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Conserved domains on  [gi|1654854340|ref|NP_001357587|]
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biotinidase isoform 1 precursor [Homo sapiens]

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 ...
38-341 3.36e-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: 459.79  E-value: 3.36e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  38 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 117
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 118 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 197
Cdd:cd07567    73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 198 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 277
Cdd:cd07567   153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654854340 278 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 341
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 ...
373-523 3.89e-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: 140.19  E-value: 3.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 373 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 448
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 449 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 518
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 1654854340 519 LYERD 523
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 ...
38-341 3.36e-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: 459.79  E-value: 3.36e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  38 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 117
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 118 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 197
Cdd:cd07567    73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 198 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 277
Cdd:cd07567   153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654854340 278 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 341
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 ...
373-523 3.89e-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: 140.19  E-value: 3.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 373 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 448
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 449 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 518
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 1654854340 519 LYERD 523
Cdd:pfam19018 161 NYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
69-280 2.77e-19

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 87.61  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  69 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPqvvrwnpclephrfndteVLQRLSCMAIRGDMF 148
Cdd:COG0388    19 NLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGP------------------ALAALAELARELGIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 149 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPlkvdliTFDTPFaG 218
Cdd:COG0388    81 VVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLpnygvfdekrYFTPGDELV------VFDTDG-G 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654854340 219 RFGIFTCFDiLFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN 280
Cdd:COG0388   143 RIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
68-280 1.95e-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: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  68 QNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFtrtsiypfldfmpspqvvrWNPCLEPHRFNDTEVLQRLSCMAIRGDM 147
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPC-------------------WAHFLEAAEVGDGETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 148 FLVANLgtkepchssDPRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLYFEAA------FDVPLKVDLIT-FDTPFaGRF 220
Cdd:pfam00795  77 AIVIGL---------IERWLTGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEPRppgfreRVLFEPGDGGTvFDTPL-GKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654854340 221 GIFTCFDILFfdpaIRVLRDYKVKHV---VYPTA--------WMNQLPLLAaieiqKAFAVAFGINVLAAN 280
Cdd:pfam00795 146 GAAICYEIRF----PELLRALALKGAeilINPSArapfpgslGPPQWLLLA-----RARALENGCFVIAAN 207
PLN02798 PLN02798
nitrilase
169-230 4.29e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 48.59  E-value: 4.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654854340 169 DGRYQFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPLKvDLITFDTPFaGRFGIFTCFDILF 230
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 ...
38-341 3.36e-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: 459.79  E-value: 3.36e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  38 YVAAVYEHPSILSLNPlalisrqEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPsPQV 117
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVP-DPE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 118 VRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCHSSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF 197
Cdd:cd07567    73 VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 198 EAAFDVPLKVDLITFDTPFAGRFGIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVL 277
Cdd:cd07567   153 EPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654854340 278 AANVHHPVLGMTGSGIHTP-LESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETD--PSHSKF 341
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 ...
373-523 3.89e-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: 140.19  E-value: 3.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 373 TFHSEMMYDNFTLVPVWGKEGYLHVCSNGLCCYLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQVCALVRCGGLGF 448
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 449 DTCGQEITEATGIFE-FHLWGNF-STSYIFPLFLTSGM-TLEvPDQLGW-------ENDHYFLRKSRLSSGLVTAALYGR 518
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLlPLD-PSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGR 160

                  ....*
gi 1654854340 519 LYERD 523
Cdd:pfam19018 161 NYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
66-280 6.08e-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: 95.08  E-value: 6.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  66 MNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTrtsiypfldfmpspqvvRWNPCLEPHRFNDTEVLQRLSCMAIRG 145
Cdd:cd07197    13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFE-----------------SAKEDLDLAEELDGPTLEALAELAKEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 146 DMFLVAnlGTKEpchssdprcpKDGRYQFNTNVVFSNNGTLVDRYRKHNLYF--EAAFDVPLKvDLITFDTPFaGRFGIF 223
Cdd:cd07197    76 GIYIVA--GIAE----------KDGDKLYNTAVVIDPDGEIIGKYRKIHLFDfgERRYFSPGD-EFPVFDTPG-GKIGLL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1654854340 224 TCFDIlFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQkAFAVAFGINVLAAN 280
Cdd:cd07197   142 ICYDL-RFPELARELALKGADIILVPAAWPTARREHWELLLR-ARAIENGVYVVAAN 196
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
69-280 2.77e-19

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 87.61  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  69 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRTSIYPFLDFMPSPqvvrwnpclephrfndteVLQRLSCMAIRGDMF 148
Cdd:COG0388    19 NLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGP------------------ALAALAELARELGIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 149 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPlkvdliTFDTPFaG 218
Cdd:COG0388    81 VVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLpnygvfdekrYFTPGDELV------VFDTDG-G 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654854340 219 RFGIFTCFDiLFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN 280
Cdd:COG0388   143 RIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
68-280 1.95e-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: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  68 QNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFtrtsiypfldfmpspqvvrWNPCLEPHRFNDTEVLQRLSCMAIRGDM 147
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPC-------------------WAHFLEAAEVGDGETLAGLAALARKNGI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 148 FLVANLgtkepchssDPRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLYFEAA------FDVPLKVDLIT-FDTPFaGRF 220
Cdd:pfam00795  77 AIVIGL---------IERWLTGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEPRppgfreRVLFEPGDGGTvFDTPL-GKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654854340 221 GIFTCFDILFfdpaIRVLRDYKVKHV---VYPTA--------WMNQLPLLAaieiqKAFAVAFGINVLAAN 280
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); ...
68-251 3.72e-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: 66.68  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  68 QNLDIYEQQVMTAAQKDVQIIVFPEdgihGFNF-TRTSIYPFLDFMPSPqvvrwnpclephrfnDTEVLQRLSCMAIRGD 146
Cdd:cd07572    15 ANLARAKELIEEAAAQGAKLVVLPE----CFNYpGGTDAFKLALAEEEG---------------DGPTLQALSELAKEHG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 147 MFLVAnlGTkEPChssdpRCPKDGRYqFNTNVVFSNNGTLVDRYRKHNLyfeaaFDV--PLKV------------DLITF 212
Cdd:cd07572    76 IWLVG--GS-IPE-----RDDDDGKV-YNTSLVFDPDGELVARYRKIHL-----FDVdvPGGIsyresdtltpgdEVVVV 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1654854340 213 DTPFaGRFGIFTCFDILFfdPAI-RVLRDYKVKHVVYPTA 251
Cdd:cd07572   142 DTPF-GKIGLGICYDLRF--PELaRALARQGADILTVPAA 178
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
80-271 3.73e-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: 57.55  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  80 AAQKDVQIIVFPEDGIHGFnftrtsiypFLDfmpspqvVRWNPCLEphrfNDTEVLQRLSCMAIRGDMFLVAnlGT-KEP 158
Cdd:cd07583    28 AAAAGADLIVLPEMWNTGY---------FLD-------DLYELADE----DGGETVSFLSELAKKHGVNIVA--GSvAEK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 159 chssdprcpKDGRYqFNTNVVFSNNGTLVDRYRKHNL--------YFEAAfdvplkVDLITFDTPFaGRFGIFTCFDILF 230
Cdd:cd07583    86 ---------EGGKL-YNTAYVIDPDGELIATYRKIHLfglmgedkYLTAG------DELEVFELDG-GKVGLFICYDLRF 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1654854340 231 fdPAI-RVLRDYKVKHVVYPTAWmnqlP---------LLA--AIEIQkAFAVA 271
Cdd:cd07583   149 --PELfRKLALEGAEILFVPAEW----PaariehwrtLLRarAIENQ-AFVVA 194
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
69-255 9.54e-08

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: 53.35  E-value: 9.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  69 NLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNftrtsiypfldfmPSPQVVRWNpclEPHrfnDTEVLQRLSCMAIRGDMF 148
Cdd:cd07576    17 NLARLDEAAARAAAAGADLLVFPELFLTGYN-------------IGDAVARLA---EPA---DGPALQALRAIARRHGIA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 149 LVanLGTKEPChssdprcpkDGRYqFNTNVVFSNNGTLVDRYRKHNLY-------FEAAFDVPlkvdliTFDtpFAG-RF 220
Cdd:cd07576    78 IV--VGYPERA---------GGAV-YNAAVLIDEDGTVLANYRKTHLFgdseraaFTPGDRFP------VVE--LRGlRV 137
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1654854340 221 GIFTCFDILFfdP-AIRVLRDYKVKHVVYPTAWMNQ 255
Cdd:cd07576   138 GLLICYDVEF--PeLVRALALAGADLVLVPTALMEP 171
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
79-255 4.43e-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: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  79 TAAQKDVQIIVFPEDGIHGFNFTR-TSIYPFLDfmpspqvvrwnpclEPHrfnDTEVLQRLSCMAIRGDMFLVANLGTKe 157
Cdd:cd07584    27 EAAAEGADLICFPELATTGYRPDLlGPKLWELS--------------EPI---DGPTVRLFSELAKELGVYIVCGFVEK- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 158 pchSSDPRCPkdgryqFNTNVVFSNNGTLVDRYRKHNL------YFEAAFDVPlkvdliTFDTPFaGRFGIFTCFDILFF 231
Cdd:cd07584    89 ---GGVPGKV------YNSAVVIDPEGESLGVYRKIHLwglekqYFREGEQYP------VFDTPF-GKIGVMICYDMGFP 152
                         170       180
                  ....*....|....*....|....
gi 1654854340 232 DPAiRVLRDYKVKHVVYPTAWMNQ 255
Cdd:cd07584   153 EVA-RILTLKGAEVIFCPSAWREQ 175
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
69-280 6.68e-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: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  69 NLDIYEQQVMTAAQKDVQIIVFPEDgIHGFNFTRTSIYPFLDFMPSPqvvrwnpclEPHrfndtEVLQRLSCMAIRGDMF 148
Cdd:cd07573    17 NLAKAEELVREAAAQGAQIVCLQEL-FETPYFCQEEDEDYFDLAEPP---------IPG-----PTTARFQALAKELGVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 149 LVANLGTKEPchssdprcpkDGRYqFNTNVVFSNNGTLVDRYRK-H---------NLYFeAAFDVPLKVdlitFDTPFaG 218
Cdd:cd07573    82 IPVSLFEKRG----------NGLY-YNSAVVIDADGSLLGVYRKmHipddpgyyeKFYF-TPGDTGFKV----FDTRY-G 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654854340 219 RFGIFTCFDILFFDPA-IRVLRDYKVkhVVYPTA--WMNQLP------LLAAIEIQKAFAVAFGINVLAAN 280
Cdd:cd07573   145 RIGVLICWDQWFPEAArLMALQGAEI--LFYPTAigSEPQEPpegldqRDAWQRVQRGHAIANGVPVAAVN 213
PLN02798 PLN02798
nitrilase
169-230 4.29e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 48.59  E-value: 4.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654854340 169 DGRYQFNTNVVFSNNGTLVDRYRKHNL----------YFEAAFDVPLKvDLITFDTPFaGRFGIFTCFDILF 230
Cdd:PLN02798   99 DDSHLYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGK-TIVAVDSPV-GRLGLTVCYDLRF 168
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
68-252 5.53e-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: 47.96  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  68 QNLDIYEQQVMTAAQKDVQIIVFPEdgihgfnftrtsiYPFLDFMPSPQVVRWNPclEPhrfNDTEVLQRLSCMAIRGDM 147
Cdd:cd07581    14 ENLEKVRRLLAEAAAAGADLVVFPE-------------YTMARFGDGLDDYARVA--EP---LDGPFVSALARLARELGI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 148 FLVANLGTKEPchssDPRCpkdgryqFNTNVVFSNNGTLVDRYRKHNLY--F---EAAF------DVPLKVDLITFdtpf 216
Cdd:cd07581    76 TVVAGMFEPAG----DGRV-------YNTLVVVGPDGEIIAVYRKIHLYdaFgfrESDTvapgdeLPPVVFVVGGV---- 140
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1654854340 217 agRFGIFTCFDILFFDPAIR-VLRDYKVkhVVYPTAW 252
Cdd:cd07581   141 --KVGLATCYDLRFPELARAlALAGADV--IVVPAAW 173
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
80-268 7.56e-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: 7.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  80 AAQKDVQIIVFPEDGIHGFN-FTRTSIYPFLDFMPSPQVvrwnpclephrfndtevlQRLSCMAIRGDMFLVanLGTKEp 158
Cdd:cd07578    29 AARAGARLIVTPEMATTGYCwYDRAEIAPFVEPIPGPTT------------------ARFAELAREHDCYIV--VGLPE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 159 chsSDPRcpkDGRYqFNTNVVFSNNGtLVDRYRK-HNLYFEAAFDVPLKVDLITFDTPFaGRFGIFTCFDILFFDPAiRV 237
Cdd:cd07578    88 ---VDSR---SGIY-YNSAVLIGPSG-VIGRHRKtHPYISEPKWAADGDLGHQVFDTEI-GRIALLICMDIHFFETA-RL 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1654854340 238 LRDYKVKHVVYPTAWM-NQLPllAAIEIQKAF 268
Cdd:cd07578   158 LALGGADVICHISNWLaERTP--APYWINRAF 187
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
67-227 2.68e-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: 45.77  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  67 NQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNFTRtsiyPFLDFMPSPqvvrwnpclephrfnDTEVLQRLSCMAIRGD 146
Cdd:cd07585    15 ARNLAVIARWTRKAAAQGAELVCFPEMCITGYTHVR----ALSREAEVP---------------DGPSTQALSDLARRYG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 147 MFLVAnlGTKEpchssdprcpKDGRYQFNTNVVFSNNGtLVDRYRK-H-----NLYFEAAFDVPlkvdliTFDTPFAgRF 220
Cdd:cd07585    76 LTILA--GLIE----------KAGDRPYNTYLVCLPDG-LVHRYRKlHlfrreHPYIAAGDEYP------VFATPGV-RF 135

                  ....*..
gi 1654854340 221 GIFTCFD 227
Cdd:cd07585   136 GILICYD 142
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
87-238 1.28e-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: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  87 IIVFPEDGIHGFNFTRTSiypfldfmpspQVVrwnPCLEPhrFNDTEVLQRLSCMAIRGDMFLVANLgtkepchssdprC 166
Cdd:cd07577    32 LIVLPELFNTGYAFTSKE-----------EVA---SLAES--IPDGPTTRFLQELARETGAYIVAGL------------P 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654854340 167 PKDGRYQFNTNVVFSNNGtLVDRYRK-HNLYFEAAFDVPLKVDLITFDTPFaGRFGIFTCFDiLFFDPAIRVL 238
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 ...
68-230 5.87e-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: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  68 QNLDIYEQQVMTAAQKDVQIIVFPEdgihgfnftrTSIyPFLdfmpspqvvrwnpclephRFNDTEVLQRLSCMAIRGDM 147
Cdd:cd07571    23 ATLDRYLDLTRELADEKPDLVVWPE----------TAL-PFD------------------LQRDPDALARLARAARAVGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 148 FLVANLGTKEPchssdprcpKDGRYqFNTNVVFSNNGTLVDRYRKHNL-----Y--FEAAFDVPLKVDLI---------- 210
Cdd:cd07571    74 PLLTGAPRREP---------GGGRY-YNSALLLDPGGGILGRYDKHHLvpfgeYvpLRDLLRFLGLLFDLpmgdfspgtg 143
                         170       180
                  ....*....|....*....|..
gi 1654854340 211 --TFDTPFAGRFGIFTCFDILF 230
Cdd:cd07571   144 pqPLLLGGGVRVGPLICYESIF 165
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
74-240 6.04e-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: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340  74 EQQVMTAAQKDVQIIVFPEDgihgFNFTRTSIYPflDFMPSPQV-VRWNPCLEPhrfndtEVLQRLSCMAIRGDMFLVAn 152
Cdd:cd07574    24 EYWVAEAAGYGADLLVFPEY----FTMELLSLLP--EAIDGLDEaIRALAALTP------DYVALFSELARKYGINIIA- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654854340 153 lgtkepchSSDPRcPKDGRYQfNTNVVFSNNGTlVDRYRK-HNLYFE-AAFDV----PLKVdlitFDTPFaGRFGIFTCF 226
Cdd:cd07574    91 --------GSMPV-REDGRLY-NRAYLFGPDGT-IGHQDKlHMTPFErEEWGIsggdKLKV----FDTDL-GKIGILICY 154
                         170
                  ....*....|....
gi 1654854340 227 DILFFDPAiRVLRD 240
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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