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Conserved domains on  [gi|499411823|ref|WP_011099290|]
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hypothetical protein [Clostridium tetani]

Protein Classification

C45 family peptidase( domain architecture ID 10506331)

C45 family peptidase similar to Aspergillus nidulans acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase which converts isopenicillin N to penicillin G, and Drosophila pigment protein tan which converts N-beta-alanyl dopamine to dopamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
102-321 2.18e-65

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


:

Pssm-ID: 397472  Cd Length: 223  Bit Score: 206.03  E-value: 2.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  102 RRENGSFIIGHNEDdeYRGNPSYMTTYIKDNE-GWFTTYDYFNMPFGNAFSYNSSGIIKTINYCHSEEVNLEGIPRYFIQ 180
Cdd:pfam03417   1 VNGKNGRLLGRNED--YDPETYSHRYLLTAPEdPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLRGDGFPRHFIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  181 RHITE-ATSIEDFIKRCNIEDRASGFHAIALDANKNIA-VSVEVTKDDISVKEIKDYYAHTNHYVHEKFKNKKIQQGSTT 258
Cdd:pfam03417  79 RLLLEtCSSVEEAVKLLKEIPRASSFNFILLDAAGNLAvVEVEPGSKDISVREANEYLAHTNHFVHESLTAENQNITDSS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411823  259 LFRLEKVYDLLKDKISTKgenIEIEDFNDILNY-----RGTSYEDSILALKSEPNFTCSRIVFDSTIK 321
Cdd:pfam03417 159 ISRLERIQFLLSQKESPK---DAFELLNDREDGpysklRYKSWEGTLHTALYDPADRKATLCLGNPRN 223
 
Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
102-321 2.18e-65

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


Pssm-ID: 397472  Cd Length: 223  Bit Score: 206.03  E-value: 2.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  102 RRENGSFIIGHNEDdeYRGNPSYMTTYIKDNE-GWFTTYDYFNMPFGNAFSYNSSGIIKTINYCHSEEVNLEGIPRYFIQ 180
Cdd:pfam03417   1 VNGKNGRLLGRNED--YDPETYSHRYLLTAPEdPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLRGDGFPRHFIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  181 RHITE-ATSIEDFIKRCNIEDRASGFHAIALDANKNIA-VSVEVTKDDISVKEIKDYYAHTNHYVHEKFKNKKIQQGSTT 258
Cdd:pfam03417  79 RLLLEtCSSVEEAVKLLKEIPRASSFNFILLDAAGNLAvVEVEPGSKDISVREANEYLAHTNHFVHESLTAENQNITDSS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411823  259 LFRLEKVYDLLKDKISTKgenIEIEDFNDILNY-----RGTSYEDSILALKSEPNFTCSRIVFDSTIK 321
Cdd:pfam03417 159 ISRLERIQFLLSQKESPK---DAFELLNDREDGpysklRYKSWEGTLHTALYDPADRKATLCLGNPRN 223
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
13-276 6.60e-39

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 140.12  E-value: 6.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  13 SPYENGIITGKEM-SSFIKEYGEKFKHL--LDDEDIMKKLDNISKKLEERFPTYLKEVYGRAKGAGIN-ERLHLLLMCAE 88
Cdd:NF040521   3 SPYEIGRQLGELLkELIRDLYLALLRAWglVSWRELRDFAKEFLAALEAFAPELWEELEGIADGLGLPfEDVLALNARTE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  89 ILGEGVGCTSIIRRRENGSFIIGHNED--DEYRGNpSYMTTYIKDNEGWFTTYDYFNMPFGNAFSYNSSGIIKTINYCHS 166
Cdd:NF040521  83 ILAAPDGCSTFAVLGEDGEPILARNYDwhPELYDG-CLLLTIRPDGGPRYASIGYAGLLPGRTDGMNEAGLAVTLNFLDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823 167 EEVNLEGIPRYFIQRHITE-ATSIEDFIKRcnIED--RASGFHAIALDANKNiAVSVEVTKDDISVKEIKD-YYAHTNHY 242
Cdd:NF040521 162 RKLPGVGVPVHLLARAILEnCKTVDEAIAL--LKEipRASSFNLTLADASGR-AASVEASPDRVVVVRPEDgLLVHTNHF 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 499411823 243 VHEKFKNKKIQQGSTTLFRLEKVYDLLKDKISTK 276
Cdd:NF040521 239 LSPELEEENRIATPSSRERYERLEELLKGKLDAE 272
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
4-251 5.29e-20

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 87.31  E-value: 5.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823   4 KTRFLRVNKSPYENGIITGKEMSSFIKEYGEKFKHLLDDEDIMKKLdniskkLEERFPTYLKEVYGRAKGAGINERlHLL 83
Cdd:COG4927    3 KMRFLRLRGSHYEIGLQLGKLLKELIIAYLPRGKEKRPFLAEARAA------LRRYMPELWEELEGLADGLDVPLE-ELL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  84 LMCAEILGEGVGCTSIIRRrENGSFIIGHNED---DEYRGnpSYMTTYIKDNegwfttydyfnmpfGNAFSYNSSGIIK- 159
Cdd:COG4927   76 LLNGGYYLPLSGCSQFAVA-PEGEPLLARNYDfhpDLYEG--RLLLTVQPDG--------------GYAFIGVTDGLIGr 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823 160 -----------TINYCHSEEVnLEGIPRYFIQRHITE-ATSIE---DFIKRcniEDRASGFHAIALDANKNIAVsVEVTK 224
Cdd:COG4927  139 ldgmnekglavGLNFVGRKVA-GPGFPIPLLIRYILEtCSTVDeaiALLKE---IPHASSYNLTLADASGNAAV-VEVSP 213
                        250       260
                 ....*....|....*....|....*..
gi 499411823 225 DDISVKEIKDYYAHTNHYVHEKFKNKK 251
Cdd:COG4927  214 RGVEVREPNGFLVCTNHFQSLEMAEEN 240
 
Name Accession Description Interval E-value
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
102-321 2.18e-65

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


Pssm-ID: 397472  Cd Length: 223  Bit Score: 206.03  E-value: 2.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  102 RRENGSFIIGHNEDdeYRGNPSYMTTYIKDNE-GWFTTYDYFNMPFGNAFSYNSSGIIKTINYCHSEEVNLEGIPRYFIQ 180
Cdd:pfam03417   1 VNGKNGRLLGRNED--YDPETYSHRYLLTAPEdPGFATIGYAGRLPGRTDGINEKGLAMGINFVHLRKLRGDGFPRHFIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  181 RHITE-ATSIEDFIKRCNIEDRASGFHAIALDANKNIA-VSVEVTKDDISVKEIKDYYAHTNHYVHEKFKNKKIQQGSTT 258
Cdd:pfam03417  79 RLLLEtCSSVEEAVKLLKEIPRASSFNFILLDAAGNLAvVEVEPGSKDISVREANEYLAHTNHFVHESLTAENQNITDSS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499411823  259 LFRLEKVYDLLKDKISTKgenIEIEDFNDILNY-----RGTSYEDSILALKSEPNFTCSRIVFDSTIK 321
Cdd:pfam03417 159 ISRLERIQFLLSQKESPK---DAFELLNDREDGpysklRYKSWEGTLHTALYDPADRKATLCLGNPRN 223
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
13-276 6.60e-39

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 140.12  E-value: 6.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  13 SPYENGIITGKEM-SSFIKEYGEKFKHL--LDDEDIMKKLDNISKKLEERFPTYLKEVYGRAKGAGIN-ERLHLLLMCAE 88
Cdd:NF040521   3 SPYEIGRQLGELLkELIRDLYLALLRAWglVSWRELRDFAKEFLAALEAFAPELWEELEGIADGLGLPfEDVLALNARTE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  89 ILGEGVGCTSIIRRRENGSFIIGHNED--DEYRGNpSYMTTYIKDNEGWFTTYDYFNMPFGNAFSYNSSGIIKTINYCHS 166
Cdd:NF040521  83 ILAAPDGCSTFAVLGEDGEPILARNYDwhPELYDG-CLLLTIRPDGGPRYASIGYAGLLPGRTDGMNEAGLAVTLNFLDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823 167 EEVNLEGIPRYFIQRHITE-ATSIEDFIKRcnIED--RASGFHAIALDANKNiAVSVEVTKDDISVKEIKD-YYAHTNHY 242
Cdd:NF040521 162 RKLPGVGVPVHLLARAILEnCKTVDEAIAL--LKEipRASSFNLTLADASGR-AASVEASPDRVVVVRPEDgLLVHTNHF 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 499411823 243 VHEKFKNKKIQQGSTTLFRLEKVYDLLKDKISTK 276
Cdd:NF040521 239 LSPELEEENRIATPSSRERYERLEELLKGKLDAE 272
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
4-251 5.29e-20

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 87.31  E-value: 5.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823   4 KTRFLRVNKSPYENGIITGKEMSSFIKEYGEKFKHLLDDEDIMKKLdniskkLEERFPTYLKEVYGRAKGAGINERlHLL 83
Cdd:COG4927    3 KMRFLRLRGSHYEIGLQLGKLLKELIIAYLPRGKEKRPFLAEARAA------LRRYMPELWEELEGLADGLDVPLE-ELL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823  84 LMCAEILGEGVGCTSIIRRrENGSFIIGHNED---DEYRGnpSYMTTYIKDNegwfttydyfnmpfGNAFSYNSSGIIK- 159
Cdd:COG4927   76 LLNGGYYLPLSGCSQFAVA-PEGEPLLARNYDfhpDLYEG--RLLLTVQPDG--------------GYAFIGVTDGLIGr 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499411823 160 -----------TINYCHSEEVnLEGIPRYFIQRHITE-ATSIE---DFIKRcniEDRASGFHAIALDANKNIAVsVEVTK 224
Cdd:COG4927  139 ldgmnekglavGLNFVGRKVA-GPGFPIPLLIRYILEtCSTVDeaiALLKE---IPHASSYNLTLADASGNAAV-VEVSP 213
                        250       260
                 ....*....|....*....|....*..
gi 499411823 225 DDISVKEIKDYYAHTNHYVHEKFKNKK 251
Cdd:COG4927  214 RGVEVREPNGFLVCTNHFQSLEMAEEN 240
 
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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