NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1844083952|ref|NP_001229279|]
View 

pantetheine hydrolase VNN2 isoform 3 precursor [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
nitrilase super family cl11424
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
26-180 8.73e-77

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.


The actual alignment was detected with superfamily member cd07567:

Pssm-ID: 448250  Cd Length: 299  Bit Score: 235.99  E-value: 8.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
156-266 1.55e-18

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: 80.87  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952 156 NGYFQYNTNVVYNTEgklvaryhkVCTLLKCKTTNLTTCGRPVETASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPG 233
Cdd:pfam19018  55 DGIRTYEGVDNYYVQ---------ICALVACLNDSLSSCGKLVESANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPS 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1844083952 234 KFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 266
Cdd:pfam19018 126 QWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
26-180 8.73e-77

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: 235.99  E-value: 8.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
156-266 1.55e-18

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: 80.87  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952 156 NGYFQYNTNVVYNTEgklvaryhkVCTLLKCKTTNLTTCGRPVETASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPG 233
Cdd:pfam19018  55 DGIRTYEGVDNYYVQ---------ICALVACLNDSLSSCGKLVESANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPS 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1844083952 234 KFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 266
Cdd:pfam19018 126 QWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
56-180 9.52e-12

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 63.73  E-value: 9.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKI 114
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
56-180 1.30e-06

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: 48.51  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKL 112
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
34-180 2.35e-03

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 39.26  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdp 113
Cdd:TIGR00546 163 ALVQPN---IPQDLKFDSEGLEAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL------- 219
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083952 114 hrfghtpvQARLSCLAKDNSIYVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:TIGR00546 220 --------ADRLKLLVLSKGIPILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKV 269
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
26-180 8.73e-77

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: 235.99  E-value: 8.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
156-266 1.55e-18

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: 80.87  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952 156 NGYFQYNTNVVYNTEgklvaryhkVCTLLKCKTTNLTTCGRPVETASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPG 233
Cdd:pfam19018  55 DGIRTYEGVDNYYVQ---------ICALVACLNDSLSSCGKLVESANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPS 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1844083952 234 KFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 266
Cdd:pfam19018 126 QWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
54-180 1.15e-15

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: 75.05  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  54 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKF-TRETVFPYLEDIPDPQVNWipcqdphrfghtpvqarLSCLAKDN 132
Cdd:cd07197    13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFeSAKEDLDLAEELDGPTLEA-----------------LAELAKEL 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1844083952 133 SIYVLANLGDKKPCNsrdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07197    76 GIYIVAGIAEKDGDK------------LYNTAVVIDPDGEIIGKYRKI 111
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
56-180 1.05e-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: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGwkfTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNS 133
Cdd:cd07572    15 ANLARAKELIEEAAAQGAKLVVLPEcfNYPGG---TDAFKLALAEEEGD----------------GPTLQALSELAKEHG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1844083952 134 IYVLA------NLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07572    76 IWLVGgsiperDDDDGKV---------------YNTSLVFDPDGELVARYRKI 113
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
56-180 9.52e-12

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 63.73  E-value: 9.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKI 114
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
56-180 1.34e-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: 143605  Cd Length: 255  Bit Score: 51.42  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYgwkftretvfpyleDIPDPQVNWIPCQDPhrfGHTPVQARLSCLAKDNSIY 135
Cdd:cd07581    14 ENLEKVRRLLAEAAAAGADLVVFPEYTMA--------------RFGDGLDDYARVAEP---LDGPFVSALARLARELGIT 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1844083952 136 VLANL----GDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07581    77 VVAGMfepaGDGRV---------------YNTLVVVGPDGEIIAVYRKI 110
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
56-180 3.14e-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: 50.64  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPYLEDIpdpqvnwipcqDPHrfghtPVQARLSCLAKDNS 133
Cdd:cd07573    16 ANLAKAEELVREAAAQGAQIVCLQElfETPYFCQEEDEDYFDLAEPP-----------IPG-----PTTARFQALAKELG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083952 134 IYVLANLGDKKpcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07573    80 VVIPVSLFEKR---------GNGLY--YNSAVVIDADGSLLGVYRKM 115
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
56-180 3.86e-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: 143607  Cd Length: 253  Bit Score: 50.23  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETvfpyLEDIPDPQvnwipcqdphrfgHTPVQARLSCLAKDNSIY 135
Cdd:cd07583    16 ANIERVESLIEEAAAAGADLIVLPEMWNTG--YFLDD----LYELADED-------------GGETVSFLSELAKKHGVN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1844083952 136 V----LANLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07583    77 IvagsVAEKEGGKL---------------YNTAYVIDPDGELIATYRKI 110
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
56-180 1.30e-06

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: 48.51  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKL 112
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
58-179 1.11e-05

Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.


Pssm-ID: 143588  Cd Length: 297  Bit Score: 45.94  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  58 IDILETAIKQAAEQGARIIVTPE-------------DALYGWKFTREtvfpYLE---DIPDPQVnwipcqdphrfghtpv 121
Cdd:cd07564    19 VEKACRLIEEAAANGAQLVVFPEafipgypywiwfgAPAEGRELFAR----YYEnsvEVDGPEL---------------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083952 122 qARLSCLAKDNSIYVLanLGdkkpCNSRD-STCppngyfqYNTNVVYNTEGKLVARYHK 179
Cdd:cd07564    79 -ERLAEAARENGIYVV--LG----VSERDgGTL-------YNTQLLIDPDGELLGKHRK 123
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
56-179 4.47e-05

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: 44.06  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDAL--YGWkFTRETVFPYLEDIPDpqvnwipcqdphrfghtPVQARLSCLAKDNS 133
Cdd:cd07578    17 RNIERLLALCEEAARAGARLIVTPEMATtgYCW-YDRAEIAPFVEPIPG-----------------PTTARFAELAREHD 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1844083952 134 IYVLANLGDKKpcnsrdstcPPNGYFqYNTNVVYNTEGkLVARYHK 179
Cdd:cd07578    79 CYIVVGLPEVD---------SRSGIY-YNSAVLIGPSG-VIGRHRK 113
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
57-215 9.78e-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: 43.07  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  57 NIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIYV 136
Cdd:cd07585    17 NLAVIARWTRKAAAQGAELVCFPEMCITG--YTHVRALSREAEVPD----------------GPSTQALSDLARRYGLTI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952 137 LANL---GDKKPcnsrdstcppngyfqYNTNVVYNTEGkLVARYHKvctllkcktTNLTTCGRPVETASTRFEMFSLSG- 212
Cdd:cd07585    79 LAGLiekAGDRP---------------YNTYLVCLPDG-LVHRYRK---------LHLFRREHPYIAAGDEYPVFATPGv 133

                  ...
gi 1844083952 213 TFG 215
Cdd:cd07585   134 RFG 136
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
45-180 8.95e-04

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: 40.04  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  45 VSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRE-TVFPYL-EDIPDPQVNWipcqdphrfghtpvq 122
Cdd:cd07584     5 IQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLWELsEPIDGPTVRL--------------- 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083952 123 arLSCLAKDNSIYVLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07584    70 --FSELAKELGVYIVCGFVEKGGVPGK----------VYNSAVVIDPEGESLGVYRKI 115
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
34-180 2.35e-03

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]


Pssm-ID: 273129 [Multi-domain]  Cd Length: 391  Bit Score: 39.26  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdp 113
Cdd:TIGR00546 163 ALVQPN---IPQDLKFDSEGLEAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL------- 219
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083952 114 hrfghtpvQARLSCLAKDNSIYVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:TIGR00546 220 --------ADRLKLLVLSKGIPILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKV 269
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
34-180 3.66e-03

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: 38.35  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDIPDpqvnwipcqdp 113
Cdd:cd07571     4 ALVQGN---IPQDEKWDPEQRQATLDRYLDLTRELADEKPDLVVWP-----------ETALPFDLQRDP----------- 58
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083952 114 hrfghtPVQARLSCLAKDNSIYVLANLGDKKpcnsrdstcpPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07571    59 ------DALARLARAARAVGAPLLTGAPRRE----------PGGGRYYNSALLLDPGGGILGRYDKH 109
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
56-180 4.62e-03

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 38.29  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDipdpqvnwipcQDPhrfghtPVQARLSCLAKDNSIY 135
Cdd:COG0815   217 EILDRYLDLTRELADDGPDLVVWP-----------ETALPFLLD-----------EDP------DALARLAAAAREAGAP 268
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKKPcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:COG0815   269 LLTGAPRRDG--------GGGRY--YNSALLLDPDGGILGRYDKH 303
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
57-102 5.45e-03

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


Pssm-ID: 143604  Cd Length: 268  Bit Score: 37.71  E-value: 5.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083952  57 NIDILETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPD 102
Cdd:cd07580    17 NLARSIELIREAADAGANLVVLPELANTGYVFEsRDEAFALAEEVPD 63
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
58-179 6.37e-03

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: 37.48  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  58 IDILETAIKQAAEQGARIIVTPEdALYGWKFTRETVFP---YLEDIPdpqvnwipcqdphrfgHTPVQARLSCLAKDNSI 134
Cdd:cd07568    29 IQKHVTMIREAAEAGAQIVCLQE-IFYGPYFCAEQDTKwyeFAEEIP----------------NGPTTKRFAALAKEYNM 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 135 YVLANLGDKKpcnsrdstcppNGYFQYNTNVVYNTEGKLVARYHK 179
Cdd:cd07568    92 VLILPIYEKE-----------QGGTLYNTAAVIDADGTYLGKYRK 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH