NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063727367|ref|NP_001328862|]
View 

Acetamidase/Formamidase family protein [Arabidopsis thaliana]

Protein Classification

acetamidase/formamidase family protein( domain architecture ID 10503654)

acetamidase/formamidase family protein catalyzes the hydrolysis of a monocarboxylic acid amide (acetamide or formamide) to form a monocarboxylate (acetate or formate) and ammonia

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FmdA_AmdA pfam03069
Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 ...
67-401 2.63e-170

Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 and acetamide. Swiss:Q50228 forms a homotrimer suggesting all the members of this family also do.


:

Pssm-ID: 397271  Cd Length: 271  Bit Score: 478.99  E-value: 2.63e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367  67 KNLVLTTTHHLSGPIRVvdeEGvaAKAGDLLAVEICNLGPLPGDEWGFTGSFDRENGGGFLTDHFPCATKAIWYFEGIYA 146
Cdd:pfam03069   1 RDVDLTGVHYLSGPVAV---EG--AEPGDLLVVDILDIGPLPEAPWGYTGIFAKENGGGFLTDHFPEAAKAIWDFEGIYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 147 YSPQIPGVRFPGLTHPGVIGTAPSNELLRIWNDRERQLEEsgvesltlcevvhqrplaclpttkgcllgnieegtpewer 226
Cdd:pfam03069  76 TSRHIPGVRFRGLPHPGLIGTAPSAELLDSWNAREGELIA---------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 227 ianeaartipgRENGGNCDIKNLSRGSKIYLPVFVEGANLSTGDMHFSQGDGEISFCGAIEMSGFLELKCEIIRNGMQEY 306
Cdd:pfam03069 116 -----------TENGGNCDIKNLSRGSRVYFPVFVEGAGLSVGDLHFSQGDGEITFCGAIEMAGVVTLKVDVIKGGMAKY 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 307 ltpmgptPLHvNPIFEIGPVEPRFSEWLVFEGISVDESGKQHYLDATVAYKRAVLNAIDYLFKFGYSKEQVYLLLSCCPC 386
Cdd:pfam03069 185 -------GIK-NPIFLPGPVEPRYSEYLSFEGISVDESGKQHYLDATVAYRNACLRAIEYLKKFGYTGEQAYLLLSVAPV 256
                         330
                  ....*....|....*
gi 1063727367 387 EGRLSGIVDSPNAVA 401
Cdd:pfam03069 257 EGRISGIVDIPNACA 271
 
Name Accession Description Interval E-value
FmdA_AmdA pfam03069
Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 ...
67-401 2.63e-170

Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 and acetamide. Swiss:Q50228 forms a homotrimer suggesting all the members of this family also do.


Pssm-ID: 397271  Cd Length: 271  Bit Score: 478.99  E-value: 2.63e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367  67 KNLVLTTTHHLSGPIRVvdeEGvaAKAGDLLAVEICNLGPLPGDEWGFTGSFDRENGGGFLTDHFPCATKAIWYFEGIYA 146
Cdd:pfam03069   1 RDVDLTGVHYLSGPVAV---EG--AEPGDLLVVDILDIGPLPEAPWGYTGIFAKENGGGFLTDHFPEAAKAIWDFEGIYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 147 YSPQIPGVRFPGLTHPGVIGTAPSNELLRIWNDRERQLEEsgvesltlcevvhqrplaclpttkgcllgnieegtpewer 226
Cdd:pfam03069  76 TSRHIPGVRFRGLPHPGLIGTAPSAELLDSWNAREGELIA---------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 227 ianeaartipgRENGGNCDIKNLSRGSKIYLPVFVEGANLSTGDMHFSQGDGEISFCGAIEMSGFLELKCEIIRNGMQEY 306
Cdd:pfam03069 116 -----------TENGGNCDIKNLSRGSRVYFPVFVEGAGLSVGDLHFSQGDGEITFCGAIEMAGVVTLKVDVIKGGMAKY 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 307 ltpmgptPLHvNPIFEIGPVEPRFSEWLVFEGISVDESGKQHYLDATVAYKRAVLNAIDYLFKFGYSKEQVYLLLSCCPC 386
Cdd:pfam03069 185 -------GIK-NPIFLPGPVEPRYSEYLSFEGISVDESGKQHYLDATVAYRNACLRAIEYLKKFGYTGEQAYLLLSVAPV 256
                         330
                  ....*....|....*
gi 1063727367 387 EGRLSGIVDSPNAVA 401
Cdd:pfam03069 257 EGRISGIVDIPNACA 271
FmdA COG2421
Acetamidase/formamidase [Energy production and conversion];
21-414 5.04e-101

Acetamidase/formamidase [Energy production and conversion];


Pssm-ID: 441971  Cd Length: 304  Bit Score: 304.00  E-value: 5.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367  21 QDQPLHNRWHPEIPPVAEVKAGEFFRVEMIDAMGGVIKDNDSASDIKNLVLTTTHHLSGPIRVvdeEGvaAKAGDLLAVE 100
Cdd:COG2421     8 TETVHHGRFDPDLPPVLTVKPGDTVTIETLDCFGGQIKSEDDADDVRDLDFSGVHPLTGPIYV---EG--AEPGDVLAVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 101 ICNLGPLpgDEWGFTGSFdreNGGGFLTDHFPCATKAIWYFEGIYAYSPQIPGVRFPGLTHPGVIGTAPSNEllriwndr 180
Cdd:COG2421    83 ILDIEPR--RDWGVNATI---PGFGFLPDEFPEERVKIWEIDGERGTARFLPGVRIPLRPFIGTIGVAPAEE-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 181 erqleesgvesltlcevvhqrplaclpttkgcllgnieegtpewerianEAARTIPGRENGGNCDIKNLSRGSKIYLPVF 260
Cdd:COG2421   150 -------------------------------------------------GAVSSVPPGEHGGNMDIKDLTAGSTLYLPVF 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 261 VEGANLSTGDMHFSQGDGEISFCgAIEMSGFLELKCEIIRNGMQEYltpmgptplhvnPIFEigpveprFSEWLVFEGIs 340
Cdd:COG2421   181 VPGALLSLGDLHAAQGDGEVCGT-AIEVAGTVTLRVDLIKGGGLPW------------PRLE-------TDDYWITIGS- 239
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063727367 341 vdesgkqhYLDATVAYKRAVLNAIDYLFK-FGYSKEQVYLLLSCCpCEGRLSGIVDsPNAVATLAIPTAIFDQVS 414
Cdd:COG2421   240 --------GPDLDEAARNAVREMIDLLSEeFGLSEEEAYMLLSVA-GDLRISQVVD-PNKTVHAKIPKAIFDKDG 304
 
Name Accession Description Interval E-value
FmdA_AmdA pfam03069
Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 ...
67-401 2.63e-170

Acetamidase/Formamidase family; This family includes amidohydrolases of formamide EC:3.5.1.49 and acetamide. Swiss:Q50228 forms a homotrimer suggesting all the members of this family also do.


Pssm-ID: 397271  Cd Length: 271  Bit Score: 478.99  E-value: 2.63e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367  67 KNLVLTTTHHLSGPIRVvdeEGvaAKAGDLLAVEICNLGPLPGDEWGFTGSFDRENGGGFLTDHFPCATKAIWYFEGIYA 146
Cdd:pfam03069   1 RDVDLTGVHYLSGPVAV---EG--AEPGDLLVVDILDIGPLPEAPWGYTGIFAKENGGGFLTDHFPEAAKAIWDFEGIYA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 147 YSPQIPGVRFPGLTHPGVIGTAPSNELLRIWNDRERQLEEsgvesltlcevvhqrplaclpttkgcllgnieegtpewer 226
Cdd:pfam03069  76 TSRHIPGVRFRGLPHPGLIGTAPSAELLDSWNAREGELIA---------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 227 ianeaartipgRENGGNCDIKNLSRGSKIYLPVFVEGANLSTGDMHFSQGDGEISFCGAIEMSGFLELKCEIIRNGMQEY 306
Cdd:pfam03069 116 -----------TENGGNCDIKNLSRGSRVYFPVFVEGAGLSVGDLHFSQGDGEITFCGAIEMAGVVTLKVDVIKGGMAKY 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 307 ltpmgptPLHvNPIFEIGPVEPRFSEWLVFEGISVDESGKQHYLDATVAYKRAVLNAIDYLFKFGYSKEQVYLLLSCCPC 386
Cdd:pfam03069 185 -------GIK-NPIFLPGPVEPRYSEYLSFEGISVDESGKQHYLDATVAYRNACLRAIEYLKKFGYTGEQAYLLLSVAPV 256
                         330
                  ....*....|....*
gi 1063727367 387 EGRLSGIVDSPNAVA 401
Cdd:pfam03069 257 EGRISGIVDIPNACA 271
FmdA COG2421
Acetamidase/formamidase [Energy production and conversion];
21-414 5.04e-101

Acetamidase/formamidase [Energy production and conversion];


Pssm-ID: 441971  Cd Length: 304  Bit Score: 304.00  E-value: 5.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367  21 QDQPLHNRWHPEIPPVAEVKAGEFFRVEMIDAMGGVIKDNDSASDIKNLVLTTTHHLSGPIRVvdeEGvaAKAGDLLAVE 100
Cdd:COG2421     8 TETVHHGRFDPDLPPVLTVKPGDTVTIETLDCFGGQIKSEDDADDVRDLDFSGVHPLTGPIYV---EG--AEPGDVLAVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 101 ICNLGPLpgDEWGFTGSFdreNGGGFLTDHFPCATKAIWYFEGIYAYSPQIPGVRFPGLTHPGVIGTAPSNEllriwndr 180
Cdd:COG2421    83 ILDIEPR--RDWGVNATI---PGFGFLPDEFPEERVKIWEIDGERGTARFLPGVRIPLRPFIGTIGVAPAEE-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 181 erqleesgvesltlcevvhqrplaclpttkgcllgnieegtpewerianEAARTIPGRENGGNCDIKNLSRGSKIYLPVF 260
Cdd:COG2421   150 -------------------------------------------------GAVSSVPPGEHGGNMDIKDLTAGSTLYLPVF 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727367 261 VEGANLSTGDMHFSQGDGEISFCgAIEMSGFLELKCEIIRNGMQEYltpmgptplhvnPIFEigpveprFSEWLVFEGIs 340
Cdd:COG2421   181 VPGALLSLGDLHAAQGDGEVCGT-AIEVAGTVTLRVDLIKGGGLPW------------PRLE-------TDDYWITIGS- 239
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063727367 341 vdesgkqhYLDATVAYKRAVLNAIDYLFK-FGYSKEQVYLLLSCCpCEGRLSGIVDsPNAVATLAIPTAIFDQVS 414
Cdd:COG2421   240 --------GPDLDEAARNAVREMIDLLSEeFGLSEEEAYMLLSVA-GDLRISQVVD-PNKTVHAKIPKAIFDKDG 304
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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