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Conserved domains on  [gi|496081122|ref|WP_008805629|]
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MULTISPECIES: deaminated glutathione amidase [Klebsiella]

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;
2-261 0e+00

deaminated glutathione amidase;


:

Pssm-ID: 468114  Cd Length: 260  Bit Score: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVL 81
Cdd:NF033621   1 KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  82 TLHVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLAL 161
Cdd:NF033621  81 TVHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 162 NGAELLVLPTAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEHL 241
Cdd:NF033621 161 DGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERI 240
                        250       260
                 ....*....|....*....|
gi 496081122 242 ARVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 241 AHAREQLPVLENRRFAPPQL 260
 
Name Accession Description Interval E-value
de_GSH_amidase NF033621
deaminated glutathione amidase;
2-261 0e+00

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVL 81
Cdd:NF033621   1 KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  82 TLHVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLAL 161
Cdd:NF033621  81 TVHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 162 NGAELLVLPTAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEHL 241
Cdd:NF033621 161 DGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERI 240
                        250       260
                 ....*....|....*....|
gi 496081122 242 ARVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 241 AHAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 1.74e-116

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: 333.77  E-value: 1.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   3 VAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVLT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  83 LHVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPV-IEVAGLRVGLMTCYDLRFPELALSLA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVvFVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 161 LNGAELLVLPTAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEH 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 496081122 241 LARVRERLPVLQNRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 5.52e-85

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 254.40  E-value: 5.52e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPV-WRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTT 79
Cdd:COG0388    2 MRIALAQLNPTVGdIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  80 VLTLHVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELALS 158
Cdd:COG0388   82 VVGLPERDEGGRLYNTALVIdPDGEILGRYRKIHLPNYGVFDEKRYFTPGDE-LVVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 159 LALNGAELLVLPTAWVRGPQKEhHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTLAGAGSEPQLIFA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGRGKD-HWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 496081122 235 DVSAEHLARVRERLPVLQNRRF 256
Cdd:COG0388  240 DIDLDRLREARRRFPVLRDRRP 261
PLN02798 PLN02798
nitrilase
1-258 9.70e-48

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 159.91  E-value: 9.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPE--ALLARDDNDpdmSVKSAQPLDGAFLQ---LLLAESGrn 75
Cdd:PLN02798  11 VRVAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQryrSLARESG-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  76 rltTVLTL----HVPSAEGRATNTLVVLRD-GEVIAHYHKLHLYDAFA-----MQESRRVDPGQQIPPVIEVAGlRVGLM 145
Cdd:PLN02798  86 ---LWLSLggfqEKGPDDSHLYNTHVLIDDsGEIRSSYRKIHLFDVDVpggpvLKESSFTAPGKTIVAVDSPVG-RLGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 146 TCYDLRFPELALSLAL-NGAELLVLPTAWVRgPQKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLG 219
Cdd:PLN02798 162 VCYDLRFPELYQQLRFeHGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 496081122 220 TTLAGAGS--EPQLIFADVSAEHLARVRERLPVLQNRRFAP 258
Cdd:PLN02798 241 TVVARLPDrlSTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-245 1.25e-39

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: 137.87  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122    2 RVAAGQFAVTP--VWRtNAQTCVTMMQQAAREGAALLVLPEALLArDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTT 79
Cdd:pfam00795   1 RVALVQLPQGFwdLEA-NLQKALELIEEAARYGADLIVLPELFIT-GYPCWAHFLEAAEVGDGETLAGLAALARKNGIAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   80 VLTL-HVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFA---MQESRRVDPGQQIPpVIEVAGLRVGLMTCYDLRFPE 154
Cdd:pfam00795  79 VIGLiERWLTGGRLYNTAVLLdPDGKLVGKYRKLHLFPEPRppgFRERVLFEPGDGGT-VFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  155 LALSLALNGAELLVLPTAWVRGPQK--EHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTLAGAG- 226
Cdd:pfam00795 158 LLRALALKGAEILINPSARAPFPGSlgPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGe 237
                         250
                  ....*....|....*....
gi 496081122  227 SEPQLIFADVSAEHLARVR 245
Cdd:pfam00795 238 WEEGVLIADIDLALVRAWR 256
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
25-221 3.45e-11

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: 62.38  E-value: 3.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   25 MQQAAREGAALLVLPEALLARDDNDPDmsvksaQPLDGAFLQLLLAESgrnrlTTVLT---LHVPSAEGRATNTLVVL-R 100
Cdd:TIGR00546 190 LTKQAVEKPDLVVWPETAFPFDLENSP------QKLADRLKLLVLSKG-----IPILIgapDAVPGGPYHYYNSAYLVdP 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  101 DGEVIAHYHKLHL----------------YDAFAM--QESRRVDPGQQIPPVievAGLRVGLMTCYDLRFPELALSLALN 162
Cdd:TIGR00546 259 GGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLlsQEDFSRGPGPQVLKL---PGGKIAPLICYESIFPDLVRASARQ 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496081122  163 GAELLVLPT--AWVRGP--QKEHHWATLLAARALDTTCYIVAagecgtrNIGQSRIVDPLGTT 221
Cdd:TIGR00546 336 GAELLVNLTndAWFGDSsgPWQHFALARFRAIENGRPLVRAT-------NTGISAVIDPRGRT 391
 
Name Accession Description Interval E-value
de_GSH_amidase NF033621
deaminated glutathione amidase;
2-261 0e+00

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 525.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVL 81
Cdd:NF033621   1 KVALGQFAVTPDWQENAQTCVDLMAQAAEAGADLLVLPEAVLARDDTDPDLSVKSAQPLDGPFLTQLLAESRGNDLTTVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  82 TLHVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLAL 161
Cdd:NF033621  81 TVHVPSGDGRAWNTLVALRDGEIIAQYRKLHLYDAFSMQESRRVDAGNEIPPLVEVAGMKVGLMTCYDLRFPELARRLAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 162 NGAELLVLPTAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEHL 241
Cdd:NF033621 161 DGADVLVLPAAWVRGPLKEHHWETLLAARALENTCYMVAVGECGNRNIGQSMVVDPLGVTIAAAAEAPALIFAELDPERI 240
                        250       260
                 ....*....|....*....|
gi 496081122 242 ARVRERLPVLQNRRFAPPQL 261
Cdd:NF033621 241 AHAREQLPVLENRRFAPPQL 260
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
3-255 1.74e-116

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: 333.77  E-value: 1.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   3 VAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVLT 82
Cdd:cd07581    1 VALAQFASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  83 LHVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPV-IEVAGLRVGLMTCYDLRFPELALSLA 160
Cdd:cd07581   81 MFEPAGDGRVYNTLVVVgPDGEIIAVYRKIHLYDAFGFRESDTVAPGDELPPVvFVVGGVKVGLATCYDLRFPELARALA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 161 LNGAELLVLPTAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGTRNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEH 240
Cdd:cd07581  161 LAGADVIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRGIGRSMVVDPLGVVLADLGEREGLLVADIDPER 240
                        250
                 ....*....|....*
gi 496081122 241 LARVRERLPVLQNRR 255
Cdd:cd07581  241 VEEAREALPVLENRR 255
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
1-256 5.52e-85

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 254.40  E-value: 5.52e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPV-WRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTT 79
Cdd:COG0388    2 MRIALAQLNPTVGdIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPALAALAELARELGIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  80 VLTLHVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELALS 158
Cdd:COG0388   82 VVGLPERDEGGRLYNTALVIdPDGEILGRYRKIHLPNYGVFDEKRYFTPGDE-LVVFDTDGGRIGVLICYDLWFPELARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 159 LALNGAELLVLPTAWVRGPQKEhHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTLAGAGSEPQLIFA 234
Cdd:COG0388  161 LALAGADLLLVPSASPFGRGKD-HWELLLRARAIENGCYVVAANQVGGedglVFDGGSMIVDPDGEVLAEAGDEEGLLVA 239
                        250       260
                 ....*....|....*....|..
gi 496081122 235 DVSAEHLARVRERLPVLQNRRF 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 1.24e-72

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: 223.07  E-value: 1.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPE--ALLARDDNDPDMSvkSAQPLDGAFLQLLLAESGRNRLTT 79
Cdd:cd07572    1 RVALIQMTSTADKEANLARAKELIEEAAAQGAKLVVLPEcfNYPGGTDAFKLAL--AEEEGDGPTLQALSELAKEHGIWL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  80 VL-TLHVPSA-EGRATNTLVVL-RDGEVIAHYHKLHLYDAF-----AMQESRRVDPGQQIPPViEVAGLRVGLMTCYDLR 151
Cdd:cd07572   79 VGgSIPERDDdDGKVYNTSLVFdPDGELVARYRKIHLFDVDvpggiSYRESDTLTPGDEVVVV-DTPFGKIGLGICYDLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 152 FPELALSLALNGAELLVLPTA--WVRGPqkeHHWATLLAARALDTTCYIVAAGECGTRNI-----GQSRIVDPLGTTLAG 224
Cdd:cd07572  158 FPELARALARQGADILTVPAAftMTTGP---AHWELLLRARAIENQCYVVAAAQAGDHEAgretyGHSMIVDPWGEVLAE 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 496081122 225 AGSEPQLIFADVSAEHLARVRERLPVLQNRR 255
Cdd:cd07572  235 AGEGEGVVVAEIDLDRLEEVRRQIPVLKHRR 265
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
3-255 8.03e-65

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: 202.55  E-value: 8.03e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   3 VAAGQFAVTP-VWRTNAQTCVTMMQQAAREGAALLVLPE-ALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTV 80
Cdd:cd07197    1 IAAVQLAPKIgDVEANLAKALRLIKEAAEQGADLIVLPElFLTGYSFESAKEDLDLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  81 LTLHVpSAEGRATNTLVVL-RDGEVIAHYHKLHLydaFAMQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELALSL 159
Cdd:cd07197   81 AGIAE-KDGDKLYNTAVVIdPDGEIIGKYRKIHL---FDFGERRYFSPGDE-FPVFDTPGGKIGLLICYDLRFPELAREL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 160 ALNGAELLVLPTAWVRGPqkEHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTLAGAGSEPQLIFAD 235
Cdd:cd07197  156 ALKGADIILVPAAWPTAR--REHWELLLRARAIENGVYVVAANRVGEegglEFAGGSMIVDPDGEVLAEASEEEGILVAE 233
                        250       260
                 ....*....|....*....|
gi 496081122 236 VSAEHLARVRERLPVLQNRR 255
Cdd:cd07197  234 LDLDELREARKRWSYLRDRR 253
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-255 4.84e-60

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: 190.44  E-value: 4.84e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVtpVWRT---NAQTCVTMMQQAAREGAALLVLPEalLARDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLT 78
Cdd:cd07583    1 KIALIQLDI--VWGDpeaNIERVESLIEEAAAAGADLIVLPE--MWNTGYFLDDLYELADEDGGETVSFLSELAKKHGVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  79 TVLTLHVPSAEGRATNTLVVL-RDGEVIAHYHKLHLydaFA-MQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELA 156
Cdd:cd07583   77 IVAGSVAEKEGGKLYNTAYVIdPDGELIATYRKIHL---FGlMGEDKYLTAGDE-LEVFELDGGKVGLFICYDLRFPELF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 157 LSLALNGAELLVLPTAWvrgPQK-EHHWATLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTLAGAGSEPQL 231
Cdd:cd07583  153 RKLALEGAEILFVPAEW---PAArIEHWRTLLRARAIENQAFVVACNRVGTdggnEFGGHSMVIDPWGEVLAEAGEEEEI 229
                        250       260
                 ....*....|....*....|....
gi 496081122 232 IFADVSAEHLARVRERLPVLQNRR 255
Cdd:cd07583  230 LTAEIDLEEVAEVRKKIPVFKDRR 253
PLN02798 PLN02798
nitrilase
1-258 9.70e-48

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 159.91  E-value: 9.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPE--ALLARDDNDpdmSVKSAQPLDGAFLQ---LLLAESGrn 75
Cdd:PLN02798  11 VRVAVAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPEcfSFIGDKDGE---SLAIAEPLDGPIMQryrSLARESG-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  76 rltTVLTL----HVPSAEGRATNTLVVLRD-GEVIAHYHKLHLYDAFA-----MQESRRVDPGQQIPPVIEVAGlRVGLM 145
Cdd:PLN02798  86 ---LWLSLggfqEKGPDDSHLYNTHVLIDDsGEIRSSYRKIHLFDVDVpggpvLKESSFTAPGKTIVAVDSPVG-RLGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 146 TCYDLRFPELALSLAL-NGAELLVLPTAWVRgPQKEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLG 219
Cdd:PLN02798 162 VCYDLRFPELYQQLRFeHGAQVLLVPSAFTK-PTGEAHWEVLLRARAIETQCYVIAAAQAGKHNekresYGHALIIDPWG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 496081122 220 TTLAGAGS--EPQLIFADVSAEHLARVRERLPVLQNRRFAP 258
Cdd:PLN02798 241 TVVARLPDrlSTGIAVADIDLSLLDSVRTKMPIAEHRRSLE 281
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
26-257 1.89e-46

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: 155.43  E-value: 1.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  26 QQAAREGAALLVLPEALLArDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTTVLTLHVPSAEGRATNTLVVLRDGEVI 105
Cdd:cd07576   26 ARAAAAGADLLVFPELFLT-GYNIGDAVARLAEPADGPALQALRAIARRHGIAIVVGYPERAGGAVYNAAVLIDEDGTVL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 106 AHYHKLHLydaFAMQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVLPTAWVRGPQKEHHwaT 185
Cdd:cd07576  105 ANYRKTHL---FGDSERAAFTPGDR-FPVVELRGLRVGLLICYDVEFPELVRALALAGADLVLVPTALMEPYGFVAR--T 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496081122 186 LLAARALDTTCYIVAAGECGTRN----IGQSRIVDPLGTTLAGAGSEPQLIFADVSAEHLARVRERLPVLQNRRFA 257
Cdd:cd07576  179 LVPARAFENQIFVAYANRCGAEDgltyVGLSSIAGPDGTVLARAGRGEALLVADLDPAALAAARRENPYLADRRPE 254
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
2-245 1.25e-39

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: 137.87  E-value: 1.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122    2 RVAAGQFAVTP--VWRtNAQTCVTMMQQAAREGAALLVLPEALLArDDNDPDMSVKSAQPLDGAFLQLLLAESGRNRLTT 79
Cdd:pfam00795   1 RVALVQLPQGFwdLEA-NLQKALELIEEAARYGADLIVLPELFIT-GYPCWAHFLEAAEVGDGETLAGLAALARKNGIAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   80 VLTL-HVPSAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFA---MQESRRVDPGQQIPpVIEVAGLRVGLMTCYDLRFPE 154
Cdd:pfam00795  79 VIGLiERWLTGGRLYNTAVLLdPDGKLVGKYRKLHLFPEPRppgFRERVLFEPGDGGT-VFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  155 LALSLALNGAELLVLPTAWVRGPQK--EHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTLAGAG- 226
Cdd:pfam00795 158 LLRALALKGAEILINPSARAPFPGSlgPPQWLLLARARALENGCFVIAANQVGGEEdapwpYGHSMIIDPDGRILAGAGe 237
                         250
                  ....*....|....*....
gi 496081122  227 SEPQLIFADVSAEHLARVR 245
Cdd:pfam00795 238 WEEGVLIADIDLALVRAWR 256
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
15-255 1.96e-34

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


Pssm-ID: 143608  Cd Length: 258  Bit Score: 124.40  E-value: 1.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  15 RTNAQTCVTMMQQAAREGAALLVLPEalLARDDNDPDM----SVKSAQPLDGAFLQLLLAESGRNRLTTVLtlhvPSAE- 89
Cdd:cd07584   15 KANLKKAAELCKEAAAEGADLICFPE--LATTGYRPDLlgpkLWELSEPIDGPTVRLFSELAKELGVYIVC----GFVEk 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  90 ----GRATNTLVV-LRDGEVIAHYHKLHLYDafamQESRRVDPGQQIPpVIEVAGLRVGLMTCYDLRFPELALSLALNGA 164
Cdd:cd07584   89 ggvpGKVYNSAVViDPEGESLGVYRKIHLWG----LEKQYFREGEQYP-VFDTPFGKIGVMICYDMGFPEVARILTLKGA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 165 ELLVLPTAWVRgpQKEHHWATLLAARALDTTCYIVAAGECG----TRNIGQSRIVDPLGTTLAGAGSEP-QLIFADVSAE 239
Cdd:cd07584  164 EVIFCPSAWRE--QDADIWDINLPARALENTVFVAAVNRVGnegdLVLFGKSKILNPRGQVLAEASEEAeEILYAEIDLD 241
                        250
                 ....*....|....*.
gi 496081122 240 HLARVRERLPVLQNRR 255
Cdd:cd07584  242 AIADYRMTLPYLKDRK 257
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
1-255 4.64e-34

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: 124.21  E-value: 4.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLAR---DDNDPDMSVKSAQPLDG---AFLQLLLAESGr 74
Cdd:cd07573    1 VTVALVQMACSEDPEANLAKAEELVREAAAQGAQIVCLQELFETPyfcQEEDEDYFDLAEPPIPGpttARFQALAKELG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  75 nrlttvLTLHVP----SAEGRATNTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYD 149
Cdd:cd07573   80 ------VVIPVSlfekRGNGLYYNSAVVIdADGSLLGVYRKMHIPDDPGYYEKFYFTPGDTGFKVFDTRYGRIGVLICWD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 150 LRFPELALSLALNGAELLVLPTA--WVR-----GPQKEHHWATLLAARALDTTCYIVAAGECGTRNI--------GQSRI 214
Cdd:cd07573  154 QWFPEAARLMALQGAEILFYPTAigSEPqeppeGLDQRDAWQRVQRGHAIANGVPVAAVNRVGVEGDpgsgitfyGSSFI 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 496081122 215 VDPLGTTLAGAG-SEPQLIFADVSAEHLARVRERLPVLQNRR 255
Cdd:cd07573  234 ADPFGEILAQASrDEEEILVAEFDLDEIEEVRRAWPFFRDRR 275
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-255 6.77e-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: 143609  Cd Length: 261  Bit Score: 117.80  E-value: 6.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFaVTPVWRT--NAQTCVTMMQQAAREGAALLVLPEALL---ARDDNDPdmsvKSAQPLDGAFLQLLLAESGRNR 76
Cdd:cd07585    1 RIALVQF-EARVGDKarNLAVIARWTRKAAAQGAELVCFPEMCItgyTHVRALS----REAEVPDGPSTQALSDLARRYG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  77 LTTVLTLhVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDafamQESRRVDPGQQIPpVIEVAGLRVGLMTCYDLRFPELA 156
Cdd:cd07585   76 LTILAGL-IEKAGDRPYNTYLVCLPDGLVHRYRKLHLFR----REHPYIAAGDEYP-VFATPGVRFGILICYDNHFPENV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 157 LSLALNGAELLVLP--TAWVRGPQKEHHWATLLAARALDTTCYIVAAGECGtRNIGQSR-----IVDPLGTTLAGAGS-E 228
Cdd:cd07585  150 RATALLGAEILFAPhaTPGTTSPKGREWWMRWLPARAYDNGVFVAACNGVG-RDGGEVFpggamILDPYGRVLAETTSgG 228
                        250       260
                 ....*....|....*....|....*....
gi 496081122 229 PQLIFADVSAE--HLARVRERLPVLQNRR 255
Cdd:cd07585  229 DGMVVADLDLDliNTVRGRRWISFLRARR 257
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-255 3.94e-31

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


Pssm-ID: 143604  Cd Length: 268  Bit Score: 116.29  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAvtPVW---RTNAQTCVTMMQQAAREGAALLVLPEalLAR-----DDNDpDMSVKSAQPLDGAFLQLLLAESG 73
Cdd:cd07580    1 RVACVQFD--PRVgdlDANLARSIELIREAADAGANLVVLPE--LANtgyvfESRD-EAFALAEEVPDGASTRAWAELAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  74 RnrLTTVLTLHVPSAEG-RATNTLVVLRDGEVIAHYHKLHLYDafamQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRF 152
Cdd:cd07580   76 E--LGLYIVAGFAERDGdRLYNSAVLVGPDGVIGTYRKAHLWN----EEKLLFEPGDLGLPVFDTPFGRIGVAICYDGWF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 153 PELALSLALNGAELLVLPTAWVRGP-QKEHHWA---TLLAARALDTTCYIVAAGECGT----RNIGQSRIVDPLGTTLAG 224
Cdd:cd07580  150 PETFRLLALQGADIVCVPTNWVPMPrPPEGGPPmanILAMAAAHSNGLFIACADRVGTergqPFIGQSLIVGPDGWPLAG 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496081122 225 A--GSEPQLIFA--DVSAEHLARVRERLPVLQNRR 255
Cdd:cd07580  230 PasGDEEEILLAdiDLTAARRKRIWNSNDVLRDRR 264
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
33-255 3.71e-27

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: 105.46  E-value: 3.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  33 AALLVLPE------ALLARDDndpdmSVKSAQPL-DGAFLQLLLAESGRNRLTTVLTLHVPSaEGRATNTLVVLRDGEVI 105
Cdd:cd07577   30 ADLIVLPElfntgyAFTSKEE-----VASLAESIpDGPTTRFLQELARETGAYIVAGLPERD-GDKFYNSAVVVGPEGYI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 106 AHYHKLHLYDAfamqESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVLPTAWVRgPqkehHWAT 185
Cdd:cd07577  104 GIYRKTHLFYE----EKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPEAARTLALKGADIIAHPANLVL-P----YCPK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 186 LLAARALDTTCYIVAAGECGT--------RNIGQSRIVDPLGTTLAGAGSE-PQLIFADVSAEhLAR---VRERLPVLQN 253
Cdd:cd07577  175 AMPIRALENRVFTITANRIGTeerggetlRFIGKSQITSPKGEVLARAPEDgEEVLVAEIDPR-LARdkrINEENDIFKD 253

                 ..
gi 496081122 254 RR 255
Cdd:cd07577  254 RR 255
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
2-255 1.43e-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: 143610  Cd Length: 269  Bit Score: 98.90  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTP--VwRTNAQTCVTMMQQAAREGAALLVLPEALL---ARDDNDPDMSVKSAQPLdgafLQLLLAESGRnr 76
Cdd:cd07586    1 RVAIAQIDPVLgdV-EENLEKHLEIIETARERGADLVVFPELSLtgyNLGDLVYEVAMHADDPR----LQALAEASGG-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  77 LTTVLTLHVPSAEGRATNTLVVLRDGEVIaHYH-KLHLYDAFAMQESRRVDPGQQIPpVIEVAGLRVGLMTCYDLRFPEL 155
Cdd:cd07586   74 ICVVFGFVEEGRDGRFYNSAAYLEDGRVV-HVHrKVYLPTYGLFEEGRYFAPGSHLR-AFDTRFGRAGVLICEDAWHPSL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 156 ALSLALNGAELLVLPTAWVRGPQKEHH-----WATLLAARALDTTCYIVAAG----ECGTRNIGQSRIVDPLGTTLAGAG 226
Cdd:cd07586  152 PYLLALDGADVIFIPANSPARGVGGDFdneenWETLLKFYAMMNGVYVVFANrvgvEDGVYFWGGSRVVDPDGEVVAEAP 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 496081122 227 -SEPQLIFADVSAEHLARVRERLPVLQNRR 255
Cdd:cd07586  232 lFEEDLLVAELDRSAIRRARFFSPTFRDED 261
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
27-254 2.78e-24

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: 97.61  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  27 QAAREGAALLVLPEALLARDDNDPDmsvKSAQPLDGAFLQLLLAESgrNRLTTVLTLHVPSAE-GRATNTLV-VLRDGEV 104
Cdd:cd07575   27 EQLKEKTDLIVLPEMFTTGFSMNAE---ALAEPMNGPTLQWMKAQA--KKKGAAITGSLIIKEgGKYYNRLYfVTPDGEV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 105 IaHYHKLHLydaFAM-QESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPelALSLALNGAELLVLPTAWvrgPQKE-HH 182
Cdd:cd07575  102 Y-HYDKRHL---FRMaGEHKVYTAGNE-RVIVEYKGWKILLQVCYDLRFP--VWSRNTNDYDLLLYVANW---PAPRrAA 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496081122 183 WATLLAARALDTTCYIVAAGECGT-----RNIGQSRIVDPLGTTLAGAGSEPQLIFADVSAEHLARVRERLPVLQNR 254
Cdd:cd07575  172 WDTLLKARAIENQAYVIGVNRVGTdgnglEYSGDSAVIDPLGEPLAEAEEDEGVLTATLDKEALQEFREKFPFLKDA 248
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
2-255 2.68e-23

Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer.


Pssm-ID: 143594 [Multi-domain]  Cd Length: 261  Bit Score: 95.23  E-value: 2.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPV-WRTNAQTCVTMMQQAAREGAALLVLPEallarddndpdMSVKSAQPLD----GAF-------LQLLL 69
Cdd:cd07570    1 RIALAQLNPTVGdLEGNAEKILEAIREAKAQGADLVVFPE-----------LSLTGYPPEDlllrPDFleaaeeaLEELA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  70 AESGRNRLTTVLTLHVPSaEGRATNTLVVLRDGEVIAHYHKLHL--YDAFamQESRRVDPGQQiPPVIEVAGLRVGLMTC 147
Cdd:cd07570   70 AATADLDIAVVVGLPLRH-DGKLYNAAAVLQNGKILGVVPKQLLpnYGVF--DEKRYFTPGDK-PDVLFFKGLRIGVEIC 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 148 YDLRFPE-LALSLALNGAELLVLPTA--WVRGpqKEHHWATLLAARALDTTCYIV--AAGECGTRNI--GQSRIVDPLGT 220
Cdd:cd07570  146 EDLWVPDpPSAELALAGADLILNLSAspFHLG--KQDYRRELVSSRSARTGLPYVyvNQVGGQDDLVfdGGSFIADNDGE 223
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 496081122 221 TLAgAGSEPQLIFADVSAEHLARVRERLPVLQNRR 255
Cdd:cd07570  224 LLA-EAPRFEEDLADVDLDRLRSERRRNSSFLDEE 257
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
1-261 5.84e-22

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: 91.88  E-value: 5.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPV--WRTNAQTCVTMMQQAAREGAALLVLPE-------ALLARDDNDPDMSVKSAQPLDGAFLQLLLAE 71
Cdd:cd07574    1 VRVAAAQYPLRRYasFEEFAAKVEYWVAEAAGYGADLLVFPEyftmellSLLPEAIDGLDEAIRALAALTPDYVALFSEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  72 SGRNRLTTVLTLHVPSAEGRATNTLVVL-RDGEVIAHYhKLHLYDAfaMQESRRVDPGQQIPpVIEVAGLRVGLMTCYDL 150
Cdd:cd07574   81 ARKYGINIIAGSMPVREDGRLYNRAYLFgPDGTIGHQD-KLHMTPF--EREEWGISGGDKLK-VFDTDLGKIGILICYDS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 151 RFPELALSLALNGAELLVLP--TAWVRGPQKEHHWAtllAARALDTTCYIVAAGECGT--------RNIGQSRIVDPLGT 220
Cdd:cd07574  157 EFPELARALAEAGADLLLVPscTDTRAGYWRVRIGA---QARALENQCYVVQSGTVGNapwspavdVNYGQAAVYTPCDF 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 496081122 221 TLA-------GAGSEPQLIFADVSAEHLARVRERLPVlQNRRFAPPQL 261
Cdd:cd07574  234 GFPedgilaeGEPNTEGWLIADLDLEALRRLREEGSV-RNLRDWREDL 280
PRK13981 PRK13981
NAD synthetase; Provisional
1-199 5.50e-21

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 91.76  E-value: 5.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTpV--WRTNAQTCVTMMQQAAREGAALLVLPEA---------LLARDDndpdmSVKSAQpldgAFLQLLL 69
Cdd:PRK13981   1 LRIALAQLNPT-VgdIAGNAAKILAAAAEAADAGADLLLFPELflsgyppedLLLRPA-----FLAACE----AALERLA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  70 AESGRNrlTTVLTLHVPSAEGRATNTLVVLRDGEVIAHYHKLHL--YDAFamQESRRVDPGQQiPPVIEVAGLRVGLMTC 147
Cdd:PRK13981  71 AATAGG--PAVLVGHPWREGGKLYNAAALLDGGEVLATYRKQDLpnYGVF--DEKRYFAPGPE-PGVVELKGVRIGVPIC 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496081122 148 YDLRFPELALSLALNGAELLVLPTA--WVRGPQKEHHwaTLLAARALDTTCYIV 199
Cdd:PRK13981 146 EDIWNPEPAETLAEAGAELLLVPNAspYHRGKPDLRE--AVLRARVRETGLPLV 197
PLN02747 PLN02747
N-carbamolyputrescine amidase
3-255 1.83e-18

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 82.89  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   3 VAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLAR---DDNDPDMsVKSAQPLDG----AFLQLLLAEsgrn 75
Cdd:PLN02747   9 VAALQFACSDDRAANVDKAERLVREAHAKGANIILIQELFEGYyfcQAQREDF-FQRAKPYEGhptiARMQKLAKE---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  76 rLTTVLTlhVPSAEgRATNTL-----VVLRDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDL 150
Cdd:PLN02747  84 -LGVVIP--VSFFE-EANNAHynsiaIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFDTKFAKIGVAICWDQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 151 RFPELALSLALNGAELLVLPTAWVRGPQKE-----HHWATLLAARALDTTCYIVAAGECGTRNI------------GQSR 213
Cdd:PLN02747 160 WFPEAARAMVLQGAEVLLYPTAIGSEPQDPgldsrDHWKRVMQGHAGANLVPLVASNRIGTEILetehgpskitfyGGSF 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 496081122 214 IVDPLGTTLAGAGSEPQ-LIFADVSAEHLARVRERLPVLQNRR 255
Cdd:PLN02747 240 IAGPTGEIVAEADDKAEaVLVAEFDLDQIKSKRASWGVFRDRR 282
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
35-247 1.91e-18

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


Pssm-ID: 143606  Cd Length: 294  Bit Score: 82.78  E-value: 1.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  35 LLVLPE-ALLARDDNDPD---MSVKSAQPLDGAFLQLL--LAESGRNRLTTVLTLHVPSAEGRATNTLVVLR-DGEVIAH 107
Cdd:cd07582   45 LVVLPEyALQGFPMGEPRevwQFDKAAIDIPGPETEALgeKAKELNVYIAANAYERDPDFPGLYFNTAFIIDpSGEIILR 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 108 YHKLH------------LYDAFAMQESRRVDpgqQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVLPTAWVr 175
Cdd:cd07582  125 YRKMNslaaegspsphdVWDEYIEVYGYGLD---ALFPVADTEIGNLGCLACEEGLYPEVARGLAMNGAEVLLRSSSEV- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 176 gPQKEHHWATLLA-ARALDTTCYIVAAGECGTRNI--------GQSRIVDPLGTTL--AGAGSEPQLIFADVSAEHLARV 244
Cdd:cd07582  201 -PSVELDPWEIANrARALENLAYVVSANSGGIYGSpypadsfgGGSMIVDYKGRVLaeAGYGPGSMVAGAEIDIEALRRA 279

                 ...
gi 496081122 245 RER 247
Cdd:cd07582  280 RAR 282
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
19-255 2.19e-18

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: 82.54  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  19 QTCVTMMQQAAREGAALLVLPEA-----LLARDDNDpdmSVKSAQPLDGAFLQLLLAESGRnRLTTVLTLHVPSAEGRAT 93
Cdd:cd07568   30 QKHVTMIREAAEAGAQIVCLQEIfygpyFCAEQDTK---WYEFAEEIPNGPTTKRFAALAK-EYNMVLILPIYEKEQGGT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  94 --NTLVVL-RDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVLP 170
Cdd:cd07568  106 lyNTAAVIdADGTYLGKYRKNHIPHVGGFWEKFYFRPGNLGYPVFDTAFGKIGVYICYDRHFPEGWRALGLNGAEIVFNP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 171 TAWVRGpQKEHHWATLLAARALDTTCYIVAAGECGTR---NI----GQSRIVDPLGTTLAGAGS-EPQLIFADVSAEHLA 242
Cdd:cd07568  186 SATVAG-LSEYLWKLEQPAAAVANGYFVGAINRVGTEapwNIgefyGSSYFVDPRGQFVASASRdKDELLVAELDLDLIR 264
                        250
                 ....*....|...
gi 496081122 243 RVRERLPVLQNRR 255
Cdd:cd07568  265 EVRDTWQFYRDRR 277
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
3-237 9.98e-17

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: 77.71  E-value: 9.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   3 VAAGQFAVtPVWRT------NAQTCVTMMQQAAR--EGAALLVLPEALLARDDNDPDMSVKSAQPLDGAFLQLLLAESGR 74
Cdd:cd07565    3 VAVVQYKV-PVLHTkeevleNAERIADMVEGTKRglPGMDLIVFPEYSTQGLMYDKWTMDETACTVPGPETDIFAEACKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  75 NRLTTV--LTLHVPSAEGRATNTLVVLRD-GEVIAHYHKLHLYDAFAMQEsrrvdPGQQIPPVIE-VAGLRVGLMTCYDL 150
Cdd:cd07565   82 AKVWGVfsIMERNPDHGKNPYNTAIIIDDqGEIVLKYRKLHPWVPIEPWY-----PGDLGTPVCEgPKGSKIALIICHDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 151 RFPELALSLALNGAELLVLPTAWVRgpQKEHHWATLLAARALDTTCYIVAAGECGTRNI----GQSRIVDPLGTTLAGAG 226
Cdd:cd07565  157 MYPEIARECAYKGAELIIRIQGYMY--PAKDQWIITNKANAWCNLMYTASVNLAGFDGVfsyfGESMIVNFDGRTLGEGG 234
                        250
                 ....*....|..
gi 496081122 227 SEP-QLIFADVS 237
Cdd:cd07565  235 REPdEIVTAELS 246
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
2-172 1.12e-16

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: 77.60  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRTNAQTCVTMMQQAAREGAALLVLPEALLARDDNDPDMsvksAQPLDGAFLQLLLAESGRNRLTTVL 81
Cdd:cd07579    1 RIAVAQFAPTPDIAGNLATIDRLAAEAKATGAELVVFPELALTGLDDPASE----AESDTGPAVSALRRLARRLRLYLVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  82 TLHVPSAEGRATNTLVVLRDGeVIAHYHKLHLYDafamQESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPELALSLAL 161
Cdd:cd07579   77 GFAEADGDGLYNSAVLVGPEG-LVGTYRKTHLIE----PERSWATPGDT-WPVYDLPLGRVGLLIGHDALFPEAGRVLAL 150
                        170
                 ....*....|.
gi 496081122 162 NGAELLVLPTA 172
Cdd:cd07579  151 RGCDLLACPAA 161
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
1-236 2.99e-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: 76.58  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGQFAVTPVWRTNAQTC---VTMMQQAAREGAALLVLPE-AL-------LARDDNDPD------MSVKSAQPL--- 60
Cdd:cd07569    4 VILAAAQMGPIARAETRESVVarlIALLEEAASRGAQLVVFPElALttffprwYFPDEAELDsffeteMPNPETQPLfdr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  61 ---DGAFLQLLLAEsgrnrlttvLTLHvpSAEGRATNT-LVVLRDGEVIAHYHKLHL--------YDAFAMQESRRVDPG 128
Cdd:cd07569   84 akeLGIGFYLGYAE---------LTED--GGVKRRFNTsILVDKSGKIVGKYRKVHLpghkepepYRPFQHLEKRYFEPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 129 QQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVL---PTAWVRGPQKEHHWATL-----LAARALDTTCYIVA 200
Cdd:cd07569  153 DLGFPVFRVPGGIMGMCICNDRRWPETWRVMGLQGVELVLLgynTPTHNPPAPEHDHLRLFhnllsMQAGAYQNGTWVVA 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 496081122 201 AGECGTRN----IGQSRIVDPLGTTLAGAGS-EPQLIFADV 236
Cdd:cd07569  233 AAKAGMEDgcdlIGGSCIVAPTGEIVAQATTlEDEVIVADC 273
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
85-253 6.41e-14

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 69.38  E-value: 6.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  85 VPSAEGRATNTLVVLRDGEViAHYHKLHLydaFAM-QESRRVDPGQQiPPVIEVAGLRVGLMTCYDLRFPelALSLALNG 163
Cdd:PRK10438  83 LQTESGAVNRFLLVEPGGTV-HFYDKRHL---FRMaDEHLHYKAGNA-RVIVEWRGWRILPLVCYDLRFP--VWSRNRND 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 164 AELLVLPTAWvrgPQ-KEHHWATLLAARALDTTCYIVAAGECGTRN-----IGQSRIVDPLGTTLAGAGS-EPQLIFADV 236
Cdd:PRK10438 156 YDLALYVANW---PApRSLHWQTLLTARAIENQAYVAGCNRVGSDGnghhyRGDSRIINPQGEIIATAEPhQATRIDAEL 232
                        170
                 ....*....|....*..
gi 496081122 237 SAEHLARVRERLPVLQN 253
Cdd:PRK10438 233 SLEALQEYREKFPAWRD 249
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
2-255 2.90e-13

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: 67.56  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   2 RVAAGQFAVTPVWRT-NAQTCVTMMQQAAREGAALLVLPE------ALLARDDNDPDMsvksaQPLDGAFLQLLLAESGR 74
Cdd:cd07578    2 KAAAIQFEPEMGEKErNIERLLALCEEAARAGARLIVTPEmattgyCWYDRAEIAPFV-----EPIPGPTTARFAELARE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  75 NRLTTVLTL-HVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDAfamqESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFP 153
Cdd:cd07578   77 HDCYIVVGLpEVDSRSGIYYNSAVLIGPSGVIGRHRKTHPYIS----EPKWAADGDLGHQVFDTEIGRIALLICMDIHFF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 154 ELALSLALNGAELLVLPTAWV--RGPqkehhwATLLAARALDTTCYIVAAG----ECGTRNIGQSRIVDPLGTTLAGAGS 227
Cdd:cd07578  153 ETARLLALGGADVICHISNWLaeRTP------APYWINRAFENGCYLIESNrwglERGVQFSGGSCIIEPDGTIQASIDS 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 496081122 228 EPQLIFADVSAEHlARVRE--RLPVLQNRR 255
Cdd:cd07578  227 GDGVALGEIDLDR-ARHRQfpGELVFTARR 255
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
22-223 6.57e-13

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: 66.85  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  22 VTMMQQAAREGAALLVLPE-ALLARDDNDPDmsvksaqpldgaFLQLLLAESGRNRlTTVLT--LHVPSAEGRATNTLVV 98
Cdd:cd07571   29 LDLTRELADEKPDLVVWPEtALPFDLQRDPD------------ALARLARAARAVG-APLLTgaPRREPGGGRYYNSALL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  99 L-RDGEVIAHYHKLHL-----Y----------DAFAMQESRRVDPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLALN 162
Cdd:cd07571   96 LdPGGGILGRYDKHHLvpfgeYvplrdllrflGLLFDLPMGDFSPGTGPQPLLLGGGVRVGPLICYESIFPELVRDAVRQ 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496081122 163 GAELLVLPT--AWV-RGPQKEHHWAtlLAA-RALDTTCYIVAAGecgtrNIGQSRIVDPLGTTLA 223
Cdd:cd07571  176 GADLLVNITndAWFgDSAGPYQHLA--MARlRAIETGRPLVRAA-----NTGISAVIDPDGRIVA 233
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
22-223 1.15e-12

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 67.18  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  22 VTMMQQAAREGAALLVLPE-ALLARDDNDPDmsvksaqpldgaFLQLLLAESGRNRlTTVLT--LHVPSAEGRATNTLVV 98
Cdd:COG0815  223 LDLTRELADDGPDLVVWPEtALPFLLDEDPD------------ALARLAAAAREAG-APLLTgaPRRDGGGGRYYNSALL 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  99 LR-DGEVIAHYHKLHL----------------YDAFAMQESRRVdPGQQiPPVIEVAGLRVGLMTCYDLRFPELALSLAL 161
Cdd:COG0815  290 LDpDGGILGRYDKHHLvpfgeyvplrdllrplIPFLDLPLGDFS-PGTG-PPVLDLGGVRVGPLICYESIFPELVRDAVR 367
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496081122 162 NGAELLVLPT--AW-VRGPQKEHHWAtLLAARALDTTCYIVAAGecgtrNIGQSRIVDPLGTTLA 223
Cdd:COG0815  368 AGADLLVNITndAWfGDSIGPYQHLA-IARLRAIETGRPVVRAT-----NTGISAVIDPDGRVLA 426
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
25-221 3.45e-11

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: 62.38  E-value: 3.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   25 MQQAAREGAALLVLPEALLARDDNDPDmsvksaQPLDGAFLQLLLAESgrnrlTTVLT---LHVPSAEGRATNTLVVL-R 100
Cdd:TIGR00546 190 LTKQAVEKPDLVVWPETAFPFDLENSP------QKLADRLKLLVLSKG-----IPILIgapDAVPGGPYHYYNSAYLVdP 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  101 DGEVIAHYHKLHL----------------YDAFAM--QESRRVDPGQQIPPVievAGLRVGLMTCYDLRFPELALSLALN 162
Cdd:TIGR00546 259 GGEVVQRYDKVKLvpfgeyiplgflfkwlSKLFFLlsQEDFSRGPGPQVLKL---PGGKIAPLICYESIFPDLVRASARQ 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496081122  163 GAELLVLPT--AWVRGP--QKEHHWATLLAARALDTTCYIVAagecgtrNIGQSRIVDPLGTT 221
Cdd:TIGR00546 336 GAELLVNLTndAWFGDSsgPWQHFALARFRAIENGRPLVRAT-------NTGISAVIDPRGRT 391
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
94-189 4.04e-10

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: 58.79  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  94 NTLVVL-RDGEVIAHYHKLHLYdafamqesrrVDPGQQIPPVIEVA------GLRVGLMTCYDLRFPELALSLALN-GAE 165
Cdd:cd07567  130 NTNVVFdRDGTLIARYRKYNLF----------GEPGFDVPPEPEIVtfdtdfGVTFGIFTCFDILFKEPALELVKKlGVD 199
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496081122 166 LLVLPTAWVRGP------QKEHHWA-----TLLAA 189
Cdd:cd07567  200 DIVFPTAWFSELpfltavQIQQAWAyangvNLLAA 234
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
27-223 1.71e-08

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 54.50  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  27 QAAREGAALLVLPEALLarddndPDMSVKSAQPLDGAFLQLLlaesgRNRLTTVLT----LHVPSAEGRATNTLVVLRDG 102
Cdd:PRK00302 252 RPALGPADLIIWPETAI------PFLLEDLPQAFLKALDDLA-----REKGSALITgaprAENKQGRYDYYNSIYVLGPY 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 103 EVIAHYHKLHL----------------YDAFAMQESrrvD--PGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGA 164
Cdd:PRK00302 321 GILNRYDKHHLvpfgeyvplesllrplAPFFNLPMG---DfsRGPYVQPPLLAKGLKLAPLICYEIIFPEEVRANVRQGA 397
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496081122 165 ELLVLPT--AW---VRGPQKEHHWATLlaaRALDTTCYIVAAgecgTrNIGQSRIVDPLGTTLA 223
Cdd:PRK00302 398 DLLLNISndAWfgdSIGPYQHFQMARM---RALELGRPLIRA----T-NTGITAVIDPLGRIIA 453
amiF PRK13287
formamidase; Provisional
94-248 1.30e-05

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 45.45  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  94 NTLVVLRD-GEVIAHYHKLHLYDAFAMQEsrrvdPGQQIPPVIE-VAGLRVGLMTCYDLRFPELALSLALNGAELLVLP- 170
Cdd:PRK13287 115 NTAIIIDDqGEIILKYRKLHPWVPVEPWE-----PGDLGIPVCDgPGGSKLAVCICHDGMFPEMAREAAYKGANVMIRIs 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 171 --TAWVRgpqkeHHWATLLAARALDTTCYIVAAGECGTRNI----GQSRIVDPLGTTLAGAGSEPQLIfadVSAEhlarV 244
Cdd:PRK13287 190 gySTQVR-----EQWILTNRSNAWQNLMYTASVNLAGYDGVfyyfGEGQVCNFDGTTLVQGHRNPWEI---VTAE----V 257

                 ....
gi 496081122 245 RERL 248
Cdd:PRK13287 258 RPDL 261
nadE PRK02628
NAD synthetase; Reviewed
1-248 2.26e-05

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 45.24  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122   1 MRVAAGqfavTPVWR-----TNAQTCVTMMQQAAREGAALLVLPEALLarddndpdmsvkSAQPLDGAFLQ--LL----- 68
Cdd:PRK02628  13 VRVAAA----TPKVRvadpaFNAARILALARRAADDGVALAVFPELSL------------SGYSCDDLFLQdtLLdaved 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  69 ----LAESGRNrLTTVLTLHVP-SAEGRATNTLVVLRDGEVIA------------HYHKLHLYDAFAMQESRRVDPGQQI 131
Cdd:PRK02628  77 alatLVEASAD-LDPLLVVGAPlRVRHRLYNCAVVIHRGRILGvvpksylpnyreFYEKRWFAPGDGARGETIRLCGQEV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122 132 P-------PVIEVAGLRVGLMTCYDLRFPELALS-LALNGAELLVLPTA---WVRGPQKEHHWATLLAARALDTTCYiVA 200
Cdd:PRK02628 156 PfgtdllfEAEDLPGFVFGVEICEDLWVPIPPSSyAALAGATVLANLSAsniTVGKADYRRLLVASQSARCLAAYVY-AA 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496081122 201 AGEcG--TRNI---GQSRIVDpLGTTLAGA---GSEPQLIFADVSAEHLArvRERL 248
Cdd:PRK02628 235 AGV-GesTTDLawdGQTLIYE-NGELLAESerfPREEQLIVADVDLERLR--QERL 286
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
95-173 3.30e-05

Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 3.


Pssm-ID: 143590  Cd Length: 295  Bit Score: 44.25  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  95 TLVVLRDGEVIAHYHKLHLY---DAFAMQES--------RRVDPGQQIPPVIEVAGLRVGLMTCYDL---RF--P----E 154
Cdd:cd07566  104 ALVVDPEGEVVFNYRKSFLYytdEEWGCEENpggfqtfpLPFAKDDDFDGGSVDVTLKTSIGICMDLnpyKFeaPftdfE 183
                         90
                 ....*....|....*....
gi 496081122 155 LALSLALNGAELLVLPTAW 173
Cdd:cd07566  184 FATHVLDNGTELIICPMAW 202
amiE PRK13286
aliphatic amidase;
94-237 3.15e-04

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 41.26  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  94 NTLVVLRD-GEVIAHYHKLH-------LYdafamqesrrvdPGQQIPPVIEVAGLRVGLMTCYDLRFPELALSLALNGAE 165
Cdd:PRK13286 117 NTLILINDkGEIVQKYRKIMpwcpiegWY------------PGDCTYVSEGPKGLKISLIICDDGNYPEIWRDCAMKGAE 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496081122 166 LLVLPTAWVRgPQKEHhwaTLLAARALD--TTCYIVAAGECGTRNI----GQSRIVDPLGTTLAGAGSEPQLI-FADVS 237
Cdd:PRK13286 185 LIVRCQGYMY-PAKEQ---QVLVAKAMAwaNNCYVAVANAAGFDGVysyfGHSAIIGFDGRTLGECGEEEMGIqYAQLS 259
PLN00202 PLN00202
beta-ureidopropionase
57-201 4.78e-04

beta-ureidopropionase


Pssm-ID: 177792  Cd Length: 405  Bit Score: 40.98  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496081122  57 AQPLDG---AFLQLLLAESGRNRLTTVLTLHVPSAEGRATNTLVVLRDGEVIAHYHKLHLYDAFAMQESRRVDPGQQIPP 133
Cdd:PLN00202 153 AEPVDGestKFLQELARKYNMVIVSPILERDVNHGETLWNTAVVIGNNGNIIGKHRKNHIPRVGDFNESTYYMEGNTGHP 232
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496081122 134 VIEVAGLRVGLMTCYDLRFPELALSLALNGAELLVLPTAWVrGPQKEHHWAtLLAARALDTTCYIVAA 201
Cdd:PLN00202 233 VFETAFGKIAVNICYGRHHPLNWLAFGLNGAEIVFNPSATV-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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