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Conserved domains on  [gi|446991764|ref|WP_001069020|]
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MULTISPECIES: carbon-nitrogen family hydrolase [Leptospira]

Protein Classification

carbon-nitrogen family hydrolase( domain architecture ID 10166103)

carbon-nitrogen family hydrolase similar to nitrilase, which is involved in the reduction of organic nitrogen compounds and ammonia production, breaks carbon-nitrogen bonds and depends on a Glu-Lys-Cys catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-264 1.27e-110

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: 319.87  E-value: 1.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   7 NVALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATGFTM-RSERIAEADEGPTETFLQEIANFTRAT 85
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLI----EEAAAAGADLIVLPEMWNTGYFLdDLYELADEDGGETVSFLSELAKKHGVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  86 ICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRKVA 165
Cdd:cd07583   77 IVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 166 GE-TDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSishNGHSLAVAPNGDFVDAGEGNETILFYK 244
Cdd:cd07583  157 LEgAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEF---GGHSMVIDPWGEVLAEAGEEEEILTAE 233
                        250       260
                 ....*....|....*....|
gi 446991764 245 AHKNSISDYRKDFPVLLDRK 264
Cdd:cd07583  234 IDLEEVAEVRKKIPVFKDRR 253
 
Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-264 1.27e-110

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: 319.87  E-value: 1.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   7 NVALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATGFTM-RSERIAEADEGPTETFLQEIANFTRAT 85
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLI----EEAAAAGADLIVLPEMWNTGYFLdDLYELADEDGGETVSFLSELAKKHGVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  86 ICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRKVA 165
Cdd:cd07583   77 IVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 166 GE-TDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSishNGHSLAVAPNGDFVDAGEGNETILFYK 244
Cdd:cd07583  157 LEgAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEF---GGHSMVIDPWGEVLAEAGEEEEILTAE 233
                        250       260
                 ....*....|....*....|
gi 446991764 245 AHKNSISDYRKDFPVLLDRK 264
Cdd:cd07583  234 IDLEEVAEVRKKIPVFKDRR 253
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-264 3.04e-70

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 217.42  E-value: 3.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWENQKANYEHVRNLIHSTLEKNSnkkpDLILLPETFATGFTMRSER---IAEADEGPTETFLQEIANFT 82
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGA----DLVVFPELFLTGYPPEDDDlleLAEPLDGPALAALAELAREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGG--ENRHYSAGSEILSYNLNGFRITPFICYDIRFPEI 160
Cdd:COG0388   78 GIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVfdEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 161 FRKVAGE-TDIFTIHANWPVPR-IHHWELILKTRAIENQAYVFGVNRIGVAGynqSISHNGHSLAVAPNGDFVDAGEGNE 238
Cdd:COG0388  158 ARALALAgADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGED---GLVFDGGSMIVDPDGEVLAEAGDEE 234
                        250       260
                 ....*....|....*....|....*.
gi 446991764 239 TILFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:COG0388  235 GLLVADIDLDRLREARRRFPVLRDRR 260
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
6-262 1.22e-44

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 151.43  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWENQKANYEHVRNLihstLEKNSNKkpDLILLPETFATGFTMRS-ERIAEADEgpTETFLQEIANFTRA 84
Cdd:PRK10438   4 LKITLLQQPLVWMDGPANLRHFDRQ----LEGITGR--DVIVLPEMFTTGFAMEAaASSLPQDD--VVAWMTAKAQQTNA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  85 TIcAGWIRKNQNGKPFNTVSVVNPNGIIiLRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPeIFRKV 164
Cdd:PRK10438  76 LI-AGSVALQTESGAVNRFLLVEPGGTV-HFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFP-VWSRN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 165 AGETDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSIShnGHSLAVAPNGDFVDAGEGNE-TILFY 243
Cdd:PRK10438 153 RNDYDLALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYR--GDSRIINPQGEIIATAEPHQaTRIDA 230
                        250
                 ....*....|....*....
gi 446991764 244 KAHKNSISDYRKDFPVLLD 262
Cdd:PRK10438 231 ELSLEALQEYREKFPAWRD 249
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
8-241 5.71e-36

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: 129.01  E-value: 5.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764    8 VALIQCDLSWENQKANYEHVRNLIHSTLEKNSnkkpDLILLPETFATGFTMRSERIAEADEGPTET--FLQEIANFTRAT 85
Cdd:pfam00795   2 VALVQLPQGFWDLEANLQKALELIEEAARYGA----DLIVLPELFITGYPCWAHFLEAAEVGDGETlaGLAALARKNGIA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   86 ICAGWI-RKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGGENRH-----YSAGSEILSYNLNGFRITPFICYDIRFPE 159
Cdd:pfam00795  78 IVIGLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFrervlFEPGDGGTVFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  160 IFRKVA--GETDIFTIHANWPVPRI---HHWELILKTRAIENQAYVFGVNRIGVAGynQSISHNGHSLAVAPNGDFV-DA 233
Cdd:pfam00795 158 LLRALAlkGAEILINPSARAPFPGSlgpPQWLLLARARALENGCFVIAANQVGGEE--DAPWPYGHSMIIDPDGRILaGA 235

                  ....*...
gi 446991764  234 GEGNETIL 241
Cdd:pfam00795 236 GEWEEGVL 243
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
5-210 5.75e-16

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: 77.01  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764    5 ELNVALIQCDLS-WE-NQKANYEHVRNlIHSTLEKNSNKKPDLILLPETFatgftmrserIAEADEGPTETFLQEIANFT 82
Cdd:TIGR00546 159 TLNVALVQPNIPqDLkFDSEGLEAILE-ILTSLTKQAVEKPDLVVWPETA----------FPFDLENSPQKLADRLKLLV 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   83 RATICAGWI-----RKNQNGKPFNTVSVVNPNGIIILRYSKI----------YPFTFG--------GENRHYSAGSEILS 139
Cdd:TIGR00546 228 LSKGIPILIgapdaVPGGPYHYYNSAYLVDPGGEVVQRYDKVklvpfgeyipLGFLFKwlsklfflLSQEDFSRGPGPQV 307
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446991764  140 YNLNGFRITPFICYDIRFPEIFRKVA-GETDIFTIHAN--W----PVPRIHHWelILKTRAIENQAYVFGVNRIGVAG 210
Cdd:TIGR00546 308 LKLPGGKIAPLICYESIFPDLVRASArQGAELLVNLTNdaWfgdsSGPWQHFA--LARFRAIENGRPLVRATNTGISA 383
de_GSH_amidase NF033621
deaminated glutathione amidase;
96-264 3.90e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 73.39  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  96 NGKPFNTVSVVNpNGIIILRYSKIY---PFTFGgENRHYSAGSEILSY-NLNGFRITPFICYDIRFPEIFRKVAGE-TDI 170
Cdd:NF033621  88 DGRAWNTLVALR-DGEIIAQYRKLHlydAFSMQ-ESRRVDAGNEIPPLvEVAGMKVGLMTCYDLRFPELARRLALDgADV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 171 FTIHANW---PVpRIHHWELILKTRAIENQAYVFGVNRIGvagyNQSIshnGHSLAVAPNG-DFVDAGEgNETILFYKAH 246
Cdd:NF033621 166 LVLPAAWvrgPL-KEHHWETLLAARALENTCYMVAVGECG----NRNI---GQSMVVDPLGvTIAAAAE-APALIFAELD 236
                        170
                 ....*....|....*...
gi 446991764 247 KNSISDYRKDFPVLLDRK 264
Cdd:NF033621 237 PERIAHAREQLPVLENRR 254
 
Name Accession Description Interval E-value
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-264 1.27e-110

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: 319.87  E-value: 1.27e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   7 NVALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATGFTM-RSERIAEADEGPTETFLQEIANFTRAT 85
Cdd:cd07583    1 KIALIQLDIVWGDPEANIERVESLI----EEAAAAGADLIVLPEMWNTGYFLdDLYELADEDGGETVSFLSELAKKHGVN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  86 ICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRKVA 165
Cdd:cd07583   77 IVAGSVAEKEGGKLYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 166 GE-TDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSishNGHSLAVAPNGDFVDAGEGNETILFYK 244
Cdd:cd07583  157 LEgAEILFVPAEWPAARIEHWRTLLRARAIENQAFVVACNRVGTDGGNEF---GGHSMVIDPWGEVLAEAGEEEEILTAE 233
                        250       260
                 ....*....|....*....|
gi 446991764 245 AHKNSISDYRKDFPVLLDRK 264
Cdd:cd07583  234 IDLEEVAEVRKKIPVFKDRR 253
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
6-263 2.40e-82

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: 247.84  E-value: 2.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWENQKANYEHVRNLIHSTLEKnsnkkPDLILLPETFATGFTMRSERIAEADEGPTETFLQEIANFTRAT 85
Cdd:cd07575    1 LKIALIQTDLVWEDPEANLAHFEEKIEQLKEK-----TDLIVLPEMFTTGFSMNAEALAEPMNGPTLQWMKAQAKKKGAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  86 ICAGWIRKnQNGKPFNTVSVVNPNGIIILrYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPeIFRKVA 165
Cdd:cd07575   76 ITGSLIIK-EGGKYYNRLYFVTPDGEVYH-YDKRHLFRMAGEHKVYTAGNERVIVEYKGWKILLQVCYDLRFP-VWSRNT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 166 GETDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNqsISHNGHSLAVAPNGDFVDAGEGNETILFYKA 245
Cdd:cd07575  153 NDYDLLLYVANWPAPRRAAWDTLLKARAIENQAYVIGVNRVGTDGNG--LEYSGDSAVIDPLGEPLAEAEEDEGVLTATL 230
                        250
                 ....*....|....*...
gi 446991764 246 HKNSISDYRKDFPVLLDR 263
Cdd:cd07575  231 DKEALQEFREKFPFLKDA 248
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-264 3.04e-70

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 217.42  E-value: 3.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWENQKANYEHVRNLIHSTLEKNSnkkpDLILLPETFATGFTMRSER---IAEADEGPTETFLQEIANFT 82
Cdd:COG0388    2 MRIALAQLNPTVGDIEANLAKIEELIREAAAQGA----DLVVFPELFLTGYPPEDDDlleLAEPLDGPALAALAELAREL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGG--ENRHYSAGSEILSYNLNGFRITPFICYDIRFPEI 160
Cdd:COG0388   78 GIAVVVGLPERDEGGRLYNTALVIDPDGEILGRYRKIHLPNYGVfdEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 161 FRKVAGE-TDIFTIHANWPVPR-IHHWELILKTRAIENQAYVFGVNRIGVAGynqSISHNGHSLAVAPNGDFVDAGEGNE 238
Cdd:COG0388  158 ARALALAgADLLLVPSASPFGRgKDHWELLLRARAIENGCYVVAANQVGGED---GLVFDGGSMIVDPDGEVLAEAGDEE 234
                        250       260
                 ....*....|....*....|....*.
gi 446991764 239 TILFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:COG0388  235 GLLVADIDLDRLREARRRFPVLRDRR 260
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
8-264 2.00e-64

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: 202.17  E-value: 2.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATGF----TMRSERIAEADEGPTETFLQEIANFTR 83
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLI----KEAAEQGADLIVLPELFLTGYsfesAKEDLDLAEELDGPTLEALAELAKELG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  84 ATICAGWIRKNqNGKPFNTVSVVNPNGIIILRYSKIYPFTFGgENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRK 163
Cdd:cd07197   77 IYIVAGIAEKD-GDKLYNTAVVIDPDGEIIGKYRKIHLFDFG-ERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 164 VAGE-TDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIgvaGYNQSISHNGHSLAVAPNGDFVDAGEGNETILF 242
Cdd:cd07197  155 LALKgADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRV---GEEGGLEFAGGSMIVDPDGEVLAEASEEEGILV 231
                        250       260
                 ....*....|....*....|..
gi 446991764 243 YKAHKNSISDYRKDFPVLLDRK 264
Cdd:cd07197  232 AELDLDELREARKRWSYLRDRR 253
PRK10438 PRK10438
C-N hydrolase family amidase; Provisional
6-262 1.22e-44

C-N hydrolase family amidase; Provisional


Pssm-ID: 182461  Cd Length: 256  Bit Score: 151.43  E-value: 1.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWENQKANYEHVRNLihstLEKNSNKkpDLILLPETFATGFTMRS-ERIAEADEgpTETFLQEIANFTRA 84
Cdd:PRK10438   4 LKITLLQQPLVWMDGPANLRHFDRQ----LEGITGR--DVIVLPEMFTTGFAMEAaASSLPQDD--VVAWMTAKAQQTNA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  85 TIcAGWIRKNQNGKPFNTVSVVNPNGIIiLRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPeIFRKV 164
Cdd:PRK10438  76 LI-AGSVALQTESGAVNRFLLVEPGGTV-HFYDKRHLFRMADEHLHYKAGNARVIVEWRGWRILPLVCYDLRFP-VWSRN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 165 AGETDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSIShnGHSLAVAPNGDFVDAGEGNE-TILFY 243
Cdd:PRK10438 153 RNDYDLALYVANWPAPRSLHWQTLLTARAIENQAYVAGCNRVGSDGNGHHYR--GDSRIINPQGEIIATAEPHQaTRIDA 230
                        250
                 ....*....|....*....
gi 446991764 244 KAHKNSISDYRKDFPVLLD 262
Cdd:PRK10438 231 ELSLEALQEYREKFPAWRD 249
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-264 2.02e-42

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


Pssm-ID: 143605  Cd Length: 255  Bit Score: 145.80  E-value: 2.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLS--WEnqkANYEHVRNLIhstlEKNSNKKPDLILLPETFATGFT---MRSERIAEADEGPTETFLQEIANFT 82
Cdd:cd07581    1 VALAQFASSgdKE---ENLEKVRRLL----AEAAAAGADLVVFPEYTMARFGdglDDYARVAEPLDGPFVSALARLAREL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPF-TFG-GENRHYSAGSEI--LSYNLNGFRITPFICYDIRFP 158
Cdd:cd07581   74 GITVVAGMFEPAGDGRVYNTLVVVGPDGEIIAVYRKIHLYdAFGfRESDTVAPGDELppVVFVVGGVKVGLATCYDLRFP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 159 EIFRKVA--GeTDIFTIHANWpVP---RIHHWELILKTRAIENQAYVFGVNRIGvagynqsiSHN-GHSLAVAPNGDFV- 231
Cdd:cd07581  154 ELARALAlaG-ADVIVVPAAW-VAgpgKEEHWETLLRARALENTVYVAAAGQAG--------PRGiGRSMVVDPLGVVLa 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 446991764 232 DAGEGnETILFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:cd07581  224 DLGER-EGLLVADIDPERVEEAREALPVLENRR 255
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
8-260 1.56e-40

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: 141.03  E-value: 1.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSwENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFAT---GFTMRSERIAEADEGPTETFLQEIANFTRA 84
Cdd:cd07572    2 VALIQMTST-ADKEANLARAKELI----EEAAAQGAKLVVLPECFNYpggTDAFKLALAEEEGDGPTLQALSELAKEHGI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  85 TICAGWI--RKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTF---GG----ENRHYSAGSEILSYNLNGFRITPFICYDI 155
Cdd:cd07572   77 WLVGGSIpeRDDDDGKVYNTSLVFDPDGELVARYRKIHLFDVdvpGGisyrESDTLTPGDEVVVVDTPFGKIGLGICYDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 156 RFPEIFRKVAGE-TDI------FTIH---AnwpvprihHWELILKTRAIENQAYVFGVNRIGV--AGYnqsISHnGHSLA 223
Cdd:cd07572  157 RFPELARALARQgADIltvpaaFTMTtgpA--------HWELLLRARAIENQCYVVAAAQAGDheAGR---ETY-GHSMI 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446991764 224 VAPNGDFVDAGEGNETILFYKAHKNSISDYRKDFPVL 260
Cdd:cd07572  225 VDPWGEVLAEAGEGEGVVVAEIDLDRLEEVRRQIPVL 261
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-264 4.39e-37

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: 132.11  E-value: 4.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSWENQKANYEHVRNLIHSTleknSNKKPDLILLPETFATGFTMRSE-----RIAEADEGPTETFLQEIANFT 82
Cdd:cd07584    2 VALIQMDSVLGDVKANLKKAAELCKEA----AAEGADLICFPELATTGYRPDLLgpklwELSEPIDGPTVRLFSELAKEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGWIRK-NQNGKPFNTVSVVNPNGIIILRYSKIYpfTFGGENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIF 161
Cdd:cd07584   78 GVYIVCGFVEKgGVPGKVYNSAVVIDPEGESLGVYRKIH--LWGLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPEVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 162 RKVA--GETDIFTIHAnWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSishNGHSLAVAPNGDFV-DAGEGNE 238
Cdd:cd07584  156 RILTlkGAEVIFCPSA-WREQDADIWDINLPARALENTVFVAAVNRVGNEGDLVL---FGKSKILNPRGQVLaEASEEAE 231
                        250       260
                 ....*....|....*....|....*.
gi 446991764 239 TILFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:cd07584  232 EILYAEIDLDAIADYRMTLPYLKDRK 257
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
8-241 5.71e-36

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: 129.01  E-value: 5.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764    8 VALIQCDLSWENQKANYEHVRNLIHSTLEKNSnkkpDLILLPETFATGFTMRSERIAEADEGPTET--FLQEIANFTRAT 85
Cdd:pfam00795   2 VALVQLPQGFWDLEANLQKALELIEEAARYGA----DLIVLPELFITGYPCWAHFLEAAEVGDGETlaGLAALARKNGIA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   86 ICAGWI-RKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGGENRH-----YSAGSEILSYNLNGFRITPFICYDIRFPE 159
Cdd:pfam00795  78 IVIGLIeRWLTGGRLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFrervlFEPGDGGTVFDTPLGKIGAAICYEIRFPE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  160 IFRKVA--GETDIFTIHANWPVPRI---HHWELILKTRAIENQAYVFGVNRIGVAGynQSISHNGHSLAVAPNGDFV-DA 233
Cdd:pfam00795 158 LLRALAlkGAEILINPSARAPFPGSlgpPQWLLLARARALENGCFVIAANQVGGEE--DAPWPYGHSMIIDPDGRILaGA 235

                  ....*...
gi 446991764  234 GEGNETIL 241
Cdd:pfam00795 236 GEWEEGVL 243
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
7-264 8.18e-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: 123.46  E-value: 8.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   7 NVALIQCDLSWENQKANYEhvrnLIHSTLEKNSNKKPDLILLPETFATGFTMRSERI--AEADEGPTETFLQEIANFTRA 84
Cdd:cd07576    1 RLALYQGPARDGDVAANLA----RLDEAAARAAAAGADLLVFPELFLTGYNIGDAVArlAEPADGPALQALRAIARRHGI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  85 TICAGWIRKNQnGKPFNTVSVVNPNGIIILRYSKIypFTFGGENR-HYSAGSEILSYNLNGFRITPFICYDIRFPEIFRK 163
Cdd:cd07576   77 AIVVGYPERAG-GAVYNAAVLIDEDGTVLANYRKT--HLFGDSERaAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 164 VA--GETDIFTIHANW-PVPRIHHweLILKTRAIENQAYVFGVNRIGVAGynqSISHNGHSLAVAPNGDFVDAGEGNETI 240
Cdd:cd07576  154 LAlaGADLVLVPTALMePYGFVAR--TLVPARAFENQIFVAYANRCGAED---GLTYVGLSSIAGPDGTVLARAGRGEAL 228
                        250       260
                 ....*....|....*....|....
gi 446991764 241 LFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:cd07576  229 LVADLDPAALAAARRENPYLADRR 252
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
8-242 1.64e-31

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 117.40  E-value: 1.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSWENQKANYEHVRNLIhstleknSNKKPDLILLPETFATG--FTMRSE--RIAEAD-EGPTETFLQEIANFT 82
Cdd:cd07577    2 VGYVQFNPKFGEVEKNLKKVESLI-------KGVEADLIVLPELFNTGyaFTSKEEvaSLAESIpDGPTTRFLQELARET 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGWIRKNQNgKPFNTVSVVNPNGIIiLRYSKIYpfTFGGENRHYSAGSEILS-YNLNGFRITPFICYDIRFPEIF 161
Cdd:cd07577   75 GAYIVAGLPERDGD-KFYNSAVVVGPEGYI-GIYRKTH--LFYEEKLFFEPGDTGFRvFDIGDIRIGVMICFDWYFPEAA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 162 RKVA-GETDIFTIHANWPVPrihHWELILKTRAIENQAYVFGVNRIGV-AGYNQSISHNGHSLAVAPNGDFV-DAGEGNE 238
Cdd:cd07577  151 RTLAlKGADIIAHPANLVLP---YCPKAMPIRALENRVFTITANRIGTeERGGETLRFIGKSQITSPKGEVLaRAPEDGE 227

                 ....
gi 446991764 239 TILF 242
Cdd:cd07577  228 EVLV 231
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-229 7.24e-22

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


Pssm-ID: 143609  Cd Length: 261  Bit Score: 91.61  E-value: 7.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDlSWENQKAnyehvRNL--IHSTLEKNSNKKPDLILLPETFATGFT-MRS-ERIAEADEGPTETFLQEIANFTR 83
Cdd:cd07585    2 IALVQFE-ARVGDKA-----RNLavIARWTRKAAAQGAELVCFPEMCITGYThVRAlSREAEVPDGPSTQALSDLARRYG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  84 ATICAGWIRKNQnGKPFNTVSVVNPNGIIiLRYSKIYPFTfgGENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRK 163
Cdd:cd07585   76 LTILAGLIEKAG-DRPYNTYLVCLPDGLV-HRYRKLHLFR--REHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446991764 164 VA--GETDIFTIHANwpvPRIHH------WELILKTRAIENQAYVFGVNRIgvaGYNQSISHNGHSLAVAPNGD 229
Cdd:cd07585  152 TAllGAEILFAPHAT---PGTTSpkgrewWMRWLPARAYDNGVFVAACNGV---GRDGGEVFPGGAMILDPYGR 219
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
8-242 8.04e-20

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: 86.25  E-value: 8.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATG--FTMRSERIAEADE---GPTETFLQEIANFT 82
Cdd:cd07580    2 VACVQFDPRVGDLDANLARSIELI----REAADAGANLVVLPELANTGyvFESRDEAFALAEEvpdGASTRAWAELAAEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  83 RATICAGwIRKNQNGKPFNTVSVVNPNGIIiLRYSKIYpfTFGGENRHYSAGSEilsynlnGFRI--TPF------ICYD 154
Cdd:cd07580   78 GLYIVAG-FAERDGDRLYNSAVLVGPDGVI-GTYRKAH--LWNEEKLLFEPGDL-------GLPVfdTPFgrigvaICYD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 155 IRFPEIFRKVAGE-TDIFTIHANW-PVPRI----HHWELIL-KTRAIENQAYVFGVNRIGVagyNQSISHNGHSLAVAPN 227
Cdd:cd07580  147 GWFPETFRLLALQgADIVCVPTNWvPMPRPpeggPPMANILaMAAAHSNGLFIACADRVGT---ERGQPFIGQSLIVGPD 223
                        250
                 ....*....|....*..
gi 446991764 228 GDFVD--AGEGNETILF 242
Cdd:cd07580  224 GWPLAgpASGDEEEILL 240
nitrilase_4 cd07582
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
21-239 1.94e-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: 83.16  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  21 KANYEHVRNLIHSTLEKNSNKKP-DLILLPETFATGFTM--RSERIAEAD-----EGPTETFLQEIANFTRATICAGWIR 92
Cdd:cd07582   20 LANIDRINEQIDAAVGFSGPGLPvRLVVLPEYALQGFPMgePREVWQFDKaaidiPGPETEALGEKAKELNVYIAANAYE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  93 KNQN--GKPFNTVSVVNPNGIIILRYSK-IYPFTFGGENRH--YSAGSEILSYNLNGF---------RITPFICYDIRFP 158
Cdd:cd07582  100 RDPDfpGLYFNTAFIIDPSGEIILRYRKmNSLAAEGSPSPHdvWDEYIEVYGYGLDALfpvadteigNLGCLACEEGLYP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 159 EIFRKVAGETDIFTIHANWPVPRIHH--WELILKTRAIENQAYVFGVNRIGVAGYNQSI-SHNGHSLAVAPNGD-FVDAG 234
Cdd:cd07582  180 EVARGLAMNGAEVLLRSSSEVPSVELdpWEIANRARALENLAYVVSANSGGIYGSPYPAdSFGGGSMIVDYKGRvLAEAG 259

                 ....*
gi 446991764 235 EGNET 239
Cdd:cd07582  260 YGPGS 264
PLN02798 PLN02798
nitrilase
45-231 2.56e-17

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 79.79  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  45 LILLPETFATGFTMRSERIAEAD--EGPTETFLQEIANFTRATICAGWI--RKNQNGKPFNTVSVVNPNGIIILRYSKIY 120
Cdd:PLN02798  45 LLFLPECFSFIGDKDGESLAIAEplDGPIMQRYRSLARESGLWLSLGGFqeKGPDDSHLYNTHVLIDDSGEIRSSYRKIH 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 121 PFTF---GG----ENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRKVAGETDIFTIHanwpVPRIH-------HWE 186
Cdd:PLN02798 125 LFDVdvpGGpvlkESSFTAPGKTIVAVDSPVGRLGLTVCYDLRFPELYQQLRFEHGAQVLL----VPSAFtkptgeaHWE 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446991764 187 LILKTRAIENQAYVFGVNRIGVagYNQSISHNGHSLAVAPNGDFV 231
Cdd:PLN02798 201 VLLRARAIETQCYVIAAAQAGK--HNEKRESYGHALIIDPWGTVV 243
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
6-226 6.82e-17

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 79.89  E-value: 6.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQ----CDLSWENQKANyEHVRNLIHSTLEkNSNKKPDLILLPETFATGFTMRSERIAEAdegptetfLQEIANF 81
Cdd:COG0815  195 LRVALVQgnipQDLKWDPEQRR-EILDRYLDLTRE-LADDGPDLVVWPETALPFLLDEDPDALAR--------LAAAARE 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  82 TRATICAGWIRKN-QNGKPFNTVSVVNPNGIIILRYSKIY--PFtfgGEN------------------RHYSAGSEILSY 140
Cdd:COG0815  265 AGAPLLTGAPRRDgGGGRYYNSALLLDPDGGILGRYDKHHlvPF---GEYvplrdllrplipfldlplGDFSPGTGPPVL 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 141 NLNGFRITPFICYDIRFPEIFRK-VAGETDIFTIHAN--W----PVPRIHHWelILKTRAIENQAYVFgvnRIGVAGYNQ 213
Cdd:COG0815  342 DLGGVRVGPLICYESIFPELVRDaVRAGADLLVNITNdaWfgdsIGPYQHLA--IARLRAIETGRPVV---RATNTGISA 416
                        250
                 ....*....|...
gi 446991764 214 SISHNGHSLAVAP 226
Cdd:COG0815  417 VIDPDGRVLARLP 429
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-264 8.86e-17

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: 78.10  E-value: 8.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   7 NVALIQCDLSWENQKANYEHVRNLIhstlEKNSNKKPDLILLPETFATGFtMRSERIAEADEGPTETFLQEIANFTRA-T 85
Cdd:cd07586    1 RVAIAQIDPVLGDVEENLEKHLEII----ETARERGADLVVFPELSLTGY-NLGDLVYEVAMHADDPRLQALAEASGGiC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  86 ICAGWIRKNQNGKPFNTVSVVNpNGIIILRYSKIYPFTFGG--ENRHYSAGSEILSYNLNGFRITPFICYDIRFPEIFRK 163
Cdd:cd07586   76 VVFGFVEEGRDGRFYNSAAYLE-DGRVVHVHRKVYLPTYGLfeEGRYFAPGSHLRAFDTRFGRAGVLICEDAWHPSLPYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 164 VA--GETDIFtIHANWPVPRIHH-------WELILKTRAIENQAYVFGVNRIGVAGynqSISHNGHSLAVAPNGDFVDAG 234
Cdd:cd07586  155 LAldGADVIF-IPANSPARGVGGdfdneenWETLLKFYAMMNGVYVVFANRVGVED---GVYFWGGSRVVDPDGEVVAEA 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446991764 235 E-GNETILFYKAHKNSISDYRKDFPVLLDRK 264
Cdd:cd07586  231 PlFEEDLLVAELDRSAIRRARFFSPTFRDED 261
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
5-210 5.75e-16

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: 77.01  E-value: 5.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764    5 ELNVALIQCDLS-WE-NQKANYEHVRNlIHSTLEKNSNKKPDLILLPETFatgftmrserIAEADEGPTETFLQEIANFT 82
Cdd:TIGR00546 159 TLNVALVQPNIPqDLkFDSEGLEAILE-ILTSLTKQAVEKPDLVVWPETA----------FPFDLENSPQKLADRLKLLV 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   83 RATICAGWI-----RKNQNGKPFNTVSVVNPNGIIILRYSKI----------YPFTFG--------GENRHYSAGSEILS 139
Cdd:TIGR00546 228 LSKGIPILIgapdaVPGGPYHYYNSAYLVDPGGEVVQRYDKVklvpfgeyipLGFLFKwlsklfflLSQEDFSRGPGPQV 307
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446991764  140 YNLNGFRITPFICYDIRFPEIFRKVA-GETDIFTIHAN--W----PVPRIHHWelILKTRAIENQAYVFGVNRIGVAG 210
Cdd:TIGR00546 308 LKLPGGKIAPLICYESIFPDLVRASArQGAELLVNLTNdaWfgdsSGPWQHFA--LARFRAIENGRPLVRATNTGISA 383
de_GSH_amidase NF033621
deaminated glutathione amidase;
96-264 3.90e-15

deaminated glutathione amidase;


Pssm-ID: 468114  Cd Length: 260  Bit Score: 73.39  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  96 NGKPFNTVSVVNpNGIIILRYSKIY---PFTFGgENRHYSAGSEILSY-NLNGFRITPFICYDIRFPEIFRKVAGE-TDI 170
Cdd:NF033621  88 DGRAWNTLVALR-DGEIIAQYRKLHlydAFSMQ-ESRRVDAGNEIPPLvEVAGMKVGLMTCYDLRFPELARRLALDgADV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 171 FTIHANW---PVpRIHHWELILKTRAIENQAYVFGVNRIGvagyNQSIshnGHSLAVAPNG-DFVDAGEgNETILFYKAH 246
Cdd:NF033621 166 LVLPAAWvrgPL-KEHHWETLLAARALENTCYMVAVGECG----NRNI---GQSMVVDPLGvTIAAAAE-APALIFAELD 236
                        170
                 ....*....|....*...
gi 446991764 247 KNSISDYRKDFPVLLDRK 264
Cdd:NF033621 237 PERIAHAREQLPVLENRR 254
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
6-263 5.00e-14

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: 70.28  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSWeNQKANYEHVRNLIHSTLEKNSNkkpdLILLPETFATGFTMRSERI------AEADEGPTETFLQEIA 79
Cdd:cd07573    1 VTVALVQMACSE-DPEANLAKAEELVREAAAQGAQ----IVCLQELFETPYFCQEEDEdyfdlaEPPIPGPTTARFQALA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  80 NFTRATICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIY-PFTFGGENRHY-SAGSeilsynlNGFRI--TPF----- 150
Cdd:cd07573   76 KELGVVIPVSLFEKRGNGLYYNSAVVIDADGSLLGVYRKMHiPDDPGYYEKFYfTPGD-------TGFKVfdTRYgrigv 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 151 -ICYDIRFPEIFRKVA--GETDIF--------TIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGY-NQSISHN 218
Cdd:cd07573  149 lICWDQWFPEAARLMAlqGAEILFyptaigsePQEPPEGLDQRDAWQRVQRGHAIANGVPVAAVNRVGVEGDpGSGITFY 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446991764 219 GHSLAVAPNGDFV-DAGEGNETILFYKAHKNSISDYRKDFPVLLDR 263
Cdd:cd07573  229 GSSFIADPFGEILaQASRDEEEILVAEFDLDEIEEVRRAWPFFRDR 274
aliphatic_amidase cd07565
aliphatic amidases (class 2 nitrilases); Aliphatic amidases catalyze the hydrolysis of ...
8-238 2.33e-13

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: 68.47  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDL----SWENQKANYEHVRNLIHSTleKNSNKKPDLILLPETFATGFtmrSERIAEADE------GPtetflqE 77
Cdd:cd07565    3 VAVVQYKVpvlhTKEEVLENAERIADMVEGT--KRGLPGMDLIVFPEYSTQGL---MYDKWTMDEtactvpGP------E 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  78 IANFTRATICAG-W-----IRKN--QNGKPFNTVSVVNPNGIIILRYSKIYPFTfgGENRHYsAGSEIL--SYNLNGFRI 147
Cdd:cd07565   72 TDIFAEACKEAKvWgvfsiMERNpdHGKNPYNTAIIIDDQGEIVLKYRKLHPWV--PIEPWY-PGDLGTpvCEGPKGSKI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 148 TPFICYDIRFPEIFRKVA---GETDIFTIHANWPVPriHHWELILKTRAIENQAYVFGVNrigVAGYNQSISHNGHSLAV 224
Cdd:cd07565  149 ALIICHDGMYPEIARECAykgAELIIRIQGYMYPAK--DQWIITNKANAWCNLMYTASVN---LAGFDGVFSYFGESMIV 223
                        250
                 ....*....|....
gi 446991764 225 APNGDFVDAGEGNE 238
Cdd:cd07565  224 NFDGRTLGEGGREP 237
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
6-228 1.26e-12

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: 66.08  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQ----CDLSWENQKAnYEHVRNLIHSTlEKNSNKKPDLILLPETFATGFTMRSERIAEAdegptetfLQEIANF 81
Cdd:cd07571    1 LRVALVQgnipQDEKWDPEQR-QATLDRYLDLT-RELADEKPDLVVWPETALPFDLQRDPDALAR--------LARAARA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  82 TRATICAGWIRK-NQNGKPFNTVSVVNPNGIIILRYSKIY--PF---------------TFGGENRHYSAGSEILSYNLN 143
Cdd:cd07571   71 VGAPLLTGAPRRePGGGRYYNSALLLDPGGGILGRYDKHHlvPFgeyvplrdllrflglLFDLPMGDFSPGTGPQPLLLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 144 G-FRITPFICYDIRFPEIFRK-VAGETDIFTIHAN--W----PVPRIHHWelILKTRAIEnqayvfgvNRIGVAgynqSI 215
Cdd:cd07571  151 GgVRVGPLICYESIFPELVRDaVRQGADLLVNITNdaWfgdsAGPYQHLA--MARLRAIE--------TGRPLV----RA 216
                        250
                 ....*....|...
gi 446991764 216 SHNGHSLAVAPNG 228
Cdd:cd07571  217 ANTGISAVIDPDG 229
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
6-196 2.97e-10

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 60.28  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   6 LNVALIQCDLSwENQKANYEHVRNLI--HSTLEKNSNKKPDLILLPETFATGFTmrsERIAEAdegptetFLQEIANFTR 83
Cdd:PRK00302 220 LKVALVQGNIP-QSLKWDPAGLEATLqkYLDLSRPALGPADLIIWPETAIPFLL---EDLPQA-------FLKALDDLAR 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  84 ATICA------GWIRKNQNGKPFNTVSVVNPNGIIIlRYSKIY--PFtfgGE---------------NR---HYSAGSEI 137
Cdd:PRK00302 289 EKGSAlitgapRAENKQGRYDYYNSIYVLGPYGILN-RYDKHHlvPF---GEyvplesllrplapffNLpmgDFSRGPYV 364
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446991764 138 LSY-NLNGFRITPFICYDIRFPEIFRK-VAGETDIF-TIhAN--W----PVPRIHHweLILKTRAIEN 196
Cdd:PRK00302 365 QPPlLAKGLKLAPLICYEIIFPEEVRAnVRQGADLLlNI-SNdaWfgdsIGPYQHF--QMARMRALEL 429
amiF PRK13287
formamidase; Provisional
3-238 4.16e-10

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 59.32  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   3 PNELNVALIQCDL----SWENQKANYEHVRNLIHSTleKNSNKKPDLILLPETFATGFTMR---SERIAEADEGPtetfl 75
Cdd:PRK13287  11 IEGVLVALIQYPVpvveSRADIDKQIEQIIKTVHKT--KAGYPGLDLIVFPEYSTQGLNTKkwtTEEFLCTVDGP----- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  76 qEIANFTRATI------CAGWIRKNQNG-KPFNTVSVVNPNGIIILRYSKIYPFTfggENRHYSAGseilsyNL------ 142
Cdd:PRK13287  84 -EVDAFAQACKenkvwgVFSIMERNPDGnEPYNTAIIIDDQGEIILKYRKLHPWV---PVEPWEPG------DLgipvcd 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 143 --NGFRITPFICYDIRFPEIFRKVAGE-TDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNrigVAGYNQSISHNG 219
Cdd:PRK13287 154 gpGGSKLAVCICHDGMFPEMAREAAYKgANVMIRISGYSTQVREQWILTNRSNAWQNLMYTASVN---LAGYDGVFYYFG 230
                        250
                 ....*....|....*....
gi 446991764 220 HSLAVAPNGDFVDAGEGNE 238
Cdd:PRK13287 231 EGQVCNFDGTTLVQGHRNP 249
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
45-236 1.06e-08

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: 54.85  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  45 LILLPETFATGFT-MRSERIA---EADEGPTETFLQEIANFTRATICAGWIR-KNQNGKPFNTVSVVNPNGIIiLRYSKI 119
Cdd:cd07578   36 LIVTPEMATTGYCwYDRAEIApfvEPIPGPTTARFAELAREHDCYIVVGLPEvDSRSGIYYNSAVLIGPSGVI-GRHRKT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 120 YPFTfgGENRHYSAGS---EILSYNLNgfRITPFICYDIRFPEIFRKVA-GETDIFTIHANW-----PVPrihHWelilK 190
Cdd:cd07578  115 HPYI--SEPKWAADGDlghQVFDTEIG--RIALLICMDIHFFETARLLAlGGADVICHISNWlaertPAP---YW----I 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446991764 191 TRAIENQAYVFGVNRIGVagyNQSISHNGHSLAVAPNGDFV---DAGEG 236
Cdd:cd07578  184 NRAFENGCYLIESNRWGL---ERGVQFSGGSCIIEPDGTIQasiDSGDG 229
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
8-200 1.29e-08

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: 54.51  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQCDLSWENQKANYE-HVRNLIhstlEKNSNKKPDLILLPETFATG-FTMRSERIAEADE----GP--TETF---LQ 76
Cdd:cd07574    3 VAAAQYPLRRYASFEEFAaKVEYWV----AEAAGYGADLLVFPEYFTMElLSLLPEAIDGLDEairaLAalTPDYvalFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  77 EIANFTRATICAG---WIRknqNGKPFNTVSVVNPNGIIIlRYSKIYPFTFGGENRHYSAGSEILSYNLNGFRITPFICY 153
Cdd:cd07574   79 ELARKYGINIIAGsmpVRE---DGRLYNRAYLFGPDGTIG-HQDKLHMTPFEREEWGISGGDKLKVFDTDLGKIGILICY 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446991764 154 DIRFPEIFRKVAGE----------TDifTIHANWPVpRIHHWelilkTRAIENQAYV 200
Cdd:cd07574  155 DSEFPELARALAEAgadlllvpscTD--TRAGYWRV-RIGAQ-----ARALENQCYV 203
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
21-118 6.91e-07

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: 49.64  E-value: 6.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  21 KANYEHVRNLIHSTLEKNSNKKPDLILLPEtFA-TGFTMRS-ERI----AEADEGPTETFLQEIANFTRATICAGWIRKN 94
Cdd:cd07566   15 EENLSRAWELLDKTKKRAKLKKPDILVLPE-LAlTGYNFHSlEHIkpylEPTTSGPSFEWAREVAKKFNCHVVIGYPEKV 93
                         90       100
                 ....*....|....*....|....*.
gi 446991764  95 QNGKP--FNTVSVVNPNGIIILRYSK 118
Cdd:cd07566   94 DESSPklYNSALVVDPEGEVVFNYRK 119
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
65-266 1.04e-06

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: 49.03  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  65 EADEGPTETFLQEIANFTRATICAGWIRKNQNGKPFNTVSVVNPNGIIILRYSKIYPFTFGG--ENRHYSAGSeiLSYNL 142
Cdd:cd07568   72 EIPNGPTTKRFAALAKEYNMVLILPIYEKEQGGTLYNTAAVIDADGTYLGKYRKNHIPHVGGfwEKFYFRPGN--LGYPV 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 143 --NGF-RITPFICYDIRFPEIFRK--VAGETDIFTIHANWPVPRIHHWELILKTRAIENQAYVFGVNRIGVAGYNQSISH 217
Cdd:cd07568  150 fdTAFgKIGVYICYDRHFPEGWRAlgLNGAEIVFNPSATVAGLSEYLWKLEQPAAAVANGYFVGAINRVGTEAPWNIGEF 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446991764 218 NGHSLAVAPNGDFVDAGEGNET-ILFYKAHKNSISDYRKDFPVLLDRKDP 266
Cdd:cd07568  230 YGSSYFVDPRGQFVASASRDKDeLLVAELDLDLIREVRDTWQFYRDRRPE 279
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
8-231 2.94e-06

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: 47.46  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   8 VALIQC-----DLswenqKANYEHVRNLIHSTLEKNSnkkpDLILLPETFATGFT-----MRSERIAEADEGptetfLQE 77
Cdd:cd07570    2 IALAQLnptvgDL-----EGNAEKILEAIREAKAQGA----DLVVFPELSLTGYPpedllLRPDFLEAAEEA-----LEE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  78 IANFTRA---TICAGWIRKNqNGKPFNTVSVVNpNGIIILRYSKIY-P----FTfggENRHYSAGSEILSYNLNGFRITP 149
Cdd:cd07570   68 LAAATADldiAVVVGLPLRH-DGKLYNAAAVLQ-NGKILGVVPKQLlPnygvFD---EKRYFTPGDKPDVLFFKGLRIGV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 150 FICYDIRFPE---IFRKVAGETDIFTIHA-NWPVPRIHHWELILKTRAIENQAYVFGVNRIGvaGyNQSISHNGHSLAVA 225
Cdd:cd07570  143 EICEDLWVPDppsAELALAGADLILNLSAsPFHLGKQDYRRELVSSRSARTGLPYVYVNQVG--G-QDDLVFDGGSFIAD 219

                 ....*.
gi 446991764 226 PNGDFV 231
Cdd:cd07570  220 NDGELL 225
amiE PRK13286
aliphatic amidase;
96-255 3.26e-06

aliphatic amidase;


Pssm-ID: 237335  Cd Length: 345  Bit Score: 47.81  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  96 NGKPFNTVSVVNPNGIIILRYSKIYPFT-----FGGENRHYSAGSEilsynlnGFRITPFICYDIRFPEIFRKVA--GET 168
Cdd:PRK13286 112 RKAPYNTLILINDKGEIVQKYRKIMPWCpiegwYPGDCTYVSEGPK-------GLKISLIICDDGNYPEIWRDCAmkGAE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 169 DIFTIHAnWPVPRIHHWELILKTRAIENQAYVFGVNrigVAGYNQSISHNGHSLAVAPNGDFV-DAGEGNETILFYKAHK 247
Cdd:PRK13286 185 LIVRCQG-YMYPAKEQQVLVAKAMAWANNCYVAVAN---AAGFDGVYSYFGHSAIIGFDGRTLgECGEEEMGIQYAQLSV 260

                 ....*...
gi 446991764 248 NSISDYRK 255
Cdd:PRK13286 261 SQIRDARR 268
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
27-240 1.30e-05

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: 45.76  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  27 VRNLIhSTLEKNSNKKPDLILLPETFATGFTMR--SERIAEADEgpteTFLQEIAN------FTRAT-----ICAGWIRK 93
Cdd:cd07569   24 VARLI-ALLEEAASRGAQLVVFPELALTTFFPRwyFPDEAELDS----FFETEMPNpetqplFDRAKelgigFYLGYAEL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  94 NQNG---KPFNTVSVVNPNGIIILRYSKIY------PFTFGG----ENRHYSAGseilSYNLNGFRITP-----FICYDI 155
Cdd:cd07569   99 TEDGgvkRRFNTSILVDKSGKIVGKYRKVHlpghkePEPYRPfqhlEKRYFEPG----DLGFPVFRVPGgimgmCICNDR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 156 RFPEIFRKVA-GETDIF-------TIHANWPVP---RIHHWELILKTRAIENQAYVFGVNRigvAGYNQSISHNGHSLAV 224
Cdd:cd07569  175 RWPETWRVMGlQGVELVllgyntpTHNPPAPEHdhlRLFHNLLSMQAGAYQNGTWVVAAAK---AGMEDGCDLIGGSCIV 251
                        250
                 ....*....|....*...
gi 446991764 225 APNGDFV--DAGEGNETI 240
Cdd:cd07569  252 APTGEIVaqATTLEDEVI 269
PRK13981 PRK13981
NAD synthetase; Provisional
44-207 4.34e-05

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 44.38  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  44 DLILLPETFATGF-----TMRSERIAEADEGptetfLQEIANFTRATICA--GWIRKnQNGKPFNTVSVVNpNGIIILRY 116
Cdd:PRK13981  35 DLLLFPELFLSGYppedlLLRPAFLAACEAA-----LERLAAATAGGPAVlvGHPWR-EGGKLYNAAALLD-GGEVLATY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 117 SKIYPFTFG--GENRHYSAGSEILSYNLNGFRITPFICYDIRFPE-IFRKVAGETDIFTI------HANWPVPRihhwEL 187
Cdd:PRK13981 108 RKQDLPNYGvfDEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPEpAETLAEAGAELLLVpnaspyHRGKPDLR----EA 183
                        170       180
                 ....*....|....*....|
gi 446991764 188 ILKTRAIENQAYVFGVNRIG 207
Cdd:PRK13981 184 VLRARVRETGLPLVYLNQVG 203
PRK12291 PRK12291
apolipoprotein N-acyltransferase; Reviewed
3-182 2.64e-04

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 237042 [Multi-domain]  Cd Length: 418  Bit Score: 41.89  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   3 PNELNVALIQC----DLSWENQKANyEHVRNLIHStLEKNSNKKPDLILLPETfATGFTMRSEriaeadegptETFLQEI 78
Cdd:PRK12291 192 LPLVNIELVNTnipqDLKWDKENLK-SIINENLKE-IDKAIDEKKDLIVLPET-AFPLALNNS----------PILLDKL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  79 ANFT-RATICAGWIRKnQNGKPFN-TVSVVNPNgiiILRYSKIY--PF----------------TFGGENRHYSAGSEIL 138
Cdd:PRK12291 259 KELShKITIITGALRV-EDGHIYNsTYIFSKGN---VQIADKVIlvPFgeeiplpkffkkpinkLFFGGASDFSKASKFS 334
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446991764 139 SYNLNGFRITPFICYDIRFPEIFrkvAGETDIFTIHAN--WPVPRI 182
Cdd:PRK12291 335 DFTLDGVKFRNAICYEATSEELY---EGNPKIVIAISNnaWFVPSI 377
PLN02747 PLN02747
N-carbamolyputrescine amidase
1-274 5.28e-04

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 40.91  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764   1 MNPN-ELNVALIQCDLSwENQKANYEHVRNLIHSTLEKNSNkkpdLILLPETFATGFTMRSER-----IAEADEG-PTET 73
Cdd:PLN02747   1 MGMGrKVVVAALQFACS-DDRAANVDKAERLVREAHAKGAN----IILIQELFEGYYFCQAQRedffqRAKPYEGhPTIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764  74 FLQEIANFTRATICAGWIRKNQNGKpFNTVSVVNPNGIIILRYSKIY-PFTFGGENRHY-SAGSeilsynlNGFRI--TP 149
Cdd:PLN02747  76 RMQKLAKELGVVIPVSFFEEANNAH-YNSIAIIDADGTDLGLYRKSHiPDGPGYQEKFYfNPGD-------TGFKVfdTK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446991764 150 F------ICYDIRFPEIFRKVA--GETDIFTIHANWPVPR------IHHWELILKTRAIENQAYVFGVNRIGV-----AG 210
Cdd:PLN02747 148 FakigvaICWDQWFPEAARAMVlqGAEVLLYPTAIGSEPQdpgldsRDHWKRVMQGHAGANLVPLVASNRIGTeiletEH 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446991764 211 YNQSISHNGHSLAVAPNGDFV-DAGEGNETILFYKAHKNSISDYRKDFPVLLDRKdPNLIGIKVT 274
Cdd:PLN02747 228 GPSKITFYGGSFIAGPTGEIVaEADDKAEAVLVAEFDLDQIKSKRASWGVFRDRR-PDLYKVLLT 291
 
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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