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Conserved domains on  [gi|24640061|ref|NP_572298|]
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biotinidase [Drosophila melanogaster]

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 ...
29-308 4.01e-128

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: 376.58  E-value: 4.01e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  29 YTAAVVEHSQPVGDSP--RARTTSASESFQKIIREVG--DVDIIVFPEHILNSQATATFVP-----------HESQNITP 93
Cdd:cd07567   1 YIAAVVEHHPILSPDPdaLQIMEKNLDIYEEIIKSAAkqGADIIVFPEDGLTGFIFTRFVIypfledvpdpeVNWNPCLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  94 CYQTDYELFLIELSCSARANHLYVVINVVEKELCahgagSDTYNPCPSSGVRYFNTNVVFDRRGRIVSRYRKTHLWrHEY 173
Cdd:cd07567  81 PDRFDYTEVLQRLSCAARENSIYVVANLGEKQPC-----DSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLF-GEP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 174 vSTSVLRSPDISIFRTDFGVTFGHFICFDMLFYDPAMKLVKEHKITDIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLA 253
Cdd:cd07567 155 -GFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640061 254 ADASNPDGRTSGSGIYAGRGGRLVAEIFEQPTTKLLIAEVPKREHGQLAPTFTPI 308
Cdd:cd07567 234 ANYNNPSAGMTGSGIYAGRSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKV 288
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
325-511 5.90e-37

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: 134.41  E-value: 5.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   325 RDNNVDIFESELLDDDflSFERQLCHGSFCCTFSIERKVTSaaenelpssgAKSYRYRIGVYWGNeTTVIGVDRTEQATC 404
Cdd:pfam19018   5 RDPNLDNFTSVLLTGS--NGTATVCHGDLCCDFEYETSTTD----------PSSYLYRLGAFDGI-RTYEGVDNYYVQIC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   405 ALFACTDVRLASCGYIYPENeeviNThHFTKLSISGNFPaaprGRRLIMPSSLNALFLPVSVSDYEWIESpeaaNNLDKT 484
Cdd:pfam19018  72 ALVACLNDSLSSCGKLVESA----NT-TFTSLTISGNFP----KTTYVFPSTLDSSLLPLDPSQWEYSSQ----EISEDV 138
                         170       180
                  ....*....|....*....|....*..
gi 24640061   485 ILVDLKLAKAQNDLLTFAIWANYYTDI 511
Cdd:pfam19018 139 TVTLMSLTKPQSNLLTFGIYGRNYDRD 165
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
29-308 4.01e-128

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: 376.58  E-value: 4.01e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  29 YTAAVVEHSQPVGDSP--RARTTSASESFQKIIREVG--DVDIIVFPEHILNSQATATFVP-----------HESQNITP 93
Cdd:cd07567   1 YIAAVVEHHPILSPDPdaLQIMEKNLDIYEEIIKSAAkqGADIIVFPEDGLTGFIFTRFVIypfledvpdpeVNWNPCLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  94 CYQTDYELFLIELSCSARANHLYVVINVVEKELCahgagSDTYNPCPSSGVRYFNTNVVFDRRGRIVSRYRKTHLWrHEY 173
Cdd:cd07567  81 PDRFDYTEVLQRLSCAARENSIYVVANLGEKQPC-----DSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLF-GEP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 174 vSTSVLRSPDISIFRTDFGVTFGHFICFDMLFYDPAMKLVKEHKITDIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLA 253
Cdd:cd07567 155 -GFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640061 254 ADASNPDGRTSGSGIYAGRGGRLVAEIFEQPTTKLLIAEVPKREHGQLAPTFTPI 308
Cdd:cd07567 234 ANYNNPSAGMTGSGIYAGRSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKV 288
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
325-511 5.90e-37

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: 134.41  E-value: 5.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   325 RDNNVDIFESELLDDDflSFERQLCHGSFCCTFSIERKVTSaaenelpssgAKSYRYRIGVYWGNeTTVIGVDRTEQATC 404
Cdd:pfam19018   5 RDPNLDNFTSVLLTGS--NGTATVCHGDLCCDFEYETSTTD----------PSSYLYRLGAFDGI-RTYEGVDNYYVQIC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   405 ALFACTDVRLASCGYIYPENeeviNThHFTKLSISGNFPaaprGRRLIMPSSLNALFLPVSVSDYEWIESpeaaNNLDKT 484
Cdd:pfam19018  72 ALVACLNDSLSSCGKLVESA----NT-TFTSLTISGNFP----KTTYVFPSTLDSSLLPLDPSQWEYSSQ----EISEDV 138
                         170       180
                  ....*....|....*....|....*..
gi 24640061   485 ILVDLKLAKAQNDLLTFAIWANYYTDI 511
Cdd:pfam19018 139 TVTLMSLTKPQSNLLTFGIYGRNYDRD 165
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
28-293 2.64e-13

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 70.28  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  28 TYTAAVVEHSQPVGDspRARTTSASESFqkiIREVGD--VDIIVFPEhilnsqATATFVPHESQNITPCYQTDYELFLIE 105
Cdd:COG0388   1 TMRIALAQLNPTVGD--IEANLAKIEEL---IREAAAqgADLVVFPE------LFLTGYPPEDDDLLELAEPLDGPALAA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 106 LSCSARANHLYVVINVVEKElcAHGagsdtynpcpssgvRYFNTNVVFDRRGRIVSRYRKTHLWRHE------YVStsvl 179
Cdd:COG0388  70 LAELARELGIAVVVGLPERD--EGG--------------RLYNTALVIDPDGEILGRYRKIHLPNYGvfdekrYFT---- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 180 RSPDISIFRTDfGVTFGHFICFDMLFYDPAMKLVKEH-KItdIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLAADA-- 256
Cdd:COG0388 130 PGDELVVFDTD-GGRIGVLICYDLWFPELARALALAGaDL--LLVPSASPFGRGKDHWELLLRARAIENGCYVVAANQvg 206
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24640061 257 SNPDGRTSG-SGIYAGRgGRLVAEIFEQPTtkLLIAEV 293
Cdd:COG0388 207 GEDGLVFDGgSMIVDPD-GEVLAEAGDEEG--LLVADI 241
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
30-223 3.20e-11

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: 63.91  E-value: 3.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061    30 TAAVVEHSQPVGDsprarttsASESFQKI---IREVGD--VDIIVFPEhilnsqaTATFVPHESQNITPCYQTDYELFLI 104
Cdd:pfam00795   1 RVALVQLPQGFWD--------LEANLQKAlelIEEAARygADLIVLPE-------LFITGYPCWAHFLEAAEVGDGETLA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   105 ELSCSARANHLYVVINVVEKELcahgagsdtYNPcpssgvRYFNTNVVFDRRGRIVSRYRKTHLWRHEYVSTSVLRS--- 181
Cdd:pfam00795  66 GLAALARKNGIAIVIGLIERWL---------TGG------RLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFRERVlfe 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 24640061   182 --PDISIFRTDFGVtFGHFICFDMLFYDPAMKLVKEHkiTDIVY 223
Cdd:pfam00795 131 pgDGGTVFDTPLGK-IGAAICYEIRFPELLRALALKG--AEILI 171
amiF PRK13287
formamidase; Provisional
21-169 1.03e-04

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 44.68  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   21 LSKPEDPTYTAAVvEHSQPVGDSPRARTTSAsesfQKIIREVG-------DVDIIVFPEHILNSQATATFVPHESQnitp 93
Cdd:PRK13287   7 LNKPIEGVLVALI-QYPVPVVESRADIDKQI----EQIIKTVHktkagypGLDLIVFPEYSTQGLNTKKWTTEEFL---- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640061   94 CYQTDYELFLIELSCsaRANHLYVVINVVEkelcahgagsdtYNPCPSSGvryFNTNVVFDRRGRIVSRYRKTHLW 169
Cdd:PRK13287  78 CTVDGPEVDAFAQAC--KENKVWGVFSIME------------RNPDGNEP---YNTAIIIDDQGEIILKYRKLHPW 136
 
Name Accession Description Interval E-value
biotinidase_like cd07567
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ...
29-308 4.01e-128

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: 376.58  E-value: 4.01e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  29 YTAAVVEHSQPVGDSP--RARTTSASESFQKIIREVG--DVDIIVFPEHILNSQATATFVP-----------HESQNITP 93
Cdd:cd07567   1 YIAAVVEHHPILSPDPdaLQIMEKNLDIYEEIIKSAAkqGADIIVFPEDGLTGFIFTRFVIypfledvpdpeVNWNPCLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  94 CYQTDYELFLIELSCSARANHLYVVINVVEKELCahgagSDTYNPCPSSGVRYFNTNVVFDRRGRIVSRYRKTHLWrHEY 173
Cdd:cd07567  81 PDRFDYTEVLQRLSCAARENSIYVVANLGEKQPC-----DSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKYNLF-GEP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 174 vSTSVLRSPDISIFRTDFGVTFGHFICFDMLFYDPAMKLVKEHKITDIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLA 253
Cdd:cd07567 155 -GFDVPPEPEIVTFDTDFGVTFGIFTCFDILFKEPALELVKKLGVDDIVFPTAWFSELPFLTAVQIQQAWAYANGVNLLA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640061 254 ADASNPDGRTSGSGIYAGRGGRLVAEIFEQPTTKLLIAEVPKREHGQLAPTFTPI 308
Cdd:cd07567 234 ANYNNPSAGMTGSGIYAGRSGALVYHYDNEPGGKLLVAEVPKLPSRRPTELEAKV 288
Vanin_C pfam19018
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ...
325-511 5.90e-37

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: 134.41  E-value: 5.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   325 RDNNVDIFESELLDDDflSFERQLCHGSFCCTFSIERKVTSaaenelpssgAKSYRYRIGVYWGNeTTVIGVDRTEQATC 404
Cdd:pfam19018   5 RDPNLDNFTSVLLTGS--NGTATVCHGDLCCDFEYETSTTD----------PSSYLYRLGAFDGI-RTYEGVDNYYVQIC 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   405 ALFACTDVRLASCGYIYPENeeviNThHFTKLSISGNFPaaprGRRLIMPSSLNALFLPVSVSDYEWIESpeaaNNLDKT 484
Cdd:pfam19018  72 ALVACLNDSLSSCGKLVESA----NT-TFTSLTISGNFP----KTTYVFPSTLDSSLLPLDPSQWEYSSQ----EISEDV 138
                         170       180
                  ....*....|....*....|....*..
gi 24640061   485 ILVDLKLAKAQNDLLTFAIWANYYTDI 511
Cdd:pfam19018 139 TVTLMSLTKPQSNLLTFGIYGRNYDRD 165
nitrilase cd07197
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ...
57-297 9.46e-21

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: 91.62  E-value: 9.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  57 KIIREVGD--VDIIVFPEhilnsQATATFVPHESQNITPCYQTDYELFLIELSCSARANHLYVVINVVEKElcahgagsd 134
Cdd:cd07197  22 RLIKEAAEqgADLIVLPE-----LFLTGYSFESAKEDLDLAEELDGPTLEALAELAKELGIYIVAGIAEKD--------- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 135 tynpcpssGVRYFNTNVVFDRRGRIVSRYRKTHLWR---HEYVStsvlRSPDISIFRTDFGvTFGHFICFDMLFYDPAMK 211
Cdd:cd07197  88 --------GDKLYNTAVVIDPDGEIIGKYRKIHLFDfgeRRYFS----PGDEFPVFDTPGG-KIGLLICYDLRFPELARE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 212 LVKEH-KItdIVYPTYWFSELPFLGAVQLQeGWAFGNDVNVLAADASNPDGRTS---GSGIYAGrGGRLVAEIFEQPTtk 287
Cdd:cd07197 155 LALKGaDI--ILVPAAWPTARREHWELLLR-ARAIENGVYVVAANRVGEEGGLEfagGSMIVDP-DGEVLAEASEEEG-- 228
                       250
                ....*....|
gi 24640061 288 LLIAEVPKRE 297
Cdd:cd07197 229 ILVAELDLDE 238
Nit2 COG0388
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];
28-293 2.64e-13

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


Pssm-ID: 440157 [Multi-domain]  Cd Length: 264  Bit Score: 70.28  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  28 TYTAAVVEHSQPVGDspRARTTSASESFqkiIREVGD--VDIIVFPEhilnsqATATFVPHESQNITPCYQTDYELFLIE 105
Cdd:COG0388   1 TMRIALAQLNPTVGD--IEANLAKIEEL---IREAAAqgADLVVFPE------LFLTGYPPEDDDLLELAEPLDGPALAA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 106 LSCSARANHLYVVINVVEKElcAHGagsdtynpcpssgvRYFNTNVVFDRRGRIVSRYRKTHLWRHE------YVStsvl 179
Cdd:COG0388  70 LAELARELGIAVVVGLPERD--EGG--------------RLYNTALVIDPDGEILGRYRKIHLPNYGvfdekrYFT---- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 180 RSPDISIFRTDfGVTFGHFICFDMLFYDPAMKLVKEH-KItdIVYPTYWFSELPFLGAVQLQEGWAFGNDVNVLAADA-- 256
Cdd:COG0388 130 PGDELVVFDTD-GGRIGVLICYDLWFPELARALALAGaDL--LLVPSASPFGRGKDHWELLLRARAIENGCYVVAANQvg 206
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 24640061 257 SNPDGRTSG-SGIYAGRgGRLVAEIFEQPTtkLLIAEV 293
Cdd:COG0388 207 GEDGLVFDGgSMIVDPD-GEVLAEAGDEEG--LLVADI 241
CN_hydrolase pfam00795
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ...
30-223 3.20e-11

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: 63.91  E-value: 3.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061    30 TAAVVEHSQPVGDsprarttsASESFQKI---IREVGD--VDIIVFPEhilnsqaTATFVPHESQNITPCYQTDYELFLI 104
Cdd:pfam00795   1 RVALVQLPQGFWD--------LEANLQKAlelIEEAARygADLIVLPE-------LFITGYPCWAHFLEAAEVGDGETLA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   105 ELSCSARANHLYVVINVVEKELcahgagsdtYNPcpssgvRYFNTNVVFDRRGRIVSRYRKTHLWRHEYVSTSVLRS--- 181
Cdd:pfam00795  66 GLAALARKNGIAIVIGLIERWL---------TGG------RLYNTAVLLDPDGKLVGKYRKLHLFPEPRPPGFRERVlfe 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 24640061   182 --PDISIFRTDFGVtFGHFICFDMLFYDPAMKLVKEHkiTDIVY 223
Cdd:pfam00795 131 pgDGGTVFDTPLGK-IGAAICYEIRFPELLRALALKG--AEILI 171
nitrilase_3 cd07581
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
57-229 4.22e-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: 143605  Cd Length: 255  Bit Score: 63.36  E-value: 4.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  57 KIIREVGD--VDIIVFPEhilnsqATATFVPHESQNITPCYQTDYELFLIELSCSARANHLYVVINVVEkelcahgagsd 134
Cdd:cd07581  21 RLLAEAAAagADLVVFPE------YTMARFGDGLDDYARVAEPLDGPFVSALARLARELGITVVAGMFE----------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 135 tynpcPSSGVRYFNTNVVFDRRGRIVSRYRKTHL-----WRhEyvSTSVLRSPDIS-IFRTDFGVTFGHFICFDMLFYDP 208
Cdd:cd07581  84 -----PAGDGRVYNTLVVVGPDGEIIAVYRKIHLydafgFR-E--SDTVAPGDELPpVVFVVGGVKVGLATCYDLRFPEL 155
                       170       180
                ....*....|....*....|..
gi 24640061 209 AMKLVKE-HKItdIVYPTYWFS 229
Cdd:cd07581 156 ARALALAgADV--IVVPAAWVA 175
nitrilase_6 cd07584
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
56-205 1.09e-09

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


Pssm-ID: 143608  Cd Length: 258  Bit Score: 59.30  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  56 QKIIREVGD--VDIIVFPE--------HILNSQATATFVPHESqnitPCYQTdyelflieLSCSARANHLYVVINVVEKe 125
Cdd:cd07584  22 AELCKEAAAegADLICFPElattgyrpDLLGPKLWELSEPIDG----PTVRL--------FSELAKELGVYIVCGFVEK- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 126 lcahgaGSDTYNPcpssgvryFNTNVVFDRRGRIVSRYRKTHLWRHEYVSTSvlRSPDISIFRTDFGvTFGHFICFDMLF 205
Cdd:cd07584  89 ------GGVPGKV--------YNSAVVIDPEGESLGVYRKIHLWGLEKQYFR--EGEQYPVFDTPFG-KIGVMICYDMGF 151
nitrilase_5 cd07583
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
56-215 1.65e-09

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


Pssm-ID: 143607  Cd Length: 253  Bit Score: 58.70  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  56 QKIIREV--GDVDIIVFPE-----HILNSQATATfVPHESQNITpcyqtdyelFLIELscsARANHLYVVI-NVVEKElc 127
Cdd:cd07583  22 ESLIEEAaaAGADLIVLPEmwntgYFLDDLYELA-DEDGGETVS---------FLSEL---AKKHGVNIVAgSVAEKE-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 128 ahgagsdtynpcpssGVRYFNTNVVFDRRGRIVSRYRKTHLWR----HEYVStsvlRSPDISIFRTDfGVTFGHFICFDM 203
Cdd:cd07583  87 ---------------GGKLYNTAYVIDPDGELIATYRKIHLFGlmgeDKYLT----AGDELEVFELD-GGKVGLFICYDL 146
                       170
                ....*....|..
gi 24640061 204 LFYDPAMKLVKE 215
Cdd:cd07583 147 RFPELFRKLALE 158
nit cd07572
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ...
102-214 2.30e-08

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: 55.51  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 102 FLIELSCSARANHLYVVinvvekelcahgAGSdTYNPCPSSGvRYFNTNVVFDRRGRIVSRYRKTHL----------WRh 171
Cdd:cd07572  63 TLQALSELAKEHGIWLV------------GGS-IPERDDDDG-KVYNTSLVFDPDGELVARYRKIHLfdvdvpggisYR- 127
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24640061 172 EyvSTSVLRSPDISIFRTDFGvTFGHFICFDMLFYDPAMKLVK 214
Cdd:cd07572 128 E--SDTLTPGDEVVVVDTPFG-KIGLGICYDLRFPELARALAR 167
Lnt COG0815
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis];
20-205 6.56e-06

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


Pssm-ID: 440577 [Multi-domain]  Cd Length: 472  Bit Score: 48.69  E-value: 6.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  20 QLSKPEDPTYTAAVVehsQP-VGDSPRARTTSASESFQKIIREV-----GDVDIIVFPEhilnsqaTATfvphesqnitP 93
Cdd:COG0815 186 PWTEPAGEPLRVALV---QGnIPQDLKWDPEQRREILDRYLDLTreladDGPDLVVWPE-------TAL----------P 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  94 CYQTDYELFLIELSCSARANHLYVVInvvekelcahgaGSDTYNPcpsSGVRYFNTNVVFDRRGRIVSRYRKTHLwr-hE 172
Cdd:COG0815 246 FLLDEDPDALARLAAAAREAGAPLLT------------GAPRRDG---GGGRYYNSALLLDPDGGILGRYDKHHLvpfgE 310
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640061 173 YV-STSVLR--SPDISIFRTDF------------GVTFGHFICFDMLF 205
Cdd:COG0815 311 YVpLRDLLRplIPFLDLPLGDFspgtgppvldlgGVRVGPLICYESIF 358
R-amidase_like cd07576
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ...
145-205 1.56e-05

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: 46.80  E-value: 1.56e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640061 145 RYFNTNVVFDRRGRIVSRYRKTHLWrHEYVSTSVLRSPDISIFRTDfGVTFGHFICFDMLF 205
Cdd:cd07576  89 AVYNAAVLIDEDGTVLANYRKTHLF-GDSERAAFTPGDRFPVVELR-GLRVGLLICYDVEF 147
nitrilase_2 cd07580
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
139-258 2.11e-05

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


Pssm-ID: 143604  Cd Length: 268  Bit Score: 46.19  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 139 CPSSGVRYFNTNVVFDRRGRIvSRYRKTHLW--RHEYVSTSVLRSPdisIFRTDFGvTFGHFICFDMLFYDPAMKLVKEH 216
Cdd:cd07580  86 AERDGDRLYNSAVLVGPDGVI-GTYRKAHLWneEKLLFEPGDLGLP---VFDTPFG-RIGVAICYDGWFPETFRLLALQG 160
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 24640061 217 kiTDIV-YPTYWfselpFLGAVQLQEGWAFGNdVNVLAADASN 258
Cdd:cd07580 161 --ADIVcVPTNW-----VPMPRPPEGGPPMAN-ILAMAAAHSN 195
DCase cd07569
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ...
65-202 2.12e-05

N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. 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 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers.


Pssm-ID: 143593  Cd Length: 302  Bit Score: 46.53  E-value: 2.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  65 VDIIVFPE----------HILNSQATATFVPHESQNitPCYQTdyeLFlielscsARANHLYVVINVVEKELCAHGAGSd 134
Cdd:cd07569  39 AQLVVFPElalttffprwYFPDEAELDSFFETEMPN--PETQP---LF-------DRAKELGIGFYLGYAELTEDGGVK- 105
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24640061 135 tynpcpssgvRYFNTNVVFDRRGRIVSRYRKTHL--------WR-HEYVSTSVLRSPDIS--IFRTdFGVTFGHFICFD 202
Cdd:cd07569 106 ----------RRFNTSILVDKSGKIVGKYRKVHLpghkepepYRpFQHLEKRYFEPGDLGfpVFRV-PGGIMGMCICND 173
ALP_N-acyl_transferase cd07571
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ...
64-215 3.10e-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: 45.67  E-value: 3.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  64 DVDIIVFPEhilnsqaTATfvphesqnitPCYQTDYELFLIELSCSARANHLYVVInvvekelcahgaGSDTYNPcpsSG 143
Cdd:cd07571  39 KPDLVVWPE-------TAL----------PFDLQRDPDALARLARAARAVGAPLLT------------GAPRREP---GG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 144 VRYFNTNVVFDRRGRIVSRYRKTHL------------WRHEYVSTSVLRS-----PDISIFRTDFGVTFGHFICFDMLFY 206
Cdd:cd07571  87 GRYYNSALLLDPGGGILGRYDKHHLvpfgeyvplrdlLRFLGLLFDLPMGdfspgTGPQPLLLGGGVRVGPLICYESIFP 166

                ....*....
gi 24640061 207 DPAMKLVKE 215
Cdd:cd07571 167 ELVRDAVRQ 175
amiF PRK13287
formamidase; Provisional
21-169 1.03e-04

formamidase; Provisional


Pssm-ID: 183950  Cd Length: 333  Bit Score: 44.68  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   21 LSKPEDPTYTAAVvEHSQPVGDSPRARTTSAsesfQKIIREVG-------DVDIIVFPEHILNSQATATFVPHESQnitp 93
Cdd:PRK13287   7 LNKPIEGVLVALI-QYPVPVVESRADIDKQI----EQIIKTVHktkagypGLDLIVFPEYSTQGLNTKKWTTEEFL---- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640061   94 CYQTDYELFLIELSCsaRANHLYVVINVVEkelcahgagsdtYNPCPSSGvryFNTNVVFDRRGRIVSRYRKTHLW 169
Cdd:PRK13287  78 CTVDGPEVDAFAQAC--KENKVWGVFSIME------------RNPDGNEP---YNTAIIIDDQGEIILKYRKLHPW 136
nitrilase_7 cd07585
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ...
31-202 4.43e-04

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


Pssm-ID: 143609  Cd Length: 261  Bit Score: 42.30  E-value: 4.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  31 AAVVEHSQPVGDSprARTTSASESFQKIIREVGdVDIIVFPEHILNSQATATFVPHESQNIT-PCYQtdyelFLIELscs 109
Cdd:cd07585   2 IALVQFEARVGDK--ARNLAVIARWTRKAAAQG-AELVCFPEMCITGYTHVRALSREAEVPDgPSTQ-----ALSDL--- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 110 ARANHLYVVINVVEKelcahgagsdtynpcpsSGVRYFNTNVVFDRRGRiVSRYRKTHLWRHEyvsTSVLRSPD-ISIFR 188
Cdd:cd07585  71 ARRYGLTILAGLIEK-----------------AGDRPYNTYLVCLPDGL-VHRYRKLHLFRRE---HPYIAAGDeYPVFA 129
                       170
                ....*....|....
gi 24640061 189 TDfGVTFGHFICFD 202
Cdd:cd07585 130 TP-GVRFGILICYD 142
Ph0642_like cd07577
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ...
57-205 5.30e-04

Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.


Pssm-ID: 143601  Cd Length: 259  Bit Score: 41.90  E-value: 5.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061  57 KIIREVgDVDIIVFPEhILNS-------QATATFVphESQNITPCYQtdyelFLIELscsARANHLYVVINVVEKelcah 129
Cdd:cd07577  23 SLIKGV-EADLIVLPE-LFNTgyaftskEEVASLA--ESIPDGPTTR-----FLQEL---ARETGAYIVAGLPER----- 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24640061 130 gagsdtynpcpsSGVRYFNTNVVFDRRGRIvSRYRKTHLWRHEyvstSVLRSPDISIF--RTDFGVTFGHFICFDMLF 205
Cdd:cd07577  86 ------------DGDKFYNSAVVVGPEGYI-GIYRKTHLFYEE----KLFFEPGDTGFrvFDIGDIRIGVMICFDWYF 146
ML_beta-AS_like cd07568
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ...
110-212 6.05e-04

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


Pssm-ID: 143592  Cd Length: 287  Bit Score: 42.10  E-value: 6.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061 110 ARANHLYVVINVVEKElcahGAGSdtynpcpssgvrYFNTNVVFDRRGRIVSRYRKTHL------WRHEYVSTSVLRSPd 183
Cdd:cd07568  86 AKEYNMVLILPIYEKE----QGGT------------LYNTAAVIDADGTYLGKYRKNHIphvggfWEKFYFRPGNLGYP- 148
                        90       100
                ....*....|....*....|....*....
gi 24640061 184 isIFRTDFGvTFGHFICFDMLFYDPAMKL 212
Cdd:cd07568 149 --VFDTAFG-KIGVYICYDRHFPEGWRAL 174
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
63-168 2.74e-03

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 40.25  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640061   63 GDVDIIVFPEhilnsqaTAtfvphesqnITPCYQTDYELFLIELSCSARANHLYVVINVVEKELcahgagsdtynpcPSS 142
Cdd:PRK00302 256 GPADLIIWPE-------TA---------IPFLLEDLPQAFLKALDDLAREKGSALITGAPRAEN-------------KQG 306
                         90       100
                 ....*....|....*....|....*.
gi 24640061  143 GVRYFNTNVVFDrRGRIVSRYRKTHL 168
Cdd:PRK00302 307 RYDYYNSIYVLG-PYGILNRYDKHHL 331
 
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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