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Conserved domains on  [gi|1844084012|ref|NP_511043|]
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pantetheine hydrolase VNN2 isoform 2 [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 ...
 1-276 4.30e-150

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: 429.36  E-value: 4.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   1 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNS 80
Cdd:cd07567    22 MEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEVNWNPCLDPDRFDYTEVLQRLSCAARENS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFG-RFGIFTCF 159
Cdd:cd07567   102 IYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPGFDVPPEPEIVTFDTDFGvTFGIFTCF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 160 DIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAP-NGPKVYHYD 238
Cdd:cd07567   182 DILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAANYNNPSAGMTGSGIYAGrSGALVYHYD 261

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1844084012 239 MKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 276
Cdd:cd07567   262 NEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 291-434 5.47e-36

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: 130.56  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 291 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 367
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084012 368 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 434
Cdd:pfam19018  90 SANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPSQWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 1-276 4.30e-150

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: 429.36  E-value: 4.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   1 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNS 80
Cdd:cd07567    22 MEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEVNWNPCLDPDRFDYTEVLQRLSCAARENS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFG-RFGIFTCF 159
Cdd:cd07567   102 IYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPGFDVPPEPEIVTFDTDFGvTFGIFTCF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 160 DIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAP-NGPKVYHYD 238
Cdd:cd07567   182 DILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAANYNNPSAGMTGSGIYAGrSGALVYHYD 261

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1844084012 239 MKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 276
Cdd:cd07567   262 NEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 291-434 5.47e-36

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: 130.56  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 291 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 367
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084012 368 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 434
Cdd:pfam19018  90 SANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPSQWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-231 4.78e-24

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 100.71  E-value: 4.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 82
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK------PELVTFNTAFGRFGIF 156
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKIHLPNYGVFD--EKryftpgDELVVFDTDGGRIGVL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 157 TCFDIFFYDPGVTLVKDfHVDTILFPTAWM------NVLPLLT--AIEFHSAWAMgmgvnllvANT--HHVSLNMTG-SG 225
Cdd:COG0388   148 ICYDLWFPELARALALA-GADLLLVPSASPfgrgkdHWELLLRarAIENGCYVVA--------ANQvgGEDGLVFDGgSM 218


                  ....*.
gi 1844084012 226 IYAPNG 231
Cdd:COG0388   219 IVDPDG 224
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 3-231 1.26e-13

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: 70.46  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 82
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL---YSEPQFNVPEKPE----LVTFNTAFGRFGI 155
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKLHLfpePRPPGFRERVLFEpgdgGTVFDTPLGKIGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 156 FTCFDIFFYDPGVTLVKDfHVDTILFPTA--------WMNVLPLLTAiefHSAWAMGMGVNLLV-ANTHHVSLNMTG-SG 225
Cdd:pfam00795 148 AICYEIRFPELLRALALK-GAEILINPSArapfpgslGPPQWLLLAR---ARALENGCFVIAANqVGGEEDAPWPYGhSM 223


                  ....*.
gi 1844084012 226 IYAPNG 231
Cdd:pfam00795 224 IIDPDG 229
PLN02747 PLN02747
N-carbamolyputrescine amidase
 3-252 7.62e-08

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 53.62  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPyledipdpqvnwipCQDPHRfGHtPVQARLSCLAKD-- 78
Cdd:PLN02747   22 ANVDKAERLVREAHAKGANIILIQElfEGYYFCQAQREDFFQ--------------RAKPYE-GH-PTIARMQKLAKElg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  79 ----NSIYVLANlgdkkpcnsrdstcppNGYfqYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTA 149
Cdd:PLN02747   86 vvipVSFFEEAN----------------NAH--YNSIAIIDADGTDLGLYRKSHIpdgpgYQEKFYFNPGDTGFKVFDTK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 150 FGRFGIFTCFDIFFYDPGVTLVKDfHVDTILFPTAwMNVLPLLTAIEFHSAWAMGM----GVNL--LVAN---------T 214
Cdd:PLN02747  148 FAKIGVAICWDQWFPEAARAMVLQ-GAEVLLYPTA-IGSEPQDPGLDSRDHWKRVMqghaGANLvpLVASnrigteileT 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1844084012 215 HHVSLNMT---GSGIYAPNGPKVYHYDMKTElgKLLLSEVD 252
Cdd:PLN02747  226 EHGPSKITfygGSFIAGPTGEIVAEADDKAE--AVLVAEFD 264
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 2-163 2.04e-04

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: 43.50  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   2 NENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdphrfghtpvQARLSCLAKDNSI 81
Cdd:TIGR00546 181 EAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL---------------ADRLKLLVLSKGI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  82 YVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHL-------------------YSEPQFNVPEK-P 141
Cdd:TIGR00546 233 PILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgflfkwlsklFFLLSQEDFSRgP 303

                         170       180
                  ....*....|....*....|..
gi 1844084012 142 ELVTFNTAFGRFGIFTCFDIFF 163
Cdd:TIGR00546 304 GPQVLKLPGGKIAPLICYESIF 325
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 1-276 4.30e-150

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: 429.36  E-value: 4.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   1 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNS 80
Cdd:cd07567    22 MEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEVNWNPCLDPDRFDYTEVLQRLSCAARENS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFG-RFGIFTCF 159
Cdd:cd07567   102 IYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGEPGFDVPPEPEIVTFDTDFGvTFGIFTCF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 160 DIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAP-NGPKVYHYD 238
Cdd:cd07567   182 DILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLAANYNNPSAGMTGSGIYAGrSGALVYHYD 261

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1844084012 239 MKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 276
Cdd:cd07567   262 NEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 291-434 5.47e-36

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: 130.56  E-value: 5.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 291 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 367
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084012 368 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 434
Cdd:pfam19018  90 SANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPSQWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 1-252 2.56e-33

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: 126.29  E-value: 2.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   1 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKF-TRETVFPYLEDIPDPQVNWipcqdphrfghtpvqarLSCLAKDN 79
Cdd:cd07197    13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFeSAKEDLDLAEELDGPTLEA-----------------LAELAKEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  80 SIYVLANLGDKKPCNsrdstcppngyfQYNTNVVYNTEGKLVARYHKYHLYS--EPQFNVPEKpELVTFNTAFGRFGIFT 157
Cdd:cd07197    76 GIYIVAGIAEKDGDK------------LYNTAVVIDPDGEIIGKYRKIHLFDfgERRYFSPGD-EFPVFDTPGGKIGLLI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 158 CFDIFFYDPGVTLVKDfHVDTILFPTAWM-----NVLPLLT--AIEFHSAWAMgmgVNLlvANTHHVSLNMTGSGIYAPN 230
Cdd:cd07197   143 CYDLRFPELARELALK-GADIILVPAAWPtarreHWELLLRarAIENGVYVVA---ANR--VGEEGGLEFAGGSMIVDPD 216

                         250       260
                  ....*....|....*....|..
gi 1844084012 231 GPKVYHYDMKTElgkLLLSEVD 252
Cdd:cd07197   217 GEVLAEASEEEG---ILVAELD 235
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
3-231 4.78e-24

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 100.71  E-value: 4.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 82
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK------PELVTFNTAFGRFGIF 156
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKIHLPNYGVFD--EKryftpgDELVVFDTDGGRIGVL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 157 TCFDIFFYDPGVTLVKDfHVDTILFPTAWM------NVLPLLT--AIEFHSAWAMgmgvnllvANT--HHVSLNMTG-SG 225
Cdd:COG0388   148 ICYDLWFPELARALALA-GADLLLVPSASPfgrgkdHWELLLRarAIENGCYVVA--------ANQvgGEDGLVFDGgSM 218


                  ....*.
gi 1844084012 226 IYAPNG 231
Cdd:COG0388   219 IVDPDG 224
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 3-163 2.41e-20

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: 90.18  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPE--DALYGwkfTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNS 80
Cdd:cd07572    15 ANLARAKELIEEAAAQGAKLVVLPEcfNYPGG---TDAFKLALAEEEGD----------------GPTLQALSELAKEHG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLA------NLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLYSepqFNVPEKP------------E 142
Cdd:cd07572    76 IWLVGgsiperDDDDGKV---------------YNTSLVFDPDGELVARYRKIHLFD---VDVPGGIsyresdtltpgdE 137

                         170       180
                  ....*....|....*....|.
gi 1844084012 143 LVTFNTAFGRFGIFTCFDIFF 163
Cdd:cd07572   138 VVVVDTPFGKIGLGICYDLRF 158
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 3-185 3.80e-15

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: 74.92  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYgwkftretvfpyleDIPDPQVNWIPCQDPhrfGHTPVQARLSCLAKDNSIY 82
Cdd:cd07581    14 ENLEKVRRLLAEAAAAGADLVVFPEYTMA--------------RFGDGLDDYARVAEP---LDGPFVSALARLARELGIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANL----GDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLY-----SEPQFNVP-EKPELVTFNTAFGR 152
Cdd:cd07581    77 VVAGMfepaGDGRV---------------YNTLVVVGPDGEIIAVYRKIHLYdafgfRESDTVAPgDELPPVVFVVGGVK 141

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1844084012 153 FGIFTCFDIFFydPGV--TLVKDfHVDTILFPTAW 185
Cdd:cd07581   142 VGLATCYDLRF--PELarALALA-GADVIVVPAAW 173
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 3-163 4.49e-15

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: 74.88  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETvfpyLEDIPDPQvnwipcqdphrfgHTPVQARLSCLAKDNSIY 82
Cdd:cd07583    16 ANIERVESLIEEAAAAGADLIVLPEMWNTG--YFLDD----LYELADED-------------GGETVSFLSELAKKHGVN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 V----LANLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLYS---EPQFNVPEKpELVTFNTAFGRFGI 155
Cdd:cd07583    77 IvagsVAEKEGGKL---------------YNTAYVIDPDGELIATYRKIHLFGlmgEDKYLTAGD-ELEVFELDGGKVGL 140


                  ....*...
gi 1844084012 156 FTCFDIFF 163
Cdd:cd07583   141 FICYDLRF 148
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 3-186 2.95e-14

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: 72.56  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDAL--YGWkFTRETVFPYLEDIPDPqvnwipcqdphrfghtpVQARLSCLAKDNS 80
Cdd:cd07578    17 RNIERLLALCEEAARAGARLIVTPEMATtgYCW-YDRAEIAPFVEPIPGP-----------------TTARFAELAREHD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLANLGDKKPcnsrdstcpPNGYFqYNTNVVYNTEGkLVARYHKYHLY-SEPQFNVPEKPELVTFNTAFGRFGIFTCF 159
Cdd:cd07578    79 CYIVVGLPEVDS---------RSGIY-YNSAVLIGPSG-VIGRHRKTHPYiSEPKWAADGDLGHQVFDTEIGRIALLICM 147

                         170       180
                  ....*....|....*....|....*..
gi 1844084012 160 DIFFYDPGvTLVKDFHVDTILFPTAWM 186
Cdd:cd07578   148 DIHFFETA-RLLALGGADVICHISNWL 173
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 4-254 9.91e-14

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: 70.86  E-value: 9.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   4 NIDILETAIKQAAEQGARIIVTPEDALYGWKFTRE-TVFPYL-EDIPDPQVNWipcqdphrfghtpvqarLSCLAKDNSI 81
Cdd:cd07584    17 NLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLWELsEPIDGPTVRL-----------------FSELAKELGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  82 YVLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFGRFGIFTCFDI 161
Cdd:cd07584    80 YIVCGFVEKGGVPGK----------VYNSAVVIDPEGESLGVYRKIHLWGLEKQYFREGEQYPVFDTPFGKIGVMICYDM 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 162 FFydPGVTLVKDFH-VDTILFPTAW----MNVLPLLTAiefhsAWAMGMGVNLLVANTHHVSLNMT---GSGIYAPNGPK 233
Cdd:cd07584   150 GF--PEVARILTLKgAEVIFCPSAWreqdADIWDINLP-----ARALENTVFVAAVNRVGNEGDLVlfgKSKILNPRGQV 222

                         250       260
                  ....*....|....*....|.
gi 1844084012 234 VYHYDMKTElgKLLLSEVDSH 254
Cdd:cd07584   223 LAEASEEAE--EILYAEIDLD 241
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 3-231 1.26e-13

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: 70.46  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 82
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL---YSEPQFNVPEKPE----LVTFNTAFGRFGI 155
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKLHLfpePRPPGFRERVLFEpgdgGTVFDTPLGKIGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 156 FTCFDIFFYDPGVTLVKDfHVDTILFPTA--------WMNVLPLLTAiefHSAWAMGMGVNLLV-ANTHHVSLNMTG-SG 225
Cdd:pfam00795 148 AICYEIRFPELLRALALK-GAEILINPSArapfpgslGPPQWLLLAR---ARALENGCFVIAANqVGGEEDAPWPYGhSM 223


                  ....*.
gi 1844084012 226 IYAPNG 231
Cdd:pfam00795 224 IIDPDG 229
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 3-163 3.30e-12

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: 66.82  E-value: 3.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPYLEDIpdpqvnwipcqDPHrfghtPVQARLSCLAKDNS 80
Cdd:cd07573    16 ANLAKAEELVREAAAQGAQIVCLQElfETPYFCQEEDEDYFDLAEPP-----------IPG-----PTTARFQALAKELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  81 IYVLANLGDKKpcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK----P---ELVTFNTAFGRF 153
Cdd:cd07573    80 VVIPVSLFEKR---------GNGLY--YNSAVVIDADGSLLGVYRKMHIPDDPGYY--EKfyftPgdtGFKVFDTRYGRI 146

                         170
                  ....*....|
gi 1844084012 154 GIFTCFDIFF 163
Cdd:cd07573   147 GVLICWDQWF 156
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 4-185 8.09e-11

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: 62.36  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   4 NIDILETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 82
Cdd:cd07580    17 NLARSIELIREAADAGANLVVLPELANTGYVFEsRDEAFALAEEVPD----------------GASTRAWAELAAELGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDkkpcnsRDSTCppngyfQYNTNVVYNTEGkLVARYHKYHLYS-EPQFNVPEKPELVTFNTAFGRFGIFTCFDI 161
Cdd:cd07580    81 IVAGFAE------RDGDR------LYNSAVLVGPDG-VIGTYRKAHLWNeEKLLFEPGDLGLPVFDTPFGRIGVAICYDG 147

                         170       180
                  ....*....|....*....|....
gi 1844084012 162 FFYDPGVTLVKDfHVDTILFPTAW 185
Cdd:cd07580   148 WFPETFRLLALQ-GADIVCVPTNW 170
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 3-186 4.33e-09

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: 57.20  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPEDALYGWkftretvfpyleDIPDpqvnWIPCQDPHRFGhtPVQARLSCLAKDNSIY 82
Cdd:cd07576    16 ANLARLDEAAARAAAAGADLLVFPELFLTGY------------NIGD----AVARLAEPADG--PALQALRAIARRHGIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDkkpcnsRDstcpPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEP---QFNVPEKPELVTFNtafG-RFGIFTC 158
Cdd:cd07576    78 IVVGYPE------RA----GGAV--YNAAVLIDEDGTVLANYRKTHLFGDSeraAFTPGDRFPVVELR---GlRVGLLIC 142

                         170       180
                  ....*....|....*....|....*...
gi 1844084012 159 FDIFFYDPgVTLVKDFHVDTILFPTAWM 186
Cdd:cd07576   143 YDVEFPEL-VRALALAGADLVLVPTALM 169
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 8-231 7.64e-09

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: 56.54  E-value: 7.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   8 LETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIYVLAN 86
Cdd:cd07577    18 LKKVESLIKGVEADLIVLPELFNTGYAFTsKEEVASLAESIPD----------------GPTTRFLQELARETGAYIVAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  87 LGDKKpcnsrdstcppNGYFqYNTNVVYNTEGkLVARYHKYHL-YSEPQFNVPEKPELVTFNTAFGRFGIFTCFDIFFYD 165
Cdd:cd07577    82 LPERD-----------GDKF-YNSAVVVGPEG-YIGIYRKTHLfYEEKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPE 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844084012 166 PGVTLVKDfHVDTILFPTAWmnVLPL------LTAIEFHsawamgmgVNLLVANTHHV------SLNMTG-SGIYAPNG 231
Cdd:cd07577   149 AARTLALK-GADIIAHPANL--VLPYcpkampIRALENR--------VFTITANRIGTeerggeTLRFIGkSQITSPKG 216
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 4-163 3.23e-08

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: 54.63  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   4 NIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIYV 83
Cdd:cd07585    17 NLAVIARWTRKAAAQGAELVCFPEMCITG--YTHVRALSREAEVPD----------------GPSTQALSDLARRYGLTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  84 LANL---GDKKPcnsrdstcppngyfqYNTNVVYNTEGkLVARYHKYHLYSepqfnvPEKP------ELVTFNTAFGRFG 154
Cdd:cd07585    79 LAGLiekAGDRP---------------YNTYLVCLPDG-LVHRYRKLHLFR------REHPyiaagdEYPVFATPGVRFG 136


                  ....*....
gi 1844084012 155 IFTCFDIFF 163
Cdd:cd07585   137 ILICYDNHF 145
PLN02747 PLN02747
N-carbamolyputrescine amidase
 3-252 7.62e-08

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 53.62  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPyledipdpqvnwipCQDPHRfGHtPVQARLSCLAKD-- 78
Cdd:PLN02747   22 ANVDKAERLVREAHAKGANIILIQElfEGYYFCQAQREDFFQ--------------RAKPYE-GH-PTIARMQKLAKElg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  79 ----NSIYVLANlgdkkpcnsrdstcppNGYfqYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTA 149
Cdd:PLN02747   86 vvipVSFFEEAN----------------NAH--YNSIAIIDADGTDLGLYRKSHIpdgpgYQEKFYFNPGDTGFKVFDTK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012 150 FGRFGIFTCFDIFFYDPGVTLVKDfHVDTILFPTAwMNVLPLLTAIEFHSAWAMGM----GVNL--LVAN---------T 214
Cdd:PLN02747  148 FAKIGVAICWDQWFPEAARAMVLQ-GAEVLLYPTA-IGSEPQDPGLDSRDHWKRVMqghaGANLvpLVASnrigteileT 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1844084012 215 HHVSLNMT---GSGIYAPNGPKVYHYDMKTElgKLLLSEVD 252
Cdd:PLN02747  226 EHGPSKITfygGSFIAGPTGEIVAEADDKAE--AVLVAEFD 264
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
 5-163 9.73e-08

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: 53.27  E-value: 9.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   5 IDILETAIKQAAEQGARIIVTPEdALYGWKFTRETVFP---YLEDIPdpqvnwipcqdphrfgHTPVQARLSCLAKDNSI 81
Cdd:cd07568    29 IQKHVTMIREAAEAGAQIVCLQE-IFYGPYFCAEQDTKwyeFAEEIP----------------NGPTTKRFAALAKEYNM 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  82 YVLANLGDKKpcnsrdstcppNGYFQYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTAFGRFGIF 156
Cdd:cd07568    92 VLILPIYEKE-----------QGGTLYNTAAVIDADGTYLGKYRKNHIphvggFWEKFYFRPGNLGYPVFDTAFGKIGVY 160


                  ....*..
gi 1844084012 157 TCFDIFF 163
Cdd:cd07568   161 ICYDRHF 167
PLN02798 PLN02798
nitrilase
 4-184 1.06e-06

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 50.13  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   4 NIDILETAIKQAAEQGARIIVTPEdalygwkftretVFPYLEDIPDPQVNWIPCQDphrfghTPVQARLSCLAKDNSIYV 83
Cdd:PLN02798   27 NFATCSRLAKEAAAAGAKLLFLPE------------CFSFIGDKDGESLAIAEPLD------GPIMQRYRSLARESGLWL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  84 -LANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL----------YSEPQFNVPEKpELVTFNTAFGR 152
Cdd:PLN02798   89 sLGGFQEKGPDDSH----------LYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGK-TIVAVDSPVGR 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1844084012 153 FGIFTCFDIFFYDPGVTLVKDFHVDTILFPTA 184
Cdd:PLN02798  158 LGLTVCYDLRFPELYQQLRFEHGAQVLLVPSA 189
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
 5-154 7.74e-06

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: 47.48  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   5 IDILETAIKQAAEQGARIIVTPE-------------DALYGWKFTREtvfpYLE---DIPDPQVnwipcqdphrfghtpv 68
Cdd:cd07564    19 VEKACRLIEEAAANGAQLVVFPEafipgypywiwfgAPAEGRELFAR----YYEnsvEVDGPEL---------------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  69 qARLSCLAKDNSIYVLanLGdkkpCNSRD-STCppngyfqYNTNVVYNTEGKLVARYHKYhlysepqfnVPEKPE----- 142
Cdd:cd07564    79 -ERLAEAARENGIYVV--LG----VSERDgGTL-------YNTQLLIDPDGELLGKHRKL---------KPTHAErlvwg 135

                         170
                  ....*....|....*...
gi 1844084012 143 ------LVTFNTAFGRFG 154
Cdd:cd07564   136 qgdgsgLRVVDTPIGRLG 153
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
3-163 3.72e-05

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 45.99  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDipdpqvnwipcQDPhrfghtPVQARLSCLAKDNSIY 82
Cdd:COG0815   217 EILDRYLDLTRELADDGPDLVVWP-----------ETALPFLLD-----------EDP------DALARLAAAAREAGAP 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKKPcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKYHL--YSE------------PQFNVPEK-----PEL 143
Cdd:COG0815   269 LLTGAPRRDG--------GGGRY--YNSALLLDPDGGILGRYDKHHLvpFGEyvplrdllrpliPFLDLPLGdfspgTGP 338

                         170       180
                  ....*....|....*....|
gi 1844084012 144 VTFNTAFGRFGIFTCFDIFF 163
Cdd:COG0815   339 PVLDLGGVRVGPLICYESIF 358
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 3-163 6.26e-05

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: 44.51  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   3 ENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDIPDpqvnwipcqdphrfghtPVQARLSCLAKDNSIY 82
Cdd:cd07571    23 ATLDRYLDLTRELADEKPDLVVWP-----------ETALPFDLQRDP-----------------DALARLARAARAVGAP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  83 VLANLGDKKpcnsrdstcpPNGYFQYNTNVVYNTEGKLVARYHKYHL--YSE------------PQFNVP-------EKP 141
Cdd:cd07571    75 LLTGAPRRE----------PGGGRYYNSALLLDPGGGILGRYDKHHLvpFGEyvplrdllrflgLLFDLPmgdfspgTGP 144

                         170       180
                  ....*....|....*....|..
gi 1844084012 142 ELVTFNtAFGRFGIFTCFDIFF 163
Cdd:cd07571   145 QPLLLG-GGVRVGPLICYESIF 165
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 5-184 1.56e-04

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: 43.34  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   5 IDILETAIKQAAEQGARIIVTPEdalYgwkFTRE--TVFPYLEDIPDPQVNWIPcqdphrfGHTP-VQARLSCLAKDNSI 81
Cdd:cd07574    20 AAKVEYWVAEAAGYGADLLVFPE---Y---FTMEllSLLPEAIDGLDEAIRALA-------ALTPdYVALFSELARKYGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  82 YVLAnlgdkkpcnsrdSTCP---PNGYfqYNTNVVYNTEGKlVARYHKYHL--YSEPQFNVPEKPELVTFNTAFGRFGIF 156
Cdd:cd07574    87 NIIA------------GSMPvreDGRL--YNRAYLFGPDGT-IGHQDKLHMtpFEREEWGISGGDKLKVFDTDLGKIGIL 151

                         170       180
                  ....*....|....*....|....*...
gi 1844084012 157 TCFDIFFYDPGVTLVkDFHVDTILFPTA 184
Cdd:cd07574   152 ICYDSEFPELARALA-EAGADLLLVPSC 178
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 2-163 2.04e-04

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: 43.50  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012   2 NENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdphrfghtpvQARLSCLAKDNSI 81
Cdd:TIGR00546 181 EAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL---------------ADRLKLLVLSKGI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084012  82 YVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHL-------------------YSEPQFNVPEK-P 141
Cdd:TIGR00546 233 PILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgflfkwlsklFFLLSQEDFSRgP 303

                         170       180
                  ....*....|....*....|..
gi 1844084012 142 ELVTFNTAFGRFGIFTCFDIFF 163
Cdd:TIGR00546 304 GPQVLKLPGGKIAPLICYESIF 325
 
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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