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Conserved domains on  [gi|515201419|ref|WP_016809275|]
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deaminated glutathione amidase [Klebsiella oxytoca]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
de_GSH_amidase NF033621
deaminated glutathione amidase;
3-261 0e+00

deaminated glutathione amidase;


:

Pssm-ID: 468114  Cd Length: 260  Bit Score: 522.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTVLT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  83 LHVPSAEGRATNTLVALRHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALS 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 163 GAQLIVLPAAWVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQ 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 515201419 243 QVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 242 HAREQLPVLENRRFAPPQL 260
 
Name Accession Description Interval E-value
de_GSH_amidase NF033621
deaminated glutathione amidase;
3-261 0e+00

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 522.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTVLT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  83 LHVPSAEGRATNTLVALRHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALS 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 163 GAQLIVLPAAWVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQ 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 515201419 243 QVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 242 HAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 4.48e-115

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: 330.31  E-value: 4.48e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTVLT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  83 LHVPSAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPL-IEVDGMRVGLMTCYDLRFPELALSLA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVvFVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 161 LSGAQLIVLPAAWVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDY 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 515201419 241 IQQVRERLPVLQNRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 4.58e-77

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 234.37  E-value: 4.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   1 MLVAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTT 79
Cdd:COG0388    2 MRIALAQLNPTVgDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  80 VLTLHVPSAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALS 158
Cdd:COG0388   82 VVGLPERDEGGRLYNTALVIdPDGEILGRYRKIHLPNYGVFDEKRYFTPGDE-LVVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 159 LALSGAQLIVLPAAWVKGPlKEHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTIAGAGEQPQLIFA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGR-GKDHWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 515201419 235 ELSTDYIQQVRERLPVLQNRRF 256
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRP 261
PLN02798 PLN02798
nitrilase
3-258 1.69e-41

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 143.73  E-value: 1.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPE--ALLARNDADadlSVKSAQQLDGGFLQLL--LAESENSPLT 78
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQRYrsLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  79 TVLTLHVPSAEGRATNTLVALRH-GKIITQYQKLHLYD-----AFNIQESRLVDAGQQIpplIEVDGM--RVGLMTCYDL 150
Cdd:PLN02798  90 LGGFQEKGPDDSHLYNTHVLIDDsGEIRSSYRKIHLFDvdvpgGPVLKESSFTAPGKTI---VAVDSPvgRLGLTVCYDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 151 RFPELALSLALS-GAQLIVLPAAWVKgPLKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTIAG 224
Cdd:PLN02798 167 RFPELYQQLRFEhGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWGTVVAR 245
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515201419 225 AGE--QPQLIFAELSTDYIQQVRERLPVLQNRRFAP 258
Cdd:PLN02798 246 LPDrlSTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-245 1.91e-34

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: 124.39  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419    2 LVAAGQFAVT-PDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLsVKSAQQLDGGFLQLLLAES-ENSPLTT 79
Cdd:pfam00795   1 RVALVQLPQGfWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHF-LEAAEVGDGETLAGLAALArKNGIAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   80 VLTLHVPSAEGRATNTLVALRH-GKIITQYQKLHLYDAFNIQ---ESRLVDAGQQIPPlIEVDGMRVGLMTCYDLRFPEL 155
Cdd:pfam00795  80 IGLIERWLTGGRLYNTAVLLDPdGKLVGKYRKLHLFPEPRPPgfrERVLFEPGDGGTV-FDTPLGKIGAAICYEIRFPEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  156 ALSLALSGAQLIVLPAA--WVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTIAGAGEQ 228
Cdd:pfam00795 159 LRALALKGAEILINPSAraPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGEW 238
                         250
                  ....*....|....*...
gi 515201419  229 P-QLIFAELSTDYIQQVR 245
Cdd:pfam00795 239 EeGVLIADIDLALVRAWR 256
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
22-221 2.24e-09

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 56.98  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   22 VSMMRQAGERgATLLVLPEALLArndadADLSvKSAQQLDGGFLQLLLaeSENSPLTTVLTLHVPSAEGRATNTLVAL-R 100
Cdd:TIGR00546 188 TSLTKQAVEK-PDLVVWPETAFP-----FDLE-NSPQKLADRLKLLVL--SKGIPILIGAPDAVPGGPYHYYNSAYLVdP 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  101 HGKIITQYQKLHL----------------YDAFNIQESRLVDAGQQIPPLiEVDGMRVGLMTCYDLRFPELALSLALSGA 164
Cdd:TIGR00546 259 GGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLLSQEDFSRGPGPQVL-KLPGGKIAPLICYESIFPDLVRASARQGA 337
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515201419  165 QLIVLPA--AWVKGP--LKEHHWATLLAARALDTTCYIVAagecgtrNIGQSRIVDPLGTT 221
Cdd:TIGR00546 338 ELLVNLTndAWFGDSsgPWQHFALARFRAIENGRPLVRAT-------NTGISAVIDPRGRT 391
 
Name Accession Description Interval E-value
de_GSH_amidase NF033621
deaminated glutathione amidase;
3-261 0e+00

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 522.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTVLT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  83 LHVPSAEGRATNTLVALRHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALS 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 163 GAQLIVLPAAWVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQ 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 515201419 243 QVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 242 HAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 4.48e-115

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: 330.31  E-value: 4.48e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTVLT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  83 LHVPSAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPL-IEVDGMRVGLMTCYDLRFPELALSLA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVvFVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 161 LSGAQLIVLPAAWVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDY 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 515201419 241 IQQVRERLPVLQNRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 4.58e-77

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 234.37  E-value: 4.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   1 MLVAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTT 79
Cdd:COG0388    2 MRIALAQLNPTVgDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  80 VLTLHVPSAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALS 158
Cdd:COG0388   82 VVGLPERDEGGRLYNTALVIdPDGEILGRYRKIHLPNYGVFDEKRYFTPGDE-LVVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 159 LALSGAQLIVLPAAWVKGPlKEHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTIAGAGEQPQLIFA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGR-GKDHWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 515201419 235 ELSTDYIQQVRERLPVLQNRRF 256
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRP 261
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
2-255 2.16e-71

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: 219.61  E-value: 2.16e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   2 LVAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPE--ALLARNDAdadlsvksaqqldggFLQLLLAESENSPLTT 79
Cdd:cd07572    1 RVALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPEcfNYPGGTDA---------------FKLALAEEEGDGPTLQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  80 VL--------------TLHVPSA-EGRATNTLVAL-RHGKIITQYQKLHLYDaFNI------QESRLVDAGQQIPPlIEV 137
Cdd:cd07572   66 ALselakehgiwlvggSIPERDDdDGKVYNTSLVFdPDGELVARYRKIHLFD-VDVpggisyRESDTLTPGDEVVV-VDT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 138 DGMRVGLMTCYDLRFPELALSLALSGAQLIVLPAA--WVKGPLkehHWATLLAARALDTTCYIVAAGECGTRNI-----G 210
Cdd:cd07572  144 PFGKIGLGICYDLRFPELARALARQGADILTVPAAftMTTGPA---HWELLLRARAIENQCYVVAAAQAGDHEAgretyG 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 515201419 211 QSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07572  221 HSMIVDPWGEVLAEAGEGEGVVVAEIDLDRLEEVRRQIPVLKHRR 265
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 5.54e-61

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: 192.75  E-value: 5.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPEalLARNDADADLSVKSAQQLDGGFLQLL--LAESENspltt 79
Cdd:cd07583    2 IALIQLDIVWgDPEANIERVESLIEEAAAAGADLIVLPE--MWNTGYFLDDLYELADEDGGETVSFLseLAKKHG----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  80 vLTLH----VPSAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNiqESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPE 154
Cdd:cd07583   75 -VNIVagsvAEKEGGKLYNTAYVIdPDGELIATYRKIHLFGLMG--EDKYLTAGDE-LEVFELDGGKVGLFICYDLRFPE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 155 LALSLALSGAQLIVLPAAWvkgPLK-EHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTIAGAGEQP 229
Cdd:cd07583  151 LFRKLALEGAEILFVPAEW---PAArIEHWRTLLRARAIENQAFVVACNRVGTdggnEFGGHSMVIDPWGEVLAEAGEEE 227
                        250       260
                 ....*....|....*....|....*.
gi 515201419 230 QLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07583  228 EILTAEIDLEEVAEVRKKIPVFKDRR 253
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
3-255 2.08e-58

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: 186.38  E-value: 2.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPE-ALLARNDADADLSVKSAQQLDGGFLQLLLAESENSPLTTV 80
Cdd:cd07197    1 IAAVQLAPKIgDVEANLAKALRLIKEAAEQGADLIVLPElFLTGYSFESAKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  81 LTLHVpSAEGRATNTLVAL-RHGKIITQYQKLHLydaFNIQESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALSL 159
Cdd:cd07197   81 AGIAE-KDGDKLYNTAVVIdPDGEIIGKYRKIHL---FDFGERRYFSPGDE-FPVFDTPGGKIGLLICYDLRFPELAREL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 160 ALSGAQLIVLPAAWVKGPLkeHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTIAGAGEQPQLIFAE 235
Cdd:cd07197  156 ALKGADIILVPAAWPTARR--EHWELLLRARAIENGVYVVAANRVGEegglEFAGGSMIVDPDGEVLAEASEEEGILVAE 233
                        250       260
                 ....*....|....*....|
gi 515201419 236 LSTDYIQQVRERLPVLQNRR 255
Cdd:cd07197  234 LDLDELREARKRWSYLRDRR 253
PLN02798 PLN02798
nitrilase
3-258 1.69e-41

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 143.73  E-value: 1.69e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPE--ALLARNDADadlSVKSAQQLDGGFLQLL--LAESENSPLT 78
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQRYrsLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  79 TVLTLHVPSAEGRATNTLVALRH-GKIITQYQKLHLYD-----AFNIQESRLVDAGQQIpplIEVDGM--RVGLMTCYDL 150
Cdd:PLN02798  90 LGGFQEKGPDDSHLYNTHVLIDDsGEIRSSYRKIHLFDvdvpgGPVLKESSFTAPGKTI---VAVDSPvgRLGLTVCYDL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 151 RFPELALSLALS-GAQLIVLPAAWVKgPLKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTIAG 224
Cdd:PLN02798 167 RFPELYQQLRFEhGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWGTVVAR 245
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515201419 225 AGE--QPQLIFAELSTDYIQQVRERLPVLQNRRFAP 258
Cdd:PLN02798 246 LPDrlSTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
26-257 1.97e-37

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: 132.32  E-value: 1.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  26 RQAGERGATLLVLPEALLARNDADADLsVKSAQQLDGGFLQLLLAESENSPLTTVLTLHVPSAEGRATNTLVALRHGKII 105
Cdd:cd07576   26 ARAAAAGADLLVFPELFLTGYNIGDAV-ARLAEPADGPALQALRAIARRHGIAIVVGYPERAGGAVYNAAVLIDEDGTVL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 106 TQYQKLHLYDAFniqESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVLPAAWVKGPLKEHHwaT 185
Cdd:cd07576  105 ANYRKTHLFGDS---ERAAFTPGDR-FPVVELRGLRVGLLICYDVEFPELVRALALAGADLVLVPTALMEPYGFVAR--T 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515201419 186 LLAARALDTTCYIVAAGECGTRN----IGQSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQQVRERLPVLQNRRFA 257
Cdd:cd07576  179 LVPARAFENQIFVAYANRCGAEDgltyVGLSSIAGPDGTVLARAGRGEALLVADLDPAALAAARRENPYLADRRPE 254
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-245 1.91e-34

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: 124.39  E-value: 1.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419    2 LVAAGQFAVT-PDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLsVKSAQQLDGGFLQLLLAES-ENSPLTT 79
Cdd:pfam00795   1 RVALVQLPQGfWDLEANLQKALELIEEAARYGADLIVLPELFITGYPCWAHF-LEAAEVGDGETLAGLAALArKNGIAIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   80 VLTLHVPSAEGRATNTLVALRH-GKIITQYQKLHLYDAFNIQ---ESRLVDAGQQIPPlIEVDGMRVGLMTCYDLRFPEL 155
Cdd:pfam00795  80 IGLIERWLTGGRLYNTAVLLDPdGKLVGKYRKLHLFPEPRPPgfrERVLFEPGDGGTV-FDTPLGKIGAAICYEIRFPEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  156 ALSLALSGAQLIVLPAA--WVKGPLKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTIAGAGEQ 228
Cdd:pfam00795 159 LRALALKGAEILINPSAraPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGEW 238
                         250
                  ....*....|....*...
gi 515201419  229 P-QLIFAELSTDYIQQVR 245
Cdd:pfam00795 239 EeGVLIADIDLALVRAWR 256
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 2.45e-32

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: 119.01  E-value: 2.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQF-AVTPDWTVNAQTCVSMMRQAGERGATLLVLPEalLARNDADADLSvksaqqldgGFLQLLLAESENSPLTTVL 81
Cdd:cd07584    2 VALIQMdSVLGDVKANLKKAAELCKEAAAEGADLICFPE--LATTGYRPDLL---------GPKLWELSEPIDGPTVRLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  82 T-------LHV--PSAE-----GRATNTLVA-LRHGKIITQYQKLHLYDafniQESRLVDAGQQIPpLIEVDGMRVGLMT 146
Cdd:cd07584   71 SelakelgVYIvcGFVEkggvpGKVYNSAVViDPEGESLGVYRKIHLWG----LEKQYFREGEQYP-VFDTPFGKIGVMI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 147 CYDLRFPELALSLALSGAQLIVLPAAWVKgpLKEHHWATLLAARALDTTCYIVAAGECG----TRNIGQSRIVDPLGTTI 222
Cdd:cd07584  146 CYDMGFPEVARILTLKGAEVIFCPSAWRE--QDADIWDINLPARALENTVFVAAVNRVGnegdLVLFGKSKILNPRGQVL 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 515201419 223 AGAG-EQPQLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07584  224 AEASeEAEEILYAEIDLDAIADYRMTLPYLKDRK 257
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 4.76e-27

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: 105.09  E-value: 4.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADLSvKSAQQLDGGFLQLLLAESENSPLTTVL 81
Cdd:cd07585    2 IALVQFEARVgDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALS-REAEVPDGPSTQALSDLARRYGLTILA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  82 TLhVPSAEGRATNTLVALRHGKIITQYQKLHLydaFNIQESRLVdAGQQIPpLIEVDGMRVGLMTCYDLRFPELALSLAL 161
Cdd:cd07585   81 GL-IEKAGDRPYNTYLVCLPDGLVHRYRKLHL---FRREHPYIA-AGDEYP-VFATPGVRFGILICYDNHFPENVRATAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 162 SGAQLIVLPAA--WVKGPLKEHHWATLLAARALDTTCYIVAAGECGtRNIGQSR-----IVDPLGTTIAGAGE-QPQLIF 233
Cdd:cd07585  155 LGAEILFAPHAtpGTTSPKGREWWMRWLPARAYDNGVFVAACNGVG-RDGGEVFpggamILDPYGRVLAETTSgGDGMVV 233
                        250       260
                 ....*....|....*....|....
gi 515201419 234 AELSTDYIQQVRER--LPVLQNRR 255
Cdd:cd07585  234 ADLDLDLINTVRGRrwISFLRARR 257
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
24-236 3.58e-25

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: 100.07  E-value: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  24 MMRQAGERGATLLVLPE------ALLARNDAdadlsVKSAQQLDGG----FLQLLlAESENSPLTTVLTLhvpSAEGRAT 93
Cdd:cd07577   21 VESLIKGVEADLIVLPElfntgyAFTSKEEV-----ASLAESIPDGpttrFLQEL-ARETGAYIVAGLPE---RDGDKFY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  94 NTLVALRHGKIITQYQKLHLYDAfniqESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVLPAAW 173
Cdd:cd07577   92 NSAVVVGPEGYIGIYRKTHLFYE----EKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPANL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515201419 174 VKgPlkehHWATLLAARALDTTCYIVAAGECGT--------RNIGQSRIVDPLGTTIAGAGEQ-PQLIFAEL 236
Cdd:cd07577  168 VL-P----YCPKAMPIRALENRVFTITANRIGTeerggetlRFIGKSQITSPKGEVLARAPEDgEEVLVAEI 234
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 1.40e-24

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: 98.96  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFA-VTPDWTVNAQTCVSMMRQAGERGATLLVLPEalLARN----DADADLSVKSAQQLDGGFLQLLLAESenSPL 77
Cdd:cd07580    2 VACVQFDpRVGDLDANLARSIELIREAADAGANLVVLPE--LANTgyvfESRDEAFALAEEVPDGASTRAWAELA--AEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  78 TTVLTLHVPSAEG-RATNTLVALRHGKIITQYQKLHLYDafniQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELA 156
Cdd:cd07580   78 GLYIVAGFAERDGdRLYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWFPETF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 157 LSLALSGAQLIVLPAAWVKGP-LKEHHWA---TLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTIAGA--G 226
Cdd:cd07580  154 RLLALQGADIVCVPTNWVPMPrPPEGGPPmanILAMAAAHSNGLFIACADRVGTergqPFIGQSLIVGPDGWPLAGPasG 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 515201419 227 EQPQLIFAELstDYIQQVRERL----PVLQNRR 255
Cdd:cd07580  234 DEEEILLADI--DLTAARRKRIwnsnDVLRDRR 264
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
3-255 1.01e-22

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: 94.17  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLAR---NDADADLSvKSAQQLDGG----FLQLLLAEsens 75
Cdd:cd07573    3 VALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPyfcQEEDEDYF-DLAEPPIPGpttaRFQALAKE---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  76 pLTTVLtlHVP----SAEGRATNTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDL 150
Cdd:cd07573   78 -LGVVI--PVSlfekRGNGLYYNSAVVIdADGSLLGVYRKMHIPDDPGYYEKFYFTPGDTGFKVFDTRYGRIGVLICWDQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 151 RFPELALSLALSGAQLIVLPAA--WV-----KGPLKEHHWATLLAARALDTTCYIVAAGECGTRNI--------GQSRIV 215
Cdd:cd07573  155 WFPEAARLMALQGAEILFYPTAigSEpqeppEGLDQRDAWQRVQRGHAIANGVPVAAVNRVGVEGDpgsgitfyGSSFIA 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 515201419 216 DPLGTTIAGAG-EQPQLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07573  235 DPFGEILAQASrDEEEILVAEFDLDEIEEVRRAWPFFRDRR 275
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
3-255 1.80e-20

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: 87.53  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPEA---------LLARNDAdadlsVKSAQQLdggfLQLLLAES 72
Cdd:cd07570    2 IALAQLNPTVgDLEGNAEKILEAIREAKAQGADLVVFPELsltgyppedLLLRPDF-----LEAAEEA----LEELAAAT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  73 ENSPLTTVLTLHVPSaEGRATNTLVALRHGKIITQYQKLHL--YDAFniQESRLVDAGQQiPPLIEVDGMRVGLMTCYDL 150
Cdd:cd07570   73 ADLDIAVVVGLPLRH-DGKLYNAAAVLQNGKILGVVPKQLLpnYGVF--DEKRYFTPGDK-PDVLFFKGLRIGVEICEDL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 151 RFPE-LALSLALSGAQLIVLPAA--WVKGplKEHHWATLLAARALDTTCYIV--AAGECGTRNI--GQSRIVDPLGTTIA 223
Cdd:cd07570  149 WVPDpPSAELALAGADLILNLSAspFHLG--KQDYRRELVSSRSARTGLPYVyvNQVGGQDDLVfdGGSFIADNDGELLA 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 515201419 224 gAGEQPQLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07570  227 -EAPRFEEDLADVDLDRLRSERRRNSSFLDEE 257
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
105-254 1.11e-19

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: 85.28  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 105 ITQYQKLHLydaFNI-QESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVlpAAWVKgpLKEHHW 183
Cdd:cd07575  101 VYHYDKRHL---FRMaGEHKVYTAGNE-RVIVEYKGWKILLQVCYDLRFPVWSRNTNDYDLLLYV--ANWPA--PRRAAW 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515201419 184 ATLLAARALDTTCYIVAAGECGT-----RNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDYIQQVRERLPVLQNR 254
Cdd:cd07575  173 DTLLKARAIENQAYVIGVNRVGTdgnglEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDKEALQEFREKFPFLKDA 248
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 2.84e-19

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143610  Cd Length: 269  Bit Score: 84.26  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTP-DWTVNAQTCVSMMRQAGERGATLLVLPE-ALLARNDADADLSVksAQQLDGGFLQLLLAESENspLTTV 80
Cdd:cd07586    2 VAIAQIDPVLgDVEENLEKHLEIIETARERGADLVVFPElSLTGYNLGDLVYEV--AMHADDPRLQALAEASGG--ICVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  81 LTLHVPSAEGRATNTLVALRHGKIITQYQKLHL--YDAFniQESRLVDAGQQIPPLiEVDGMRVGLMTCYDLRFPELALS 158
Cdd:cd07586   78 FGFVEEGRDGRFYNSAAYLEDGRVVHVHRKVYLptYGLF--EEGRYFAPGSHLRAF-DTRFGRAGVLICEDAWHPSLPYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 159 LALSGAQLIVLPAAWVKGPLKEHH-----WATLLAARALDTTCYIVAAG----ECGTRNIGQSRIVDPLGTTIAGAGE-Q 228
Cdd:cd07586  155 LALDGADVIFIPANSPARGVGGDFdneenWETLLKFYAMMNGVYVVFANrvgvEDGVYFWGGSRVVDPDGEVVAEAPLfE 234
                        250       260
                 ....*....|....*....|....*..
gi 515201419 229 PQLIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:cd07586  235 EDLLVAELDRSAIRRARFFSPTFRDED 261
PRK13981 PRK13981
NAD synthetase; Provisional
1-223 2.00e-17

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 81.36  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   1 MLVAAGQFavtpDWTV-----NAQTCVSMMRQAGERGATLLVLPE---------------ALLARNDADADlsvKSAQQL 60
Cdd:PRK13981   1 LRIALAQL----NPTVgdiagNAAKILAAAAEAADAGADLLLFPElflsgyppedlllrpAFLAACEAALE---RLAAAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  61 DGGflqlllaesensplTTVLTLHVPSAEGRATNTLVALRHGKIITQYQKLHL--YDAFNiqESRLVDAGQQiPPLIEVD 138
Cdd:PRK13981  74 AGG--------------PAVLVGHPWREGGKLYNAAALLDGGEVLATYRKQDLpnYGVFD--EKRYFAPGPE-PGVVELK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 139 GMRVGLMTCYDLRFPELALSLALSGAQLIVLPAA---WV-KGPLKEhhwaTLLAARALDTTCYIVAAGECGtrniGQ--- 211
Cdd:PRK13981 137 GVRIGVPICEDIWNPEPAETLAEAGAELLLVPNAspyHRgKPDLRE----AVLRARVRETGLPLVYLNQVG----GQdel 208
                        250
                 ....*....|....*..
gi 515201419 212 -----SRIVDPLGTTIA 223
Cdd:PRK13981 209 vfdgaSFVLNADGELAA 225
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
19-255 3.92e-16

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: 76.00  E-value: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  19 QTCVSMMRQAGERGATLLVLPEA-----LLARNDADAdlsVKSAQQLDGGFLQLLLAESENSpLTTVLTLHVPSAEGRAT 93
Cdd:cd07568   30 QKHVTMIREAAEAGAQIVCLQEIfygpyFCAEQDTKW---YEFAEEIPNGPTTKRFAALAKE-YNMVLILPIYEKEQGGT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  94 --NTLVALRH-GKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVLP 170
Cdd:cd07568  106 lyNTAAVIDAdGTYLGKYRKNHIPHVGGFWEKFYFRPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFNP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 171 AAWVKGpLKEHHWATLLAARALDTTCYIVAAGECGTR---NI----GQSRIVDPLGTTIA-GAGEQPQLIFAELSTDYIQ 242
Cdd:cd07568  186 SATVAG-LSEYLWKLEQPAAAVANGYFVGAINRVGTEapwNIgefyGSSYFVDPRGQFVAsASRDKDELLVAELDLDLIR 264
                        250
                 ....*....|...
gi 515201419 243 QVRERLPVLQNRR 255
Cdd:cd07568  265 EVRDTWQFYRDRR 277
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
1-261 4.84e-16

Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143598  Cd Length: 280  Bit Score: 75.70  E-value: 4.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   1 MLVAAGQFAVTP--DWTVNAQTCVSMMRQAGERGATLLVLPE----ALLARNDADA---DLSVKSAQQLDGGFLQLL--L 69
Cdd:cd07574    1 VRVAAAQYPLRRyaSFEEFAAKVEYWVAEAAGYGADLLVFPEyftmELLSLLPEAIdglDEAIRALAALTPDYVALFseL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  70 AESENsplTTVLTLHVPSAE-GRATNT-LVALRHGKIITQYqKLHLY----DAFNIQesrlvdAGQQIPpLIEVDGMRVG 143
Cdd:cd07574   81 ARKYG---INIIAGSMPVREdGRLYNRaYLFGPDGTIGHQD-KLHMTpferEEWGIS------GGDKLK-VFDTDLGKIG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 144 LMTCYDLRFPELALSLALSGAQLIVLPAAW--VKGPLKEHHWAtllAARALDTTCYIVAAGECGT--------RNIGQSR 213
Cdd:cd07574  150 ILICYDSEFPELARALAEAGADLLLVPSCTdtRAGYWRVRIGA---QARALENQCYVVQSGTVGNapwspavdVNYGQAA 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515201419 214 IVDPL-------GTTIAGAGEQPQLIFAELSTDYIQQVRERLPVlQNRRFAPPQL 261
Cdd:cd07574  227 VYTPCdfgfpedGILAEGEPNTEGWLIADLDLEALRRLREEGSV-RNLRDWREDL 280
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-248 7.77e-16

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: 75.42  E-value: 7.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   1 MLVAAGQFAVTPDWTVNAQTC---VSMMRQAGERGATLLVLPE-AL-------LARNDADADLSVKS------------- 56
Cdd:cd07569    4 VILAAAQMGPIARAETRESVVarlIALLEEAASRGAQLVVFPElALttffprwYFPDEAELDSFFETempnpetqplfdr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  57 AQQLDGGFlQLLLAEsensplttvLTLHVPSAEGRATNTLVAlRHGKIITQYQKLHL--------YDAFNIQESRLVDAG 128
Cdd:cd07569   84 AKELGIGF-YLGYAE---------LTEDGGVKRRFNTSILVD-KSGKIVGKYRKVHLpghkepepYRPFQHLEKRYFEPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 129 QQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVL---PAAWVKGP-----LKEHHWATLLAARALDTTCYIVA 200
Cdd:cd07569  153 DLGFPVFRVPGGIMGMCICNDRRWPETWRVMGLQGVELVLLgynTPTHNPPApehdhLRLFHNLLSMQAGAYQNGTWVVA 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515201419 201 AGECGTRN----IGQSRIVDPLGTTIAGA-GEQPQLIFAELSTDYIQQVRERL 248
Cdd:cd07569  233 AAKAGMEDgcdlIGGSCIVAPTGEIVAQAtTLEDEVIVADCDLDLCREGRETV 285
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
85-253 4.33e-15

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 72.85  E-value: 4.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  85 VPSAEGRATNTLVALRHGKIiTQYQKLHLYdafniqesRLVD------AGQQiPPLIEVDGMRVGLMTCYDLRFP----- 153
Cdd:PRK10438  83 LQTESGAVNRFLLVEPGGTV-HFYDKRHLF--------RMADehlhykAGNA-RVIVEWRGWRILPLVCYDLRFPvwsrn 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 154 ----ELALSLAlsgaqliVLPAAwvkgplKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTIAG 224
Cdd:PRK10438 153 rndyDLALYVA-------NWPAP------RSLHWQTLLTARAIENQAYVAGCNRVGSDGnghhyRGDSRIINPQGEIIAT 219
                        170       180       190
                 ....*....|....*....|....*....|
gi 515201419 225 AGE-QPQLIFAELSTDYIQQVRERLPVLQN 253
Cdd:PRK10438 220 AEPhQATRIDAELSLEALQEYREKFPAWRD 249
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
2-185 2.45e-13

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: 67.97  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   2 LVAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLARNDADADlsvkSAQQLDGGFLQLLLAESENSPLTTVL 81
Cdd:cd07579    1 RIAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPELALTGLDDPAS----EAESDTGPAVSALRRLARRLRLYLVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  82 TLHVPSAEGRATNTLVALRHGkIITQYQKLHLydafNIQESRLVDAGQQiPPLIEVDGMRVGLMTCYDLRFPELALSLAL 161
Cdd:cd07579   77 GFAEADGDGLYNSAVLVGPEG-LVGTYRKTHL----IEPERSWATPGDT-WPVYDLPLGRVGLLIGHDALFPEAGRVLAL 150
                        170       180
                 ....*....|....*....|....
gi 515201419 162 SGAQLIVLPAAwVKGPLKEHHWAT 185
Cdd:cd07579  151 RGCDLLACPAA-IAIPFVGAHAGT 173
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
16-247 1.41e-12

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143606  Cd Length: 294  Bit Score: 66.21  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  16 VNAQTCVSMMRQAGERGATLLVLPE-ALLARNDADADL---SVKSAQQLDGGFLQLL--LAESENSPLTTVLTLHVPSAE 89
Cdd:cd07582   26 INEQIDAAVGFSGPGLPVRLVVLPEyALQGFPMGEPREvwqFDKAAIDIPGPETEALgeKAKELNVYIAANAYERDPDFP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  90 GRATNTLVALR-HGKIITQYQKLH------------LYDAFNIQESRLVDAgqqIPPLIEVDGMRVGLMTCYDLRFPELA 156
Cdd:cd07582  106 GLYFNTAFIIDpSGEIILRYRKMNslaaegspsphdVWDEYIEVYGYGLDA---LFPVADTEIGNLGCLACEEGLYPEVA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 157 LSLALSGAQLIVLPAAWVkgPLKEHHWATLLA-ARALDTTCYIVAAGECGTRNI--------GQSRIVDPLGTTI--AGA 225
Cdd:cd07582  183 RGLAMNGAEVLLRSSSEV--PSVELDPWEIANrARALENLAYVVSANSGGIYGSpypadsfgGGSMIVDYKGRVLaeAGY 260
                        250       260
                 ....*....|....*....|..
gi 515201419 226 GEQPQLIFAELSTDYIQQVRER 247
Cdd:cd07582  261 GPGSMVAGAEIDIEALRRARAR 282
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-255 2.23e-11

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 62.48  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   3 VAAGQFAVTPDWTVNAQTCVSMMRQAGERGATLLVLPEALLArndadadLSVKSAQQLDggFLQLLlAESENSPLTTVL- 81
Cdd:PLN02747   9 VAALQFACSDDRAANVDKAERLVREAHAKGANIILIQELFEG-------YYFCQAQRED--FFQRA-KPYEGHPTIARMq 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  82 --------TLHVPSAEgRATNTL---VAL--RHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCY 148
Cdd:PLN02747  79 klakelgvVIPVSFFE-EANNAHynsIAIidADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFDTKFAKIGVAICW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 149 DLRFPELALSLALSGAQLIVLPAAWVKGP----LKEH-HWATLLAARALDTTCYIVAAGECGTRNI------------GQ 211
Cdd:PLN02747 158 DQWFPEAARAMVLQGAEVLLYPTAIGSEPqdpgLDSRdHWKRVMQGHAGANLVPLVASNRIGTEILetehgpskitfyGG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 515201419 212 SRIVDPLGTTIAGAGEQPQ-LIFAELSTDYIQQVRERLPVLQNRR 255
Cdd:PLN02747 238 SFIAGPTGEIVAEADDKAEaVLVAEFDLDQIKSKRASWGVFRDRR 282
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
2-246 2.72e-11

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: 62.30  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   2 LVAAGQFAV----TP-DWTVNAQTCVSMMRQ--AGERGATLLVLPEALLARNDADADLSVKSAQQLDGGFLQLLLAESEN 74
Cdd:cd07565    2 GVAVVQYKVpvlhTKeEVLENAERIADMVEGtkRGLPGMDLIVFPEYSTQGLMYDKWTMDETACTVPGPETDIFAEACKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  75 SPLTTV--LTLHVPSAEGRATNTLVALR-HGKIITQYQKLHLYDAFNIQEsrlvdAGQQIPPLIE-VDGMRVGLMTCYDL 150
Cdd:cd07565   82 AKVWGVfsIMERNPDHGKNPYNTAIIIDdQGEIVLKYRKLHPWVPIEPWY-----PGDLGTPVCEgPKGSKIALIICHDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 151 RFPELALSLALSGAQLIVLPAAWVKgPLKeHHWATLLAARALDTTCYIVAAGECGTRNI----GQSRIVDPLGTTIAGAG 226
Cdd:cd07565  157 MYPEIARECAYKGAELIIRIQGYMY-PAK-DQWIITNKANAWCNLMYTASVNLAGFDGVfsyfGESMIVNFDGRTLGEGG 234
                        250       260
                 ....*....|....*....|.
gi 515201419 227 EQP-QLIFAELSTDYIQQVRE 246
Cdd:cd07565  235 REPdEIVTAELSPSLVRDARK 255
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
85-255 8.55e-10

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: 57.54  E-value: 8.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  85 VPSAEGRATNTLVALRHGKIITQYQKLHLYdafnIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGA 164
Cdd:cd07578   88 VDSRSGIYYNSAVLIGPSGVIGRHRKTHPY----ISEPKWAADGDLGHQVFDTEIGRIALLICMDIHFFETARLLALGGA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 165 QLIVLPAAWvkgpLKEHHWATLLAARALDTTCYIVAAG----ECGTRNIGQSRIVDPLGTTIAGAGEQPQLIFAELSTDY 240
Cdd:cd07578  164 DVICHISNW----LAERTPAPYWINRAFENGCYLIESNrwglERGVQFSGGSCIIEPDGTIQASIDSGDGVALGEIDLDR 239
                        170
                 ....*....|....*.
gi 515201419 241 IQQVR-ERLPVLQNRR 255
Cdd:cd07578  240 ARHRQfPGELVFTARR 255
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
22-221 2.24e-09

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 56.98  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419   22 VSMMRQAGERgATLLVLPEALLArndadADLSvKSAQQLDGGFLQLLLaeSENSPLTTVLTLHVPSAEGRATNTLVAL-R 100
Cdd:TIGR00546 188 TSLTKQAVEK-PDLVVWPETAFP-----FDLE-NSPQKLADRLKLLVL--SKGIPILIGAPDAVPGGPYHYYNSAYLVdP 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  101 HGKIITQYQKLHL----------------YDAFNIQESRLVDAGQQIPPLiEVDGMRVGLMTCYDLRFPELALSLALSGA 164
Cdd:TIGR00546 259 GGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLLSQEDFSRGPGPQVL-KLPGGKIAPLICYESIFPDLVRASARQGA 337
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515201419  165 QLIVLPA--AWVKGP--LKEHHWATLLAARALDTTCYIVAagecgtrNIGQSRIVDPLGTT 221
Cdd:TIGR00546 338 ELLVNLTndAWFGDSsgPWQHFALARFRAIENGRPLVRAT-------NTGISAVIDPRGRT 391
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
22-223 4.39e-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: 55.68  E-value: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  22 VSMMRQAGERGATLLVLPEALLarndaDADLsvksaqQLDGGFLQLLLAESENSPlTTVLT--LHVPSAEGRATNTLVAL 99
Cdd:cd07571   29 LDLTRELADEKPDLVVWPETAL-----PFDL------QRDPDALARLARAARAVG-APLLTgaPRREPGGGRYYNSALLL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 100 RHGKIITQ-YQKLHL----------------YDAFNIQESRLVdAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALS 162
Cdd:cd07571   97 DPGGGILGrYDKHHLvpfgeyvplrdllrflGLLFDLPMGDFS-PGTGPQPLLLGGGVRVGPLICYESIFPELVRDAVRQ 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515201419 163 GAQLIVLPA--AWVK---GPlKEHHWATLLaaRALDTTCYIVAAGecgtrNIGQSRIVDPLGTTIA 223
Cdd:cd07571  176 GADLLVNITndAWFGdsaGP-YQHLAMARL--RAIETGRPLVRAA-----NTGISAVIDPDGRIVA 233
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
22-223 2.71e-08

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 54.08  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  22 VSMMRQAGERGATLLVLPEAllarndadadlSVKSAQQLDGGFLQLL--LAESENSPLttvLT--LHVPSAEGRATNTLV 97
Cdd:COG0815  223 LDLTRELADDGPDLVVWPET-----------ALPFLLDEDPDALARLaaAAREAGAPL---LTgaPRRDGGGGRYYNSAL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  98 ALR-HGKIITQYQKLHL----------------YDAFNIQESRLVdAGQQiPPLIEVDGMRVGLMTCYDLRFPELALSLA 160
Cdd:COG0815  289 LLDpDGGILGRYDKHHLvpfgeyvplrdllrplIPFLDLPLGDFS-PGTG-PPVLDLGGVRVGPLICYESIFPELVRDAV 366
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515201419 161 LSGAQLIVLPA--AWVK---GPlKEHHWATLLaaRALDTTCYIVAAGecgtrNIGQSRIVDPLGTTIA 223
Cdd:COG0815  367 RAGADLLVNITndAWFGdsiGP-YQHLAIARL--RAIETGRPVVRAT-----NTGISAVIDPDGRVLA 426
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
94-189 2.46e-06

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143591  Cd Length: 299  Bit Score: 47.62  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  94 NTLVAL-RHGKIITQYQKLHLY--DAFNIQESrlvdagqqiPPLI--EVD-GMRVGLMTCYDLRFPELALSLA-LSGAQL 166
Cdd:cd07567  130 NTNVVFdRDGTLIARYRKYNLFgePGFDVPPE---------PEIVtfDTDfGVTFGIFTCFDILFKEPALELVkKLGVDD 200
                         90       100       110
                 ....*....|....*....|....*....|....
gi 515201419 167 IVLPAAWVKGP-----LKEHH-WA-----TLLAA 189
Cdd:cd07567  201 IVFPTAWFSELpfltaVQIQQaWAyangvNLLAA 234
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
31-223 5.84e-06

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 46.80  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  31 RGATLLVLPEAllarndADADLsvksAQQLDGGFLQLL--LAESENSPLTTVLTLHVPSAEG-RATNTLVALRHGKIITQ 107
Cdd:PRK00302 256 GPADLIIWPET------AIPFL----LEDLPQAFLKALddLAREKGSALITGAPRAENKQGRyDYYNSIYVLGPYGILNR 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 108 YQKLHL----------------YDAFNIQESRLvDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVLPA 171
Cdd:PRK00302 326 YDKHHLvpfgeyvplesllrplAPFFNLPMGDF-SRGPYVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQGADLLLNIS 404
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515201419 172 --AWVK---GPLKEHHWATLlaaRALDTTCYIVAAgecgTrNIGQSRIVDPLGTTIA 223
Cdd:PRK00302 405 ndAWFGdsiGPYQHFQMARM---RALELGRPLIRA----T-NTGITAVIDPLGRIIA 453
amiE PRK13286
aliphatic amidase;
139-245 1.84e-05

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 45.12  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 139 GMRVGLMTCYDLRFPELALSLALSGAQLIVLPAAWVKgPLKEHhwaTLLAARALD--TTCYIVAAGECGTRNI----GQS 212
Cdd:PRK13286 158 GLKISLIICDDGNYPEIWRDCAMKGAELIVRCQGYMY-PAKEQ---QVLVAKAMAwaNNCYVAVANAAGFDGVysyfGHS 233
                         90       100       110
                 ....*....|....*....|....*....|....
gi 515201419 213 RIVDPLGTTIAGAGEQPQLI-FAELSTDYIQQVR 245
Cdd:PRK13286 234 AIIGFDGRTLGECGEEEMGIqYAQLSVSQIRDAR 267
nadE PRK02628
NAD synthetase; Reviewed
17-168 2.90e-05

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 44.85  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  17 NAQTCVSMMRQAGERGATLLVLPEallarndadadLSVkSAQQLDGGFLQ-LLLAESEN---------SPLTTVLTLHVP 86
Cdd:PRK02628  30 NAARILALARRAADDGVALAVFPE-----------LSL-SGYSCDDLFLQdTLLDAVEDalatlveasADLDPLLVVGAP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  87 -SAEGRATNTLVALRHGKII------------TQYQKLHLYDAFNIQESRLVDAGQQIP---PLI----EVDGMRVGLMT 146
Cdd:PRK02628  98 lRVRHRLYNCAVVIHRGRILgvvpksylpnyrEFYEKRWFAPGDGARGETIRLCGQEVPfgtDLLfeaeDLPGFVFGVEI 177
                        170       180
                 ....*....|....*....|...
gi 515201419 147 CYDLRFPELALS-LALSGAQLIV 168
Cdd:PRK02628 178 CEDLWVPIPPSSyAALAGATVLA 200
amiF PRK13287
formamidase; Provisional
101-246 5.89e-04

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 40.45  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419 101 HGKIITQYQKLHLYdaFNIQESRLVDAGQqipPLIE-VDGMRVGLMTCYDLRFPELALSLALSGAQLIVLPAAWvKGPLK 179
Cdd:PRK13287 123 QGEIILKYRKLHPW--VPVEPWEPGDLGI---PVCDgPGGSKLAVCICHDGMFPEMAREAAYKGANVMIRISGY-STQVR 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515201419 180 eHHWATLLAARALDTTCYIVAAGECGTRNI----GQSRIVDPLGTTIA-GAGEQPQLIFAELSTDYIQQVRE 246
Cdd:PRK13287 197 -EQWILTNRSNAWQNLMYTASVNLAGYDGVfyyfGEGQVCNFDGTTLVqGHRNPWEIVTAEVRPDLADEARL 267
PLN00202 PLN00202
beta-ureidopropionase
94-201 3.70e-03

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 38.28  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515201419  94 NTLVAL-RHGKIITQYQKLHLYDAFNIQESRLVDAGQQIPPLIEVDGMRVGLMTCYDLRFPELALSLALSGAQLIVLPAA 172
Cdd:PLN00202 192 NTAVVIgNNGNIIGKHRKNHIPRVGDFNESTYYMEGNTGHPVFETAFGKIAVNICYGRHHPLNWLAFGLNGAEIVFNPSA 271
                         90       100
                 ....*....|....*....|....*....
gi 515201419 173 WVkGPLKEHHWAtLLAARALDTTCYIVAA 201
Cdd:PLN00202 272 TV-GDLSEPMWP-IEARNAAIANSYFVGS 298
 
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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