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Conserved domains on  [gi|446417925|ref|WP_000495780|]
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MULTISPECIES: deaminated glutathione amidase [Salmonella]

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: 499.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVALRAGHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 163 GADVLALPTGWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRNIGQSRIIDPLGVTIAAAADRPALIVAEIFRERID 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 446417925 243 QVREQLPLLQQRRFAPPQL 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: 499.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVALRAGHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 163 GADVLALPTGWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRNIGQSRIIDPLGVTIAAAADRPALIVAEIFRERID 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 446417925 243 QVREQLPLLQQRRFAPPQL 261
Cdd:NF033621 242 HAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 3.64e-111

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: 320.29  E-value: 3.64e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVAL-RAGHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVL-DVEGVKVGLMTCYDLRFPDMALALA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVVfVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 161 LQGADVLALPTGWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRNIGQSRIIDPLGVTIAAAADRPALIVAEIFRER 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 446417925 241 IDQVREQLPLLQQRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 6.91e-71

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 218.58  E-value: 6.91e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   1 MFVAAGQFVVSSV-WEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTT 79
Cdd:COG0388    2 MRIALAQLNPTVGdIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  80 IFTILVPSTPGRAVN-MLVALRAGHIVARYAKLHLYDAFSMQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALA 158
Cdd:COG0388   82 VVGLPERDEGGRLYNtALVIDPDGEILGRYRKIHLPNYGVFDEKRYFTPGDEL-VVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 159 LALQGADVLALPTGWVRGPLKEqQWSTLLAARALDTTSYMIAAGECGN----RNIGQSRIIDPLGVTIAAAADRPALIVA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGRGKD-HWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 446417925 235 EIFRERIDQVREQLPLLQQRRF 256
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRP 261
PLN02798 PLN02798
nitrilase
3-258 2.82e-39

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 137.95  E-value: 2.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPE--GILARDDIDldlPIRAAQPLDGAFMTRLLEESAHNNMTTI 80
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQRYRSLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  81 ---FTILVPStPGRAVNMLVALR-AGHIVARYAKLHLYD-----AFSMQESQSIDAGTVIAPVlDVEGVKVGLMTCYDLR 151
Cdd:PLN02798  90 lggFQEKGPD-DSHLYNTHVLIDdSGEIRSSYRKIHLFDvdvpgGPVLKESSFTAPGKTIVAV-DSPVGRLGLTVCYDLR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 152 FPDMALALAL-QGADVLALPTGWVRgPLKEQQWSTLLAARALDTTSYMIAAGECGNRN-----IGQSRIIDPLGVTIAAA 225
Cdd:PLN02798 168 FPELYQQLRFeHGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWGTVVARL 246
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446417925 226 ADR--PALIVAEIFRERIDQVREQLPLLQQRRFAP 258
Cdd:PLN02798 247 PDRlsTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
15-245 2.66e-31

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: 116.30  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   15 EENAQVCVSLMAQAAGRGVSLLVLPE-GILARDDidLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFTIL-VPSTPGRA 92
Cdd:pfam00795  15 EANLQKALELIEEAARYGADLIVLPElFITGYPC--WAHFLEAAEVGDGETLAGLAALARKNGIAIVIGLIeRWLTGGRL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   93 VNMLVALRA-GHIVARYAKLHLYDAF---SMQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLA 168
Cdd:pfam00795  93 YNTAVLLDPdGKLVGKYRKLHLFPEPrppGFRERVLFEPGDGG-TVFDTPLGKIGAAICYEIRFPELLRALALKGAEILI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  169 LPT--GWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRN-----IGQSRIIDPLGVTIAAAADRPA-LIVAEIFRER 240
Cdd:pfam00795 172 NPSarAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGEWEEgVLIADIDLAL 251

                  ....*
gi 446417925  241 IDQVR 245
Cdd:pfam00795 252 VRAWR 256
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
22-221 5.06e-10

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: 58.91  E-value: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   22 VSLMAQAAGRgVSLLVLPEGILArddIDLDLPIRAAQpldgafmTRLLEESAHNNMTTIFTIL--VPSTPGRAVNMLVAL 99
Cdd:TIGR00546 188 TSLTKQAVEK-PDLVVWPETAFP---FDLENSPQKLA-------DRLKLLVLSKGIPILIGAPdaVPGGPYHYYNSAYLV 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  100 -RAGHIVARYAKLHL----------------YDAFSMQESQSIDAGTvIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:TIGR00546 257 dPGGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLLSQEDFSRGP-GPQVLKLPGGKIAPLICYESIFPDLVRASARQ 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446417925  163 GADVLALPT--GWVRGPLKEQQWSTLLAARALDTTSYMIAAGecgnrNIGQSRIIDPLGVT 221
Cdd:TIGR00546 336 GAELLVNLTndAWFGDSSGPWQHFALARFRAIENGRPLVRAT-----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: 499.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFT 82
Cdd:NF033621   2 VALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVALRAGHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:NF033621  82 VHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 163 GADVLALPTGWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRNIGQSRIIDPLGVTIAAAADRPALIVAEIFRERID 242
Cdd:NF033621 162 GADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERIA 241
                        250
                 ....*....|....*....
gi 446417925 243 QVREQLPLLQQRRFAPPQL 261
Cdd:NF033621 242 HAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 3.64e-111

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: 320.29  E-value: 3.64e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVAL-RAGHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVL-DVEGVKVGLMTCYDLRFPDMALALA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVVfVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 161 LQGADVLALPTGWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRNIGQSRIIDPLGVTIAAAADRPALIVAEIFRER 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 446417925 241 IDQVREQLPLLQQRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 6.91e-71

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 218.58  E-value: 6.91e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   1 MFVAAGQFVVSSV-WEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTT 79
Cdd:COG0388    2 MRIALAQLNPTVGdIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  80 IFTILVPSTPGRAVN-MLVALRAGHIVARYAKLHLYDAFSMQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALA 158
Cdd:COG0388   82 VVGLPERDEGGRLYNtALVIDPDGEILGRYRKIHLPNYGVFDEKRYFTPGDEL-VVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 159 LALQGADVLALPTGWVRGPLKEqQWSTLLAARALDTTSYMIAAGECGN----RNIGQSRIIDPLGVTIAAAADRPALIVA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGRGKD-HWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 446417925 235 EIFRERIDQVREQLPLLQQRRF 256
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRP 261
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
3-255 2.48e-60

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: 191.49  E-value: 2.48e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPE--GILARDDIDLDLpiRAAQPLDGAFMTRLLEESAHNNMTTI 80
Cdd:cd07572    2 VALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPEcfNYPGGTDAFKLA--LAEEEGDGPTLQALSELAKEHGIWLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  81 F-TILVPS-TPGRAVN-MLVALRAGHIVARYAKLHLYDAF-----SMQESQSIDAGTVIAPVlDVEGVKVGLMTCYDLRF 152
Cdd:cd07572   80 GgSIPERDdDDGKVYNtSLVFDPDGELVARYRKIHLFDVDvpggiSYRESDTLTPGDEVVVV-DTPFGKIGLGICYDLRF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 153 PDMALALALQGADVLALP------TGwvrgplkEQQWSTLLAARALDTTSYMIAAGECGNRNI-----GQSRIIDPLGVT 221
Cdd:cd07572  159 PELARALARQGADILTVPaaftmtTG-------PAHWELLLRARAIENQCYVVAAAQAGDHEAgretyGHSMIVDPWGEV 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 446417925 222 IAAAADRPALIVAEIFRERIDQVREQLPLLQQRR 255
Cdd:cd07572  232 LAEAGEGEGVVVAEIDLDRLEEVRRQIPVLKHRR 265
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 3.51e-54

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: 175.42  E-value: 3.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQF-VVSSVWEENAQVCVSLMAQAAGRGVSLLVLPE----GIlarddiDLDLPIRAAQPLDGAFMTRLLEESAHNNM 77
Cdd:cd07583    2 IALIQLdIVWGDPEANIERVESLIEEAAAAGADLIVLPEmwntGY------FLDDLYELADEDGGETVSFLSELAKKHGV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  78 TTIFTILVPSTPGRAVN-MLVALRAGHIVARYAKLHLydaFS-MQESQSIDAGTVIAPVlDVEGVKVGLMTCYDLRFPDM 155
Cdd:cd07583   76 NIVAGSVAEKEGGKLYNtAYVIDPDGELIATYRKIHL---FGlMGEDKYLTAGDELEVF-ELDGGKVGLFICYDLRFPEL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 156 ALALALQGADVLALPTGWvrgPLK-EQQWSTLLAARALDTTSYMIAAGECG----NRNIGQSRIIDPLGVTIAAAADRPA 230
Cdd:cd07583  152 FRKLALEGAEILFVPAEW---PAArIEHWRTLLRARAIENQAFVVACNRVGtdggNEFGGHSMVIDPWGEVLAEAGEEEE 228
                        250       260
                 ....*....|....*....|....*
gi 446417925 231 LIVAEIFRERIDQVREQLPLLQQRR 255
Cdd:cd07583  229 ILTAEIDLEEVAEVRKKIPVFKDRR 253
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
3-255 8.60e-54

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: 174.43  E-value: 8.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQF-VVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDL-DLPIRAAQPLDGAFMTRLLEESAHNNMTTI 80
Cdd:cd07197    1 IAAVQLaPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESaKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  81 FTILVpSTPGRAVNMLVAL-RAGHIVARYAKLHLYDafsMQESQSIDAGTvIAPVLDVEGVKVGLMTCYDLRFPDMALAL 159
Cdd:cd07197   81 AGIAE-KDGDKLYNTAVVIdPDGEIIGKYRKIHLFD---FGERRYFSPGD-EFPVFDTPGGKIGLLICYDLRFPELAREL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 160 ALQGADVLALPTGWVRGPLKeqQWSTLLAARALDTTSYMIAAGECG----NRNIGQSRIIDPLGVTIAAAADRPALIVAE 235
Cdd:cd07197  156 ALKGADIILVPAAWPTARRE--HWELLLRARAIENGVYVVAANRVGeeggLEFAGGSMIVDPDGEVLAEASEEEGILVAE 233
                        250       260
                 ....*....|....*....|
gi 446417925 236 IFRERIDQVREQLPLLQQRR 255
Cdd:cd07197  234 LDLDELREARKRWSYLRDRR 253
PLN02798 PLN02798
nitrilase
3-258 2.82e-39

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 137.95  E-value: 2.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPE--GILARDDIDldlPIRAAQPLDGAFMTRLLEESAHNNMTTI 80
Cdd:PLN02798  13 VAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQRYRSLARESGLWLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  81 ---FTILVPStPGRAVNMLVALR-AGHIVARYAKLHLYD-----AFSMQESQSIDAGTVIAPVlDVEGVKVGLMTCYDLR 151
Cdd:PLN02798  90 lggFQEKGPD-DSHLYNTHVLIDdSGEIRSSYRKIHLFDvdvpgGPVLKESSFTAPGKTIVAV-DSPVGRLGLTVCYDLR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 152 FPDMALALAL-QGADVLALPTGWVRgPLKEQQWSTLLAARALDTTSYMIAAGECGNRN-----IGQSRIIDPLGVTIAAA 225
Cdd:PLN02798 168 FPELYQQLRFeHGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWGTVVARL 246
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446417925 226 ADR--PALIVAEIFRERIDQVREQLPLLQQRRFAP 258
Cdd:PLN02798 247 PDRlsTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
26-257 1.17e-34

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: 125.00  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  26 AQAAGRGVSLLVLPEGILARDDIDLDLPiRAAQPLDGAFMTRLLEESAHNNMTtiftILVP---STPGRAVNMLVAL-RA 101
Cdd:cd07576   26 ARAAAAGADLLVFPELFLTGYNIGDAVA-RLAEPADGPALQALRAIARRHGIA----IVVGypeRAGGAVYNAAVLIdED 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 102 GHIVARYAKLHLYDAFsmqESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLALPTGWVRGPLKEQ 181
Cdd:cd07576  101 GTVLANYRKTHLFGDS---ERAAFTPGDRF-PVVELRGLRVGLLICYDVEFPELVRALALAGADLVLVPTALMEPYGFVA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 182 QwsTLLAARALDTTSYMIAAGECGNRN----IGQSRIIDPLGVTIAAAADRPALIVAEIFRERIDQVREQLPLLQQRRFA 257
Cdd:cd07576  177 R--TLVPARAFENQIFVAYANRCGAEDgltyVGLSSIAGPDGTVLARAGRGEALLVADLDPAALAAARRENPYLADRRPE 254
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
15-245 2.66e-31

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: 116.30  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   15 EENAQVCVSLMAQAAGRGVSLLVLPE-GILARDDidLDLPIRAAQPLDGAFMTRLLEESAHNNMTTIFTIL-VPSTPGRA 92
Cdd:pfam00795  15 EANLQKALELIEEAARYGADLIVLPElFITGYPC--WAHFLEAAEVGDGETLAGLAALARKNGIAIVIGLIeRWLTGGRL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   93 VNMLVALRA-GHIVARYAKLHLYDAF---SMQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLA 168
Cdd:pfam00795  93 YNTAVLLDPdGKLVGKYRKLHLFPEPrppGFRERVLFEPGDGG-TVFDTPLGKIGAAICYEIRFPELLRALALKGAEILI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  169 LPT--GWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGNRN-----IGQSRIIDPLGVTIAAAADRPA-LIVAEIFRER 240
Cdd:pfam00795 172 NPSarAPFPGSLGPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGEWEEgVLIADIDLAL 251

                  ....*
gi 446417925  241 IDQVR 245
Cdd:pfam00795 252 VRAWR 256
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
17-255 1.10e-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: 143608  Cd Length: 258  Bit Score: 109.38  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  17 NAQVCVSLMAQAAGRGVSLLVLPEgiLARDDIDLDL----PIRAAQPLDGAfMTRLLEESAHNNMTTIFTILVP--STPG 90
Cdd:cd07584   17 NLKKAAELCKEAAAEGADLICFPE--LATTGYRPDLlgpkLWELSEPIDGP-TVRLFSELAKELGVYIVCGFVEkgGVPG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  91 RAVNMLVA-LRAGHIVARYAKLHLYdafsmQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLAL 169
Cdd:cd07584   94 KVYNSAVViDPEGESLGVYRKIHLW-----GLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVARILTLKGAEVIFC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 170 PTGWVRgpLKEQQWSTLLAARALDTTSYMIAAGECGN----RNIGQSRIIDPLGVTIAAAADRP-ALIVAEIFRERIDQV 244
Cdd:cd07584  169 PSAWRE--QDADIWDINLPARALENTVFVAAVNRVGNegdlVLFGKSKILNPRGQVLAEASEEAeEILYAEIDLDAIADY 246
                        250
                 ....*....|.
gi 446417925 245 REQLPLLQQRR 255
Cdd:cd07584  247 RMTLPYLKDRK 257
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 5.29e-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: 5.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVvSSVW--EENAQVCVSLMAQAAGRGVSLLVLPEGILARDDIDLDLPiRAAQPLDGAFMTRLLEESAHNNMTTI 80
Cdd:cd07585    2 IALVQFE-ARVGdkARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALS-REAEVPDGPSTQALSDLARRYGLTIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  81 FTiLVPSTPGRAVNMLVALRAGHIVARYAKLHLYDafsmQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALALA 160
Cdd:cd07585   80 AG-LIEKAGDRPYNTYLVCLPDGLVHRYRKLHLFR----REHPYIAAGDEY-PVFATPGVRFGILICYDNHFPENVRATA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 161 LQGADVLALP--TGWVRGPLKEQQWSTLLAARALDTTSYMIA---AGECGNRNI-GQSRIIDPLGVTIAAAAD-RPALIV 233
Cdd:cd07585  154 LLGAEILFAPhaTPGTTSPKGREWWMRWLPARAYDNGVFVAAcngVGRDGGEVFpGGAMILDPYGRVLAETTSgGDGMVV 233
                        250       260
                 ....*....|....*....|....
gi 446417925 234 AEIFRERIDQVR--EQLPLLQQRR 255
Cdd:cd07585  234 ADLDLDLINTVRgrRWISFLRARR 257
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
3-255 5.09e-23

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: 94.94  E-value: 5.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILAR---DDIDLDLPIRAAQPLDGAFMTRLLEESAHNNMTT 79
Cdd:cd07573    3 VALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPyfcQEEDEDYFDLAEPPIPGPTTARFQALAKELGVVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  80 IFTILVPSTPGRAVNMLVALRA-GHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALA 158
Cdd:cd07573   83 PVSLFEKRGNGLYYNSAVVIDAdGSLLGVYRKMHIPDDPGYYEKFYFTPGDTGFKVFDTRYGRIGVLICWDQWFPEAARL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 159 LALQGADVLALPT--GWVRGPLKEQQ-----WSTLLAARALDTTSYMIAAGECG-----NRNI---GQSRIIDPLGVTIA 223
Cdd:cd07573  163 MALQGAEILFYPTaiGSEPQEPPEGLdqrdaWQRVQRGHAIANGVPVAAVNRVGvegdpGSGItfyGSSFIADPFGEILA 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 446417925 224 -AAADRPALIVAEIFRERIDQVREQLPLLQQRR 255
Cdd:cd07573  243 qASRDEEEILVAEFDLDEIEEVRRAWPFFRDRR 275
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 1.42e-21

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: 90.87  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQF--VVSSVwEENAQVCVSLMAQAAGRGVSLLVLPEgiLAR-----DDIDlDLPIRAAQPLDGAFMTRLLEESAHN 75
Cdd:cd07580    2 VACVQFdpRVGDL-DANLARSIELIREAADAGANLVVLPE--LANtgyvfESRD-EAFALAEEVPDGASTRAWAELAAEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  76 NmttifTILVPSTPGRA----VNMLVALRAGHIVARYAKLHLYDafsmQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLR 151
Cdd:cd07580   78 G-----LYIVAGFAERDgdrlYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDLGLPVFDTPFGRIGVAICYDGW 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 152 FPDMALALALQGADVLALPTGWVRGP-LKEQQW--STLLAARALDTTSYMIAAG-----ECGNRNIGQSRIIDPLGVTIA 223
Cdd:cd07580  149 FPETFRLLALQGADIVCVPTNWVPMPrPPEGGPpmANILAMAAAHSNGLFIACAdrvgtERGQPFIGQSLIVGPDGWPLA 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446417925 224 --AAADRPALIVAEI--FRERIDQVREQLPLLQQRR 255
Cdd:cd07580  229 gpASGDEEEILLADIdlTAARRKRIWNSNDVLRDRR 264
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
35-236 5.32e-19

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: 83.50  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  35 LLVLPE----GIL--ARDDIdldlpIRAAQPLDGAFMTRLLEESAHNNMTTIFTILVPSTPGRAVNMLVALRAGHIVARY 108
Cdd:cd07577   32 LIVLPElfntGYAftSKEEV-----ASLAESIPDGPTTRFLQELARETGAYIVAGLPERDGDKFYNSAVVVGPEGYIGIY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 109 AKLHLYDAfsmqESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLALPTGWVRgPLkeqqWSTLLA 188
Cdd:cd07577  107 RKTHLFYE----EKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPANLVL-PY----CPKAMP 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446417925 189 ARALDTTSYMIAAGECGN--------RNIGQSRIIDPLGVTIA-AAADRPALIVAEI 236
Cdd:cd07577  178 IRALENRVFTITANRIGTeerggetlRFIGKSQITSPKGEVLArAPEDGEEVLVAEI 234
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-251 1.16e-18

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


Pssm-ID: 143610  Cd Length: 269  Bit Score: 82.72  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQF--VVSSVwEENAQVCVSLMAQAAGRGVSLLVLPE----GILARDDIdLDLPIRAAQPldgafmtRLLEES-AHN 75
Cdd:cd07586    2 VAIAQIdpVLGDV-EENLEKHLEIIETARERGADLVVFPElsltGYNLGDLV-YEVAMHADDP-------RLQALAeASG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  76 NMTTIFTILVPSTPGRAVNMLVALRAGHIVARYAKLHL--YDAFsmQESQSIDAGTVIApVLDVEGVKVGLMTCYDLRFP 153
Cdd:cd07586   73 GICVVFGFVEEGRDGRFYNSAAYLEDGRVVHVHRKVYLptYGLF--EEGRYFAPGSHLR-AFDTRFGRAGVLICEDAWHP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 154 DMALALALQGADVLALPT-----GWVRGPLKEQQWSTLLAARALDTTSYMIAAGECGN----RNIGQSRIIDPLGVTIAA 224
Cdd:cd07586  150 SLPYLLALDGADVIFIPAnsparGVGGDFDNEENWETLLKFYAMMNGVYVVFANRVGVedgvYFWGGSRVVDPDGEVVAE 229
                        250       260
                 ....*....|....*....|....*...
gi 446417925 225 AADR-PALIVAEIFRERIDQVREQLPLL 251
Cdd:cd07586  230 APLFeEDLLVAELDRSAIRRARFFSPTF 257
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
19-255 1.48e-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: 77.15  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  19 QVCVSLMAQAAGRGVSLLVLPE-----GILARDDIDLdlpIRAAQPLDGAFMTRLLEESAHN-NMTTIFTILVPSTPGRA 92
Cdd:cd07568   30 QKHVTMIREAAEAGAQIVCLQEifygpYFCAEQDTKW---YEFAEEIPNGPTTKRFAALAKEyNMVLILPIYEKEQGGTL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  93 VNMLVALRA-GHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLALPT 171
Cdd:cd07568  107 YNTAAVIDAdGTYLGKYRKNHIPHVGGFWEKFYFRPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFNPS 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 172 GWVRGpLKEQQWSTLLAARALDTTSYMIAAGECG-------NRNIGQSRIIDPLGVTIAAAA-DRPALIVAEIFRERIDQ 243
Cdd:cd07568  187 ATVAG-LSEYLWKLEQPAAAVANGYFVGAINRVGteapwniGEFYGSSYFVDPRGQFVASASrDKDELLVAELDLDLIRE 265
                        250
                 ....*....|..
gi 446417925 244 VREQLPLLQQRR 255
Cdd:cd07568  266 VRDTWQFYRDRR 277
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
108-251 3.67e-16

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: 75.65  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 108 YAKLHLydaFSM-QESQSIDAGT--VIAPVLdveGVKVGLMTCYDLRFP---------DMALALAlqgadvlalptGWvr 175
Cdd:cd07575  104 YDKRHL---FRMaGEHKVYTAGNerVIVEYK---GWKILLQVCYDLRFPvwsrntndyDLLLYVA-----------NW-- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 176 gPLKEQQ-WSTLLAARALDTTSYMIAAGECGN-----RNIGQSRIIDPLGVTIAAAADRPALIVAEIFRERIDQVREQLP 249
Cdd:cd07575  165 -PAPRRAaWDTLLKARAIENQAYVIGVNRVGTdgnglEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDKEALQEFREKFP 243

                 ..
gi 446417925 250 LL 251
Cdd:cd07575  244 FL 245
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
17-225 2.39e-15

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: 73.92  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  17 NAQVCVSLMAQAAGRGVSLLVLPEGILA-------RDDIDLDlpiRAAQPLDGAFMTRLLEESAHNN---MTTIFTiLVP 86
Cdd:cd07582   27 NEQIDAAVGFSGPGLPVRLVVLPEYALQgfpmgepREVWQFD---KAAIDIPGPETEALGEKAKELNvyiAANAYE-RDP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  87 STPGRAVNMLVALR-AGHIVARYAKLH------------LYDAFSMQESQSIDAgtvIAPVLDVEGVKVGLMTCYDLRFP 153
Cdd:cd07582  103 DFPGLYFNTAFIIDpSGEIILRYRKMNslaaegspsphdVWDEYIEVYGYGLDA---LFPVADTEIGNLGCLACEEGLYP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 154 DMALALALQGADVLALPTGWVrgPLKEQQWSTLLA-ARALDTTSYMIAAGECGNRNI--------GQSRIIDPLGVTIAA 224
Cdd:cd07582  180 EVARGLAMNGAEVLLRSSSEV--PSVELDPWEIANrARALENLAYVVSANSGGIYGSpypadsfgGGSMIVDYKGRVLAE 257

                 .
gi 446417925 225 A 225
Cdd:cd07582  258 A 258
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
3-247 4.58e-15

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


Pssm-ID: 143598  Cd Length: 280  Bit Score: 73.00  E-value: 4.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSV--WEENAQVCVSLMAQAAGRGVSLLVLPE-------GILARDDIDLDLPIRAAQPLDGAFMTRLLEESA 73
Cdd:cd07574    3 VAAAQYPLRRYasFEEFAAKVEYWVAEAAGYGADLLVFPEyftmellSLLPEAIDGLDEAIRALAALTPDYVALFSELAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  74 HNNMTtiftILVPSTP----GRAVNMLVALRAGHIVARYAKLHLYDafSMQESQSIDAGTVIApVLDVEGVKVGLMTCYD 149
Cdd:cd07574   83 KYGIN----IIAGSMPvredGRLYNRAYLFGPDGTIGHQDKLHMTP--FEREEWGISGGDKLK-VFDTDLGKIGILICYD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 150 LRFPDMALALALQGADVLALP--TGWVRGplkeqQWSTLL--AARALDTTSYMIAAGECGN--------RNIGQSRIIDP 217
Cdd:cd07574  156 SEFPELARALAEAGADLLLVPscTDTRAG-----YWRVRIgaQARALENQCYVVQSGTVGNapwspavdVNYGQAAVYTP 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446417925 218 L-------GVTIAAAADRPALIVAEIFRERIDQVREQ 247
Cdd:cd07574  231 CdfgfpedGILAEGEPNTEGWLIADLDLEALRRLREE 267
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-226 1.59e-13

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: 68.87  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   1 MFVAAGQFVVSSVWEENAQVC---VSLMAQAAGRGVSLLVLPEgiLA----------RDDIDLD------LPIRAAQPLd 61
Cdd:cd07569    4 VILAAAQMGPIARAETRESVVarlIALLEEAASRGAQLVVFPE--LAlttffprwyfPDEAELDsffeteMPNPETQPL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  62 gaFmtrlleESAHNNMTTIFTILVPSTPG----RAVN--MLVAlRAGHIVARYAKLHL--------YDAFSMQESQSIDA 127
Cdd:cd07569   81 --F------DRAKELGIGFYLGYAELTEDggvkRRFNtsILVD-KSGKIVGKYRKVHLpghkepepYRPFQHLEKRYFEP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 128 GTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLAL----PTGWVRGP----LKEQQWSTLLAARALDTTSYMI 199
Cdd:cd07569  152 GDLGFPVFRVPGGIMGMCICNDRRWPETWRVMGLQGVELVLLgyntPTHNPPAPehdhLRLFHNLLSMQAGAYQNGTWVV 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446417925 200 AAGECGNRN----IGQSRIIDPLGVTIAAAA 226
Cdd:cd07569  232 AAAKAGMEDgcdlIGGSCIVAPTGEIVAQAT 262
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
14-245 2.94e-12

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: 64.80  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  14 WEENAQVCVSLMAQAAGRGVSLLVLPEgiLA-----------RDDIdldlpIRAAQpldgAFMTRLLEESAHNNMTTIFT 82
Cdd:cd07570   14 LEGNAEKILEAIREAKAQGADLVVFPE--LSltgyppedlllRPDF-----LEAAE----EALEELAAATADLDIAVVVG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPsTPGRAVNMLVALRAGHIVARYAKLHL--YDAFsmQESQSIDAGTViAPVLDVEGVKVGLMTCYDLRFPD-MALAL 159
Cdd:cd07570   83 LPLR-HDGKLYNAAAVLQNGKILGVVPKQLLpnYGVF--DEKRYFTPGDK-PDVLFFKGLRIGVEICEDLWVPDpPSAEL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 160 ALQGADVLALPTG--WVRGplKEQQWSTLLAARALDTTSYMI--AAGECGNRNI--GQSRIIDPLGvTIAAAADRPALIV 233
Cdd:cd07570  159 ALAGADLILNLSAspFHLG--KQDYRRELVSSRSARTGLPYVyvNQVGGQDDLVfdGGSFIADNDG-ELLAEAPRFEEDL 235
                        250
                 ....*....|..
gi 446417925 234 AEIFRERIDQVR 245
Cdd:cd07570  236 ADVDLDRLRSER 247
PRK13981 PRK13981
NAD synthetase; Provisional
15-245 1.52e-11

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 64.02  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  15 EENAQVCVSLMAQAAGRGVSLLVLPE----G-----ILARDDIdldlpIRAAQpldgAFMTRLLEESAHNNMTTIFTILV 85
Cdd:PRK13981  16 AGNAAKILAAAAEAADAGADLLLFPElflsGyppedLLLRPAF-----LAACE----AALERLAAATAGGPAVLVGHPWR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  86 PstPGRAVNMLVALRAGHIVARYAKLHL--YDAFSmqESQSIDAGTVIAPVlDVEGVKVGLMTCYDLRFPDMALALALQG 163
Cdd:PRK13981  87 E--GGKLYNAAALLDGGEVLATYRKQDLpnYGVFD--EKRYFAPGPEPGVV-ELKGVRIGVPICEDIWNPEPAETLAEAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 164 ADVLALPTG--WVRGplKEQQWSTLLAARALDTTSYMIAAGECGnrniGQ--------SRIIDPLGVTIAAAADrpaliv 233
Cdd:PRK13981 162 AELLLVPNAspYHRG--KPDLREAVLRARVRETGLPLVYLNQVG----GQdelvfdgaSFVLNADGELAARLPA------ 229
                        250
                 ....*....|..
gi 446417925 234 aeiFRERIDQVR 245
Cdd:PRK13981 230 ---FEEQIAVVD 238
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
22-236 2.92e-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: 61.85  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  22 VSLMAQAAGRGVSLLVLPEGILardDIDLDLpiraaqplDGAFMTRLLEESAHNNMTTIFTILVPSTPGRAV-NMLVALR 100
Cdd:cd07571   29 LDLTRELADEKPDLVVWPETAL---PFDLQR--------DPDALARLARAARAVGAPLLTGAPRREPGGGRYyNSALLLD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 101 AGH-IVARYAKLHL-----Y----------DAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGA 164
Cdd:cd07571   98 PGGgILGRYDKHHLvpfgeYvplrdllrflGLLFDLPMGDFSPGTGPQPLLLGGGVRVGPLICYESIFPELVRDAVRQGA 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446417925 165 DVLALPT--GWV-RGPLKEQQWStlLAA-RALDTTSYMIAAGecgnrNIGQSRIIDPLGVTIAAAA-DRPALIVAEI 236
Cdd:cd07571  178 DLLVNITndAWFgDSAGPYQHLA--MARlRAIETGRPLVRAA-----NTGISAVIDPDGRIVARLPlFEAGVLVAEV 247
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
88-249 3.13e-11

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 61.68  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  88 TPGRAVNMLVALRAGHIVARYAKLHLydaFSM-QESQSIDAGTViAPVLDVEGVKVGLMTCYDLRFP-------DMALAL 159
Cdd:PRK10438  85 TESGAVNRFLLVEPGGTVHFYDKRHL---FRMaDEHLHYKAGNA-RVIVEWRGWRILPLVCYDLRFPvwsrnrnDYDLAL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 160 AlqgadVLALPTGwvrgplKEQQWSTLLAARALDTTSYMIA---AGECGNRNI--GQSRIIDPLGVTIAAA-ADRPALIV 233
Cdd:PRK10438 161 Y-----VANWPAP------RSLHWQTLLTARAIENQAYVAGcnrVGSDGNGHHyrGDSRIINPQGEIIATAePHQATRID 229
                        170
                 ....*....|....*.
gi 446417925 234 AEIFRERIDQVREQLP 249
Cdd:PRK10438 230 AELSLEALQEYREKFP 245
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-255 5.99e-11

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 61.32  E-value: 5.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPE---GILARDDIDLDLPIRAAqPLDG----AFMTRLLEEsahn 75
Cdd:PLN02747   9 VAALQFACSDDRAANVDKAERLVREAHAKGANIILIQElfeGYYFCQAQREDFFQRAK-PYEGhptiARMQKLAKE---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  76 nmttiFTILVP-STPGRA----VNMLVALRA-GHIVARYAKLHLYDAFSMQESQSIDAGTVIAPVLDVEGVKVGLMTCYD 149
Cdd:PLN02747  84 -----LGVVIPvSFFEEAnnahYNSIAIIDAdGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFDTKFAKIGVAICWD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 150 LRFPDMALALALQGADVLALPTG---------------WVRgPLKEQQWSTLLAARALDTTSYMIAAGECGNRNI---GQ 211
Cdd:PLN02747 159 QWFPEAARAMVLQGAEVLLYPTAigsepqdpgldsrdhWKR-VMQGHAGANLVPLVASNRIGTEILETEHGPSKItfyGG 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 446417925 212 SRIIDPLGVTIAAAADRP-ALIVAEIFRERIDQVREQLPLLQQRR 255
Cdd:PLN02747 238 SFIAGPTGEIVAEADDKAeAVLVAEFDLDQIKSKRASWGVFRDRR 282
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
16-246 3.04e-10

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: 59.22  E-value: 3.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  16 ENAQVCVSLMAQAAG--RGVSLLVLPE----GILARDDIDLDLpiraAQPLDGAFMTRLLEESAHNNMTTIFTILV--PS 87
Cdd:cd07565   21 ENAERIADMVEGTKRglPGMDLIVFPEystqGLMYDKWTMDET----ACTVPGPETDIFAEACKEAKVWGVFSIMErnPD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  88 TPGRAVNMLVALRA-GHIVARYAKLHLYDAFSMQEsqsidAGTVIAPVLD-VEGVKVGLMTCYDLRFPDMALALALQGAD 165
Cdd:cd07565   97 HGKNPYNTAIIIDDqGEIVLKYRKLHPWVPIEPWY-----PGDLGTPVCEgPKGSKIALIICHDGMYPEIARECAYKGAE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 166 VLALPTGWVRgPLKEqQWSTLLAARALDTTSYMIAAGECGNRNI----GQSRIIDPLGVTIAAAADRPALIV-AEIFRER 240
Cdd:cd07565  172 LIIRIQGYMY-PAKD-QWIITNKANAWCNLMYTASVNLAGFDGVfsyfGESMIVNFDGRTLGEGGREPDEIVtAELSPSL 249

                 ....*.
gi 446417925 241 IDQVRE 246
Cdd:cd07565  250 VRDARK 255
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
22-221 5.06e-10

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: 58.91  E-value: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   22 VSLMAQAAGRgVSLLVLPEGILArddIDLDLPIRAAQpldgafmTRLLEESAHNNMTTIFTIL--VPSTPGRAVNMLVAL 99
Cdd:TIGR00546 188 TSLTKQAVEK-PDLVVWPETAFP---FDLENSPQKLA-------DRLKLLVLSKGIPILIGAPdaVPGGPYHYYNSAYLV 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  100 -RAGHIVARYAKLHL----------------YDAFSMQESQSIDAGTvIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:TIGR00546 257 dPGGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLLSQEDFSRGP-GPQVLKLPGGKIAPLICYESIFPDLVRASARQ 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446417925  163 GADVLALPT--GWVRGPLKEQQWSTLLAARALDTTSYMIAAGecgnrNIGQSRIIDPLGVT 221
Cdd:TIGR00546 336 GAELLVNLTndAWFGDSSGPWQHFALARFRAIENGRPLVRAT-----NTGISAVIDPRGRT 391
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
15-254 6.73e-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: 57.93  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  15 EENAQVCVSLMAQAAGRGVSLLVLPE-GILARDDIDLDLPIRAAQPLDGAFMTRLLE-ESAHNNMTTIFTILVPSTPGRA 92
Cdd:cd07578   16 ERNIERLLALCEEAARAGARLIVTPEmATTGYCWYDRAEIAPFVEPIPGPTTARFAElAREHDCYIVVGLPEVDSRSGIY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  93 VNMLVALRAGHIVARYAKLHLYDAfsmqESQSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQGADVLALPTG 172
Cdd:cd07578   96 YNSAVLIGPSGVIGRHRKTHPYIS----EPKWAADGDLGHQVFDTEIGRIALLICMDIHFFETARLLALGGADVICHISN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 173 WvrgpLKEQQWSTLLAARALDTTSYMIAAGECG-NRNI---GQSRIIDPLGvTIAA---AADRPALIVAEIFRERIDQVR 245
Cdd:cd07578  172 W----LAERTPAPYWINRAFENGCYLIESNRWGlERGVqfsGGSCIIEPDG-TIQAsidSGDGVALGEIDLDRARHRQFP 246

                 ....*....
gi 446417925 246 EQLPLLQQR 254
Cdd:cd07578  247 GELVFTARR 255
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
3-172 1.36e-09

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: 57.18  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925   3 VAAGQFVVSSVWEENAQVCVSLMAQAAGRGVSLLVLPEGILArddiDLDLPIRAAQPLDGAFMTRLLEeSAHNNMTTIFT 82
Cdd:cd07579    2 IAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPELALT----GLDDPASEAESDTGPAVSALRR-LARRLRLYLVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  83 ILVPSTPGRAVNMLVALRAGHIVARYAKLHLYDafsmQESQSIDAGTVIaPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:cd07579   77 GFAEADGDGLYNSAVLVGPEGLVGTYRKTHLIE----PERSWATPGDTW-PVYDLPLGRVGLLIGHDALFPEAGRVLALR 151
                        170
                 ....*....|
gi 446417925 163 GADVLALPTG 172
Cdd:cd07579  152 GCDLLACPAA 161
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
22-236 2.46e-09

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 57.16  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  22 VSLMAQAAGRGVSLLVLPEGILarddidldlPIRAAQplDGAFMTRLLEESAHNNMTTIF-TILVPSTPGRAVNMLVALR 100
Cdd:COG0815  223 LDLTRELADDGPDLVVWPETAL---------PFLLDE--DPDALARLAAAAREAGAPLLTgAPRRDGGGGRYYNSALLLD 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 101 A-GHIVARYAKLHL----------------YDAFSMQESqSIDAGTViAPVLDVEGVKVGLMTCYDLRFPDMALALALQG 163
Cdd:COG0815  292 PdGGILGRYDKHHLvpfgeyvplrdllrplIPFLDLPLG-DFSPGTG-PPVLDLGGVRVGPLICYESIFPELVRDAVRAG 369
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446417925 164 ADVLALPT--GW---VRGPlkEQQWStLLAARALDTTSYMIAAGecgnrNIGQSRIIDPLGVTIAAAA-DRPALIVAEI 236
Cdd:COG0815  370 ADLLVNITndAWfgdSIGP--YQHLA-IARLRAIETGRPVVRAT-----NTGISAVIDPDGRVLARLPlFTRGVLVAEV 440
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
25-225 1.15e-07

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 52.19  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  25 MAQAAGRGVSLLVLPEG---ILARDDIDldlpiraaqpldgAFMTRLLEESAHNNMTTIFTILVPSTPGRAV---NMLVA 98
Cdd:PRK00302 250 LSRPALGPADLIIWPETaipFLLEDLPQ-------------AFLKALDDLAREKGSALITGAPRAENKQGRYdyyNSIYV 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  99 LRAGHIVARYAKLHL----------------YDAFSMQESqSIDAGTVIAPVLDVEGVKVGLMTCYDLRFPDMALALALQ 162
Cdd:PRK00302 317 LGPYGILNRYDKHHLvpfgeyvplesllrplAPFFNLPMG-DFSRGPYVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQ 395
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446417925 163 GADVLALPT--GW---VRGPLKEQQWSTLlaaRALDTTSYMI-AAgecgnrNIGQSRIIDPLGVTIAAA 225
Cdd:PRK00302 396 GADLLLNISndAWfgdSIGPYQHFQMARM---RALELGRPLIrAT------NTGITAVIDPLGRIIAQL 455
amiF PRK13287
formamidase; Provisional
17-246 8.19e-07

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 49.31  E-value: 8.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  17 NAQVCVSLMAQA-AGR-GVSLLVLPE--------GILARDDIDLDLpiraaqplDGAFMTRLLEESAHNNMTTIFTIL-- 84
Cdd:PRK13287  35 QIEQIIKTVHKTkAGYpGLDLIVFPEystqglntKKWTTEEFLCTV--------DGPEVDAFAQACKENKVWGVFSIMer 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925  85 --VPSTPgraVNMLVALRA-GHIVARYAKLHLYDAFSMQEsqsidAGTVIAPVLD-VEGVKVGLMTCYDLRFPDMALALA 160
Cdd:PRK13287 107 npDGNEP---YNTAIIIDDqGEIILKYRKLHPWVPVEPWE-----PGDLGIPVCDgPGGSKLAVCICHDGMFPEMAREAA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 161 LQGADVLALPTGWVrGPLKEqQWSTLLAARALDTTSYMIAAGECGNRNI----GQSRIIDPLGVTIAAAADRPALIV-AE 235
Cdd:PRK13287 179 YKGANVMIRISGYS-TQVRE-QWILTNRSNAWQNLMYTASVNLAGYDGVfyyfGEGQVCNFDGTTLVQGHRNPWEIVtAE 256
                        250
                 ....*....|.
gi 446417925 236 IFRERIDQVRE 246
Cdd:PRK13287 257 VRPDLADEARL 267
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
100-189 2.35e-04

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: 41.85  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446417925 100 RAGHIVARYAKLHLYDafsmqesqsiDAGTVIAPVLDVE------GVKVGLMTCYDLRFPDMALALALQ-GADVLALPTG 172
Cdd:cd07567  137 RDGTLIARYRKYNLFG----------EPGFDVPPEPEIVtfdtdfGVTFGIFTCFDILFKEPALELVKKlGVDDIVFPTA 206
                         90       100
                 ....*....|....*....|....*...
gi 446417925 173 WVRGP-----LKEQQ-WS-----TLLAA 189
Cdd:cd07567  207 WFSELpfltaVQIQQaWAyangvNLLAA 234
 
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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