NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488617042|ref|WP_002553891|]
View 

MULTISPECIES: carbon-nitrogen hydrolase family protein [Pseudomonas]

Protein Classification

carbon-nitrogen hydrolase family protein( domain architecture ID 10001265)

carbon-nitrogen hydrolase family protein 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-239 4.32e-45

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


:

Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 151.94  E-value: 4.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLAR--ALALHADDARLEPIKALAMKLRLVTTI 83
Cdd:COG0388    4 IALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDllELAEPLDGPALAALAELARELGIAVVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILIGALTFTADGD-VTTYAKQYLHP----GEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAA 158
Cdd:COG0388   84 GLPERDEGGRLYNTALVIDPDGEiLGRYRKIHLPNygvfDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARALAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042 159 GGAWVYAASVLISPG-GYAQDAELLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIGGMqGAGSGLVIVTCQ 237
Cdd:COG0388  164 AGADLLLVPSASPFGrGKDHWELLLRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEA-GDEEGLLVADID 242

                 ..
gi 488617042 238 RE 239
Cdd:COG0388  243 LD 244
 
Name Accession Description Interval E-value
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-239 4.32e-45

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 151.94  E-value: 4.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLAR--ALALHADDARLEPIKALAMKLRLVTTI 83
Cdd:COG0388    4 IALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDllELAEPLDGPALAALAELARELGIAVVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILIGALTFTADGD-VTTYAKQYLHP----GEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAA 158
Cdd:COG0388   84 GLPERDEGGRLYNTALVIDPDGEiLGRYRKIHLPNygvfDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARALAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042 159 GGAWVYAASVLISPG-GYAQDAELLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIGGMqGAGSGLVIVTCQ 237
Cdd:COG0388  164 AGADLLLVPSASPFGrGKDHWELLLRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEA-GDEEGLLVADID 242

                 ..
gi 488617042 238 RE 239
Cdd:COG0388  243 LD 244
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-235 5.06e-38

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: 133.22  E-value: 5.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARA---LALHADDARLEPIKALAMKLRLVTT 82
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEdldLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLKgANDSILIGALTFTADGD-VTTYAKQYL-HPGEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGG 160
Cdd:cd07197   81 AGIAEK-DGDKLYNTAVVIDPDGEiIGKYRKIHLfDFGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARELALKG 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617042 161 AWVYAASVLISPGGYAQDAELLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIgGMQGAGSGLVIVT 235
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFAGGSMIVDPDGEVL-AEASEEEGILVAE 233
PRK13981 PRK13981
NAD synthetase; Provisional
6-197 1.32e-22

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 95.99  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEP-DLARALALHAD-DARLEPI-KALAMKLRLVtt 82
Cdd:PRK13981   3 IALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPeDLLLRPAFLAAcEAALERLaAATAGGPAVL-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLkgANDSILIGALTFTADGDV-TTYAKQYLhPG-----EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRM 156
Cdd:PRK13981  81 VGHPW--REGGKLYNAAALLDGGEVlATYRKQDL-PNygvfdEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPEPAETL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488617042 157 AAGGawvyaASVLISPGG-------YAQDAELLAGHARRHNLPVLVAN 197
Cdd:PRK13981 158 AEAG-----AELLLVPNAspyhrgkPDLREAVLRARVRETGLPLVYLN 200
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
6-242 6.91e-17

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: 77.40  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042    6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGY-EPDLARALALHADDARLEPIKALAMKLRLVTTIG 84
Cdd:pfam00795   2 VALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYpCWAHFLEAAEVGDGETLAGLAALARKNGIAIVIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   85 VPLKG-ANDSILIGALTFTADGD-VTTYAKQYLHPG-------EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQR 155
Cdd:pfam00795  82 LIERWlTGGRLYNTAVLLDPDGKlVGKYRKLHLFPEprppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLRA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  156 MAAGGAWVYAASVLISPGGY--AQDAELLAGHAR--RHNLPVLVANH-GAPTGGWESAGRSGLWDGAGRWIGGMQGAGSG 230
Cdd:pfam00795 162 LALKGAEILINPSARAPFPGslGPPQWLLLARARalENGCFVIAANQvGGEEDAPWPYGHSMIIDPDGRILAGAGEWEEG 241
                         250
                  ....*....|..
gi 488617042  231 LVIVTCQREGWQ 242
Cdd:pfam00795 242 VLIADIDLALVR 253
 
Name Accession Description Interval E-value
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
6-239 4.32e-45

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 151.94  E-value: 4.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLAR--ALALHADDARLEPIKALAMKLRLVTTI 83
Cdd:COG0388    4 IALAQLNPTVGDIEANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDllELAEPLDGPALAALAELARELGIAVVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILIGALTFTADGD-VTTYAKQYLHP----GEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAA 158
Cdd:COG0388   84 GLPERDEGGRLYNTALVIDPDGEiLGRYRKIHLPNygvfDEKRYFTPGDELVVFDTDGGRIGVLICYDLWFPELARALAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042 159 GGAWVYAASVLISPG-GYAQDAELLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIGGMqGAGSGLVIVTCQ 237
Cdd:COG0388  164 AGADLLLVPSASPFGrGKDHWELLLRARAIENGCYVVAANQVGGEDGLVFDGGSMIVDPDGEVLAEA-GDEEGLLVADID 242

                 ..
gi 488617042 238 RE 239
Cdd:COG0388  243 LD 244
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
6-235 5.06e-38

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: 133.22  E-value: 5.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARA---LALHADDARLEPIKALAMKLRLVTT 82
Cdd:cd07197    1 IAAVQLAPKIGDVEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFESAKEdldLAEELDGPTLEALAELAKELGIYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLKgANDSILIGALTFTADGD-VTTYAKQYL-HPGEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGG 160
Cdd:cd07197   81 AGIAEK-DGDKLYNTAVVIDPDGEiIGKYRKIHLfDFGERRYFSPGDEFPVFDTPGGKIGLLICYDLRFPELARELALKG 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617042 161 AWVYAASVLISPGGYAQDAELLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIgGMQGAGSGLVIVT 235
Cdd:cd07197  160 ADIILVPAAWPTARREHWELLLRARAIENGVYVVAANRVGEEGGLEFAGGSMIVDPDGEVL-AEASEEEGILVAE 233
GAT_Gln-NAD-synth cd07570
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ...
6-199 8.05e-24

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: 96.00  E-value: 8.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPD---LARALALHADDArLEPIKALAMKLRLVTT 82
Cdd:cd07570    2 IALAQLNPTVGDLEGNAEKILEAIREAKAQGADLVVFPELSLTGYPPEdllLRPDFLEAAEEA-LEELAAATADLDIAVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLKgaNDSILIGALTFTADGDV-TTYAKQYLhPG-----EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPE-HVQR 155
Cdd:cd07570   81 VGLPLR--HDGKLYNAAAVLQNGKIlGVVPKQLL-PNygvfdEKRYFTPGDKPDVLFFKGLRIGVEICEDLWVPDpPSAE 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488617042 156 MAAGGawvyaASVLISP-------GGYAQDAELLAGHARRHNLPVLVANHG 199
Cdd:cd07570  158 LALAG-----ADLILNLsaspfhlGKQDYRRELVSSRSARTGLPYVYVNQV 203
PRK13981 PRK13981
NAD synthetase; Provisional
6-197 1.32e-22

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 95.99  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEP-DLARALALHAD-DARLEPI-KALAMKLRLVtt 82
Cdd:PRK13981   3 IALAQLNPTVGDIAGNAAKILAAAAEAADAGADLLLFPELFLSGYPPeDLLLRPAFLAAcEAALERLaAATAGGPAVL-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLkgANDSILIGALTFTADGDV-TTYAKQYLhPG-----EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRM 156
Cdd:PRK13981  81 VGHPW--REGGKLYNAAALLDGGEVlATYRKQDL-PNygvfdEKRYFAPGPEPGVVELKGVRIGVPICEDIWNPEPAETL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488617042 157 AAGGawvyaASVLISPGG-------YAQDAELLAGHARRHNLPVLVAN 197
Cdd:PRK13981 158 AEAG-----AELLLVPNAspyhrgkPDLREAVLRARVRETGLPLVYLN 200
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-240 3.96e-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: 143609  Cd Length: 261  Bit Score: 86.22  E-value: 3.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARALALHADDAR-LEPIKALAMKLRLvtTIG 84
Cdd:cd07585    2 IALVQFEARVGDKARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVRALSREAEVPDGPsTQALSDLARRYGL--TIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  85 VPL-KGANDSILIGALTFTADGDVTTYAKQYLHPGEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGGawv 163
Cdd:cd07585   80 AGLiEKAGDRPYNTYLVCLPDGLVHRYRKLHLFRREHPYIAAGDEYPVFATPGVRFGILICYDNHFPENVRATALLG--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042 164 yaASVLI----SPGGYAQDA-ELLAGH--ARRHNLPVLVA--NHGAPTGGWESAGRSGLWDGAGRWIGGMQGAGSGLVIV 234
Cdd:cd07585  157 --AEILFaphaTPGTTSPKGrEWWMRWlpARAYDNGVFVAacNGVGRDGGEVFPGGAMILDPYGRVLAETTSGGDGMVVA 234

                 ....*.
gi 488617042 235 TCQREG 240
Cdd:cd07585  235 DLDLDL 240
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
6-239 7.63e-19

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: 82.63  E-value: 7.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGY-EPDLARALALHADDARLEPIKALAMKLRLVTTIG 84
Cdd:cd07576    2 LALYQGPARDGDVAANLARLDEAAARAAAAGADLLVFPELFLTGYnIGDAVARLAEPADGPALQALRAIARRHGIAIVVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  85 VPLKGAnDSILIGALTFTADGDV-TTYAKQYLHPGEDK-VFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGGA- 161
Cdd:cd07576   82 YPERAG-GAVYNAAVLIDEDGTVlANYRKTHLFGDSERaAFTPGDRFPVVELRGLRVGLLICYDVEFPELVRALALAGAd 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488617042 162 WVYAASVLISPGGYAQDAeLLAGHARRHNLPVLVANHGAPTGGWESAGRSGLWDGAGRWIgGMQGAGSGLVIVTCQRE 239
Cdd:cd07576  161 LVLVPTALMEPYGFVART-LVPARAFENQIFVAYANRCGAEDGLTYVGLSSIAGPDGTVL-ARAGRGEALLVADLDPA 236
nitrilase_8 cd07586
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-197 2.24e-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: 78.87  E-value: 2.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYE-PDLARALALHADDARLEPIKALAMKLrlvttig 84
Cdd:cd07586    2 VAIAQIDPVLGDVEENLEKHLEIIETARERGADLVVFPELSLTGYNlGDLVYEVAMHADDPRLQALAEASGGI------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  85 vplkgandSILIGALTFTADGDVTTYAkQYLHPG------------------EDKVFSEGNKDCYLSIDQHRIGLCVCAD 146
Cdd:cd07586   75 --------CVVFGFVEEGRDGRFYNSA-AYLEDGrvvhvhrkvylptyglfeEGRYFAPGSHLRAFDTRFGRAGVLICED 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617042 147 FTQPEHVQRMAAGGawvyaASVLISP--------GGYAQDAE----LLAGHARRHNLPVLVAN 197
Cdd:cd07586  146 AWHPSLPYLLALDG-----ADVIFIPanspargvGGDFDNEEnwetLLKFYAMMNGVYVVFAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
6-242 6.91e-17

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: 77.40  E-value: 6.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042    6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGY-EPDLARALALHADDARLEPIKALAMKLRLVTTIG 84
Cdd:pfam00795   2 VALVQLPQGFWDLEANLQKALELIEEAARYGADLIVLPELFITGYpCWAHFLEAAEVGDGETLAGLAALARKNGIAIVIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   85 VPLKG-ANDSILIGALTFTADGD-VTTYAKQYLHPG-------EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQR 155
Cdd:pfam00795  82 LIERWlTGGRLYNTAVLLDPDGKlVGKYRKLHLFPEprppgfrERVLFEPGDGGTVFDTPLGKIGAAICYEIRFPELLRA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  156 MAAGGAWVYAASVLISPGGY--AQDAELLAGHAR--RHNLPVLVANH-GAPTGGWESAGRSGLWDGAGRWIGGMQGAGSG 230
Cdd:pfam00795 162 LALKGAEILINPSARAPFPGslGPPQWLLLARARalENGCFVIAANQvGGEEDAPWPYGHSMIIDPDGRILAGAGEWEEG 241
                         250
                  ....*....|..
gi 488617042  231 LVIVTCQREGWQ 242
Cdd:pfam00795 242 VLIADIDLALVR 253
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-164 1.76e-14

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: 70.64  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARALALHADDARLEPIKALAMKLRLVTTIGV 85
Cdd:cd07583    2 IALIQLDIVWGDPEANIERVESLIEEAAAAGADLIVLPEMWNTGYFLDDLYELADEDGGETVSFLSELAKKHGVNIVAGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  86 PLKGANDSILIGALTFTADGD-VTTYAKqyLHP----GEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGG 160
Cdd:cd07583   82 VAEKEGGKLYNTAYVIDPDGElIATYRK--IHLfglmGEDKYLTAGDELEVFELDGGKVGLFICYDLRFPELFRKLALEG 159

                 ....
gi 488617042 161 AWVY 164
Cdd:cd07583  160 AEIL 163
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-197 6.73e-13

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: 66.22  E-value: 6.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   7 AVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGY----EPDLARALALHADDARLEPIKALAMKLRLVTT 82
Cdd:cd07580    3 ACVQFDPRVGDLDANLARSIELIREAADAGANLVVLPELANTGYvfesRDEAFALAEEVPDGASTRAWAELAAELGLYIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  83 IGVPLKGA----NDSILIGaltftADGDVTTYAKQYLHPGEDKVFSEGNKDcYLSIDQH--RIGLCVCADFTQPEHVQRM 156
Cdd:cd07580   83 AGFAERDGdrlyNSAVLVG-----PDGVIGTYRKAHLWNEEKLLFEPGDLG-LPVFDTPfgRIGVAICYDGWFPETFRLL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488617042 157 AAGGA--------WVYAASVLisPGGYAQDAELLAGHARRHNLPVLVAN 197
Cdd:cd07580  157 ALQGAdivcvptnWVPMPRPP--EGGPPMANILAMAAAHSNGLFIACAD 203
nitrilase_1_R2 cd07579
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
6-193 1.67e-10

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: 59.88  E-value: 1.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSArGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARALALhaDDARLEPIKALAMKLRLVTTIGV 85
Cdd:cd07579    2 IAVAQFAPT-PDIAGNLATIDRLAAEAKATGAELVVFPELALTGLDDPASEAESD--TGPAVSALRRLARRLRLYLVAGF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  86 pLKGANDSILIGALTFTADGDVTTYAKQYLHPGEDKVFSEGnkDCYLSIDQH--RIGLCVCADFTQPEHVQRMAAGGAWV 163
Cdd:cd07579   79 -AEADGDGLYNSAVLVGPEGLVGTYRKTHLIEPERSWATPG--DTWPVYDLPlgRVGLLIGHDALFPEAGRVLALRGCDL 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 488617042 164 YAASVliSPGGYAQDAelLAGHARRHNLPV 193
Cdd:cd07579  156 LACPA--AIAIPFVGA--HAGTSVPQPYPI 181
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
6-158 1.95e-10

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


Pssm-ID: 143608  Cd Length: 258  Bit Score: 59.30  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARALALHADDARLEPI----KALAMKLRLVT 81
Cdd:cd07584    2 VALIQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLGPKLWELSEPIDGPTvrlfSELAKELGVYI 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488617042  82 TIGVPLKGA-NDSILIGALTFTADGDVT-TYAKQYLHPGEDKVFSEGNKDCYLSIDQHRIGLCVCADFTQPEhVQRMAA 158
Cdd:cd07584   82 VCGFVEKGGvPGKVYNSAVVIDPEGESLgVYRKIHLWGLEKQYFREGEQYPVFDTPFGKIGVMICYDMGFPE-VARILT 159
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
6-207 4.46e-10

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: 58.08  E-value: 4.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSARGDIEQNLaghlafmQRAADL----GASYLLFPELSLTGYepdlarALALHADDARL-EPI---------K 71
Cdd:cd07577    2 VGYVQFNPKFGEVEKNL-------KKVESLikgvEADLIVLPELFNTGY------AFTSKEEVASLaESIpdgpttrflQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  72 ALAMKLRLVTTIGVPLKGANDsILIGALTFTADGDVTTYAKQYLHPGEDKVFSEGNKDCYL-SIDQHRIGLCVCADFTQP 150
Cdd:cd07577   69 ELARETGAYIVAGLPERDGDK-FYNSAVVVGPEGYIGIYRKTHLFYEEKLFFEPGDTGFRVfDIGDIRIGVMICFDWYFP 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488617042 151 EHVQRMAAGGAWVYA-ASVLISPggYAQDAelLAGHARRHNLPVLVAN-HGAPTGGWES 207
Cdd:cd07577  148 EAARTLALKGADIIAhPANLVLP--YCPKA--MPIRALENRVFTITANrIGTEERGGET 202
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
6-161 2.52e-08

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: 53.20  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSaRGDIEQNLAGHLAFMQRAADLGASYLLFPE--LSLTGYEPDLARALALHADDARLEPIKALAMKLRLVTTI 83
Cdd:cd07572    2 VALIQMTS-TADKEANLARAKELIEEAAAQGAKLVVLPEcfNYPGGTDAFKLALAEEEGDGPTLQALSELAKEHGIWLVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 G-VPLKGANDS-ILIGALTFTADGD-VTTYAKqyLH------PG-----EDKVFSEGNKDCYLSIDQHRIGLCVCADFTQ 149
Cdd:cd07572   81 GsIPERDDDDGkVYNTSLVFDPDGElVARYRK--IHlfdvdvPGgisyrESDTLTPGDEVVVVDTPFGKIGLGICYDLRF 158
                        170
                 ....*....|..
gi 488617042 150 PEHVQRMAAGGA 161
Cdd:cd07572  159 PELARALARQGA 170
nadE PRK02628
NAD synthetase; Reviewed
16-87 1.02e-07

NAD synthetase; Reviewed


Pssm-ID: 235057 [Multi-domain]  Cd Length: 679  Bit Score: 52.17  E-value: 1.02e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488617042  16 GDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPD---LARALAlhadDARLEPIKALA---MKLRLVTTIGVPL 87
Cdd:PRK02628  25 ADPAFNAARILALARRAADDGVALAVFPELSLSGYSCDdlfLQDTLL----DAVEDALATLVeasADLDPLLVVGAPL 98
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
27-163 8.59e-06

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: 45.65  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  27 AFMQRAADLGASYLLFPELS---LTGYEPDLARAL--ALHADDARLEPIKA----LAMKLRlVTTIG--VPLKGANDSIL 95
Cdd:cd07574   25 YWVAEAAGYGADLLVFPEYFtmeLLSLLPEAIDGLdeAIRALAALTPDYVAlfseLARKYG-INIIAgsMPVREDGRLYN 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  96 IGALtFTADGDVTTYAKQYLHPGEDKV--FSEGNKDCYLSIDQHRIGLCVCADFTQPEHVQRMAAGGAWV 163
Cdd:cd07574  104 RAYL-FGPDGTIGHQDKLHMTPFEREEwgISGGDKLKVFDTDLGKIGILICYDSEFPELARALAEAGADL 172
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
7-235 1.19e-05

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: 45.26  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   7 AVAQFcSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLtGYEPDLARALALHA---DDARLEPIKALAMKLRLVTTI 83
Cdd:cd07581    2 ALAQF-ASSGDKEENLEKVRRLLAEAAAAGADLVVFPEYTM-ARFGDGLDDYARVAeplDGPFVSALARLARELGITVVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILIGALTFTADG-DVTTYAKQYLHPG----EDKVFSEGNKDC--YLSIDQHRIGLCVCADFTQPEHVQRM 156
Cdd:cd07581   80 GMFEPAGDGRVYNTLVVVGPDGeIIAVYRKIHLYDAfgfrESDTVAPGDELPpvVFVVGGVKVGLATCYDLRFPELARAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042 157 AAGGA--WVYAASVLISPGGYAQDAELLAGHARRHNLPVLVANHGAPTGgwesAGRSGLWDGAGRWIGGMqGAGSGLVIV 234
Cdd:cd07581  160 ALAGAdvIVVPAAWVAGPGKEEHWETLLRARALENTVYVAAAGQAGPRG----IGRSMVVDPLGVVLADL-GEREGLLVA 234

                 .
gi 488617042 235 T 235
Cdd:cd07581  235 D 235
Xc-1258_like cd07575
Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily ...
17-146 2.03e-04

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: 41.37  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  17 DIEQNLAgHLAFMQRAADLGASYLLFPELSLTGYEPDlARALALHADDARLEPIKALAMKLRLVTTIGVPLKgANDSILI 96
Cdd:cd07575   14 DPEANLA-HFEEKIEQLKEKTDLIVLPEMFTTGFSMN-AEALAEPMNGPTLQWMKAQAKKKGAAITGSLIIK-EGGKYYN 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488617042  97 GALTFTADGDVTTYAKQYL--HPGEDKVFSEGNKDCYLSIDQHRIGLCVCAD 146
Cdd:cd07575   91 RLYFVTPDGEVYHYDKRHLfrMAGEHKVYTAGNERVIVEYKGWKILLQVCYD 142
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
7-129 3.12e-04

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: 41.17  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   7 AVAQFCSARGDIEQNLAghLA------FMQRAADLGASYLLFPELSLTGYE-PDLARALAlHADDARLEPIKALA----M 75
Cdd:cd07566    3 ACLQLNPQIGQVEENLS--RAwelldkTKKRAKLKKPDILVLPELALTGYNfHSLEHIKP-YLEPTTSGPSFEWArevaK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488617042  76 KLRLVTTIGVPLKGANDSILI--GALTFTADGDVT-TYAKQYLHPGEDKVFSEGNKD 129
Cdd:cd07566   80 KFNCHVVIGYPEKVDESSPKLynSALVVDPEGEVVfNYRKSFLYYTDEEWGCEENPG 136
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
7-161 7.76e-04

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: 39.82  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   7 AVAQFCSARGDIEQNLAGHLAFMQRAADLGASYLLFPELSLTGYEPDLARALALHADD---ARLEPIKALAMKLRLVTTI 83
Cdd:cd07578    4 AAIQFEPEMGEKERNIERLLALCEEAARAGARLIVTPEMATTGYCWYDRAEIAPFVEPipgPTTARFAELAREHDCYIVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILI-GALTFTADGDVTTYAKQYLHPGEDKVFSEGNK-DCYLSIDQHRIGLCVCADFTQPEHVQRMAAGGA 161
Cdd:cd07578   84 GLPEVDSRSGIYYnSAVLIGPSGVIGRHRKTHPYISEPKWAADGDLgHQVFDTEIGRIALLICMDIHFFETARLLALGGA 163
PLN02798 PLN02798
nitrilase
6-177 5.91e-03

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 37.03  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042   6 LAVAQFCSArGDIEQNLAGHLAFMQRAADLGASYLLFPE-LSLTGYEPDLARALALHADDARLEPIKALAMKLRLVTTI- 83
Cdd:PLN02798  13 VAVAQMTST-NDLAANFATCSRLAKEAAAAGAKLLFLPEcFSFIGDKDGESLAIAEPLDGPIMQRYRSLARESGLWLSLg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617042  84 GVPLKGANDSILIGA-LTFTADGDV-TTYAKQYLH----PG-----EDKVFSEGNKdcYLSIDQ--HRIGLCVCADFTQP 150
Cdd:PLN02798  92 GFQEKGPDDSHLYNThVLIDDSGEIrSSYRKIHLFdvdvPGgpvlkESSFTAPGKT--IVAVDSpvGRLGLTVCYDLRFP 169
                        170       180
                 ....*....|....*....|....*..
gi 488617042 151 EHVQRMaaggAWVYAASVLISPGGYAQ 177
Cdd:PLN02798 170 ELYQQL----RFEHGAQVLLVPSAFTK 192
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH