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Conserved domains on  [gi|134047954|sp|O95498|]
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RecName: Full=Pantetheine hydrolase VNN2; AltName: Full=Glycosylphosphatidyl inositol-anchored protein GPI-80; AltName: Full=Protein FOAP-4; AltName: Full=Vascular non-inflammatory molecule 2; Short=Vanin-2; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 26-329 1.67e-158

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: 452.47  E-value: 1.67e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSE 185
Cdd:cd07567   74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 186 PQFNVPEKPELVTFNTAFG-RFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLV 264
Cdd:cd07567  154 PGFDVPPEPEIVTFDTDFGvTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134047954 265 ANTHHVSLNMTGSGIYAP-NGPKVYHYDMKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 329
Cdd:cd07567  234 ANYNNPSAGMTGSGIYAGrSGALVYHYDNEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 344-487 7.60e-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: 130.95  E-value: 7.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  344 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 420
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047954  421 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 487
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 ...
 26-329 1.67e-158

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: 452.47  E-value: 1.67e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSE 185
Cdd:cd07567   74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 186 PQFNVPEKPELVTFNTAFG-RFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLV 264
Cdd:cd07567  154 PGFDVPPEPEIVTFDTDFGvTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134047954 265 ANTHHVSLNMTGSGIYAP-NGPKVYHYDMKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 329
Cdd:cd07567  234 ANYNNPSAGMTGSGIYAGrSGALVYHYDNEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 344-487 7.60e-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: 130.95  E-value: 7.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  344 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 420
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047954  421 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 487
Cdd:pfam19018  90 SANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPSQWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
56-284 6.90e-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: 6.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388   18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK------PELVTFNTAFGRFGIF 209
Cdd:COG0388   81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKIHLPNYGVFD--EKryftpgDELVVFDTDGGRIGVL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 210 TCFDIFFYDPGVTLVKDfHVDTILFPTAWM------NVLPLLT--AIEFHSAWAMgmgvnllvANT--HHVSLNMTG-SG 278
Cdd:COG0388  148 ICYDLWFPELARALALA-GADLLLVPSASPfgrgkdHWELLLRarAIENGCYVVA--------ANQvgGEDGLVFDGgSM 218


                 ....*.
gi 134047954 279 IYAPNG 284
Cdd:COG0388  219 IVDPDG 224
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 56-284 1.49e-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: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954   56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  136 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL---YSEPQFNVPEKPE----LVTFNTAFGRFGI 208
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKLHLfpePRPPGFRERVLFEpgdgGTVFDTPLGKIGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  209 FTCFDIFFYDPGVTLVKDfHVDTILFPTA--------WMNVLPLLTAiefHSAWAMGMGVNLLV-ANTHHVSLNMTG-SG 278
Cdd:pfam00795 148 AICYEIRFPELLRALALK-GAEILINPSArapfpgslGPPQWLLLAR---ARALENGCFVIAANqVGGEEDAPWPYGhSM 223


                  ....*.
gi 134047954  279 IYAPNG 284
Cdd:pfam00795 224 IIDPDG 229
PLN02747 PLN02747
N-carbamolyputrescine amidase
 56-305 8.97e-08

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 53.62  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPyledipdpqvnwipCQDPHRfGHtPVQARLSCLAKD-- 131
Cdd:PLN02747  22 ANVDKAERLVREAHAKGANIILIQElfEGYYFCQAQREDFFQ--------------RAKPYE-GH-PTIARMQKLAKElg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 132 ----NSIYVLANlgdkkpcnsrdstcppNGYfqYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTA 202
Cdd:PLN02747  86 vvipVSFFEEAN----------------NAH--YNSIAIIDADGTDLGLYRKSHIpdgpgYQEKFYFNPGDTGFKVFDTK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 203 FGRFGIFTCFDIFFYDPGVTLVKDfHVDTILFPTAwMNVLPLLTAIEFHSAWAMGM----GVNL--LVAN---------T 267
Cdd:PLN02747 148 FAKIGVAICWDQWFPEAARAMVLQ-GAEVLLYPTA-IGSEPQDPGLDSRDHWKRVMqghaGANLvpLVASnrigteileT 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 134047954 268 HHVSLNMT---GSGIYAPNGPKVYHYDMKTElgKLLLSEVD 305
Cdd:PLN02747 226 EHGPSKITfygGSFIAGPTGEIVAEADDKAE--AVLVAEFD 264
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 34-216 1.46e-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: 44.27  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954   34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdp 113
Cdd:TIGR00546 163 ALVQPN---IPQDLKFDSEGLEAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL------- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  114 hrfghtpvQARLSCLAKDNSIYVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHL----------- 182
Cdd:TIGR00546 220 --------ADRLKLLVLSKGIPILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgf 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 134047954  183 --------YSEPQFNVPEK-PELVTFNTAFGRFGIFTCFDIFF 216
Cdd:TIGR00546 283 lfkwlsklFFLLSQEDFSRgPGPQVLKLPGGKIAPLICYESIF 325
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
 26-329 1.67e-158

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: 452.47  E-value: 1.67e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567    1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSE 185
Cdd:cd07567   74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLFGE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 186 PQFNVPEKPELVTFNTAFG-RFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLV 264
Cdd:cd07567  154 PGFDVPPEPEIVTFDTDFGvTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 134047954 265 ANTHHVSLNMTGSGIYAP-NGPKVYHYDMKTElGKLLLSEVDSHPLSSLAYPTA-VNWNAYATTIKP 329
Cdd:cd07567  234 ANYNNPSAGMTGSGIYAGrSGALVYHYDNEPG-GKLLVAEVPKLPSRRPTELEAkVDTSSLPSSLKN 299
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
 344-487 7.60e-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: 130.95  E-value: 7.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  344 DGFNFTELFENAGNLTVCQKELCCHLSYRM-LQKEENEVYVLGAFTGLH--GRRRREYWQVCTLLKCKTTNLTTCGRPVE 420
Cdd:pfam19018  10 DNFTSVLLTGSNGTATVCHGDLCCDFEYETsTTDPSSYLYRLGAFDGIRtyEGVDNYYVQICALVACLNDSLSSCGKLVE 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134047954  421 TASTRFEMFSLSGTF-GTEYVFPEVLLTEIH-LSPGKFEVLK-------DGRLVNKNGSSGPILTVSLFGRWYTKD 487
Cdd:pfam19018  90 SANTTFTSLTISGNFpKTTYVFPSTLDSSLLpLDPSQWEYSSqeisedvTVTLMSLTKPQSNLLTFGIYGRNYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
 54-305 4.92e-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: 4.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  54 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKF-TRETVFPYLEDIPDPQVNWipcqdphrfghtpvqarLSCLAKDN 132
Cdd:cd07197   13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFeSAKEDLDLAEELDGPTLEA-----------------LAELAKEL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 133 SIYVLANLGDKKPCNsrdstcppngyfQYNTNVVYNTEGKLVARYHKYHLYS--EPQFNVPEKpELVTFNTAFGRFGIFT 210
Cdd:cd07197   76 GIYIVAGIAEKDGDK------------LYNTAVVIDPDGEIIGKYRKIHLFDfgERRYFSPGD-EFPVFDTPGGKIGLLI 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 211 CFDIFFYDPGVTLVKDfHVDTILFPTAWM-----NVLPLLT--AIEFHSAWAMgmgVNLlvANTHHVSLNMTGSGIYAPN 283
Cdd:cd07197  143 CYDLRFPELARELALK-GADIILVPAAWPtarreHWELLLRarAIENGVYVVA---ANR--VGEEGGLEFAGGSMIVDPD 216

                        250       260
                 ....*....|....*....|..
gi 134047954 284 GPKVYHYDMKTElgkLLLSEVD 305
Cdd:cd07197  217 GEVLAEASEEEG---ILVAELD 235
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
56-284 6.90e-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: 6.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388   18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK------PELVTFNTAFGRFGIF 209
Cdd:COG0388   81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKIHLPNYGVFD--EKryftpgDELVVFDTDGGRIGVL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 210 TCFDIFFYDPGVTLVKDfHVDTILFPTAWM------NVLPLLT--AIEFHSAWAMgmgvnllvANT--HHVSLNMTG-SG 278
Cdd:COG0388  148 ICYDLWFPELARALALA-GADLLLVPSASPfgrgkdHWELLLRarAIENGCYVVA--------ANQvgGEDGLVFDGgSM 218


                 ....*.
gi 134047954 279 IYAPNG 284
Cdd:COG0388  219 IVDPDG 224
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
 56-216 3.15e-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: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGwkfTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNS 133
Cdd:cd07572   15 ANLARAKELIEEAAAQGAKLVVLPEcfNYPGG---TDAFKLALAEEEGD----------------GPTLQALSELAKEHG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 134 IYVLA------NLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLYSepqFNVPEKP------------E 195
Cdd:cd07572   76 IWLVGgsiperDDDDGKV---------------YNTSLVFDPDGELVARYRKIHLFD---VDVPGGIsyresdtltpgdE 137

                        170       180
                 ....*....|....*....|.
gi 134047954 196 LVTFNTAFGRFGIFTCFDIFF 216
Cdd:cd07572  138 VVVVDTPFGKIGLGICYDLRF 158
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 56-238 4.55e-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: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDALYgwkftretvfpyleDIPDPQVNWIPCQDPhrfGHTPVQARLSCLAKDNSIY 135
Cdd:cd07581   14 ENLEKVRRLLAEAAAAGADLVVFPEYTMA--------------RFGDGLDDYARVAEP---LDGPFVSALARLARELGIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANL----GDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLY-----SEPQFNVP-EKPELVTFNTAFGR 205
Cdd:cd07581   77 VVAGMfepaGDGRV---------------YNTLVVVGPDGEIIAVYRKIHLYdafgfRESDTVAPgDELPPVVFVVGGVK 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 134047954 206 FGIFTCFDIFFydPGV--TLVKDfHVDTILFPTAW 238
Cdd:cd07581  142 VGLATCYDLRF--PELarALALA-GADVIVVPAAW 173
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 56-216 5.37e-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: 5.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETvfpyLEDIPDPQvnwipcqdphrfgHTPVQARLSCLAKDNSIY 135
Cdd:cd07583   16 ANIERVESLIEEAAAAGADLIVLPEMWNTG--YFLDD----LYELADED-------------GGETVSFLSELAKKHGVN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 V----LANLGDKKPcnsrdstcppngyfqYNTNVVYNTEGKLVARYHKYHLYS---EPQFNVPEKpELVTFNTAFGRFGI 208
Cdd:cd07583   77 IvagsVAEKEGGKL---------------YNTAYVIDPDGELIATYRKIHLFGlmgEDKYLTAGD-ELEVFELDGGKVGL 140


                 ....*...
gi 134047954 209 FTCFDIFF 216
Cdd:cd07583  141 FICYDLRF 148
nitrilase_1_R1 cd07578
First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ...
 56-239 3.23e-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: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDAL--YGWkFTRETVFPYLEDIPDPqvnwipcqdphrfghtpVQARLSCLAKDNS 133
Cdd:cd07578   17 RNIERLLALCEEAARAGARLIVTPEMATtgYCW-YDRAEIAPFVEPIPGP-----------------TTARFAELAREHD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 134 IYVLANLGDKKPcnsrdstcpPNGYFqYNTNVVYNTEGkLVARYHKYHLY-SEPQFNVPEKPELVTFNTAFGRFGIFTCF 212
Cdd:cd07578   79 CYIVVGLPEVDS---------RSGIY-YNSAVLIGPSG-VIGRHRKTHPYiSEPKWAADGDLGHQVFDTEIGRIALLICM 147

                        170       180
                 ....*....|....*....|....*..
gi 134047954 213 DIFFYDPGvTLVKDFHVDTILFPTAWM 239
Cdd:cd07578  148 DIHFFETA-RLLALGGADVICHISNWL 173
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 45-307 8.64e-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: 71.25  E-value: 8.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  45 VSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRE-TVFPYL-EDIPDPQVNWipcqdphrfghtpvq 122
Cdd:cd07584    5 IQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLWELsEPIDGPTVRL--------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 123 arLSCLAKDNSIYVLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTA 202
Cdd:cd07584   70 --FSELAKELGVYIVCGFVEKGGVPGK----------VYNSAVVIDPEGESLGVYRKIHLWGLEKQYFREGEQYPVFDTP 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 203 FGRFGIFTCFDIFFydPGVTLVKDFH-VDTILFPTAW----MNVLPLLTAiefhsAWAMGMGVNLLVANTHHVSLNMT-- 275
Cdd:cd07584  138 FGKIGVMICYDMGF--PEVARILTLKgAEVIFCPSAWreqdADIWDINLP-----ARALENTVFVAAVNRVGNEGDLVlf 210

                        250       260       270
                 ....*....|....*....|....*....|...
gi 134047954 276 -GSGIYAPNGPKVYHYDMKTElgKLLLSEVDSH 307
Cdd:cd07584  211 gKSKILNPRGQVLAEASEEAE--EILYAEIDLD 241
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
 56-284 1.49e-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: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954   56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  136 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL---YSEPQFNVPEKPE----LVTFNTAFGRFGI 208
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKLHLfpePRPPGFRERVLFEpgdgGTVFDTPLGKIGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  209 FTCFDIFFYDPGVTLVKDfHVDTILFPTA--------WMNVLPLLTAiefHSAWAMGMGVNLLV-ANTHHVSLNMTG-SG 278
Cdd:pfam00795 148 AICYEIRFPELLRALALK-GAEILINPSArapfpgslGPPQWLLLAR---ARALENGCFVIAANqVGGEEDAPWPYGhSM 223


                  ....*.
gi 134047954  279 IYAPNG 284
Cdd:pfam00795 224 IIDPDG 229
CPA cd07573
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ...
 56-216 3.92e-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: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPYLEDIpdpqvnwipcqDPHrfghtPVQARLSCLAKDNS 133
Cdd:cd07573   16 ANLAKAEELVREAAAQGAQIVCLQElfETPYFCQEEDEDYFDLAEPP-----------IPG-----PTTARFQALAKELG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 134 IYVLANLGDKKpcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEPQFNvpEK----P---ELVTFNTAFGRF 206
Cdd:cd07573   80 VVIPVSLFEKR---------GNGLY--YNSAVVIDADGSLLGVYRKMHIPDDPGYY--EKfyftPgdtGFKVFDTRYGRI 146

                        170
                 ....*....|
gi 134047954 207 GIFTCFDIFF 216
Cdd:cd07573  147 GVLICWDQWF 156
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 57-238 9.54e-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: 9.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  57 NIDILETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:cd07580   17 NLARSIELIREAADAGANLVVLPELANTGYVFEsRDEAFALAEEVPD----------------GASTRAWAELAAELGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANLGDkkpcnsRDSTCppngyfQYNTNVVYNTEGkLVARYHKYHLYS-EPQFNVPEKPELVTFNTAFGRFGIFTCFDI 214
Cdd:cd07580   81 IVAGFAE------RDGDR------LYNSAVLVGPDG-VIGTYRKAHLWNeEKLLFEPGDLGLPVFDTPFGRIGVAICYDG 147

                        170       180
                 ....*....|....*....|....
gi 134047954 215 FFYDPGVTLVKDfHVDTILFPTAW 238
Cdd:cd07580  148 WFPETFRLLALQ-GADIVCVPTNW 170
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
 56-239 5.07e-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: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWkftretvfpyleDIPDpqvnWIPCQDPHRFGhtPVQARLSCLAKDNSIY 135
Cdd:cd07576   16 ANLARLDEAAARAAAAGADLLVFPELFLTGY------------NIGD----AVARLAEPADG--PALQALRAIARRHGIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANLGDkkpcnsRDstcpPNGYfqYNTNVVYNTEGKLVARYHKYHLYSEP---QFNVPEKPELVTFNtafG-RFGIFTC 211
Cdd:cd07576   78 IVVGYPE------RA----GGAV--YNAAVLIDEDGTVLANYRKTHLFGDSeraAFTPGDRFPVVELR---GlRVGLLIC 142

                        170       180
                 ....*....|....*....|....*...
gi 134047954 212 FDIFFYDPgVTLVKDFHVDTILFPTAWM 239
Cdd:cd07576  143 YDVEFPEL-VRALALAGADLVLVPTALM 169
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
 61-284 8.94e-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: 8.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  61 LETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIYVLAN 139
Cdd:cd07577   18 LKKVESLIKGVEADLIVLPELFNTGYAFTsKEEVASLAESIPD----------------GPTTRFLQELARETGAYIVAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 140 LGDKKpcnsrdstcppNGYFqYNTNVVYNTEGkLVARYHKYHL-YSEPQFNVPEKPELVTFNTAFGRFGIFTCFDIFFYD 218
Cdd:cd07577   82 LPERD-----------GDKF-YNSAVVVGPEG-YIGIYRKTHLfYEEKLFFEPGDTGFRVFDIGDIRIGVMICFDWYFPE 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 134047954 219 PGVTLVKDfHVDTILFPTAWmnVLPL------LTAIEFHsawamgmgVNLLVANTHHV------SLNMTG-SGIYAPNG 284
Cdd:cd07577  149 AARTLALK-GADIIAHPANL--VLPYcpkampIRALENR--------VFTITANRIGTeerggeTLRFIGkSQITSPKG 216
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
 57-216 3.77e-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: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  57 NIDILETAIKQAAEQGARIIVTPEDALYGwkFTRETVFPYLEDIPDpqvnwipcqdphrfghTPVQARLSCLAKDNSIYV 136
Cdd:cd07585   17 NLAVIARWTRKAAAQGAELVCFPEMCITG--YTHVRALSREAEVPD----------------GPSTQALSDLARRYGLTI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 137 LANL---GDKKPcnsrdstcppngyfqYNTNVVYNTEGkLVARYHKYHLYSepqfnvPEKP------ELVTFNTAFGRFG 207
Cdd:cd07585   79 LAGLiekAGDRP---------------YNTYLVCLPDG-LVHRYRKLHLFR------REHPyiaagdEYPVFATPGVRFG 136


                 ....*....
gi 134047954 208 IFTCFDIFF 216
Cdd:cd07585  137 ILICYDNHF 145
PLN02747 PLN02747
N-carbamolyputrescine amidase
 56-305 8.97e-08

N-carbamolyputrescine amidase


Pssm-ID: 215398  Cd Length: 296  Bit Score: 53.62  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPyledipdpqvnwipCQDPHRfGHtPVQARLSCLAKD-- 131
Cdd:PLN02747  22 ANVDKAERLVREAHAKGANIILIQElfEGYYFCQAQREDFFQ--------------RAKPYE-GH-PTIARMQKLAKElg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 132 ----NSIYVLANlgdkkpcnsrdstcppNGYfqYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTA 202
Cdd:PLN02747  86 vvipVSFFEEAN----------------NAH--YNSIAIIDADGTDLGLYRKSHIpdgpgYQEKFYFNPGDTGFKVFDTK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 203 FGRFGIFTCFDIFFYDPGVTLVKDfHVDTILFPTAwMNVLPLLTAIEFHSAWAMGM----GVNL--LVAN---------T 267
Cdd:PLN02747 148 FAKIGVAICWDQWFPEAARAMVLQ-GAEVLLYPTA-IGSEPQDPGLDSRDHWKRVMqghaGANLvpLVASnrigteileT 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 134047954 268 HHVSLNMT---GSGIYAPNGPKVYHYDMKTElgKLLLSEVD 305
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 ...
 58-216 1.03e-07

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: 53.65  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  58 IDILETAIKQAAEQGARIIVTPEdALYGWKFTRETVFP---YLEDIPdpqvnwipcqdphrfgHTPVQARLSCLAKDNSI 134
Cdd:cd07568   29 IQKHVTMIREAAEAGAQIVCLQE-IFYGPYFCAEQDTKwyeFAEEIP----------------NGPTTKRFAALAKEYNM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 135 YVLANLGDKKpcnsrdstcppNGYFQYNTNVVYNTEGKLVARYHKYHL-----YSEPQFNVPEKPELVTFNTAFGRFGIF 209
Cdd:cd07568   92 VLILPIYEKE-----------QGGTLYNTAAVIDADGTYLGKYRKNHIphvggFWEKFYFRPGNLGYPVFDTAFGKIGVY 160


                 ....*..
gi 134047954 210 TCFDIFF 216
Cdd:cd07568  161 ICYDRHF 167
PLN02798 PLN02798
nitrilase
 45-237 4.39e-07

nitrilase


Pssm-ID: 215428  Cd Length: 286  Bit Score: 51.67  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  45 VSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEdalygwkftretVFPYLEDIPDPQVNWIPCQDphrfghTPVQAR 124
Cdd:PLN02798  15 VAQMTSTNDLAANFATCSRLAKEAAAAGAKLLFLPE------------CFSFIGDKDGESLAIAEPLD------GPIMQR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 125 LSCLAKDNSIYV-LANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKYHL----------YSEPQFNVPEK 193
Cdd:PLN02798  77 YRSLARESGLWLsLGGFQEKGPDDSH----------LYNTHVLIDDSGEIRSSYRKIHLfdvdvpggpvLKESSFTAPGK 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 134047954 194 pELVTFNTAFGRFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTA 237
Cdd:PLN02798 147 -TIVAVDSPVGRLGLTVCYDLRFPELYQQLRFEHGAQVLLVPSA 189
nitrilases_CHs cd07564
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ...
 58-207 9.05e-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: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  58 IDILETAIKQAAEQGARIIVTPE-------------DALYGWKFTREtvfpYLE---DIPDPQVnwipcqdphrfghtpv 121
Cdd:cd07564   19 VEKACRLIEEAAANGAQLVVFPEafipgypywiwfgAPAEGRELFAR----YYEnsvEVDGPEL---------------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 122 qARLSCLAKDNSIYVLanLGdkkpCNSRD-STCppngyfqYNTNVVYNTEGKLVARYHKYhlysepqfnVPEKPE----- 195
Cdd:cd07564   79 -ERLAEAARENGIYVV--LG----VSERDgGTL-------YNTQLLIDPDGELLGKHRKL---------KPTHAErlvwg 135

                        170
                 ....*....|....*...
gi 134047954 196 ------LVTFNTAFGRFG 207
Cdd:cd07564  136 qgdgsgLRVVDTPIGRLG 153
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
 34-216 5.91e-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: 44.90  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDIPDpqvnwipcqdp 113
Cdd:cd07571    4 ALVQGN---IPQDEKWDPEQRQATLDRYLDLTRELADEKPDLVVWP-----------ETALPFDLQRDP----------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 114 hrfghtPVQARLSCLAKDNSIYVLANLGDKKpcnsrdstcpPNGYFQYNTNVVYNTEGKLVARYHKYHL--YSE------ 185
Cdd:cd07571   59 ------DALARLARAARAVGAPLLTGAPRRE----------PGGGRYYNSALLLDPGGGILGRYDKHHLvpFGEyvplrd 122

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 134047954 186 ------PQFNVP-------EKPELVTFNtAFGRFGIFTCFDIFF 216
Cdd:cd07571  123 llrflgLLFDLPmgdfspgTGPQPLLLG-GGVRVGPLICYESIF 165
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
56-216 6.37e-05

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 45.60  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  56 ENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDipdpqvnwipcQDPhrfghtPVQARLSCLAKDNSIY 135
Cdd:COG0815  217 EILDRYLDLTRELADDGPDLVVWP-----------ETALPFLLD-----------EDP------DALARLAAAAREAGAP 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 136 VLANLGDKKPcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKYHL--YSE------------PQFNVPEK-----PEL 196
Cdd:COG0815  269 LLTGAPRRDG--------GGGRY--YNSALLLDPDGGILGRYDKHHLvpFGEyvplrdllrpliPFLDLPLGdfspgTGP 338

                        170       180
                 ....*....|....*....|
gi 134047954 197 VTFNTAFGRFGIFTCFDIFF 216
Cdd:COG0815  339 PVLDLGGVRVGPLICYESIF 358
lnt TIGR00546
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ...
 34-216 1.46e-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: 44.27  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954   34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdp 113
Cdd:TIGR00546 163 ALVQPN---IPQDLKFDSEGLEAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL------- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  114 hrfghtpvQARLSCLAKDNSIYVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHL----------- 182
Cdd:TIGR00546 220 --------ADRLKLLVLSKGIPILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKVKLvpfgeyiplgf 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 134047954  183 --------YSEPQFNVPEK-PELVTFNTAFGRFGIFTCFDIFF 216
Cdd:TIGR00546 283 lfkwlsklFFLLSQEDFSRgPGPQVLKLPGGKIAPLICYESIF 325
nitrilase_Rim1_like cd07574
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ...
 58-237 1.81e-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: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954  58 IDILETAIKQAAEQGARIIVTPEdalYgwkFTRE--TVFPYLEDIPDPQVNWIPcqdphrfGHTP-VQARLSCLAKDNSI 134
Cdd:cd07574   20 AAKVEYWVAEAAGYGADLLVFPE---Y---FTMEllSLLPEAIDGLDEAIRALA-------ALTPdYVALFSELARKYGI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134047954 135 YVLAnlgdkkpcnsrdSTCP---PNGYfqYNTNVVYNTEGKlVARYHKYHL--YSEPQFNVPEKPELVTFNTAFGRFGIF 209
Cdd:cd07574   87 NIIA------------GSMPvreDGRL--YNRAYLFGPDGT-IGHQDKLHMtpFEREEWGISGGDKLKVFDTDLGKIGIL 151

                        170       180
                 ....*....|....*....|....*...
gi 134047954 210 TCFDIFFYDPGVTLVkDFHVDTILFPTA 237
Cdd:cd07574  152 ICYDSEFPELARALA-EAGADLLLVPSC 178
 
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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