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Conserved domains on  [gi|18859539|ref|NP_572297|]
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vanin-like [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
33-304 3.40e-132

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


:

Pssm-ID: 143591  Cd Length: 299  Bit Score: 386.98  E-value: 3.40e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  33 YTAGVVEFKQsILS-----LSAWSDSLAGYVEIINSENASATDIIVFPESTLNSAGSTTFVPNPEDQI--------NPCL 99
Cdd:cd07567   1 YIAAVVEHHP-ILSpdpdaLQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDvpdpevnwNPCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 100 sDPNATYYEEFLVTLSCAARNASKYIVINLTEKQKCEDipeDTRPCASNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAK 179
Cdd:cd07567  80 -DPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDS---SDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 180 NSTFL-PELITFETDFGVTFGHFICFDILFYTPAHQLIVEQGITDFVYPAMWFSQLPFLTAVQTQQGWAYANDVNLLASG 258
Cdd:cd07567 156 FDVPPePEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAAN 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 18859539 259 ASRPSIGNSGSGIYHGRSGTLTSVMRQDSGERaIYVAQVPKYTRSR 304
Cdd:cd07567 236 YNNPSAGMTGSGIYAGRSGALVYHYDNEPGGK-LLVAEVPKLPSRR 280
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
328-512 2.50e-55

Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins.


:

Pssm-ID: 465946  Cd Length: 165  Bit Score: 183.72  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   328 FYMKRD-YVENYESELLkldegTSGAINRTICQGSFCCNFDIAWrslgtATENGSYYSYRLGTYDGWRNENNVDANYIRN 406
Cdd:pfam19018   1 LKLLRDpNLDNFTSVLL-----TGSNGTATVCHGDLCCDFEYET-----STTDPSSYLYRLGAFDGIRTYEGVDNYYVQI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   407 CALFTCSGDSIDDCGKLLPTegelqqSRVTFTRLAIGVTYPESRefLLFPDTLQDSLLPLEPSQFEWSQRKPTEDsyVQE 486
Cdd:pfam19018  71 CALVACLNDSLSSCGKLVES------ANTTFTSLTISGNFPKTT--YVFPSTLDSSLLPLDPSQWEYSSQEISED--VTV 140
                         170       180
                  ....*....|....*....|....*.
gi 18859539   487 VRFALkeTQELSNLLTFGIYGNYYDN 512
Cdd:pfam19018 141 TLMSL--TKPQSNLLTFGIYGRNYDR 164
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
33-304 3.40e-132

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


Pssm-ID: 143591  Cd Length: 299  Bit Score: 386.98  E-value: 3.40e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  33 YTAGVVEFKQsILS-----LSAWSDSLAGYVEIINSENASATDIIVFPESTLNSAGSTTFVPNPEDQI--------NPCL 99
Cdd:cd07567   1 YIAAVVEHHP-ILSpdpdaLQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDvpdpevnwNPCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 100 sDPNATYYEEFLVTLSCAARNASKYIVINLTEKQKCEDipeDTRPCASNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAK 179
Cdd:cd07567  80 -DPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDS---SDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 180 NSTFL-PELITFETDFGVTFGHFICFDILFYTPAHQLIVEQGITDFVYPAMWFSQLPFLTAVQTQQGWAYANDVNLLASG 258
Cdd:cd07567 156 FDVPPePEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAAN 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 18859539 259 ASRPSIGNSGSGIYHGRSGTLTSVMRQDSGERaIYVAQVPKYTRSR 304
Cdd:cd07567 236 YNNPSAGMTGSGIYAGRSGALVYHYDNEPGGK-LLVAEVPKLPSRR 280
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
328-512 2.50e-55

Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins.


Pssm-ID: 465946  Cd Length: 165  Bit Score: 183.72  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   328 FYMKRD-YVENYESELLkldegTSGAINRTICQGSFCCNFDIAWrslgtATENGSYYSYRLGTYDGWRNENNVDANYIRN 406
Cdd:pfam19018   1 LKLLRDpNLDNFTSVLL-----TGSNGTATVCHGDLCCDFEYET-----STTDPSSYLYRLGAFDGIRTYEGVDNYYVQI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   407 CALFTCSGDSIDDCGKLLPTegelqqSRVTFTRLAIGVTYPESRefLLFPDTLQDSLLPLEPSQFEWSQRKPTEDsyVQE 486
Cdd:pfam19018  71 CALVACLNDSLSSCGKLVES------ANTTFTSLTISGNFPKTT--YVFPSTLDSSLLPLDPSQWEYSSQEISED--VTV 140
                         170       180
                  ....*....|....*....|....*.
gi 18859539   487 VRFALkeTQELSNLLTFGIYGNYYDN 512
Cdd:pfam19018 141 TLMSL--TKPQSNLLTFGIYGRNYDR 164
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
34-276 7.37e-14

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 71.82  E-value: 7.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  34 TAGVVEFKQSILSLSAWSDSLAGYVEIINSENAsatDIIVFPESTLnsagsTTFVPNPEDqinpcLSDPNATYYEEFLVT 113
Cdd:COG0388   3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGA---DLVVFPELFL-----TGYPPEDDD-----LLELAEPLDGPALAA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 114 LSCAARNASKYIVINLTEKqkcediPEDTRpcasnglnVFNTNVVFDRQGVVVSRYRKVHL-----YGEAKnsTFLP--E 186
Cdd:COG0388  70 LAELARELGIAVVVGLPER------DEGGR--------LYNTALVIDPDGEILGRYRKIHLpnygvFDEKR--YFTPgdE 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 187 LITFETDfGVTFGHFICFDILFYTPAHQLiVEQGITDFVYPAMWFSQLPFLTAVQTQQGWAYANDVNLLASGasrpSIGN 266
Cdd:COG0388 134 LVVFDTD-GGRIGVLICYDLWFPELARAL-ALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN----QVGG 207
                       250
                ....*....|
gi 18859539 267 SGSGIYHGRS 276
Cdd:COG0388 208 EDGLVFDGGS 217
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
68-208 4.57e-08

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: 54.28  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539    68 ATDIIVFPEStlnsagSTTFVPNPEDQInpclsdPNATYYE-EFLVTLSCAARNASKYIVINLTEKQKCEDipedtrpca 146
Cdd:pfam00795  32 GADLIVLPEL------FITGYPCWAHFL------EAAEVGDgETLAGLAALARKNGIAIVIGLIERWLTGG--------- 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   147 snglNVFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTF----LPE----LITFETDFGVtFGHFICFDILF 208
Cdd:pfam00795  91 ----RLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFrervLFEpgdgGTVFDTPLGK-IGAAICYEIRF 155
PLN02747 PLN02747
N-carbamolyputrescine amidase
153-297 6.73e-04

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 42.06  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  153 FNTNVVFDRQGVVVSRYRKVHL---YGEAKNSTFLP---ELITFETDFGvTFGHFICFDILFYTPAHQLIVeQGITDFVY 226
Cdd:PLN02747 101 YNSIAIIDADGTDLGLYRKSHIpdgPGYQEKFYFNPgdtGFKVFDTKFA-KIGVAICWDQWFPEAARAMVL-QGAEVLLY 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  227 PAMWFS--QLPFLTA----VQTQQGWAYANDVNLLAS---GASRPSIGNSGSGI-YHGRS---GTLTSVMRQ-DSGERAI 292
Cdd:PLN02747 179 PTAIGSepQDPGLDSrdhwKRVMQGHAGANLVPLVASnriGTEILETEHGPSKItFYGGSfiaGPTGEIVAEaDDKAEAV 258

                 ....*
gi 18859539  293 YVAQV 297
Cdd:PLN02747 259 LVAEF 263
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
33-304 3.40e-132

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


Pssm-ID: 143591  Cd Length: 299  Bit Score: 386.98  E-value: 3.40e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  33 YTAGVVEFKQsILS-----LSAWSDSLAGYVEIINSENASATDIIVFPESTLNSAGSTTFVPNPEDQI--------NPCL 99
Cdd:cd07567   1 YIAAVVEHHP-ILSpdpdaLQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDvpdpevnwNPCL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 100 sDPNATYYEEFLVTLSCAARNASKYIVINLTEKQKCEDipeDTRPCASNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAK 179
Cdd:cd07567  80 -DPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDS---SDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 180 NSTFL-PELITFETDFGVTFGHFICFDILFYTPAHQLIVEQGITDFVYPAMWFSQLPFLTAVQTQQGWAYANDVNLLASG 258
Cdd:cd07567 156 FDVPPePEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAAN 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 18859539 259 ASRPSIGNSGSGIYHGRSGTLTSVMRQDSGERaIYVAQVPKYTRSR 304
Cdd:cd07567 236 YNNPSAGMTGSGIYAGRSGALVYHYDNEPGGK-LLVAEVPKLPSRR 280
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
328-512 2.50e-55

Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins.


Pssm-ID: 465946  Cd Length: 165  Bit Score: 183.72  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   328 FYMKRD-YVENYESELLkldegTSGAINRTICQGSFCCNFDIAWrslgtATENGSYYSYRLGTYDGWRNENNVDANYIRN 406
Cdd:pfam19018   1 LKLLRDpNLDNFTSVLL-----TGSNGTATVCHGDLCCDFEYET-----STTDPSSYLYRLGAFDGIRTYEGVDNYYVQI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   407 CALFTCSGDSIDDCGKLLPTegelqqSRVTFTRLAIGVTYPESRefLLFPDTLQDSLLPLEPSQFEWSQRKPTEDsyVQE 486
Cdd:pfam19018  71 CALVACLNDSLSSCGKLVES------ANTTFTSLTISGNFPKTT--YVFPSTLDSSLLPLDPSQWEYSSQEISED--VTV 140
                         170       180
                  ....*....|....*....|....*.
gi 18859539   487 VRFALkeTQELSNLLTFGIYGNYYDN 512
Cdd:pfam19018 141 TLMSL--TKPQSNLLTFGIYGRNYDR 164
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
54-299 3.42e-17

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: 81.60  E-value: 3.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  54 LAGYVEIINSENASATDIIVFPESTLnsagsTTFVPNPEDQINPCLSDPNATYYEEflvtLSCAARNASKYIVINLTEKq 133
Cdd:cd07197  17 LAKALRLIKEAAEQGADLIVLPELFL-----TGYSFESAKEDLDLAEELDGPTLEA----LAELAKELGIYIVAGIAEK- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 134 kcedipedtrpcasNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTFLP--ELITFETDFGvTFGHFICFDILFYTP 211
Cdd:cd07197  87 --------------DGDKLYNTAVVIDPDGEIIGKYRKIHLFDFGERRYFSPgdEFPVFDTPGG-KIGLLICYDLRFPEL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 212 AHQLIVeQGITDFVYPAMWFSQ--LPFLTAVQTQqgwAYANDVNLLASGasrpSIGNSGSGIYHGRSGTLT---SVMRQD 286
Cdd:cd07197 152 ARELAL-KGADIILVPAAWPTArrEHWELLLRAR---AIENGVYVVAAN----RVGEEGGLEFAGGSMIVDpdgEVLAEA 223
                       250
                ....*....|...
gi 18859539 287 SGERAIYVAQVPK 299
Cdd:cd07197 224 SEEEGILVAELDL 236
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
34-276 7.37e-14

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 71.82  E-value: 7.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  34 TAGVVEFKQSILSLSAWSDSLAGYVEIINSENAsatDIIVFPESTLnsagsTTFVPNPEDqinpcLSDPNATYYEEFLVT 113
Cdd:COG0388   3 RIALAQLNPTVGDIEANLAKIEELIREAAAQGA---DLVVFPELFL-----TGYPPEDDD-----LLELAEPLDGPALAA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 114 LSCAARNASKYIVINLTEKqkcediPEDTRpcasnglnVFNTNVVFDRQGVVVSRYRKVHL-----YGEAKnsTFLP--E 186
Cdd:COG0388  70 LAELARELGIAVVVGLPER------DEGGR--------LYNTALVIDPDGEILGRYRKIHLpnygvFDEKR--YFTPgdE 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 187 LITFETDfGVTFGHFICFDILFYTPAHQLiVEQGITDFVYPAMWFSQLPFLTAVQTQQGWAYANDVNLLASGasrpSIGN 266
Cdd:COG0388 134 LVVFDTD-GGRIGVLICYDLWFPELARAL-ALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN----QVGG 207
                       250
                ....*....|
gi 18859539 267 SGSGIYHGRS 276
Cdd:COG0388 208 EDGLVFDGGS 217
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
58-230 1.64e-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: 143607  Cd Length: 253  Bit Score: 70.64  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  58 VEIINSENASA-TDIIVFPESTlnsagSTTFVPNPEDQinpcLSDPNAtyyEEFLVTLSCAARNASKYIV----INLTEK 132
Cdd:cd07583  21 VESLIEEAAAAgADLIVLPEMW-----NTGYFLDDLYE----LADEDG---GETVSFLSELAKKHGVNIVagsvAEKEGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 133 QkcedipedtrpcasnglnVFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTFLP---ELITFETDfGVTFGHFICFDI--- 206
Cdd:cd07583  89 K------------------LYNTAYVIDPDGELIATYRKIHLFGLMGEDKYLTagdELEVFELD-GGKVGLFICYDLrfp 149
                       170       180
                ....*....|....*....|....*
gi 18859539 207 -LFytpahQLIVEQGITDFVYPAMW 230
Cdd:cd07583 150 eLF-----RKLALEGAEILFVPAEW 169
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
70-232 4.07e-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: 143605  Cd Length: 255  Bit Score: 69.53  E-value: 4.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  70 DIIVFPESTLnsagstTFVPNPEDQINPcLSDPNAtyyEEFLVTLSCAARNASKYIVINLTEKqkcediPEDTRpcasng 149
Cdd:cd07581  32 DLVVFPEYTM------ARFGDGLDDYAR-VAEPLD---GPFVSALARLARELGITVVAGMFEP------AGDGR------ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 150 lnVFNTNVVFDRQGVVVSRYRKVHLY---GEAKNSTFLP--ELI-TFETDFGVTFGHFICFDILFYTPAHQLiVEQGITD 223
Cdd:cd07581  90 --VYNTLVVVGPDGEIIAVYRKIHLYdafGFRESDTVAPgdELPpVVFVVGGVKVGLATCYDLRFPELARAL-ALAGADV 166

                ....*....
gi 18859539 224 FVYPAMWFS 232
Cdd:cd07581 167 IVVPAAWVA 175
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
70-228 5.46e-12

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: 66.30  E-value: 5.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  70 DIIVFPESTlNSAGSTtfvpnPEDQINPCLSDPNatyyEEFLVTLSCAARNASKYIVINltekqkceDIPEdtrPCASNG 149
Cdd:cd07572  33 KLVVLPECF-NYPGGT-----DAFKLALAEEEGD----GPTLQALSELAKEHGIWLVGG--------SIPE---RDDDDG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 150 lNVFNTNVVFDRQGVVVSRYRKVHL----------YGEAKnsTFLP--ELITFETDFGvTFGHFICFDILFYTPAHQLiV 217
Cdd:cd07572  92 -KVYNTSLVFDPDGELVARYRKIHLfdvdvpggisYRESD--TLTPgdEVVVVDTPFG-KIGLGICYDLRFPELARAL-A 166
                       170
                ....*....|.
gi 18859539 218 EQGITDFVYPA 228
Cdd:cd07572 167 RQGADILTVPA 177
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
58-230 7.63e-12

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


Pssm-ID: 143608  Cd Length: 258  Bit Score: 65.85  E-value: 7.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  58 VEIINSENASATDIIVFPEstlnsAGSTTFVPNPEDQINPCLSDPNATYYEEflvTLSCAARNASKYIVINLTEKqkced 137
Cdd:cd07584  22 AELCKEAAAEGADLICFPE-----LATTGYRPDLLGPKLWELSEPIDGPTVR---LFSELAKELGVYIVCGFVEK----- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 138 ipedtrpcASNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAKnSTFLP--ELITFETDFGvTFGHFICFDILFYTPAHQL 215
Cdd:cd07584  89 --------GGVPGKVYNSAVVIDPEGESLGVYRKIHLWGLEK-QYFREgeQYPVFDTPFG-KIGVMICYDMGFPEVARIL 158
                       170
                ....*....|....*
gi 18859539 216 IVEQGITDFVyPAMW 230
Cdd:cd07584 159 TLKGAEVIFC-PSAW 172
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
66-208 6.45e-11

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: 62.98  E-value: 6.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  66 ASATDIIVFPEstlnsagstTFVP--NPEDQInPCLSDPNATYYEEFLVTLSCAARNAskyIVINLTEKqkcedipedtr 143
Cdd:cd07576  30 AAGADLLVFPE---------LFLTgyNIGDAV-ARLAEPADGPALQALRAIARRHGIA---IVVGYPER----------- 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18859539 144 pcasNGLNVFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTFLP--ELITFETDfGVTFGHFICFDILF 208
Cdd:cd07576  86 ----AGGAVYNAAVLIDEDGTVLANYRKTHLFGDSERAAFTPgdRFPVVELR-GLRVGLLICYDVEF 147
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
68-208 4.57e-08

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: 54.28  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539    68 ATDIIVFPEStlnsagSTTFVPNPEDQInpclsdPNATYYE-EFLVTLSCAARNASKYIVINLTEKQKCEDipedtrpca 146
Cdd:pfam00795  32 GADLIVLPEL------FITGYPCWAHFL------EAAEVGDgETLAGLAALARKNGIAIVIGLIERWLTGG--------- 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   147 snglNVFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTF----LPE----LITFETDFGVtFGHFICFDILF 208
Cdd:pfam00795  91 ----RLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFrervLFEpgdgGTVFDTPLGK-IGAAICYEIRF 155
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
70-205 3.50e-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: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  70 DIIVFPESTLnsagsTTFVP-----NPEDQinpclsdpnATYYEEFL-----VTLSCAARNASkyIVINLTEKQKCEDiP 139
Cdd:cd07569  40 QLVVFPELAL-----TTFFPrwyfpDEAEL---------DSFFETEMpnpetQPLFDRAKELG--IGFYLGYAELTED-G 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859539 140 EDTRPcasnglnvFNTNVVFDRQGVVVSRYRKVHLYGEAKNSTFLP----ELITFE---TDFGV------TFGHFICFD 205
Cdd:cd07569 103 GVKRR--------FNTSILVDKSGKIVGKYRKVHLPGHKEPEPYRPfqhlEKRYFEpgdLGFPVfrvpggIMGMCICND 173
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
54-208 1.68e-04

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: 43.74  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  54 LAGYVEIINSENASATDIIVFPESTLnsagsttfvpnPEDQINPclsdpnatyyEEFLVTLSCAARNASKYIVINLTEKQ 133
Cdd:cd07571  25 LDRYLDLTRELADEKPDLVVWPETAL-----------PFDLQRD----------PDALARLARAARAVGAPLLTGAPRRE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 134 kcedipedtrpcaSNGLNVFNTNVVFDRQGVVVSRYRKVHL--YGE----------------AKNSTFLP--ELITFETD 193
Cdd:cd07571  84 -------------PGGGRYYNSALLLDPGGGILGRYDKHHLvpFGEyvplrdllrflgllfdLPMGDFSPgtGPQPLLLG 150
                       170
                ....*....|....*
gi 18859539 194 FGVTFGHFICFDILF 208
Cdd:cd07571 151 GGVRVGPLICYESIF 165
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
5-208 2.73e-04

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 43.68  E-value: 2.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539   5 WWWLSVVLLILGLMPGMSQ-QAALAESDYYTAGVVE--FKQSI-LSLSAWSDSLAGYVEIINSENASATDIIVFPESTLn 80
Cdd:COG0815 166 LAALALALALLLAALRLSPvPWTEPAGEPLRVALVQgnIPQDLkWDPEQRREILDRYLDLTRELADDGPDLVVWPETAL- 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  81 sagsttfvPNPEDQInpclsdpnatyyEEFLVTLSCAARNASKYIVINltekqkcedIPEDTRpcasNGLNVFNTNVVFD 160
Cdd:COG0815 245 --------PFLLDED------------PDALARLAAAAREAGAPLLTG---------APRRDG----GGGRYYNSALLLD 291
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859539 161 RQGVVVSRYRKVHL--YGE---AKNstFLPELITF----ETDF------------GVTFGHFICFDILF 208
Cdd:COG0815 292 PDGGILGRYDKHHLvpFGEyvpLRD--LLRPLIPFldlpLGDFspgtgppvldlgGVRVGPLICYESIF 358
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
70-195 5.96e-04

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of 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 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 42.09  E-value: 5.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  70 DIIVFPEstlnsagstTFVP---------NPEDQinpclSDPNATYYEEFLV-------TLSCAARNASKYIVINLTEKq 133
Cdd:cd07564  35 QLVVFPE---------AFIPgypywiwfgAPAEG-----RELFARYYENSVEvdgpeleRLAEAARENGIYVVLGVSER- 99
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859539 134 kcedipedtrpcaSNGlNVFNTNVVFDRQGVVVSRYRKV---H----LYGEAKNSTflpeLITFETDFG 195
Cdd:cd07564 100 -------------DGG-TLYNTQLLIDPDGELLGKHRKLkptHaerlVWGQGDGSG----LRVVDTPIG 150
PLN02747 PLN02747
N-carbamolyputrescine amidase
153-297 6.73e-04

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 42.06  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  153 FNTNVVFDRQGVVVSRYRKVHL---YGEAKNSTFLP---ELITFETDFGvTFGHFICFDILFYTPAHQLIVeQGITDFVY 226
Cdd:PLN02747 101 YNSIAIIDADGTDLGLYRKSHIpdgPGYQEKFYFNPgdtGFKVFDTKFA-KIGVAICWDQWFPEAARAMVL-QGAEVLLY 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  227 PAMWFS--QLPFLTA----VQTQQGWAYANDVNLLAS---GASRPSIGNSGSGI-YHGRS---GTLTSVMRQ-DSGERAI 292
Cdd:PLN02747 179 PTAIGSepQDPGLDSrdhwKRVMQGHAGANLVPLVASnriGTEILETEHGPSKItFYGGSfiaGPTGEIVAEaDDKAEAV 258

                 ....*
gi 18859539  293 YVAQV 297
Cdd:PLN02747 259 LVAEF 263
ScNTA1_like cd07566
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ...
59-206 8.33e-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: 41.56  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539  59 EIINSENASAT----DIIVFPESTLnsagSTTFVPNPEdQINPCLSDPNATyyeeflVTLSCAARNASK---YIVINLTE 131
Cdd:cd07566  23 ELLDKTKKRAKlkkpDILVLPELAL----TGYNFHSLE-HIKPYLEPTTSG------PSFEWAREVAKKfncHVVIGYPE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859539 132 KQKcEDIPEdtrpcasnglnVFNTNVVFDRQGVVVSRYRKVHLY--------GEAKNStFLPELITF---------ETDF 194
Cdd:cd07566  92 KVD-ESSPK-----------LYNSALVVDPEGEVVFNYRKSFLYytdeewgcEENPGG-FQTFPLPFakdddfdggSVDV 158
                       170
                ....*....|..
gi 18859539 195 GVTFGHFICFDI 206
Cdd:cd07566 159 TLKTSIGICMDL 170
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
151-205 2.11e-03

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: 39.99  E-value: 2.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859539 151 NVFNTNVVFDRQGVVvSRYRKVHLyGEAKNSTFLP--ELITFETDfGVTFGHFICFD 205
Cdd:cd07585  89 RPYNTYLVCLPDGLV-HRYRKLHL-FRREHPYIAAgdEYPVFATP-GVRFGILICYD 142
PLN02798 PLN02798
nitrilase
152-220 4.90e-03

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 38.96  E-value: 4.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859539  152 VFNTNVVFDRQGVVVSRYRKVHL----------YGEAKNSTFLPELITFETDFGvTFGHFICFDILFYTPAHQLIVEQG 220
Cdd:PLN02798 103 LYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGKTIVAVDSPVG-RLGLTVCYDLRFPELYQQLRFEHG 180
 
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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