
Cdd:cd07569  161 VPGGIMGMCICNDRRWPETWRVMGLQGVELVLLGYNTPTHNPPAP-EHDHLRLFHNLLSMQAGAYQNGTWVVAAAKAGME 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488811876 238 DGHHLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKATVFDFARHRRIEHYQRI 298
Cdd:cd07569  240 DGCDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDLCREGRETVFNFARHRRPEHYGLI 300
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-295 2.36e-73

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.67  E-value: 2.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   3 KMIVGGAQMGPIqqADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMdrwfesEMPNGATQPLFD 82
Cdd:COG0388    1 TMRIALAQLNPT--VGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAE------PLDGPALAALAE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  83 LAREMGMAFTFGFAELTPDGHHFNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDlGFNVWRNEGVV 162
Cdd:COG0388   73 LARELGIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFD--------EKRYFTPGD-ELVVFDTDGGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 163 MGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNSQkgaeglrqrlFHSDLSMQAGAYQNSTYVVGVAKAGTEDGHHL 242
Cdd:COG0388  144 IGVLICYDLWFPELARALALAGADLLLVPSASPFGRGK----------DHWELLLRARAIENGCYVVAANQVGGEDGLVF 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488811876 243 MGGSIIVDPDGEVIARAEtEGDELIFAECDFDRCTFGKATvFDFARHRRIEHY 295
Cdd:COG0388  214 DGGSMIVDPDGEVLAEAG-DEEGLLVADIDLDRLREARRR-FPVLRDRRPDLY 264
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
19-277 6.86e-44

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: 150.58  E-value: 6.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   19 SRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemDRWFES-EMPNGAT-QPLFDLAREMGMAFTFGFA 96
Cdd:pfam00795  13 DLEANLQKALELIEEAARYGADLIVLPELFITGYPCW---------AHFLEAaEVGDGETlAGLAALARKNGIAIVIGLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   97 ELTPD-GHHFNTSILTDAQANIVGTYRKVHLpghveFDPERTHQHLEKRYFEPGDLGFnVWRNEGVVMGMAICNDRRWPE 175
Cdd:pfam00795  84 ERWLTgGRLYNTAVLLDPDGKLVGKYRKLHL-----FPEPRPPGFRERVLFEPGDGGT-VFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  176 TYRELGLQGVELVTIGYNTPSVNSQKGAeglrqrlFHSDLSMQAGAYQNSTYVVGVAKAGTE-DGHHLMGGSIIVDPDGE 254
Cdd:pfam00795 158 LLRALALKGAEILINPSARAPFPGSLGP-------PQWLLLARARALENGCFVIAANQVGGEeDAPWPYGHSMIIDPDGR 230
                         250       260
                  ....*....|....*....|...
gi 488811876  255 VIARAETEGDELIFAECDFDRCT 277
Cdd:pfam00795 231 ILAGAGEWEEGVLIADIDLALVR 253
PLN02747 PLN02747
N-carbamolyputrescine amidase
2-296 7.43e-28

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 109.47  E-value: 7.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   2 RKMIVGGAQMGpiqQADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMDRWFESempNGATQPLF 81
Cdd:PLN02747   5 RKVVVAALQFA---CSDDRAANVDKAERLVREAHAKGANIILIQELFEGYYFCQAQREDFFQRAKPYEG---HPTIARMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  82 DLAREMGMAFTFGFAElTPDGHHFNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDLGFNVWRNEGV 161
Cdd:PLN02747  79 KLAKELGVVIPVSFFE-EANNAHYNSIAIIDADGTDLGLYRKSHIPDGPGYQ--------EKFYFNPGDTGFKVFDTKFA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 162 VMGMAICNDRRWPETYRELGLQGVELVTigYNTpSVNSQKGAEGLRQRLfHSDLSMQAGAYQNSTYVVGVAKAGTE---- 237
Cdd:PLN02747 150 KIGVAICWDQWFPEAARAMVLQGAEVLL--YPT-AIGSEPQDPGLDSRD-HWKRVMQGHAGANLVPLVASNRIGTEilet 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488811876 238 ----DGHHLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKAT--VFdfaRHRRIEHYQ 296
Cdd:PLN02747 226 ehgpSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASwgVF---RDRRPDLYK 287
 
Name Accession Description Interval E-value
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-298 0e+00

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: 519.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   1 MRKMIVGGAQMGPIQQADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMDRWFESEMPNGATQPL 80
Cdd:cd07569    1 SRQVILAAAQMGPIARAETRESVVARLIALLEEAASRGAQLVVFPELALTTFFPRWYFPDEAELDSFFETEMPNPETQPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  81 FDLAREMGMAFTFGFAELTPDG---HHFNTSILTDAQANIVGTYRKVHLPGHVEFDPERTHQHLEKRYFEPGDLGFNVWR 157
Cdd:cd07569   81 FDRAKELGIGFYLGYAELTEDGgvkRRFNTSILVDKSGKIVGKYRKVHLPGHKEPEPYRPFQHLEKRYFEPGDLGFPVFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 158 NEGVVMGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNSQKGaEGLRQRLFHSDLSMQAGAYQNSTYVVGVAKAGTE 237
Cdd:cd07569  161 VPGGIMGMCICNDRRWPETWRVMGLQGVELVLLGYNTPTHNPPAP-EHDHLRLFHNLLSMQAGAYQNGTWVVAAAKAGME 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488811876 238 DGHHLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKATVFDFARHRRIEHYQRI 298
Cdd:cd07569  240 DGCDLIGGSCIVAPTGEIVAQATTLEDEVIVADCDLDLCREGRETVFNFARHRRPEHYGLI 300
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-295 2.36e-73

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 226.67  E-value: 2.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   3 KMIVGGAQMGPIqqADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMdrwfesEMPNGATQPLFD 82
Cdd:COG0388    1 TMRIALAQLNPT--VGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAE------PLDGPALAALAE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  83 LAREMGMAFTFGFAELTPDGHHFNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDlGFNVWRNEGVV 162
Cdd:COG0388   73 LARELGIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVFD--------EKRYFTPGD-ELVVFDTDGGR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 163 MGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNSQkgaeglrqrlFHSDLSMQAGAYQNSTYVVGVAKAGTEDGHHL 242
Cdd:COG0388  144 IGVLICYDLWFPELARALALAGADLLLVPSASPFGRGK----------DHWELLLRARAIENGCYVVAANQVGGEDGLVF 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488811876 243 MGGSIIVDPDGEVIARAEtEGDELIFAECDFDRCTFGKATvFDFARHRRIEHY 295
Cdd:COG0388  214 DGGSMIVDPDGEVLAEAG-DEEGLLVADIDLDRLREARRR-FPVLRDRRPDLY 264
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-275 1.00e-57

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: 185.99  E-value: 1.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   6 VGGAQMgPIQQADSRETVvARMMELMRKAHAEGVKMLVYPELALTTFFPrwyaeDRAEMDRWFESEMPNGATQPLFDLAR 85
Cdd:cd07197    1 IAAVQL-APKIGDVEANL-AKALRLIKEAAEQGADLIVLPELFLTGYSF-----ESAKEDLDLAEELDGPTLEALAELAK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  86 EMGMAFTFGFAELTPDgHHFNTSILTDAQANIVGTYRKVHLPghvefdperthQHLEKRYFEPGDlGFNVWRNEGVVMGM 165
Cdd:cd07197   74 ELGIYIVAGIAEKDGD-KLYNTAVVIDPDGEIIGKYRKIHLF-----------DFGERRYFSPGD-EFPVFDTPGGKIGL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 166 AICNDRRWPETYRELGLQGVELVTIGYNTPSvnsqkgaeglrQRLFHSDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMGG 245
Cdd:cd07197  141 LICYDLRFPELARELALKGADIILVPAAWPT-----------ARREHWELLLRARAIENGVYVVAANRVGEEGGLEFAGG 209
                        250       260       270
                 ....*....|....*....|....*....|
gi 488811876 246 SIIVDPDGEVIARAEtEGDELIFAECDFDR 275
Cdd:cd07197  210 SMIVDPDGEVLAEAS-EEEGILVAELDLDE 238
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
14-298 7.80e-47

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: 158.88  E-value: 7.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  14 IQQA--DSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaEDRAEMDRWFESEMPNGATQPLFDLAREMGMAF 91
Cdd:cd07573    6 VQMAcsEDPEANLAKAEELVREAAAQGAQIVCLQELFETPYFCQ---EEDEDYFDLAEPPIPGPTTARFQALAKELGVVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  92 TFGFAELTPDGHHFNTSILTDAQANIVGTYRKVHLPGhvefDPerthQHLEKRYFEPGDLGFNVWRNEGVVMGMAICNDR 171
Cdd:cd07573   83 PVSLFEKRGNGLYYNSAVVIDADGSLLGVYRKMHIPD----DP----GYYEKFYFTPGDTGFKVFDTRYGRIGVLICWDQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 172 RWPETYRELGLQGVELV----TIGYNTpsvnsQKGAEGLRQRLfHSDLSMQAGAYQNSTYVVGVAKAGTED----GHHLM 243
Cdd:cd07573  155 WFPEAARLMALQGAEILfyptAIGSEP-----QEPPEGLDQRD-AWQRVQRGHAIANGVPVAAVNRVGVEGdpgsGITFY 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488811876 244 GGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKATvFDFARHRRIEHYQRI 298
Cdd:cd07573  229 GSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRA-WPFFRDRRPDLYGAL 282
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
19-277 6.86e-44

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: 150.58  E-value: 6.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   19 SRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemDRWFES-EMPNGAT-QPLFDLAREMGMAFTFGFA 96
Cdd:pfam00795  13 DLEANLQKALELIEEAARYGADLIVLPELFITGYPCW---------AHFLEAaEVGDGETlAGLAALARKNGIAIVIGLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   97 ELTPD-GHHFNTSILTDAQANIVGTYRKVHLpghveFDPERTHQHLEKRYFEPGDLGFnVWRNEGVVMGMAICNDRRWPE 175
Cdd:pfam00795  84 ERWLTgGRLYNTAVLLDPDGKLVGKYRKLHL-----FPEPRPPGFRERVLFEPGDGGT-VFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  176 TYRELGLQGVELVTIGYNTPSVNSQKGAeglrqrlFHSDLSMQAGAYQNSTYVVGVAKAGTE-DGHHLMGGSIIVDPDGE 254
Cdd:pfam00795 158 LLRALALKGAEILINPSARAPFPGSLGP-------PQWLLLARARALENGCFVIAANQVGGEeDAPWPYGHSMIIDPDGR 230
                         250       260
                  ....*....|....*....|...
gi 488811876  255 VIARAETEGDELIFAECDFDRCT 277
Cdd:pfam00795 231 ILAGAGEWEEGVLIADIDLALVR 253
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
24-291 5.17e-42

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: 145.37  E-value: 5.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemDRWFESEMPNGATQPLF-DLAREMGMAFTFG-FAELTPd 101
Cdd:cd07583   18 IERVESLIEEAAAAGADLIVLPEMWNTGYFLD---------DLYELADEDGGETVSFLsELAKKHGVNIVAGsVAEKEG- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 102 GHHFNTSILTDAQANIVGTYRKVHLpghveFDPERthqhlEKRYFEPGDlGFNVWRNEGVVMGMAICNDRRWPETYRELG 181
Cdd:cd07583   88 GKLYNTAYVIDPDGELIATYRKIHL-----FGLMG-----EDKYLTAGD-ELEVFELDGGKVGLFICYDLRFPELFRKLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 182 LQGVELVTIGYNTPSVnsqkgaeglrqRLFHSDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMGGSIIVDPDGEVIARAEt 261
Cdd:cd07583  157 LEGAEILFVPAEWPAA-----------RIEHWRTLLRARAIENQAFVVACNRVGTDGGNEFGGHSMVIDPWGEVLAEAG- 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488811876 262 EGDELIFAECDFD-----RCTFgkaTVFdfaRHRR 291
Cdd:cd07583  225 EEEEILTAEIDLEevaevRKKI---PVF---KDRR 253
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-295 1.24e-40

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: 142.49  E-value: 1.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   6 VGGAQMGPIQQAdsRETVVARMMELMRKAHAEGVKMLVYPELALTTFFprwyAEDRAEMdRWFESEMPNGAT-QPLFDLA 84
Cdd:cd07580    2 VACVQFDPRVGD--LDANLARSIELIREAADAGANLVVLPELANTGYV----FESRDEA-FALAEEVPDGAStRAWAELA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  85 REMGMAFTFGFAElTPDGHHFNTSILTDAQANIvGTYRKVHLPGhvefdperthqhLEKRYFEPGDLGFNVWRNEGVVMG 164
Cdd:cd07580   75 AELGLYIVAGFAE-RDGDRLYNSAVLVGPDGVI-GTYRKAHLWN------------EEKLLFEPGDLGLPVFDTPFGRIG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 165 MAICNDRRWPETYRELGLQGVELVTIGYN-TPSVNSQKGAEGLRQRLfhsdlsMQAGAYQNSTYVVGVAKAGTEDGHHLM 243
Cdd:cd07580  141 VAICYDGWFPETFRLLALQGADIVCVPTNwVPMPRPPEGGPPMANIL------AMAAAHSNGLFIACADRVGTERGQPFI 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488811876 244 GGSIIVDPDGEVIAR-AETEGDELIFAECDFDRCTFGKATVFDFA-RHRRIEHY 295
Cdd:cd07580  215 GQSLIVGPDGWPLAGpASGDEEEILLADIDLTAARRKRIWNSNDVlRDRRPDLY 268
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
6-293 2.17e-40

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: 141.18  E-value: 2.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   6 VGGAQMgPIQQADSRETVvARMMELMRKAHAEGVKMLVYPELALTTffprwYAEDRAEMDRwfeSEMPNG-ATQPLFDLA 84
Cdd:cd07576    2 LALYQG-PARDGDVAANL-ARLDEAAARAAAAGADLLVFPELFLTG-----YNIGDAVARL---AEPADGpALQALRAIA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  85 REMGMAFTFGFAELTpDGHHFNTSILTDAQANIVGTYRKVHLPGHvefdperthqhLEKRYFEPGDlGFNVWRNEGVVMG 164
Cdd:cd07576   72 RRHGIAIVVGYPERA-GGAVYNAAVLIDEDGTVLANYRKTHLFGD-----------SERAAFTPGD-RFPVVELRGLRVG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 165 MAICNDRRWPETYRELGLQGVELVTIgyntPSVNSQkgaeglrQRLFHSDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMG 244
Cdd:cd07576  139 LLICYDVEFPELVRALALAGADLVLV----PTALME-------PYGFVARTLVPARAFENQIFVAYANRCGAEDGLTYVG 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488811876 245 GSIIVDPDGEVIARAEtEGDELIFAECDFDRctFGKA-TVFDFARHRRIE 293
Cdd:cd07576  208 LSSIAGPDGTVLARAG-RGEALLVADLDPAA--LAAArRENPYLADRRPE 254
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
24-274 1.66e-36

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: 131.34  E-value: 1.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTffprwYAEDRAEMDRWFESEMPNGATQPLF-DLAREMGMAFTFGFAELTPD- 101
Cdd:cd07584   18 LKKAAELCKEAAAEGADLICFPELATTG-----YRPDLLGPKLWELSEPIDGPTVRLFsELAKELGVYIVCGFVEKGGVp 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 102 GHHFNTSILTDAQANIVGTYRKVHLPGhvefdperthqhLEKRYFEPGDLgFNVWRNEGVVMGMAICNDRRWPETYRELG 181
Cdd:cd07584   93 GKVYNSAVVIDPEGESLGVYRKIHLWG------------LEKQYFREGEQ-YPVFDTPFGKIGVMICYDMGFPEVARILT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 182 LQGVELVTIgyntPSVNSQKGAEGLrqrlfhsDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMGGSIIVDPDGEVIARAET 261
Cdd:cd07584  160 LKGAEVIFC----PSAWREQDADIW-------DINLPARALENTVFVAAVNRVGNEGDLVLFGKSKILNPRGQVLAEASE 228
                        250
                 ....*....|...
gi 488811876 262 EGDELIFAECDFD 274
Cdd:cd07584  229 EAEEILYAEIDLD 241
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
24-275 1.05e-34

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: 126.66  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTffprwYAEDRAeMDRWfESEMPNGATQPLFDLAREMGMAFTFGFAELTPDgH 103
Cdd:cd07585   18 LAVIARWTRKAAAQGAELVCFPEMCITG-----YTHVRA-LSRE-AEVPDGPSTQALSDLARRYGLTILAGLIEKAGD-R 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 104 HFNTSILTDAQANiVGTYRKVHLpghveFDPErthqhleKRYFEPGDlGFNVWRNEGVVMGMAICNDRRWPETYRELGLQ 183
Cdd:cd07585   90 PYNTYLVCLPDGL-VHRYRKLHL-----FRRE-------HPYIAAGD-EYPVFATPGVRFGILICYDNHFPENVRATALL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 184 GVELVTIGYNTPSVNSQKGAEGLrQRlfhsdlSMQAGAYQNSTYVVGVAKAGTEDGHHLMGGSIIVDPDGEVIARAETEG 263
Cdd:cd07585  156 GAEILFAPHATPGTTSPKGREWW-MR------WLPARAYDNGVFVAACNGVGRDGGEVFPGGAMILDPYGRVLAETTSGG 228
                        250
                 ....*....|..
gi 488811876 264 DELIFAECDFDR 275
Cdd:cd07585  229 DGMVVADLDLDL 240
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
20-295 3.39e-33

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: 123.38  E-value: 3.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  20 RETVVARMMELMRKAHAEGVKMLVYPELALTTFF-----PRWYAedraemdrwFESEMPNGATQPLF-DLAREMGMAFTF 93
Cdd:cd07568   25 KEAMIQKHVTMIREAAEAGAQIVCLQEIFYGPYFcaeqdTKWYE---------FAEEIPNGPTTKRFaALAKEYNMVLIL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  94 GFAELTPDGHHFNTSILTDAQANIVGTYRKVHLPgHVEfdperthQHLEKRYFEPGDLGFNVWRNEGVVMGMAICNDRRW 173
Cdd:cd07568   96 PIYEKEQGGTLYNTAAVIDADGTYLGKYRKNHIP-HVG-------GFWEKFYFRPGNLGYPVFDTAFGKIGVYICYDRHF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 174 PETYRELGLQGVELVtigYNtPSVNSQkgaeGLRQRLFHsdLSMQAGAYQNSTYVVGVAKAGTE----DGhHLMGGSIIV 249
Cdd:cd07568  168 PEGWRALGLNGAEIV---FN-PSATVA----GLSEYLWK--LEQPAAAVANGYFVGAINRVGTEapwnIG-EFYGSSYFV 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488811876 250 DPDGEVIARAETEGDELIFAECDFDRCTFGKATvFDFARHRRIEHY 295
Cdd:cd07568  237 DPRGQFVASASRDKDELLVAELDLDLIREVRDT-WQFYRDRRPETY 281
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
24-275 2.69e-32

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: 120.22  E-value: 2.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPE----LALTTFFPRWYAEdraemdrwfesEMPNGATQPLF-DLAREMGMAFTFG-FAE 97
Cdd:cd07572   17 LARAKELIEEAAAQGAKLVVLPEcfnyPGGTDAFKLALAE-----------EEGDGPTLQALsELAKEHGIWLVGGsIPE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  98 LTP-DGHHFNTSILTDAQANIVGTYRKVHLpghveFD----PERTHQhlEKRYFEPGDlGFNVWRNEGVVMGMAICNDRR 172
Cdd:cd07572   86 RDDdDGKVYNTSLVFDPDGELVARYRKIHL-----FDvdvpGGISYR--ESDTLTPGD-EVVVVDTPFGKIGLGICYDLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 173 WPETYRELGLQGVELVTIgyntPSV-NSQKGAEglrqrlfHSDLSMQAGAYQNSTYVVGVAKAGT-EDGHHLMGGSIIVD 250
Cdd:cd07572  158 FPELARALARQGADILTV----PAAfTMTTGPA-------HWELLLRARAIENQCYVVAAAQAGDhEAGRETYGHSMIVD 226
                        250       260
                 ....*....|....*....|....*
gi 488811876 251 PDGEVIARAEtEGDELIFAECDFDR 275
Cdd:cd07572  227 PWGEVLAEAG-EGEGVVVAEIDLDR 250
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
14-275 1.06e-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: 143610  Cd Length: 269  Bit Score: 118.93  E-value: 1.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  14 IQQADSR----ETVVARMMELMRKAHAEGVKMLVYPELALTTFfprwYAEDRA-EMDRWFESEmpngATQPLFDLARemG 88
Cdd:cd07586    4 IAQIDPVlgdvEENLEKHLEIIETARERGADLVVFPELSLTGY----NLGDLVyEVAMHADDP----RLQALAEASG--G 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  89 MAFTFGFAELTPDGHHFNTS-ILTDAQanIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDlGFNVWRNEGVVMGMAI 167
Cdd:cd07586   74 ICVVFGFVEEGRDGRFYNSAaYLEDGR--VVHVHRKVYLPTYGLFE--------EGRYFAPGS-HLRAFDTRFGRAGVLI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 168 CNDRRWPETYRELGLQGVELVTIGYNTPsvnsqkgAEGLRQRLFHSD---LSMQAGAYQNSTYVVGVAKAGTEDGHHLMG 244
Cdd:cd07586  143 CEDAWHPSLPYLLALDGADVIFIPANSP-------ARGVGGDFDNEEnweTLLKFYAMMNGVYVVFANRVGVEDGVYFWG 215
                        250       260       270
                 ....*....|....*....|....*....|.
gi 488811876 245 GSIIVDPDGEVIARAETEGDELIFAECDFDR 275
Cdd:cd07586  216 GSRVVDPDGEVVAEAPLFEEDLLVAELDRSA 246
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
24-295 3.02e-31

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: 117.40  E-value: 3.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEgvkMLVYPELALTTFFprwyAEDRAEMDRWFESEmPNG-ATQPLFDLAREMGMAFTFGFAElTPDG 102
Cdd:cd07577   18 LKKVESLIKGVEAD---LIVLPELFNTGYA----FTSKEEVASLAESI-PDGpTTRFLQELARETGAYIVAGLPE-RDGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 103 HHFNTSILTDAQAnIVGTYRKVHLpghveFDPErthqhleKRYFEPGDLGFNVWRNEGVVMGMAICNDRRWPETYRELGL 182
Cdd:cd07577   89 KFYNSAVVVGPEG-YIGIYRKTHL-----FYEE-------KLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 183 QGVELVTIGYNTPSVNSQKGaeglrqrlfhsdlsMQAGAYQNSTYVVGVAKAGTE----DGHHLMGGSIIVDPDGEVIAR 258
Cdd:cd07577  156 KGADIIAHPANLVLPYCPKA--------------MPIRALENRVFTITANRIGTEerggETLRFIGKSQITSPKGEVLAR 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488811876 259 AETEGDELIFAECDFDRCTFGKATVF-DFARHRRIEHY 295
Cdd:cd07577  222 APEDGEEVLVAEIDPRLARDKRINEEnDIFKDRRPEFY 259
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-275 4.11e-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: 143605  Cd Length: 255  Bit Score: 116.91  E-value: 4.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   6 VGGAQMGPiqQADSRETVvARMMELMRKAHAEGVKMLVYPELALTTF-FPRWYAEDRAE-MDRWFESEMPngatqplfDL 83
Cdd:cd07581    1 VALAQFAS--SGDKEENL-EKVRRLLAEAAAAGADLVVFPEYTMARFgDGLDDYARVAEpLDGPFVSALA--------RL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  84 AREMGMAFTFGFAELTPDGHHFNTSILTDAQANIVGTYRKVHLpghveFDperTHQHLEKRYFEPGD----LGFNVwrnE 159
Cdd:cd07581   70 ARELGITVVAGMFEPAGDGRVYNTLVVVGPDGEIIAVYRKIHL-----YD---AFGFRESDTVAPGDelppVVFVV---G 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 160 GVVMGMAICNDRRWPETYRELGLQGVELVTIgyntPSV-NSQKGAEGlrqrlfHSDLSMQAGAYQNSTYVVGVAKAgted 238
Cdd:cd07581  139 GVKVGLATCYDLRFPELARALALAGADVIVV----PAAwVAGPGKEE------HWETLLRARALENTVYVAAAGQA---- 204
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488811876 239 GHHLMGGSIIVDPDGEVIARAEtEGDELIFAECDFDR 275
Cdd:cd07581  205 GPRGIGRSMVVDPLGVVLADLG-EREGLLVADIDPER 240
PLN02747 PLN02747
N-carbamolyputrescine amidase
2-296 7.43e-28

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 109.47  E-value: 7.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   2 RKMIVGGAQMGpiqQADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRWYAEDRAEMDRWFESempNGATQPLF 81
Cdd:PLN02747   5 RKVVVAALQFA---CSDDRAANVDKAERLVREAHAKGANIILIQELFEGYYFCQAQREDFFQRAKPYEG---HPTIARMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  82 DLAREMGMAFTFGFAElTPDGHHFNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDLGFNVWRNEGV 161
Cdd:PLN02747  79 KLAKELGVVIPVSFFE-EANNAHYNSIAIIDADGTDLGLYRKSHIPDGPGYQ--------EKFYFNPGDTGFKVFDTKFA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 162 VMGMAICNDRRWPETYRELGLQGVELVTigYNTpSVNSQKGAEGLRQRLfHSDLSMQAGAYQNSTYVVGVAKAGTE---- 237
Cdd:PLN02747 150 KIGVAICWDQWFPEAARAMVLQGAEVLL--YPT-AIGSEPQDPGLDSRD-HWKRVMQGHAGANLVPLVASNRIGTEilet 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488811876 238 ----DGHHLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKAT--VFdfaRHRRIEHYQ 296
Cdd:PLN02747 226 ehgpSKITFYGGSFIAGPTGEIVAEADDKAEAVLVAEFDLDQIKSKRASwgVF---RDRRPDLYK 287
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
24-291 1.52e-23

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: 96.77  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemDRWFESEMPNGATQPLFDLARE---MGMAFTFGFAELTp 100
Cdd:cd07570   18 AEKILEAIREAKAQGADLVVFPELSLTGYPPE---------DLLLRPDFLEAAEEALEELAAAtadLDIAVVVGLPLRH- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 101 DGHHFNTSILTDaQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDlGFNVWRNEGVVMGMAICNDRRWPETY-RE 179
Cdd:cd07570   88 DGKLYNAAAVLQ-NGKILGVVPKQLLPNYGVFD--------EKRYFTPGD-KPDVLFFKGLRIGVEICEDLWVPDPPsAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 180 LGLQGVELVTigynTPS-VNSQKGAEGLRQRLFhSDLSMQAGA---YQNStyvVGvakAGTE---DGHhlmggSIIVDPD 252
Cdd:cd07570  158 LALAGADLIL----NLSaSPFHLGKQDYRRELV-SSRSARTGLpyvYVNQ---VG---GQDDlvfDGG-----SFIADND 221
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488811876 253 GEVIARAETEgdELIFAECDFDRCTFGKATVFDFARHRR 291
Cdd:cd07570  222 GELLAEAPRF--EEDLADVDLDRLRSERRRNSSFLDEEA 258
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
10-292 2.27e-23

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: 96.45  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  10 QMGPIQQADSREtvVARMMELMRKAHAEGVKMLVYPELALTTFFprWYaeDRAEMDRWFESeMPNGATQPLFDLAREMGM 89
Cdd:cd07578    7 QFEPEMGEKERN--IERLLALCEEAARAGARLIVTPEMATTGYC--WY--DRAEIAPFVEP-IPGPTTARFAELAREHDC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  90 AFTFGFAELTPD-GHHFNTSILTDAQAnIVGTYRKvhlpghvefdperTHQHL-EKRYFEPGDLGFNVWRNEGVVMGMAI 167
Cdd:cd07578   80 YIVVGLPEVDSRsGIYYNSAVLIGPSG-VIGRHRK-------------THPYIsEPKWAADGDLGHQVFDTEIGRIALLI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 168 CNDRRWPETYRELGLQGVELVTIGYN-----TPSVnsqkgaeglrqrlfhsdlSMQAGAYQNSTYVVGVAKAGTEDGHHL 242
Cdd:cd07578  146 CMDIHFFETARLLALGGADVICHISNwlaerTPAP------------------YWINRAFENGCYLIESNRWGLERGVQF 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488811876 243 MGGSIIVDPDGEVIARAETeGDELIFAECDFDRctfgkatvfdfARHRRI 292
Cdd:cd07578  208 SGGSCIIEPDGTIQASIDS-GDGVALGEIDLDR-----------ARHRQF 245
PLN02798 PLN02798
nitrilase
6-260 2.19e-22

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 94.43  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   6 VGGAQMGPIQQADSRETVVARmmeLMRKAHAEGVKMLVYPELAltTFFPRWYAEDRAEMDrwfesemPngATQPLFD--- 82
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSR---LAKEAAAAGAKLLFLPECF--SFIGDKDGESLAIAE-------P--LDGPIMQryr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  83 -LAREMGMAFTFG-FAELTPDGHH-FNTSILTDAQANIVGTYRKVHLpghveFDPERTHQHL--EKRYFEPGDLGFNVWR 157
Cdd:PLN02798  79 sLARESGLWLSLGgFQEKGPDDSHlYNTHVLIDDSGEIRSSYRKIHL-----FDVDVPGGPVlkESSFTAPGKTIVAVDS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 158 NEGVVmGMAICNDRRWPETYRELGL-QGVELVTIgyntPSVNSQKGAEGlrqrlfHSDLSMQAGAYQNSTYVVGVAKAGT 236
Cdd:PLN02798 154 PVGRL-GLTVCYDLRFPELYQQLRFeHGAQVLLV----PSAFTKPTGEA------HWEVLLRARAIETQCYVIAAAQAGK 222
                        250       260
                 ....*....|....*....|....*
gi 488811876 237 E-DGHHLMGGSIIVDPDGEVIARAE 260
Cdd:PLN02798 223 HnEKRESYGHALIIDPWGTVVARLP 247
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
24-270 7.52e-22

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: 93.12  E-value: 7.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMrKAHAEGVKMLVYPELALTTFFPrwyaeDRAEMDRwFESEMPNGATQPLFDLAREMGMAFTFGFAELTPD-- 101
Cdd:cd07565   26 IADMVEGT-KRGLPGMDLIVFPEYSTQGLMY-----DKWTMDE-TACTVPGPETDIFAEACKEAKVWGVFSIMERNPDhg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 102 GHHFNTSILTDAQANIVGTYRKVHlPgHVEFDPerthqhlekryFEPGDLGFNVWRN-EGVVMGMAICNDRRWPETYREL 180
Cdd:cd07565   99 KNPYNTAIIIDDQGEIVLKYRKLH-P-WVPIEP-----------WYPGDLGTPVCEGpKGSKIALIICHDGMYPEIAREC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 181 GLQGVELV--TIGYNTPSVNSQkgaeglrqrlfhsDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMGGSIIVDPDGEVIAR 258
Cdd:cd07565  166 AYKGAELIirIQGYMYPAKDQW-------------IITNKANAWCNLMYTASVNLAGFDGVFSYFGESMIVNFDGRTLGE 232
                        250
                 ....*....|..
gi 488811876 259 AETEGDELIFAE 270
Cdd:cd07565  233 GGREPDEIVTAE 244
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
4-297 3.24e-19

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: 85.62  E-value: 3.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   4 MIVGGAQMGPIqqADSRETVVARMMELMRKAHAEGVKMLVYPElaltTF---FPRW-----YAEDRAEMDRWFES--EMP 73
Cdd:cd07564    1 VKVAAVQAAPV--FLDLAATVEKACRLIEEAAANGAQLVVFPE----AFipgYPYWiwfgaPAEGRELFARYYENsvEVD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  74 NGATQPLFDLAREMGMAFTFGFAELtpDGHH-FNTSILTDAQANIVGTYRKVhLPGHVEfdpeRThqhlekrYFEPGD-L 151
Cdd:cd07564   75 GPELERLAEAARENGIYVVLGVSER--DGGTlYNTQLLIDPDGELLGKHRKL-KPTHAE----RL-------VWGQGDgS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 152 GFNVWRNEGVVMGMAICndrrW----PETYRELGLQGVElVTIGYNTPSVNSQKGAEGLRqrlfhsdLSMQAGAYQNSTY 227
Cdd:cd07564  141 GLRVVDTPIGRLGALIC----WenymPLARYALYAQGEQ-IHVAPWPDFSPYYLSREAWL-------AASRHYALEGRCF 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 228 VVGVAKAGTEDGHHLM---------------GGSIIVDPDGEVIARAETEGDELIFAECDFDRCTFGKATvFDFArhrri 292
Cdd:cd07564  209 VLSACQVVTEEDIPADceddeeadplevlggGGSAIVGPDGEVLAGPLPDEEGILYADIDLDDIVEAKLD-FDPV----- 282

                 ....*
gi 488811876 293 EHYQR 297
Cdd:cd07564  283 GHYSR 287
PRK13981 PRK13981
NAD synthetase; Provisional
24-259 7.03e-19

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 86.75  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTFFPR-------WYAEDRAEMDRwfesempngatqplfdLARE--MGMAFTFG 94
Cdd:PRK13981  19 AAKILAAAAEAADAGADLLLFPELFLSGYPPEdlllrpaFLAACEAALER----------------LAAAtaGGPAVLVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  95 FAELtPDGHHFNT-SILTDAQanIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDLGfNVWRNEGVVMGMAICNDRRW 173
Cdd:PRK13981  83 HPWR-EGGKLYNAaALLDGGE--VLATYRKQDLPNYGVFD--------EKRYFAPGPEP-GVVELKGVRIGVPICEDIWN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 174 PETYRELGLQGVELVTIGYNTP-SVNSQKgaegLRQRLfhsdlsMQAGAYQNSTYVVGVAKAGTEDghHLM--GGSIIVD 250
Cdd:PRK13981 151 PEPAETLAEAGAELLLVPNASPyHRGKPD----LREAV------LRARVRETGLPLVYLNQVGGQD--ELVfdGASFVLN 218

                 ....*....
gi 488811876 251 PDGEVIARA 259
Cdd:PRK13981 219 ADGELAARL 227
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
24-274 4.88e-18

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: 82.39  E-value: 4.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEG-----VKMLVYPELALTTFFPRWYAEDRAEMDrwFESEMPNGATQPLFDLAREMGMAFTFGFAEL 98
Cdd:cd07582   23 IDRINEQIDAAVGFSgpglpVRLVVLPEYALQGFPMGEPREVWQFDK--AAIDIPGPETEALGEKAKELNVYIAANAYER 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  99 TPD--GHHFNTSILTDAQANIVGTYRKVHLPGHVEF-DPERTHQHLEKRYFEPGDLGFNVWRNEGVVMGMAICNDRRWPE 175
Cdd:cd07582  101 DPDfpGLYFNTAFIIDPSGEIILRYRKMNSLAAEGSpSPHDVWDEYIEVYGYGLDALFPVADTEIGNLGCLACEEGLYPE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 176 TYRELGLQGVELVTIGYN-TPSVNsqkgaeglrQRLFHsdLSMQAGAYQNSTYVVGvAKAGTEDGHHLM-----GGSIIV 249
Cdd:cd07582  181 VARGLAMNGAEVLLRSSSeVPSVE---------LDPWE--IANRARALENLAYVVS-ANSGGIYGSPYPadsfgGGSMIV 248
                        250       260
                 ....*....|....*....|....*.
gi 488811876 250 DPDGEVIARAE-TEGDELIFAECDFD 274
Cdd:cd07582  249 DYKGRVLAEAGyGPGSMVAGAEIDIE 274
amiF PRK13287
formamidase; Provisional
33-270 7.11e-18

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 82.43  E-value: 7.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  33 KAHAEGVKMLVYPElalttffprwYAEDRAEMDRWFESEMPNGATQPLFDL----AREMGMAFTFGFAELTPDGHH-FNT 107
Cdd:PRK13287  47 KAGYPGLDLIVFPE----------YSTQGLNTKKWTTEEFLCTVDGPEVDAfaqaCKENKVWGVFSIMERNPDGNEpYNT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 108 SILTDAQANIVGTYRKVHlPgHVEFDPerthqhlekryFEPGDLGFNVWRN-EGVVMGMAICNDRRWPETYRELGLQGVE 186
Cdd:PRK13287 117 AIIIDDQGEIILKYRKLH-P-WVPVEP-----------WEPGDLGIPVCDGpGGSKLAVCICHDGMFPEMAREAAYKGAN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 187 LV--TIGYNTPsVNSQkgaeglrqrlfhSDLSMQAGAYQNSTYVVGVAKAGTEDGHHLMGGSIIVDPDGEVIARAETEGD 264
Cdd:PRK13287 184 VMirISGYSTQ-VREQ------------WILTNRSNAWQNLMYTASVNLAGYDGVFYYFGEGQVCNFDGTTLVQGHRNPW 250

                 ....*.
gi 488811876 265 ELIFAE 270
Cdd:PRK13287 251 EIVTAE 256
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
24-188 5.91e-14

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: 70.66  E-value: 5.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTFFprwYAEDRAEMDrwfesemPNGATQPLFDLAREMGMAFTFGFAELTPDGh 103
Cdd:cd07579   17 LATIDRLAAEAKATGAELVVFPELALTGLD---DPASEAESD-------TGPAVSALRRLARRLRLYLVAGFAEADGDG- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 104 HFNTSILTdAQANIVGTYRKVHLPGhvefdPERThqhlekrYFEPGDlGFNVWRNEGVVMGMAICNDRRWPETYRELGLQ 183
Cdd:cd07579   86 LYNSAVLV-GPEGLVGTYRKTHLIE-----PERS-------WATPGD-TWPVYDLPLGRVGLLIGHDALFPEAGRVLALR 151

                 ....*
gi 488811876 184 GVELV 188
Cdd:cd07579  152 GCDLL 156
amiE PRK13286
aliphatic amidase;
24-270 1.04e-10

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 61.68  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMrKAHAEGVKMLVYPELALTTFFprwYaeDRAEMdrwFE--SEMPNGATQPLFDLAREmgmAFTFGFAELTPD 101
Cdd:PRK13286  38 IADMIVGM-KQGLPGMDLVIFPEYSTHGIM---Y--DRQEM---YEtaSTIPGEETAIFAEACRK---AKVWGVFSLTGE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 102 GHH-------FNTSILTDAQANIVGTYRKVhLPghveFDPerthqhLEKRYfePGDLGFNVWRNEGVVMGMAICNDRRWP 174
Cdd:PRK13286 106 RHEehprkapYNTLILINDKGEIVQKYRKI-MP----WCP------IEGWY--PGDCTYVSEGPKGLKISLIICDDGNYP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 175 ETYRELGLQGVELVT--IGYNTPSVNSQKgaeglrqrlfhsdLSMQAGAYQNSTYvVGVAKAGTEDG-HHLMGGSIIVDP 251
Cdd:PRK13286 173 EIWRDCAMKGAELIVrcQGYMYPAKEQQV-------------LVAKAMAWANNCY-VAVANAAGFDGvYSYFGHSAIIGF 238
                        250
                 ....*....|....*....
gi 488811876 252 DGEVIARAETEGDELIFAE 270
Cdd:PRK13286 239 DGRTLGECGEEEMGIQYAQ 257
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
16-190 3.50e-10

Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 60.63  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  16 QADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemdrwfesemPNGATQPLFDLAREMGMAFTFGF 95
Cdd:COG0815  211 DPEQRREILDRYLDLTRELADDGPDLVVWPETALPFLLDE-----------------DPDALARLAAAAREAGAPLLTGA 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  96 AELTPD-GHHFNTSILTDAQANIVGTYRKVHL-PGhVEFDPER-------THQHLEKRYFEPGDlGFNVWRNEGVVMGMA 166
Cdd:COG0815  274 PRRDGGgGRYYNSALLLDPDGGILGRYDKHHLvPF-GEYVPLRdllrpliPFLDLPLGDFSPGT-GPPVLDLGGVRVGPL 351
                        170       180
                 ....*....|....*....|....*
gi 488811876 167 ICNDRRWPETYRELGLQGVE-LVTI 190
Cdd:COG0815  352 ICYESIFPELVRDAVRAGADlLVNI 376
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
4-275 3.96e-10

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: 59.52  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876   4 MIVGGAQMgPIQQADSRETVVARMMELMRKAHAEGVKMLVYPELA---LTTFFPRWYAEDRAEM-------DRWFEsemp 73
Cdd:cd07574    1 VRVAAAQY-PLRRYASFEEFAAKVEYWVAEAAGYGADLLVFPEYFtmeLLSLLPEAIDGLDEAIralaaltPDYVA---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  74 ngatqpLF-DLAREMGMAFTFGFAELTPDGHHFNTSILTDAQaNIVGTYRKVHLPGHvefdpERTHQHLEkryfePGDlG 152
Cdd:cd07574   76 ------LFsELARKYGINIIAGSMPVREDGRLYNRAYLFGPD-GTIGHQDKLHMTPF-----EREEWGIS-----GGD-K 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 153 FNVWRNEGVVMGMAICNDRRWPETYRELGLQGVELVTIGYNTPSVNsqkGAegLRQRlfhsdLSMQAGAYQNSTYVVGVA 232
Cdd:cd07574  138 LKVFDTDLGKIGILICYDSEFPELARALAEAGADLLLVPSCTDTRA---GY--WRVR-----IGAQARALENQCYVVQSG 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488811876 233 KAGTEDGHHLM----GGSIIVDP-------DGeVIARAETEGDELIFAECDFDR 275
Cdd:cd07574  208 TVGNAPWSPAVdvnyGQAAVYTPcdfgfpeDG-ILAEGEPNTEGWLIADLDLEA 260
PLN00202 PLN00202
beta-ureidopropionase
17-276 7.79e-10

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 59.09  E-value: 7.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  17 ADSRETVVARMMELMRKAHAEGVKMLVYPElALTTFFPRWYAEDRaemdrWFE-SEMPNG-ATQPLFDLAREMGMAFTFG 94
Cdd:PLN00202 105 ADQKRAIMDKVKPMIDAAGAAGVNILCLQE-AWTMPFAFCTREKR-----WCEfAEPVDGeSTKFLQELARKYNMVIVSP 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  95 FAEltPDGHH----FNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDLGFNVWRNEGVVMGMAICND 170
Cdd:PLN00202 179 ILE--RDVNHgetlWNTAVVIGNNGNIIGKHRKNHIPRVGDFN--------ESTYYMEGNTGHPVFETAFGKIAVNICYG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 171 RRWPETYRELGLQGVELVtigYNtPSVNSQKGAEGLRQrlfhsdLSMQAGAYQNSTYVVGVAKAGTE---------DGH- 240
Cdd:PLN00202 249 RHHPLNWLAFGLNGAEIV---FN-PSATVGDLSEPMWP------IEARNAAIANSYFVGSINRVGTEvfpnpftsgDGKp 318
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 488811876 241 ------HLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRC 276
Cdd:PLN00202 319 qhkdfgHFYGSSHFSAPDASCTPSLSRYKDGLLISDMDLNLC 360
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
16-168 7.85e-09

Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. 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 9.


Pssm-ID: 143595  Cd Length: 270  Bit Score: 55.30  E-value: 7.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  16 QADSRETVVARMMELMRKAHAEGVKMLVYPELALTTFFPRwyaedraemdrwfesemPNGATQPLFDLAREMGMAFTFGF 95
Cdd:cd07571   17 DPEQRQATLDRYLDLTRELADEKPDLVVWPETALPFDLQR-----------------DPDALARLARAARAVGAPLLTGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  96 AELTPDGHH-FNTSILTDAQANIVGTYRKVHL-PGhVEFDPER-------THQHLEKRYFEPGDlGFNVWRNEGVV-MGM 165
Cdd:cd07571   80 PRREPGGGRyYNSALLLDPGGGILGRYDKHHLvPF-GEYVPLRdllrflgLLFDLPMGDFSPGT-GPQPLLLGGGVrVGP 157

                 ...
gi 488811876 166 AIC 168
Cdd:cd07571  158 LIC 160
ML_beta-AS cd07587
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
17-276 4.23e-07

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: 50.83  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  17 ADSRETVVARMMELMRKAHAEGVKMLVYPElALTTFFprwyAEDRAEMDRW--FESEMPNGA-TQPLFDLAREMGMAFTF 93
Cdd:cd07587   82 AEQREAIHDRIKKIIEAAAMAGVNIICFQE-AWTMPF----AFCTREKLPWceFAESAEDGPtTKFCQELAKKYNMVIVS 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  94 GFAEltPDGHH----FNTSILTDAQANIVGTYRKVHLPGHVEFDperthqhlEKRYFEPGDLGFNVWRNEGVVMGMAICN 169
Cdd:cd07587  157 PILE--RDEEHgdtiWNTAVVISNSGNVLGKSRKNHIPRVGDFN--------ESTYYMEGNTGHPVFETQFGKIAVNICY 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876 170 DRRWPETYRELGLQGVELV-----TIGyntpsvnsqkgaeGLRQRLFHsdLSMQAGAYQNSTYVVGVAKAGTE------- 237
Cdd:cd07587  227 GRHHPLNWLMYGLNGAEIVfnpsaTVG-------------ALSEPMWP--IEARNAAIANSYFTVGINRVGTEvfpneft 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488811876 238 --DG---H----HLMGGSIIVDPDGEVIARAETEGDELIFAECDFDRC 276
Cdd:cd07587  292 sgDGkpaHkdfgHFYGSSYVAAPDGSRTPGLSRTRDGLLVAELDLNLC 339
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
209-260 3.12e-06

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 47.43  E-value: 3.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488811876 209 RLFHSDLSMQAGAYQNSTYVVGVAKAGTED-GHHLMGGSIIVDPDGEVIARAE 260
Cdd:PRK10438 169 RSLHWQTLLTARAIENQAYVAGCNRVGSDGnGHHYRGDSRIINPQGEIIATAE 221
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
10-126 3.29e-05

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: 44.64  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  10 QMGPIQQADSR-ETVVARmmeLMRKAHAEGVKMLVYPELALTTF-FP-----RWYAEDRAEmdrwfesempnGATqplFD 82
Cdd:cd07566   10 QIGQVEENLSRaWELLDK---TKKRAKLKKPDILVLPELALTGYnFHslehiKPYLEPTTS-----------GPS---FE 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488811876  83 LAREMGMAF----TFGFAELTPDGHH--FNTSILTDAQANIVGTYRKVHL 126
Cdd:cd07566   73 WAREVAKKFnchvVIGYPEKVDESSPklYNSALVVDPEGEVVFNYRKSFL 122
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
218-272 1.05e-04

Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup belonging 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; this subgroup either represents 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. XC1258 is a homotetramer.


Pssm-ID: 143599  Cd Length: 252  Bit Score: 42.91  E-value: 1.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488811876 218 QAGAYQNSTYVVGVAKAGT-EDGHHLMGGSIIVDPDGEVIARAEtEGDELIFAECD 272
Cdd:cd07575  177 KARAIENQAYVIGVNRVGTdGNGLEYSGDSAVIDPLGEPLAEAE-EDEGVLTATLD 231
nadE PRK02628
NAD synthetase; Reviewed
24-150 1.23e-04

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 43.70  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  24 VARMMELMRKAHAEGVKMLVYPELALTTffprwYAEDraemDRWFESEMPNGATQPLFDLA---REMGMAFTFGfAELTP 100
Cdd:PRK02628  31 AARILALARRAADDGVALAVFPELSLSG-----YSCD----DLFLQDTLLDAVEDALATLVeasADLDPLLVVG-APLRV 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488811876 101 DGHHFNTSILTdAQANIVGTYRKVHLPGHVEFdperthqhLEKRYFEPGD 150
Cdd:PRK02628 101 RHRLYNCAVVI-HRGRILGVVPKSYLPNYREF--------YEKRWFAPGD 141
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
14-168 6.80e-03

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 37.94  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  14 IQQA-----DSRETVVARMMELMRKAHaEGVKMLVYPELALTTFFPRwyaedraemdrwfeseMPNGATQPLFDLAREMG 88
Cdd:PRK00302 229 IPQSlkwdpAGLEATLQKYLDLSRPAL-GPADLIIWPETAIPFLLED----------------LPQAFLKALDDLAREKG 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488811876  89 MAFTFG--FAELTPDGHHFNTSILTDAQANIVGTYRKVHLpghV---EFDPerthqhLEK--RY-----------FEPGD 150
Cdd:PRK00302 292 SALITGapRAENKQGRYDYYNSIYVLGPYGILNRYDKHHL---VpfgEYVP------LESllRPlapffnlpmgdFSRGP 362
                        170
                 ....*....|....*...
gi 488811876 151 LGFNVWRNEGVVMGMAIC 168
Cdd:PRK00302 363 YVQPPLLAKGLKLAPLIC 380
 
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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