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Conserved domains on  [gi|968558930|ref|WP_058586114|]
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amidohydrolase [Pseudoalteromonas sp. XI10]

Protein Classification

nitrilase family protein( domain architecture ID 10166093)

nitrilase family protein is a member of a large superfamily and predicted to act as a carbon-nitrogen hydrolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-255 3.55e-143

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: 401.15  E-value: 3.55e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQSSLHWLDKSANLANFTEQLNSFNEQVDLIVLPETFATGFTINLDC-SEPEQGEVLSWLKATAKQKNAVVAGSV 82
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEAlAEPMNGPTLQWMKAQAKKKGAAITGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  83 LVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDVMIN 162
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 163 VANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQsGIIIQRLEKSPLDDFR 242
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239

                        250
                 ....*....|...
gi 968558930 243 RAFPAHLDADQFQ 255
Cdd:cd07575  240 EKFPFLKDADSFT 252
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-255 3.55e-143

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: 401.15  E-value: 3.55e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQSSLHWLDKSANLANFTEQLNSFNEQVDLIVLPETFATGFTINLDC-SEPEQGEVLSWLKATAKQKNAVVAGSV 82
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEAlAEPMNGPTLQWMKAQAKKKGAAITGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  83 LVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDVMIN 162
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 163 VANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQsGIIIQRLEKSPLDDFR 242
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239

                        250
                 ....*....|...
gi 968558930 243 RAFPAHLDADQFQ 255
Cdd:cd07575  240 EKFPFLKDADSFT 252
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-257 8.07e-93

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 273.93  E-value: 8.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   1 MPTLTLALVQSSLHWLDKSANLANFTEQLNSFNeQVDLIVLPETFATGFTINLDCSEPEQGEVLSWLKATAKQKNAVVAG 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGIT-GRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  81 SVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDVM 160
Cdd:PRK10438  80 SVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 161 INVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQSGIIIQRLEKSPLDD 240
Cdd:PRK10438 160 LYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQE 239

                        250
                 ....*....|....*..
gi 968558930 241 FRRAFPAHLDADQFQLL 257
Cdd:PRK10438 240 YREKFPAWRDADEFTLR 256
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-254 7.16e-61

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 192.77  E-value: 7.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   3 TLTLALVQSSLHWLDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGFTINLDC----SEPEQGEVLSWLKATAKQKN-A 76
Cdd:COG0388    1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQgADLVVFPELFLTGYPPEDDDllelAEPLDGPALAALAELARELGiA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  77 VVAGSVLVAKGDKKANRFYWVWPNGEVK-YYDKRHLFCLG--NEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRN 153
Cdd:COG0388   81 VVVGLPERDEGGRLYNTALVIDPDGEILgRYRKIHLPNYGvfDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 154 C--NDYDVMINVANWPAAR-RHVWDTLLKARAMENLCYVVGVNRIGADGNNVaHSGGTAVYDFKGDTLAKLEDDQsGIII 230
Cdd:COG0388  161 LalAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGEDGLV-FDGGSMIVDPDGEVLAEAGDEE-GLLV 238

                        250       260
                 ....*....|....*....|....
gi 968558930 231 QRLEKSPLDDFRRAFPAHLDADQF 254
Cdd:COG0388  239 ADIDLDRLREARRRFPVLRDRRPD 262
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-230 3.83e-28

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: 107.83  E-value: 3.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930    5 TLALVQSSLHWLDKSANLANfTEQL--NSFNEQVDLIVLPETFATGFTIN---LDCSEPEQGEVLSWLKATAKQKN-AVV 78
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQK-ALELieEAARYGADLIVLPELFITGYPCWahfLEAAEVGDGETLAGLAALARKNGiAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   79 AG-SVLVAKGDKKANRFYWVWPNGE-VKYYDKRHLFCLGNEGNFV-----AAGEQREIFAINDFRILPQVCYDLRFPVFQ 151
Cdd:pfam00795  80 IGlIERWLTGGRLYNTAVLLDPDGKlVGKYRKLHLFPEPRPPGFRervlfEPGDGGTVFDTPLGKIGAAICYEIRFPELL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  152 RNC--NDYDVMINVAN----WPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQ 225
Cdd:pfam00795 160 RALalKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWE 239


                  ....*
gi 968558930  226 SGIII 230
Cdd:pfam00795 240 EGVLI 244
de_GSH_amidase NF033621
deaminated glutathione amidase;
34-197 3.99e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 72.62  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  34 EQVDLIVLPET-FATGFT---INLDCSEPEQGEVLSWLKATAKQKNAVVAGSVLVAKGDKKANRFYWVWPNGE-VKYYDK 108
Cdd:NF033621  30 AGADLLVLPEAvLARDDTdpdLSVKSAQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDGRAWNTLVALRDGEiIAQYRK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 109 RHL---FCLgNEGNFVAAGEQ-REIFAINDFRILPQVCYDLRFPVFQRN--CNDYDVMINVANW---PAARRHvWDTLLK 179
Cdd:NF033621 110 LHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARRlaLDGADVLVLPAAWvrgPLKEHH-WETLLA 187

                        170       180
                 ....*....|....*....|...
gi 968558930 180 ARAMENLCYVVGV----NR-IGA 197
Cdd:NF033621 188 ARALENTCYMVAVgecgNRnIGQ 210
 
Name Accession Description Interval E-value
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
 4-255 3.55e-143

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: 401.15  E-value: 3.55e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQSSLHWLDKSANLANFTEQLNSFNEQVDLIVLPETFATGFTINLDC-SEPEQGEVLSWLKATAKQKNAVVAGSV 82
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEKTDLIVLPEMFTTGFSMNAEAlAEPMNGPTLQWMKAQAKKKGAAITGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  83 LVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDVMIN 162
Cdd:cd07575   81 IIKEGGKYYNRLYFVTPDGEVYHYDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 163 VANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQsGIIIQRLEKSPLDDFR 242
Cdd:cd07575  161 VANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNGLEYSGDSAVIDPLGEPLAEAEEDE-GVLTATLDKEALQEFR 239

                        250
                 ....*....|...
gi 968558930 243 RAFPAHLDADQFQ 255
Cdd:cd07575  240 EKFPFLKDADSFT 252
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
 1-257 8.07e-93

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 273.93  E-value: 8.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   1 MPTLTLALVQSSLHWLDKSANLANFTEQLNSFNeQVDLIVLPETFATGFTINLDCSEPEQGEVLSWLKATAKQKNAVVAG 80
Cdd:PRK10438   1 MSGLKITLLQQPLVWMDGPANLRHFDRQLEGIT-GRDVIVLPEMFTTGFAMEAAASSLPQDDVVAWMTAKAQQTNALIAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  81 SVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDVM 160
Cdd:PRK10438  80 SVALQTESGAVNRFLLVEPGGTVHFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFPVWSRNRNDYDLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 161 INVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQSGIIIQRLEKSPLDD 240
Cdd:PRK10438 160 LYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYRGDSRIINPQGEIIATAEPHQATRIDAELSLEALQE 239

                        250
                 ....*....|....*..
gi 968558930 241 FRRAFPAHLDADQFQLL 257
Cdd:PRK10438 240 YREKFPAWRDADEFTLR 256
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-250 3.72e-67

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: 208.55  E-value: 3.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLA---NFTEQLNSfnEQVDLIVLPETFATGFT--INLDCSEPEQGEVLSWLKATAKQKNA-VV 78
Cdd:cd07583    1 KIALIQLDIVWGDPEANIErveSLIEEAAA--AGADLIVLPEMWNTGYFldDLYELADEDGGETVSFLSELAKKHGVnIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  79 AGSVLVAKGDKKANRFYWVWPNGEVKY-YDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFP-VFQRNCND 156
Cdd:cd07583   79 AGSVAEKEGGKLYNTAYVIDPDGELIAtYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPeLFRKLALE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 157 -YDVMINVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNvAHSGGTAVYDFKGDTLAKLEDDQsGIIIQRLEK 235
Cdd:cd07583  159 gAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGN-EFGGHSMVIDPWGEVLAEAGEEE-EILTAEIDL 236

                        250
                 ....*....|....*
gi 968558930 236 SPLDDFRRAFPAHLD 250
Cdd:cd07583  237 EEVAEVRKKIPVFKD 251
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-254 7.16e-61

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 192.77  E-value: 7.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   3 TLTLALVQSSLHWLDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGFTINLDC----SEPEQGEVLSWLKATAKQKN-A 76
Cdd:COG0388    1 TMRIALAQLNPTVGDIEANLAKIEELIREAAAQgADLVVFPELFLTGYPPEDDDllelAEPLDGPALAALAELARELGiA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  77 VVAGSVLVAKGDKKANRFYWVWPNGEVK-YYDKRHLFCLG--NEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRN 153
Cdd:COG0388   81 VVVGLPERDEGGRLYNTALVIDPDGEILgRYRKIHLPNYGvfDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 154 C--NDYDVMINVANWPAAR-RHVWDTLLKARAMENLCYVVGVNRIGADGNNVaHSGGTAVYDFKGDTLAKLEDDQsGIII 230
Cdd:COG0388  161 LalAGADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGEDGLV-FDGGSMIVDPDGEVLAEAGDEE-GLLV 238

                        250       260
                 ....*....|....*....|....
gi 968558930 231 QRLEKSPLDDFRRAFPAHLDADQF 254
Cdd:COG0388  239 ADIDLDRLREARRRFPVLRDRRPD 262
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 6-250 2.41e-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: 183.29  E-value: 2.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   6 LALVQSSLHWLDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGF-----TINLDCSEPEQGEVLSWLKATAKQKNAVVA 79
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQgADLIVLPELFLTGYsfesaKEDLDLAEELDGPTLEALAELAKELGIYIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  80 GSVLVAKGDKKANRFYWVWPNGE-VKYYDKRHLFClGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQR--NCND 156
Cdd:cd07197   81 AGIAEKDGDKLYNTAVVIDPDGEiIGKYRKIHLFD-FGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARelALKG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 157 YDVMINVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHsGGTAVYDFKGDTLAKLEdDQSGIIIQRLEKS 236
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFA-GGSMIVDPDGEVLAEAS-EEEGILVAELDLD 237

                        250
                 ....*....|....
gi 968558930 237 PLDDFRRAFPAHLD 250
Cdd:cd07197  238 ELREARKRWSYLRD 251
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 5-247 4.58e-34

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: 123.69  E-value: 4.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQ-SSLHwlDKSANLANFTEQLNSFNEQ-VDLIVLPETFAT-----GFTINLDcSEPEQGEVLSWLKATAKQKN-A 76
Cdd:cd07572    1 RVALIQmTSTA--DKEANLARAKELIEEAAAQgAKLVVLPECFNYpggtdAFKLALA-EEEGDGPTLQALSELAKEHGiW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  77 VVAGSV--LVAKGDKKANRFYWVWPNGE-VKYYDKRHLF--CLGN-----EGNFVAAGEQREIFAINDFRILPQVCYDLR 146
Cdd:cd07572   78 LVGGSIpeRDDDDGKVYNTSLVFDPDGElVARYRKIHLFdvDVPGgisyrESDTLTPGDEVVVVDTPFGKIGLGICYDLR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 147 FPVF-----QRNCndyDVMINvanwPAA------RRHvWDTLLKARAMENLCYVVGVNRIGADGNN-VAHsGGTAVYDFK 214
Cdd:cd07572  158 FPELaralaRQGA---DILTV----PAAftmttgPAH-WELLLRARAIENQCYVVAAAQAGDHEAGrETY-GHSMIVDPW 228

                        250       260       270
                 ....*....|....*....|....*....|...
gi 968558930 215 GDTLAKLEDDQsGIIIQRLEKSPLDDFRRAFPA 247
Cdd:cd07572  229 GEVLAEAGEGE-GVVVAEIDLDRLEEVRRQIPV 260
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-246 5.91e-30

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: 112.46  E-value: 5.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLANFTEQL-NSFNEQVDLIVLPETFATGFTINL------DCSEPEQGEVLSWLKATAKQKNA- 76
Cdd:cd07584    1 KVALIQMDSVLGDVKANLKKAAELCkEAAAEGADLICFPELATTGYRPDLlgpklwELSEPIDGPTVRLFSELAKELGVy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  77 VVAGsvLVAKGDKkANRFY---WVW-PNGEVK-YYDKRHLFclGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQ 151
Cdd:cd07584   81 IVCG--FVEKGGV-PGKVYnsaVVIdPEGESLgVYRKIHLW--GLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 152 R--NCNDYDVMINVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHsGGTAVYDFKGDTLAKLEDDQSGII 229
Cdd:cd07584  156 RilTLKGAEVIFCPSAWREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVLF-GKSKILNPRGQVLAEASEEAEEIL 234

                        250
                 ....*....|....*..
gi 968558930 230 IQRLEKSPLDDFRRAFP 246
Cdd:cd07584  235 YAEIDLDAIADYRMTLP 251
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 5-230 3.83e-28

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: 107.83  E-value: 3.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930    5 TLALVQSSLHWLDKSANLANfTEQL--NSFNEQVDLIVLPETFATGFTIN---LDCSEPEQGEVLSWLKATAKQKN-AVV 78
Cdd:pfam00795   1 RVALVQLPQGFWDLEANLQK-ALELieEAARYGADLIVLPELFITGYPCWahfLEAAEVGDGETLAGLAALARKNGiAIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   79 AG-SVLVAKGDKKANRFYWVWPNGE-VKYYDKRHLFCLGNEGNFV-----AAGEQREIFAINDFRILPQVCYDLRFPVFQ 151
Cdd:pfam00795  80 IGlIERWLTGGRLYNTAVLLDPDGKlVGKYRKLHLFPEPRPPGFRervlfEPGDGGTVFDTPLGKIGAAICYEIRFPELL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  152 RNC--NDYDVMINVAN----WPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLEDDQ 225
Cdd:pfam00795 160 RALalKGAEILINPSArapfPGSLGPPQWLLLARARALENGCFVIAANQVGGEEDAPWPYGHSMIIDPDGRILAGAGEWE 239


                  ....*
gi 968558930  226 SGIII 230
Cdd:pfam00795 240 EGVLI 244
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 7-246 4.03e-28

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: 107.66  E-value: 4.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   7 ALVQ--SSLhwlDKSANLANFTEQLN-SFNEQVDLIVLPETFATGFTINLDC----SEPEQGEVLSWLKATAKQ-KNAVV 78
Cdd:cd07581    2 ALAQfaSSG---DKEENLEKVRRLLAeAAAAGADLVVFPEYTMARFGDGLDDyarvAEPLDGPFVSALARLARElGITVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  79 AGSVLVAKGDKKANRFYWVWPNGEVK-YYDKRHLF-CLG-NEGNFVAAGEQRE--IFAINDFRILPQVCYDLRFP-VFQR 152
Cdd:cd07581   79 AGMFEPAGDGRVYNTLVVVGPDGEIIaVYRKIHLYdAFGfRESDTVAPGDELPpvVFVVGGVKVGLATCYDLRFPeLARA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 153 NC-NDYDVMINVANW---PAARRHvWDTLLKARAMENLCYVVGVNRIGADGnnvahSGGTAVYDFKGDTLAKLEDDQsGI 228
Cdd:cd07581  159 LAlAGADVIVVPAAWvagPGKEEH-WETLLRARALENTVYVAAAGQAGPRG-----IGRSMVVDPLGVVLADLGERE-GL 231

                        250
                 ....*....|....*...
gi 968558930 229 IIQRLEKSPLDDFRRAFP 246
Cdd:cd07581  232 LVADIDPERVEEAREALP 249
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 5-230 6.06e-26

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: 101.99  E-value: 6.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLANfTEQLnSFNEQVDLIVLPETFATGFTIN-----LDCSEP-EQGEVLSWLKATAKQKNAVV 78
Cdd:cd07577    1 KVGYVQFNPKFGEVEKNLKK-VESL-IKGVEADLIVLPELFNTGYAFTskeevASLAESiPDGPTTRFLQELARETGAYI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  79 AGSVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFclGNEGNFVAAGEQR-EIFAINDFRILPQVCYDLRFPVFQRN--CN 155
Cdd:cd07577   79 VAGLPERDGDKFYNSAVVVGPEGYIGIYRKTHLF--YEEKLFFEPGDTGfRVFDIGDIRIGVMICFDWYFPEAARTlaLK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 156 DYDVMINVANW--PAARRhvwdtLLKARAMENLCYVVGVNRIGAD---GNNVAHSGGTAVYDFKGDTLAKLEDDQSGIII 230
Cdd:cd07577  157 GADIIAHPANLvlPYCPK-----AMPIRALENRVFTITANRIGTEergGETLRFIGKSQITSPKGEVLARAPEDGEEVLV 231
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 5-250 1.34e-22

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: 93.03  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGFTINLDC---SEPEQGEVLSWLKATAKQKN-AVVA 79
Cdd:cd07576    1 RLALYQGPARDGDVAANLARLDEAAARAAAAgADLLVFPELFLTGYNIGDAVarlAEPADGPALQALRAIARRHGiAIVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  80 GSVLVAKGdkkanRFY----WVWPNGEV-KYYDKRHLFcLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFP-----V 149
Cdd:cd07576   81 GYPERAGG-----AVYnaavLIDEDGTVlANYRKTHLF-GDSERAAFTPGDRFPVVELRGLRVGLLICYDVEFPelvraL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 150 FQRNCndyDVMI----NVANWPaarrHVWDTLLKARAMENLCYVVGVNRIGADGnNVAHSGGTAVYDFKGDTLAKLEDDQ 225
Cdd:cd07576  155 ALAGA---DLVLvptaLMEPYG----FVARTLVPARAFENQIFVAYANRCGAED-GLTYVGLSSIAGPDGTVLARAGRGE 226

                        250       260
                 ....*....|....*....|....*
gi 968558930 226 sGIIIQRLEKSPLDDFRRAFPaHLD 250
Cdd:cd07576  227 -ALLVADLDPAALAAARRENP-YLA 249
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 6-238 9.37e-22

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: 90.84  E-value: 9.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   6 LALVQSSLHWLDKSANLA---NFTEQLNSfnEQVDLIVLPETFATGFT--INLDCSEPE-QGEVLSWLKATAKQKNAVVA 79
Cdd:cd07585    2 IALVQFEARVGDKARNLAviaRWTRKAAA--QGAELVCFPEMCITGYThvRALSREAEVpDGPSTQALSDLARRYGLTIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  80 GSVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEgnFVAAGEQREIFAINDFRILPQVCYDLRFPVFQRNCNDYDV 159
Cdd:cd07585   80 AGLIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFRREHP--YIAAGDEYPVFATPGVRFGILICYDNHFPENVRATALLGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 160 MINVA------NWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVaHSGGTAVYDFKGDTLAKLEDDQSGIIIQRL 233
Cdd:cd07585  158 EILFAphatpgTTSPKGREWWMRWLPARAYDNGVFVAACNGVGRDGGEV-FPGGAMILDPYGRVLAETTSGGDGMVVADL 236


                 ....*
gi 968558930 234 EKSPL 238
Cdd:cd07585  237 DLDLI 241
de_GSH_amidase NF033621
deaminated glutathione amidase;
34-197 3.99e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 72.62  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  34 EQVDLIVLPET-FATGFT---INLDCSEPEQGEVLSWLKATAKQKNAVVAGSVLVAKGDKKANRFYWVWPNGE-VKYYDK 108
Cdd:NF033621  30 AGADLLVLPEAvLARDDTdpdLSVKSAQPLDGPFLTQLLAESRGNDLTTVLTVHVPSGDGRAWNTLVALRDGEiIAQYRK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 109 RHL---FCLgNEGNFVAAGEQ-REIFAINDFRILPQVCYDLRFPVFQRN--CNDYDVMINVANW---PAARRHvWDTLLK 179
Cdd:NF033621 110 LHLydaFSM-QESRRVDAGNEiPPLVEVAGMKVGLMTCYDLRFPELARRlaLDGADVLVLPAAWvrgPLKEHH-WETLLA 187

                        170       180
                 ....*....|....*....|...
gi 968558930 180 ARAMENLCYVVGV----NR-IGA 197
Cdd:NF033621 188 ARALENTCYMVAVgecgNRnIGQ 210
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
2-229 1.61e-13

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 69.49  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   2 PTLTLALVQ----SSLHWL--DKSANLANFTEQ-LNSFNEQVDLIVLPETfATGFTINldcsepEQGEVLSWLKATAKQK 74
Cdd:COG0815  193 EPLRVALVQgnipQDLKWDpeQRREILDRYLDLtRELADDGPDLVVWPET-ALPFLLD------EDPDALARLAAAAREA 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  75 NA-VVAGSVLVakgDKKANRFY---WVW-PNGEVKY-YDKRHLFCLG------------------NEGNFVaAGEQREIF 130
Cdd:COG0815  266 GApLLTGAPRR---DGGGGRYYnsaLLLdPDGGILGrYDKHHLVPFGeyvplrdllrplipfldlPLGDFS-PGTGPPVL 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 131 AINDFRILPQVCYDLRFP--VFQRNCNDYDVMINVAN--W----PAARRHVWDTLLkaRAMENLCYVVgvnrigadgnNV 202
Cdd:COG0815  342 DLGGVRVGPLICYESIFPelVRDAVRAGADLLVNITNdaWfgdsIGPYQHLAIARL--RAIETGRPVV----------RA 409

                        250       260
                 ....*....|....*....|....*..
gi 968558930 203 AHSGGTAVYDFKGDTLAKLEDDQSGII 229
Cdd:COG0815  410 TNTGISAVIDPDGRVLARLPLFTRGVL 436
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 4-243 1.98e-13

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: 68.38  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQSSLHWLDksaNLANFTEQLNSFNEQV-----DLIVLPETFATGF--TINLDCSEPEQ---------GEVLSWL 67
Cdd:cd07574    1 VRVAAAQYPLRRYA---SFEEFAAKVEYWVAEAagygaDLLVFPEYFTMELlsLLPEAIDGLDEairalaaltPDYVALF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  68 KATAKQKNA-VVAGSVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFCLGNEGNFVAAGEQREIFAINDFRILPQVCYDLR 146
Cdd:cd07574   78 SELARKYGInIIAGSMPVREDGRLYNRAYLFGPDGTIGHQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICYDSE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 147 FPVFQRNCNDYDV-MINVANWPAARRHVWDTLL--KARAMENLCYVVGVNRIG-ADG--NNVAHSGGTAVY-----DFKG 215
Cdd:cd07574  158 FPELARALAEAGAdLLLVPSCTDTRAGYWRVRIgaQARALENQCYVVQSGTVGnAPWspAVDVNYGQAAVYtpcdfGFPE 237

                        250       260
                 ....*....|....*....|....*....
gi 968558930 216 D-TLAKLEDDQSGIIIQRLeksPLDDFRR 243
Cdd:cd07574  238 DgILAEGEPNTEGWLIADL---DLEALRR 263
PLN02798 PLN02798
nitrilase
 17-246 2.55e-13

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 67.85  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  17 DKSANLANFTEQLN-SFNEQVDLIVLPETFA-----TGFTINLdcSEPEQGEVLSWLKATAKQKNA-VVAGSVLVAKGD- 88
Cdd:PLN02798  23 DLAANFATCSRLAKeAAAAGAKLLFLPECFSfigdkDGESLAI--AEPLDGPIMQRYRSLARESGLwLSLGGFQEKGPDd 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  89 -KKANRFYWVWPNGEVK-YYDKRHLF-------CLGNEGNFVAAGEQreIFAIND--FRILPQVCYDLRFP-VFQ--RNC 154
Cdd:PLN02798 101 sHLYNTHVLIDDSGEIRsSYRKIHLFdvdvpggPVLKESSFTAPGKT--IVAVDSpvGRLGLTVCYDLRFPeLYQqlRFE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 155 NDYDVMInvanWPAARRHV-----WDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVYDFKGDTLAKLED-DQSGI 228
Cdd:PLN02798 179 HGAQVLL----VPSAFTKPtgeahWEVLLRARAIETQCYVIAAAQAGKHNEKRESYGHALIIDPWGTVVARLPDrLSTGI 254

                        250
                 ....*....|....*...
gi 968558930 229 IIQRLEKSPLDDFRRAFP 246
Cdd:PLN02798 255 AVADIDLSLLDSVRTKMP 272
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 4-233 1.34e-11

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: 63.00  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQS----SLHWLDKS-----ANLANFTEQLNsfNEQVDLIVLPETfAtgftinLDCSEPEQGEVLSWLKATAKQK 74
Cdd:cd07571    1 LRVALVQGnipqDEKWDPEQrqatlDRYLDLTRELA--DEKPDLVVWPET-A------LPFDLQRDPDALARLARAARAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  75 NA-VVAGSVLVAKGDKKA-NRFYWVWPNGEVK-YYDKRHL------------------FCLGNEGNFVAAGEQREIFAIN 133
Cdd:cd07571   72 GApLLTGAPRREPGGGRYyNSALLLDPGGGILgRYDKHHLvpfgeyvplrdllrflglLFDLPMGDFSPGTGPQPLLLGG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 134 DFRILPQVCYDLRFP-VFQRNCNDY-DVMINVAN--W----PAARRHvwdtLLKA--RAMENLCYVVgvnRigadgnnVA 203
Cdd:cd07571  152 GVRVGPLICYESIFPeLVRDAVRQGaDLLVNITNdaWfgdsAGPYQH----LAMArlRAIETGRPLV---R-------AA 217

                        250       260       270
                 ....*....|....*....|....*....|
gi 968558930 204 HSGGTAVYDFKGDTLAKLEDDQSGIIIQRL 233
Cdd:cd07571  218 NTGISAVIDPDGRIVARLPLFEAGVLVAEV 247
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
 2-229 5.73e-11

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 61.82  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   2 PTLTLALVQ----SSLHWLDKS--ANLANFTEQLNSFNEQVDLIVLPETFATGFTinldcsEPEQGEVLSWLKATAKQKN 75
Cdd:PRK00302 218 PALKVALVQgnipQSLKWDPAGleATLQKYLDLSRPALGPADLIIWPETAIPFLL------EDLPQAFLKALDDLAREKG 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  76 -AVVAGSVLVAKGDKKA---NRFYWVWPNGEVKYYDKRHL------------------FCLGNEGNFVAAGEQREIFAIN 133
Cdd:PRK00302 292 sALITGAPRAENKQGRYdyyNSIYVLGPYGILNRYDKHHLvpfgeyvplesllrplapFFNLPMGDFSRGPYVQPPLLAK 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 134 DFRILPQVCYDLRFP--VFQRNCNDYDVMINVAN--W----PAARRHvwdtLLKA--RAMENLCYVVgvnRigadgnnVA 203
Cdd:PRK00302 372 GLKLAPLICYEIIFPeeVRANVRQGADLLLNISNdaWfgdsIGPYQH----FQMArmRALELGRPLI---R-------AT 437

                        250       260
                 ....*....|....*....|....*.
gi 968558930 204 HSGGTAVYDFKGDTLAKLEDDQSGII 229
Cdd:PRK00302 438 NTGITAVIDPLGRIIAQLPQFTEGVL 463
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-252 1.19e-10

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: 59.99  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGFTIN---LDCSEPEQGEVLSWLkATAKQKNAVVAG 80
Cdd:cd07586    1 RVAIAQIDPVLGDVEENLEKHLEIIETARERgADLVVFPELSLTGYNLGdlvYEVAMHADDPRLQAL-AEASGGICVVFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  81 SV-LVAKGdkkanRFY---WVWPNGEVK-YYDKRHLFCLG--NEGNFVAAGEQREIFAINDFRILPQVCYDLRFP--VFQ 151
Cdd:cd07586   80 FVeEGRDG-----RFYnsaAYLEDGRVVhVHRKVYLPTYGlfEEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPslPYL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 152 RNCNDYDVMINVANWPA---ARRH----VWDTLLKARAMENLCYVVGVNRIGADGnNVAHSGGTAVYDFKGDTLAKLEDD 224
Cdd:cd07586  155 LALDGADVIFIPANSPArgvGGDFdneeNWETLLKFYAMMNGVYVVFANRVGVED-GVYFWGGSRVVDPDGEVVAEAPLF 233

                        250       260
                 ....*....|....*....|....*...
gi 968558930 225 QSGIIIQRLEKSPLDDFRRAFPAHLDAD 252
Cdd:cd07586  234 EEDLLVAELDRSAIRRARFFSPTFRDED 261
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 5-244 7.65e-10

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: 57.74  E-value: 7.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   5 TLALVQSSLHWLDKSANLANFTEQLN-SFNEQVDLIVLPETFATGFT------INLDCSEPEQGEVLSWLKATAKQKNAV 77
Cdd:cd07580    1 RVACVQFDPRVGDLDANLARSIELIReAADAGANLVVLPELANTGYVfesrdeAFALAEEVPDGASTRAWAELAAELGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  78 VAGSVLVAKGDKKANRFYWVWPNGEVKYYDKRHLFclGNEGNFVAAGEQR-EIFAINDFRILPQVCYDLRFPVFQRNC-- 154
Cdd:cd07580   81 IVAGFAERDGDRLYNSAVLVGPDGVIGTYRKAHLW--NEEKLLFEPGDLGlPVFDTPFGRIGVAICYDGWFPETFRLLal 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 155 NDYDVMINVANWP------AARRHVWDTLLKARAMENLCYVVGVNRIGADgNNVAHSGGTAVYDFKGDTLAKLE-DDQSG 227
Cdd:cd07580  159 QGADIVCVPTNWVpmprppEGGPPMANILAMAAAHSNGLFIACADRVGTE-RGQPFIGQSLIVGPDGWPLAGPAsGDEEE 237

                        250
                 ....*....|....*..
gi 968558930 228 IIIQRLeksPLDDFRRA 244
Cdd:cd07580  238 ILLADI---DLTAARRK 251
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
 99-243 3.55e-09

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: 56.14  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  99 PNGEVK-YYDKRHLFC------LGNEGNFVAAGEQREIFAINdfrilpqVCYDLRFPVFQRNC--NDYDVMINVANWPAA 169
Cdd:cd07565  110 DQGEIVlKYRKLHPWVpiepwyPGDLGTPVCEGPKGSKIALI-------ICHDGMYPEIARECayKGAELIIRIQGYMYP 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 968558930 170 RRHVWDTLLKARAMENLCYVVGVNRIGADGnNVAHSGGTAVYDFKGDTLAKLEDDQSGIIIQRLEKSPLDDFRR 243
Cdd:cd07565  183 AKDQWIITNKANAWCNLMYTASVNLAGFDG-VFSYFGESMIVNFDGRTLGEGGREPDEIVTAELSPSLVRDARK 255
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 4-246 5.99e-07

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: 49.48  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930   4 LTLALVQSSLHWlDKSANLANFTEQLNSFNEQ-VDLIVLPETFATGF------TINLDCSEP-EQGEVLSWLKATAKQKN 75
Cdd:cd07573    1 VTVALVQMACSE-DPEANLAKAEELVREAAAQgAQIVCLQELFETPYfcqeedEDYFDLAEPpIPGPTTARFQALAKELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  76 AVVAGSVLvakgDKKANRFYW-----VWPNGEV-------------KYYDKrHLFCLGNEGnFvaageqrEIFAINDFRI 137
Cdd:cd07573   80 VVIPVSLF----EKRGNGLYYnsavvIDADGSLlgvyrkmhipddpGYYEK-FYFTPGDTG-F-------KVFDTRYGRI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 138 LPQVCYDLRFPVFQRNC--NDYDVMI---------NVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGA---DGNNVA 203
Cdd:cd07573  147 GVLICWDQWFPEAARLMalQGAEILFyptaigsepQEPPEGLDQRDAWQRVQRGHAIANGVPVAAVNRVGVegdPGSGIT 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 968558930 204 HSGGTAVYDFKGDTLAKLEDDQSGIIIQRLEKSPLDDFRRAFP 246
Cdd:cd07573  227 FYGSSFIADPFGEILAQASRDEEEILVAEFDLDEIEEVRRAWP 269
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 36-220 9.40e-07

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: 48.88  E-value: 9.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  36 VDLIVLPETFATGFT--------------INLDCSEPEQgevlswLKATAKQKNAVVAGSVLVAKGDKKANRF---YWVW 98
Cdd:cd07582   43 VRLVVLPEYALQGFPmgeprevwqfdkaaIDIPGPETEA------LGEKAKELNVYIAANAYERDPDFPGLYFntaFIID 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  99 PNGEV--KYYDKRHLFCLGN--------EGNFVAAGEQREIFAINDF---RILPQVCYDLRFPVFQRNC--NDYDVMIN- 162
Cdd:cd07582  117 PSGEIilRYRKMNSLAAEGSpsphdvwdEYIEVYGYGLDALFPVADTeigNLGCLACEEGLYPEVARGLamNGAEVLLRs 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 968558930 163 VANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHS---GGTAVYDFKGDTLAK 220
Cdd:cd07582  197 SSEVPSVELDPWEIANRARALENLAYVVSANSGGIYGSPYPADsfgGGSMIVDYKGRVLAE 257
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 17-239 2.30e-06

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: 47.55  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  17 DKSANLANFTEQLNSFN-EQVDLIVLPETFATGFTINLDCSEPEQGEVLSWLKATA-KQKNAVVAGsVLVAKGDKKANRF 94
Cdd:cd07579   12 DIAGNLATIDRLAAEAKaTGAELVVFPELALTGLDDPASEAESDTGPAVSALRRLArRLRLYLVAG-FAEADGDGLYNSA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  95 YWVWPNGEVKYYDKRHLfcLGNEGNFVAAGEQREIFAINDFRILPQVCYDLRFPVFQR-----NCNDYDVMINVA----- 164
Cdd:cd07579   91 VLVGPEGLVGTYRKTHL--IEPERSWATPGDTWPVYDLPLGRVGLLIGHDALFPEAGRvlalrGCDLLACPAAIAipfvg 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 165 ---------NWPA---ARRHVWDtLLKARAMENLCYVVGVNRIGADGnnvAHSGGTAVydFKGDTLA-----KLEDDQSG 227
Cdd:cd07579  169 ahagtsvpqPYPIptgADPTHWH-LARVRAGENNVYFAFANVPDPAR---GYTGWSGV--FGPDTFAfprqeAAIGDEEG 242

                        250
                 ....*....|..
gi 968558930 228 IIIQRLEKSPLD 239
Cdd:cd07579  243 IAWALIDTSNLD 254
PRK13981 PRK13981
NAD synthetase; Provisional
 33-237 6.89e-06

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 46.69  E-value: 6.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  33 NEQVDLIVLPETFATGFtinldcsEPE-----------QGEVLSWLKATAKQKNAVVAGSVLVAkGDKKANRfYWVWPNG 101
Cdd:PRK13981  31 DAGADLLLFPELFLSGY-------PPEdlllrpaflaaCEAALERLAAATAGGPAVLVGHPWRE-GGKLYNA-AALLDGG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 102 EVK-YYDKRHlfcLGNEGNF-----VAAGEQREIFAINDFRILPQVCYDLRF--PVFQRNCNDYDVMINVANWPAAR--R 171
Cdd:PRK13981 102 EVLaTYRKQD---LPNYGVFdekryFAPGPEPGVVELKGVRIGVPICEDIWNpePAETLAEAGAELLLVPNASPYHRgkP 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 968558930 172 HVWDTLLKARAMENLCYVVGVNRIGA------DGNNVahsggtaVYDFKGDTLAKLEDDQSGIIIQRLEKSP 237
Cdd:PRK13981 179 DLREAVLRARVRETGLPLVYLNQVGGqdelvfDGASF-------VLNADGELAARLPAFEEQIAVVDFDRGE 243
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 38-243 3.44e-05

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: 44.06  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  38 LIVLPETFATGFtinldC----------SEPEQGEVLSWLKATAKQKNA-VVAGSVLVakgDKKANRFY----WVWPNGE 102
Cdd:cd07578   36 LIVTPEMATTGY-----CwydraeiapfVEPIPGPTTARFAELAREHDCyIVVGLPEV---DSRSGIYYnsavLIGPSGV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 103 VKYYDKRHLFClgNEGNFVAAGEQ-REIFAINDFRILPQVCYDLRF--PVFQRNCNDYDVMINVANWPAARR--HVWdtl 177
Cdd:cd07578  108 IGRHRKTHPYI--SEPKWAADGDLgHQVFDTEIGRIALLICMDIHFfeTARLLALGGADVICHISNWLAERTpaPYW--- 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 968558930 178 lKARAMENLCYVVGVNRIGADgNNVAHSGGTAVYDFKGDTLAKLeDDQSGIIIQRLEkspLDDFRR 243
Cdd:cd07578  183 -INRAFENGCYLIESNRWGLE-RGVQFSGGSCIIEPDGTIQASI-DSGDGVALGEID---LDRARH 242
amiF PRK13287
formamidase; Provisional
 141-219 9.66e-05

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 42.76  E-value: 9.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930 141 VCYDLRFPVFQRNCNdY---DVMINVANWPAARRHVWDTLLKARAMENLCYVVGVNRIGADGNNVAHSGGTAVyDFKGDT 217
Cdd:PRK13287 164 ICHDGMFPEMAREAA-YkgaNVMIRISGYSTQVREQWILTNRSNAWQNLMYTASVNLAGYDGVFYYFGEGQVC-NFDGTT 241


                 ..
gi 968558930 218 LA 219
Cdd:PRK13287 242 LV 243
PRK12291 PRK12291
apolipoprotein N-acyltransferase; Reviewed
 24-143 2.14e-04

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 237042 [Multi-domain]  Cd Length: 418  Bit Score: 41.89  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 968558930  24 NFTEQLNSFNEQVDLIVLPEtfaTGFTINLDCSEpeqgevlsWLKATAKQKN---AVVAGSvLVAKGDKKANRFYwVWPN 100
Cdd:PRK12291 222 NLKEIDKAIDEKKDLIVLPE---TAFPLALNNSP--------ILLDKLKELShkiTIITGA-LRVEDGHIYNSTY-IFSK 288

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 968558930 101 GEVKYYDKRHL-------------------FCLGNEGNFVAAGEQrEIFAINDFRILPQVCY 143
Cdd:PRK12291 289 GNVQIADKVILvpfgeeiplpkffkkpinkLFFGGASDFSKASKF-SDFTLDGVKFRNAICY 349
amiE PRK13286
aliphatic amidase;
166-243 2.39e-03

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 38.57  E-value: 2.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 968558930 166 WPAARRHVwdTLLKARAMENLCYVVGVNRIGADGNnVAHSGGTAVYDFKGDTLAKLEDDQSGIIIQRLEKSPLDDFRR 243
Cdd:PRK13286 194 YPAKEQQV--LVAKAMAWANNCYVAVANAAGFDGV-YSYFGHSAIIGFDGRTLGECGEEEMGIQYAQLSVSQIRDARR 268
 
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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