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Conserved domains on  [gi|1740181664|ref|NP_001361146|]
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biotinidase isoform 2 [Mus musculus]

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 ...
 1-230 1.09e-120

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: 352.32  E-value: 1.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664   1 MPSPKlVRWNPCLEPFRFNDTEVLQRLSCMAIKGGMFLVANLGTKQPCLSSDPGCPQDGRYQFNTNVVFSDNGTLVDRYR 80
Cdd:cd07567    68 VPDPE-VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYR 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  81 KHNLYFEAAFDTPANVDLITFDTPFAGKFGVFTCFDILFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQKAFATA 160
Cdd:cd07567   147 KYNLFGEPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYA 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1740181664 161 FGVNVLAANIHHPTLGMTGSGIHTPLK-SFWYHDMDDPKGHLIIAQVATNPQGLTGTGNTTSEMD--PSHRKF 230
Cdd:cd07567   227 NGVNLLAANYNNPSAGMTGSGIYAGRSgALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 262-411 2.52e-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: 138.65  E-value: 2.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 262 TFHSEMMYDNFTLVPVWGTEGHLQVCSNSLCCHLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQTCALVKCGGLGF 337
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 338 DTCGQEITEAEGLFD-FHLWGNF-STLYIFPLFLTSGMTLDTPDQLGW-------ENDHYFLRKRGLSSGLVTAALYGRL 408
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLLPLDPSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGRN 161


                  ...
gi 1740181664 409 YER 411
Cdd:pfam19018 162 YDR 164
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 1-230 1.09e-120

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: 352.32  E-value: 1.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664   1 MPSPKlVRWNPCLEPFRFNDTEVLQRLSCMAIKGGMFLVANLGTKQPCLSSDPGCPQDGRYQFNTNVVFSDNGTLVDRYR 80
Cdd:cd07567    68 VPDPE-VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYR 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  81 KHNLYFEAAFDTPANVDLITFDTPFAGKFGVFTCFDILFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQKAFATA 160
Cdd:cd07567   147 KYNLFGEPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYA 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1740181664 161 FGVNVLAANIHHPTLGMTGSGIHTPLK-SFWYHDMDDPKGHLIIAQVATNPQGLTGTGNTTSEMD--PSHRKF 230
Cdd:cd07567   227 NGVNLLAANYNNPSAGMTGSGIYAGRSgALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 262-411 2.52e-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: 138.65  E-value: 2.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 262 TFHSEMMYDNFTLVPVWGTEGHLQVCSNSLCCHLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQTCALVKCGGLGF 337
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 338 DTCGQEITEAEGLFD-FHLWGNF-STLYIFPLFLTSGMTLDTPDQLGW-------ENDHYFLRKRGLSSGLVTAALYGRL 408
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLLPLDPSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGRN 161


                  ...
gi 1740181664 409 YER 411
Cdd:pfam19018 162 YDR 164
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
20-169 4.84e-17

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 80.29  E-value: 4.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVANLGTKQPclssdpgcpqDGRYqFNTNVVFSDNGTLVDRYRKHNLYFEAAFD-----TPA 94
Cdd:COG0388    63 DGPALAALAELARELGIAVVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLPNYGVFDekryfTPG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740181664  95 NvDLITFDTPFaGKFGVFTCFDiLFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQKAFATAFGVNVLAAN 169
Cdd:COG0388   132 D-ELVVFDTDG-GRIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 9-213 3.97e-10

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: 60.06  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664   9 WNPCLEPFRFNDTEVLQRLSCMAIKGGMFLVANLGTKQPclssdpgcpQDGRYqFNTNVVFSDNGTLVDRYRKHNLYFEA 88
Cdd:pfam00795  49 WAHFLEAAEVGDGETLAGLAALARKNGIAIVIGLIERWL---------TGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  89 AFDTPANVDL-------ITFDTPFaGKFGVFTCFDIlFFDPAVRLLRDFEVKHIVYPTA--------WMNQLPLLAaiei 153
Cdd:pfam00795 119 RPPGFRERVLfepgdggTVFDTPL-GKIGAAICYEI-RFPELLRALALKGAEILINPSArapfpgslGPPQWLLLA---- 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1740181664 154 qKAFATAFGVNVLAANihhptlgmtGSGIHTPLKSFWYHDM-DDPKGhLIIAQVATNPQGL 213
Cdd:pfam00795 193 -RARALENGCFVIAAN---------QVGGEEDAPWPYGHSMiIDPDG-RILAGAGEWEEGV 242
PLN02798 PLN02798
nitrilase
 20-140 3.72e-07

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 51.28  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLvaNLGTKQpclSSDPgcpqDGRYQFNTNVVFSDNGTLVDRYRKHNL----------YFEAA 89
Cdd:PLN02798   70 DGPIMQRYRSLARESGLWL--SLGGFQ---EKGP----DDSHLYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESS 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1740181664  90 FDTPANvDLITFDTPFaGKFGVFTCFDILFFDPAVRLLRDFEVKHIVYPTA 140
Cdd:PLN02798  141 FTAPGK-TIVAVDSPV-GRLGLTVCYDLRFPELYQQLRFEHGAQVLLVPSA 189
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 1-230 1.09e-120

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: 352.32  E-value: 1.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664   1 MPSPKlVRWNPCLEPFRFNDTEVLQRLSCMAIKGGMFLVANLGTKQPCLSSDPGCPQDGRYQFNTNVVFSDNGTLVDRYR 80
Cdd:cd07567    68 VPDPE-VNWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYR 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  81 KHNLYFEAAFDTPANVDLITFDTPFAGKFGVFTCFDILFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQKAFATA 160
Cdd:cd07567   147 KYNLFGEPGFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYA 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1740181664 161 FGVNVLAANIHHPTLGMTGSGIHTPLK-SFWYHDMDDPKGHLIIAQVATNPQGLTGTGNTTSEMD--PSHRKF 230
Cdd:cd07567   227 NGVNLLAANYNNPSAGMTGSGIYAGRSgALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKVDTSslPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 262-411 2.52e-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: 138.65  E-value: 2.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 262 TFHSEMMYDNFTLVPVWGTEGHLQVCSNSLCCHLLYER--PTLSKELYALGVFDGLHTVHG--TYYIQTCALVKCGGLGF 337
Cdd:pfam19018   2 KLLRDPNLDNFTSVLLTGSNGTATVCHGDLCCDFEYETstTDPSSYLYRLGAFDGIRTYEGvdNYYVQICALVACLNDSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 338 DTCGQEITEAEGLFD-FHLWGNF-STLYIFPLFLTSGMTLDTPDQLGW-------ENDHYFLRKRGLSSGLVTAALYGRL 408
Cdd:pfam19018  82 SSCGKLVESANTTFTsLTISGNFpKTTYVFPSTLDSSLLPLDPSQWEYssqeiseDVTVTLMSLTKPQSNLLTFGIYGRN 161


                  ...
gi 1740181664 409 YER 411
Cdd:pfam19018 162 YDR 164
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 20-169 2.48e-17

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.


Pssm-ID: 143587 [Multi-domain]  Cd Length: 253  Bit Score: 81.22  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVANLGTKqpclssdpgcpqDGRYQFNTNVVFSDNGTLVDRYRKHNLYF--EAAFDTPANvD 97
Cdd:cd07197    61 DGPTLEALAELAKELGIYIVAGIAEK------------DGDKLYNTAVVIDPDGEIIGKYRKIHLFDfgERRYFSPGD-E 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1740181664  98 LITFDTPFaGKFGVFTCFDIlFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQkAFATAFGVNVLAAN 169
Cdd:cd07197   128 FPVFDTPG-GKIGLLICYDL-RFPELARELALKGADIILVPAAWPTARREHWELLLR-ARAIENGVYVVAAN 196
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
20-169 4.84e-17

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 80.29  E-value: 4.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVANLGTKQPclssdpgcpqDGRYqFNTNVVFSDNGTLVDRYRKHNLYFEAAFD-----TPA 94
Cdd:COG0388    63 DGPALAALAELARELGIAVVVGLPERDE----------GGRL-YNTALVIDPDGEILGRYRKIHLPNYGVFDekryfTPG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740181664  95 NvDLITFDTPFaGKFGVFTCFDiLFFDPAVRLLRDFEVKHIVYPTAWMNQLPLLAAIEIQKAFATAFGVNVLAAN 169
Cdd:COG0388   132 D-ELVVFDTDG-GRIGVLICYD-LWFPELARALALAGADLLLVPSASPFGRGKDHWELLLRARAIENGCYVVAAN 203
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 20-140 8.03e-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: 65.14  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVAnlGTkQPCLSSDPGCPqdgryqFNTNVVFSDNGTLVDRYRKHNL----------YFEAA 89
Cdd:cd07572    60 DGPTLQALSELAKEHGIWLVG--GS-IPERDDDDGKV------YNTSLVFDPDGELVARYRKIHLfdvdvpggisYRESD 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1740181664  90 FDTPANvDLITFDTPFaGKFGVFTCFDILFfdPAV-RLLRDFEVKHIVYPTA 140
Cdd:cd07572   131 TLTPGD-EVVVVDTPF-GKIGLGICYDLRF--PELaRALARQGADILTVPAA 178
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 9-213 3.97e-10

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: 60.06  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664   9 WNPCLEPFRFNDTEVLQRLSCMAIKGGMFLVANLGTKQPclssdpgcpQDGRYqFNTNVVFSDNGTLVDRYRKHNLYFEA 88
Cdd:pfam00795  49 WAHFLEAAEVGDGETLAGLAALARKNGIAIVIGLIERWL---------TGGRL-YNTAVLLDPDGKLVGKYRKLHLFPEP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  89 AFDTPANVDL-------ITFDTPFaGKFGVFTCFDIlFFDPAVRLLRDFEVKHIVYPTA--------WMNQLPLLAaiei 153
Cdd:pfam00795 119 RPPGFRERVLfepgdggTVFDTPL-GKIGAAICYEI-RFPELLRALALKGAEILINPSArapfpgslGPPQWLLLA---- 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1740181664 154 qKAFATAFGVNVLAANihhptlgmtGSGIHTPLKSFWYHDM-DDPKGhLIIAQVATNPQGL 213
Cdd:pfam00795 193 -RARALENGCFVIAAN---------QVGGEEDAPWPYGHSMiIDPDG-RILAGAGEWEEGV 242
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 19-141 8.12e-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: 56.01  E-value: 8.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  19 NDTEVLQRLSCMAIKGGMFLVANLGTKQpclssdpgcpQDGRYqFNTNVVFSDNGTLVDRYRKHNLY---FEAAFDTPAN 95
Cdd:cd07583    58 DGGETVSFLSELAKKHGVNIVAGSVAEK----------EGGKL-YNTAYVIDPDGELIATYRKIHLFglmGEDKYLTAGD 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1740181664  96 vDLITFDTPFaGKFGVFTCFDILFfdPAV-RLLRDFEVKHIVYPTAW 141
Cdd:cd07583   127 -ELEVFELDG-GKVGLFICYDLRF--PELfRKLALEGAEILFVPAEW 169
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 20-144 1.28e-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: 52.37  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVANLGTKqpclSSDPGCPqdgryqFNTNVVFSDNGTLVDRYRKHNLYFEAAFDTPANVDLI 99
Cdd:cd07584    63 DGPTVRLFSELAKELGVYIVCGFVEK----GGVPGKV------YNSAVVIDPEGESLGVYRKIHLWGLEKQYFREGEQYP 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1740181664 100 TFDTPFaGKFGVFTCFDILFfdPAV-RLLRDFEVKHIVYPTAWMNQ 144
Cdd:cd07584   133 VFDTPF-GKIGVMICYDMGF--PEVaRILTLKGAEVIFCPSAWREQ 175
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 59-169 3.38e-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: 51.41  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  59 GRYqFNTNVVFSDNGTLVDRYRK-H----NLYFEAAFDTPANVDLITFDTPFaGKFGVFTCFDILFfdP-AVRL--LRDF 130
Cdd:cd07573    93 GLY-YNSAVVIDADGSLLGVYRKmHipddPGYYEKFYFTPGDTGFKVFDTRY-GRIGVLICWDQWF--PeAARLmaLQGA 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1740181664 131 EVkhIVYPTA--WMNQLP------LLAAIEIQKAFATAFGVNVLAAN 169
Cdd:cd07573   169 EI--LFYPTAigSEPQEPpegldqRDAWQRVQRGHAIANGVPVAAVN 213
PLN02798 PLN02798
nitrilase
 20-140 3.72e-07

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 51.28  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLvaNLGTKQpclSSDPgcpqDGRYQFNTNVVFSDNGTLVDRYRKHNL----------YFEAA 89
Cdd:PLN02798   70 DGPIMQRYRSLARESGLWL--SLGGFQ---EKGP----DDSHLYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESS 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1740181664  90 FDTPANvDLITFDTPFaGKFGVFTCFDILFFDPAVRLLRDFEVKHIVYPTA 140
Cdd:PLN02798  141 FTAPGK-TIVAVDSPV-GRLGLTVCYDLRFPELYQQLRFEHGAQVLLVPSA 189
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 63-141 1.17e-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: 49.50  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  63 FNTNVVFSDNGTLVDRYRKHNLY--F---EAAFDTPANVDLITFDTPFAGKFGVFTCFDILFFDPAVRL-LRDFEVkhIV 136
Cdd:cd07581    91 YNTLVVVGPDGEIIAVYRKIHLYdaFgfrESDTVAPGDELPPVVFVVGGVKVGLATCYDLRFPELARALaLAGADV--IV 168


                  ....*
gi 1740181664 137 YPTAW 141
Cdd:cd07581   169 VPAAW 173
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 20-119 1.42e-05

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: 46.14  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  20 DTEVLQRLSCMAIKGGMFLVANLgtkqpclssdpgCPQDGRYQFNTNVVFSDNGtLVDRYRK-HNLYFEAAFDTPANVDL 98
Cdd:cd07577    60 DGPTTRFLQELARETGAYIVAGL------------PERDGDKFYNSAVVVGPEG-YIGIYRKtHLFYEEKLFFEPGDTGF 126

                          90       100
                  ....*....|....*....|.
gi 1740181664  99 ITFDTPFaGKFGVFTCFDILF 119
Cdd:cd07577   127 RVFDIGD-IRIGVMICFDWYF 146
PLN02747 PLN02747
N-carbamolyputrescine amidase
 63-225 2.97e-04

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 42.45  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  63 FNTNVVFSDNGTLVDRYRKHNL-----YFEAAFDTPANVDLITFDTPFaGKFGVFTCFDILFFDPAVRL-LRDFEVkhIV 136
Cdd:PLN02747  101 YNSIAIIDADGTDLGLYRKSHIpdgpgYQEKFYFNPGDTGFKVFDTKF-AKIGVAICWDQWFPEAARAMvLQGAEV--LL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664 137 YPTAWMN--QLPLLAAIE----IQKAFATAFGVNVLAAN------IHHPTlgmTGSGIHTPLKSFwyhdMDDPKGHlIIA 204
Cdd:PLN02747  178 YPTAIGSepQDPGLDSRDhwkrVMQGHAGANLVPLVASNrigteiLETEH---GPSKITFYGGSF----IAGPTGE-IVA 249

                         170       180
                  ....*....|....*....|.
gi 1740181664 205 QVATNPQGLtgtgnTTSEMDP 225
Cdd:PLN02747  250 EADDKAEAV-----LVAEFDL 265
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 25-169 3.24e-04

mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily.


Pssm-ID: 143592  Cd Length: 287  Bit Score: 42.10  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  25 QRLSCMAIKGGMFLVAnlgtkqPCLSSDpgcpQDGRYqFNTNVVFSDNGTLVDRYRKHNL-----YFEAAFDTPANVDLI 99
Cdd:cd07568    80 KRFAALAKEYNMVLIL------PIYEKE----QGGTL-YNTAAVIDADGTYLGKYRKNHIphvggFWEKFYFRPGNLGYP 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1740181664 100 TFDTPFaGKFGVFTCFDILFFDPAVRL-LRDFEvkhIVY-PTAWMNQLP-LLAAIEiQKAFATAFGVNVLAAN 169
Cdd:cd07568   149 VFDTAF-GKIGVYICYDRHFPEGWRALgLNGAE---IVFnPSATVAGLSeYLWKLE-QPAAAVANGYFVGAIN 216
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 56-141 9.45e-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: 40.66  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  56 PQDGRYqFNTNVVFSDNGTLVDRYRKHNL-----Y--------FEAAFDTPANVDLI------TFDTPFAGKFGVFTCFD 116
Cdd:cd07571    84 PGGGRY-YNSALLLDPGGGILGRYDKHHLvpfgeYvplrdllrFLGLLFDLPMGDFSpgtgpqPLLLGGGVRVGPLICYE 162

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1740181664 117 ILFfdPavRLLRDFeVKH----IVYPT--AW 141
Cdd:cd07571   163 SIF--P--ELVRDA-VRQgadlLVNITndAW 188
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 56-144 1.09e-03

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: 40.26  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  56 PQDGRYqFNTNVVFSDNGTLVDRYRKHNLY--FEAAFDTPANvDLITFDtpFAG-KFGVFTCFDILFfdP-AVRLLRDFE 131
Cdd:cd07576    85 RAGGAV-YNAAVLIDEDGTVLANYRKTHLFgdSERAAFTPGD-RFPVVE--LRGlRVGLLICYDVEF--PeLVRALALAG 158

                          90
                  ....*....|...
gi 1740181664 132 VKHIVYPTAWMNQ 144
Cdd:cd07576   159 ADLVLVPTALMEP 171
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 56-169 1.60e-03

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


Pssm-ID: 143602  Cd Length: 258  Bit Score: 39.82  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  56 PQDGRYqFNTNVVFSDNGtLVDRYRK-HNLYFEAAFDTPANVDLITFDTPFaGKFGVFTCFDILFFDPAvRLLRDFEVKH 134
Cdd:cd07578    90 SRSGIY-YNSAVLIGPSG-VIGRHRKtHPYISEPKWAADGDLGHQVFDTEI-GRIALLICMDIHFFETA-RLLALGGADV 165

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1740181664 135 IVYPTAWM-NQLPllAAIEIQKAFATafGVNVLAAN 169
Cdd:cd07578   166 ICHISNWLaERTP--APYWINRAFEN--GCYLIESN 197
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 22-129 1.63e-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: 39.88  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740181664  22 EVLQRLSCMAIKGGMFLVAnlgtkqpclSSDPgCPQDGRYQfNTNVVFSDNGTlVDRYRK-HNLYFE-AAFDTPANVDLI 99
Cdd:cd07574    72 DYVALFSELARKYGINIIA---------GSMP-VREDGRLY-NRAYLFGPDGT-IGHQDKlHMTPFErEEWGISGGDKLK 139

                          90       100       110
                  ....*....|....*....|....*....|
gi 1740181664 100 TFDTPFaGKFGVFTCFDILFFDPAvRLLRD 129
Cdd:cd07574   140 VFDTDL-GKIGILICYDSEFPELA-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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