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Conserved domains on  [gi|226693503|sp|P43251|]
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RecName: Full=Biotinidase; Short=Biotinase; Flags: Precursor

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 ...
58-361 2.90e-161

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: 460.56  E-value: 2.90e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  58 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 137
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 138 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 217
Cdd:cd07567   73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 218 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 297
Cdd:cd07567  153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693503 298 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 361
Cdd:cd07567  233 AANYNNPSAGMTGSGIYAGrSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
393-543 2.71e-39

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: 140.96  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  393 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 468
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  469 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 538
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 226693503  539 LYERD 543
Cdd:pfam19018 161 NYDRD 165
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
58-361 2.90e-161

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: 460.56  E-value: 2.90e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  58 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 137
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 138 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 217
Cdd:cd07567   73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 218 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 297
Cdd:cd07567  153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693503 298 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 361
Cdd:cd07567  233 AANYNNPSAGMTGSGIYAGrSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
393-543 2.71e-39

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: 140.96  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  393 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 468
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  469 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 538
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 226693503  539 LYERD 543
Cdd:pfam19018 161 NYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
89-300 4.02e-19

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 87.23  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  89 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPqvvrwnpclephrfndteVLQRLSCMAIRGDMF 168
Cdd:COG0388   19 NLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGP------------------ALAALAELARELGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 169 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPlkvdliTFDTPFaG 238
Cdd:COG0388   81 VVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLpnygvfdekrYFTPGDELV------VFDTDG-G 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693503 239 RFGIFTCFDiLFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN 300
Cdd:COG0388  143 RIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
88-300 2.47e-14

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: 73.16  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503   88 QNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFtrtsiypfldfmpspqvvrWNPCLEPHRFNDTEVLQRLSCMAIRGDM 167
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPC-------------------WAHFLEAAEVGDGETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  168 FLVANLgtkepchssDPRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLYFEAA------FDVPLKVDLIT-FDTPFaGRF 240
Cdd:pfam00795  77 AIVIGL---------IERWLTGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEPRppgfreRVLFEPGDGGTvFDTPL-GKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693503  241 GIFTCFDILFfdpaIRVLRDYKVKHV---VYPTA--------WMNQLPLLAaieiqKAFAVAFGINVLAAN 300
Cdd:pfam00795 146 GAAICYEIRF----PELLRALALKGAeilINPSArapfpgslGPPQWLLLA-----RARALENGCFVIAAN 207
PLN02798 PLN02798
nitrilase
189-250 4.52e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 48.59  E-value: 4.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693503 189 DGRYQFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPLKvDLITFDTPFaGRFGIFTCFDILF 250
Cdd:PLN02798  99 DDSHLYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGK-TIVAVDSPV-GRLGLTVCYDLRF 168
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
58-361 2.90e-161

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: 460.56  E-value: 2.90e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  58 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 137
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 138 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 217
Cdd:cd07567   73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 218 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 297
Cdd:cd07567  153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693503 298 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 361
Cdd:cd07567  233 AANYNNPSAGMTGSGIYAGrSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
393-543 2.71e-39

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: 140.96  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  393 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 468
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  469 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 538
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 226693503  539 LYERD 543
Cdd:pfam19018 161 NYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
86-300 8.02e-22

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: 94.70  E-value: 8.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  86 MNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTrtsiypfldfmpspqvvRWNPCLEPHRFNDTEVLQRLSCMAIRG 165
Cdd:cd07197   13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFE-----------------SAKEDLDLAEELDGPTLEALAELAKEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 166 DMFLVAnlGTKEpchssdprcpKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF--EAAFDVPLKvDLITFDTPFaGRFGIF 243
Cdd:cd07197   76 GIYIVA--GIAE----------KDGDKLYNTAVVIDPDGEIIGKYRKIHLFDfgERRYFSPGD-EFPVFDTPG-GKIGLL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226693503 244 TCFDIlFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQkAFAVAFGINVLAAN 300
Cdd:cd07197  142 ICYDL-RFPELARELALKGADIILVPAAWPTARREHWELLLR-ARAIENGVYVVAAN 196
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
89-300 4.02e-19

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 87.23  E-value: 4.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  89 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPqvvrwnpclephrfndteVLQRLSCMAIRGDMF 168
Cdd:COG0388   19 NLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGP------------------ALAALAELARELGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 169 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPlkvdliTFDTPFaG 238
Cdd:COG0388   81 VVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLpnygvfdekrYFTPGDELV------VFDTDG-G 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693503 239 RFGIFTCFDiLFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN 300
Cdd:COG0388  143 RIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
88-300 2.47e-14

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: 73.16  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503   88 QNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFtrtsiypfldfmpspqvvrWNPCLEPHRFNDTEVLQRLSCMAIRGDM 167
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPC-------------------WAHFLEAAEVGDGETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  168 FLVANLgtkepchssDPRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLYFEAA------FDVPLKVDLIT-FDTPFaGRF 240
Cdd:pfam00795  77 AIVIGL---------IERWLTGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEPRppgfreRVLFEPGDGGTvFDTPL-GKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693503  241 GIFTCFDILFfdpaIRVLRDYKVKHV---VYPTA--------WMNQLPLLAaieiqKAFAVAFGINVLAAN 300
Cdd:pfam00795 146 GAAICYEIRF----PELLRALALKGAeilINPSArapfpgslGPPQWLLLA-----RARALENGCFVIAAN 207
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
88-271 4.52e-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: 4.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  88 QNLDIYEQQVMTAAQKDVQIIVFPEdgihGFNF-TRTSIYPFLDFMPSPqvvrwnpclephrfnDTEVLQRLSCMAIRGD 166
Cdd:cd07572   15 ANLARAKELIEEAAAQGAKLVVLPE----CFNYpGGTDAFKLALAEEEG---------------DGPTLQALSELAKEHG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 167 MFLVAnlGTkEPChssdpRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLyfeaaFDV--PLKV------------DLITF 232
Cdd:cd07572   76 IWLVG--GS-IPE-----RDDDDGKV-YNTSLVFDPDGELVARYRKIHL-----FDVdvPGGIsyresdtltpgdEVVVV 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226693503 233 DTPFaGRFGIFTCFDILFfdPAI-RVLRDYKVKHVVYPTA 271
Cdd:cd07572  142 DTPF-GKIGLGICYDLRF--PELaRALARQGADILTVPAA 178
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
100-291 4.61e-09

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: 57.16  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 100 AAQKDVQIIVFPEDGIHGFnftrtsiypFLDfmpspqvVRWNPCLEphrfNDTEVLQRLSCMAIRGDMFLVAnlGT-KEP 178
Cdd:cd07583   28 AAAAGADLIVLPEMWNTGY---------FLD-------DLYELADE----DGGETVSFLSELAKKHGVNIVA--GSvAEK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 179 chssdprcpKDGRYqFNTNVVFSNNGTLVDRYRKHNL--------YFEAAfdvplkVDLITFDTPFaGRFGIFTCFDILF 250
Cdd:cd07583   86 ---------EGGKL-YNTAYVIDPDGELIATYRKIHLfglmgedkYLTAG------DELEVFELDG-GKVGLFICYDLRF 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226693503 251 fdPAI-RVLRDYKVKHVVYPTAWmnqlP---------LLA--AIEIQkAFAVA 291
Cdd:cd07583  149 --PELfRKLALEGAEILFVPAEW----PaariehwrtLLRarAIENQ-AFVVA 194
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
89-275 1.18e-07

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: 52.97  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  89 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNftrtsiypfldfmPSPQVVRWNpclEPHrfnDTEVLQRLSCMAIRGDMF 168
Cdd:cd07576   17 NLARLDEAAARAAAAGADLLVFPELFLTGYN-------------IGDAVARLA---EPA---DGPALQALRAIARRHGIA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 169 LVanLGTKEPChssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNLY-------FEAAFDVPlkvdliTFDtpFAG-RF 240
Cdd:cd07576   78 IV--VGYPERA---------GGAV-YNAAVLIDEDGTVLANYRKTHLFgdseraaFTPGDRFP------VVE--LRGlRV 137
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226693503 241 GIFTCFDILFfdP-AIRVLRDYKVKHVVYPTAWMNQ 275
Cdd:cd07576  138 GLLICYDVEF--PeLVRALALAGADLVLVPTALMEP 171
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
99-275 4.66e-07

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: 51.22  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  99 TAAQKDVQIIVFPEDGIHGFNFTR-TSIYPFLDfmpspqvvrwnpclEPHrfnDTEVLQRLSCMAIRGDMFLVANLGTKe 177
Cdd:cd07584   27 EAAAEGADLICFPELATTGYRPDLlGPKLWELS--------------EPI---DGPTVRLFSELAKELGVYIVCGFVEK- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 178 pchSSDPRCPkdgryqFNTNVVFSNNGTLVDRYRKHNL------YFEAAFDVPlkvdliTFDTPFaGRFGIFTCFDILFF 251
Cdd:cd07584   89 ---GGVPGKV------YNSAVVIDPEGESLGVYRKIHLwglekqYFREGEQYP------VFDTPF-GKIGVMICYDMGFP 152
                        170       180
                 ....*....|....*....|....
gi 226693503 252 DPAiRVLRDYKVKHVVYPTAWMNQ 275
Cdd:cd07584  153 EVA-RILTLKGAEVIFCPSAWREQ 175
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
89-300 7.37e-07

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.


Pssm-ID: 143597  Cd Length: 284  Bit Score: 51.02  E-value: 7.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  89 NLDIYEQQVMTAAQKDVQIIVFPEDgIHGFNFTRTSIYPFLDFMPSPqvvrwnpclEPHrfndtEVLQRLSCMAIRGDMF 168
Cdd:cd07573   17 NLAKAEELVREAAAQGAQIVCLQEL-FETPYFCQEEDEDYFDLAEPP---------IPG-----PTTARFQALAKELGVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 169 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRK-H---------NLYFeAAFDVPLKVdlitFDTPFaG 238
Cdd:cd07573   82 IPVSLFEKRG----------NGLY-YNSAVVIDADGSLLGVYRKmHipddpgyyeKFYF-TPGDTGFKV----FDTRY-G 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693503 239 RFGIFTCFDILFFDPA-IRVLRDYKVkhVVYPTA--WMNQLP------LLAAIEIQKAFAVAFGINVLAAN 300
Cdd:cd07573  145 RIGVLICWDQWFPEAArLMALQGAEI--LFYPTAigSEPQEPpegldqRDAWQRVQRGHAIANGVPVAAVN 213
PLN02798 PLN02798
nitrilase
189-250 4.52e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 48.59  E-value: 4.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693503 189 DGRYQFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPLKvDLITFDTPFaGRFGIFTCFDILF 250
Cdd:PLN02798  99 DDSHLYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGK-TIVAVDSPV-GRLGLTVCYDLRF 168
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
88-272 7.11e-06

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: 47.57  E-value: 7.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  88 QNLDIYEQQVMTAAQKDVQIIVFPEdgihgfnftrtsiYPFLDFMPSPQVVRWNPclEPhrfNDTEVLQRLSCMAIRGDM 167
Cdd:cd07581   14 ENLEKVRRLLAEAAAAGADLVVFPE-------------YTMARFGDGLDDYARVA--EP---LDGPFVSALARLARELGI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 168 FLVANLGTKEPchssDPRCpkdgryqFNTNVVFSNNGTLVDRYRKHNLY--F---EAAF------DVPLKVDLITFdtpf 236
Cdd:cd07581   76 TVVAGMFEPAG----DGRV-------YNTLVVVGPDGEIIAVYRKIHLYdaFgfrESDTvapgdeLPPVVFVVGGV---- 140
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226693503 237 agRFGIFTCFDILFFDPAIR-VLRDYKVkhVVYPTAW 272
Cdd:cd07581  141 --KVGLATCYDLRFPELARAlALAGADV--IVVPAAW 173
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
100-288 9.11e-06

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: 47.53  E-value: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 100 AAQKDVQIIVFPEDGIHGFN-FTRTSIYPFLDFMPSPQVvrwnpclephrfndtevlQRLSCMAIRGDMFLVanLGTKEp 178
Cdd:cd07578   29 AARAGARLIVTPEMATTGYCwYDRAEIAPFVEPIPGPTT------------------ARFAELAREHDCYIV--VGLPE- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 179 chsSDPRcpkDGRYqFNTNVVFSNNGtLVDRYRK-HNLYFEAAFDVPLKVDLITFDTPFaGRFGIFTCFDILFFDPAiRV 257
Cdd:cd07578   88 ---VDSR---SGIY-YNSAVLIGPSG-VIGRHRKtHPYISEPKWAADGDLGHQVFDTEI-GRIALLICMDIHFFETA-RL 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226693503 258 LRDYKVKHVVYPTAWM-NQLPllAAIEIQKAF 288
Cdd:cd07578  158 LALGGADVICHISNWLaERTP--APYWINRAF 187
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
87-247 3.76e-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: 143609  Cd Length: 261  Bit Score: 45.38  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  87 NQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRtsiyPFLDFMPSPqvvrwnpclephrfnDTEVLQRLSCMAIRGD 166
Cdd:cd07585   15 ARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVR----ALSREAEVP---------------DGPSTQALSDLARRYG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 167 MFLVAnlGTKEpchssdprcpKDGRYQFNTNVVFSNNGtLVDRYRK-H-----NLYFEAAFDVPlkvdliTFDTPFAgRF 240
Cdd:cd07585   76 LTILA--GLIE----------KAGDRPYNTYLVCLPDG-LVHRYRKlHlfrreHPYIAAGDEYP------VFATPGV-RF 135

                 ....*..
gi 226693503 241 GIFTCFD 247
Cdd:cd07585  136 GILICYD 142
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
107-258 1.25e-04

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: 43.83  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 107 IIVFPEDGIHGFNFTRTSiypfldfmpspQVVrwnPCLEPhrFNDTEVLQRLSCMAIRGDMFLVANLgtkepchssdprC 186
Cdd:cd07577   32 LIVLPELFNTGYAFTSKE-----------EVA---SLAES--IPDGPTTRFLQELARETGAYIVAGL------------P 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226693503 187 PKDGRYQFNTNVVFSNNGtLVDRYRK-HNLYFEAAFDVPLKVDLITFDTPFaGRFGIFTCFDiLFFDPAIRVL 258
Cdd:cd07577   84 ERDGDKFYNSAVVVGPEG-YIGIYRKtHLFYEEKLFFEPGDTGFRVFDIGD-IRIGVMICFD-WYFPEAARTL 153
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
88-250 5.96e-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: 41.82  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  88 QNLDIYEQQVMTAAQKDVQIIVFPEdgihgfnftrTSIyPFLdfmpspqvvrwnpclephRFNDTEVLQRLSCMAIRGDM 167
Cdd:cd07571   23 ATLDRYLDLTRELADEKPDLVVWPE----------TAL-PFD------------------LQRDPDALARLARAARAVGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 168 FLVANLGTKEPchssdprcpKDGRYqFNTNVVFSNNGTLVDRYRKHNL-----Y--FEAAFDVPLKVDLI---------- 230
Cdd:cd07571   74 PLLTGAPRREP---------GGGRY-YNSALLLDPGGGILGRYDKHHLvpfgeYvpLRDLLRFLGLLFDLpmgdfspgtg 143
                        170       180
                 ....*....|....*....|..
gi 226693503 231 --TFDTPFAGRFGIFTCFDILF 250
Cdd:cd07571  144 pqPLLLGGGVRVGPLICYESIF 165
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
94-260 6.94e-03

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: 38.72  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503  94 EQQVMTAAQKDVQIIVFPEDgihgFNFTRTSIYPflDFMPSPQV-VRWNPCLEPhrfndtEVLQRLSCMAIRGDMFLVAn 172
Cdd:cd07574   24 EYWVAEAAGYGADLLVFPEY----FTMELLSLLP--EAIDGLDEaIRALAALTP------DYVALFSELARKYGINIIA- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693503 173 lgtkepchSSDPRcPKDGRYQfNTNVVFSNNGTlVDRYRK-HNLYFE-AAFDV----PLKVdlitFDTPFaGRFGIFTCF 246
Cdd:cd07574   91 --------GSMPV-REDGRLY-NRAYLFGPDGT-IGHQDKlHMTPFErEEWGIsggdKLKV----FDTDL-GKIGILICY 154
                        170
                 ....*....|....
gi 226693503 247 DILFFDPAiRVLRD 260
Cdd:cd07574  155 DSEFPELA-RALAE 167
 
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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