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Conserved domains on  [gi|446767641|ref|WP_000844897|]
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MULTISPECIES: cysteine hydrolase family protein [Bacillus]

Protein Classification

cysteine hydrolase family protein( domain architecture ID 10099067)

cysteine hydrolase family protein related to isochorismatase and nicotinamidase; catalyzes the hydrolysis of a chemical bond using an active site cysteinyl residue

EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-158 1.60e-67

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


:

Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 203.21  E-value: 1.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPaEASAYASQLLQLFRKKNEPIFHIQHVAIkeDATFFLPNTEGVHIHESVRPLREESVI 83
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNE-AALENIAALIAAARAAGIPVIHVRHIDD--EGGSFAPGSEGWEIHPELAPLEGETVI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446767641  84 LKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNATIPAVYIH 158
Cdd:cd01014   78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIH 152
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-158 1.60e-67

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 203.21  E-value: 1.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPaEASAYASQLLQLFRKKNEPIFHIQHVAIkeDATFFLPNTEGVHIHESVRPLREESVI 83
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNE-AALENIAALIAAARAAGIPVIHVRHIDD--EGGSFAPGSEGWEIHPELAPLEGETVI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446767641  84 LKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNATIPAVYIH 158
Cdd:cd01014   78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIH 152
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-173 6.00e-52

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 163.92  E-value: 6.00e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQHVAIKEDATF---------FLPNTEGVHIHESV 74
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  75 RPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSfknatipa 154
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPE-------- 152

                        170
                 ....*....|....*....
gi 446767641 155 vyIHNTILASLNGVYANVM 173
Cdd:COG1335  153 --AHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-176 4.78e-35

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 120.97  E-value: 4.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641    3 TALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQHV---------AIKEDATFFLPNTEGVHIHES 73
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVpepddadfaLKDRPSPAFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   74 VRPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFknatip 153
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEA------ 154

                         170       180
                  ....*....|....*....|...
gi 446767641  154 avyiHNTILASLNGVYANVMSTE 176
Cdd:pfam00857 155 ----HDAALERLAQRGAEVTTTE 173
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
1-140 9.64e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 55.77  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   1 MKTALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPI-------------FHIQHVAIKED-------ATF 60
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPViasqdwhpanhgsFASNHGAEPGTqgeldglPQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  61 FLP-----NTEGVHIHesvrPLREESVI--LKH-------------YPNSFR-ETDLLKQLQRLAIEHVVICGMMTHMCI 119
Cdd:PRK11609  81 WWPdhcvqNSEGAALH----PLLNQKAIdaVFHkgenplidsysafFDNGHRqKTALDDWLREHGITELIVMGLATDYCV 156

                        170       180
                 ....*....|....*....|.
gi 446767641 120 DATVRAAFDFGLQCTVIHDAC 140
Cdd:PRK11609 157 KFTVLDALALGYQVNVITDGC 177
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 4-158 1.60e-67

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 203.21  E-value: 1.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPaEASAYASQLLQLFRKKNEPIFHIQHVAIkeDATFFLPNTEGVHIHESVRPLREESVI 83
Cdd:cd01014    1 ALLVIDVQNGYFDGGLPPLNNE-AALENIAALIAAARAAGIPVIHVRHIDD--EGGSFAPGSEGWEIHPELAPLEGETVI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446767641  84 LKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNATIPAVYIH 158
Cdd:cd01014   78 EKTVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVLSAEEIH 152
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 4-173 6.00e-52

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 163.92  E-value: 6.00e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQHVAIKEDATF---------FLPNTEGVHIHESV 74
Cdd:COG1335    1 ALLVIDVQNDFVPPGALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFaefdlwpphCVPGTPGAELVPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  75 RPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSfknatipa 154
Cdd:COG1335   81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPE-------- 152

                        170
                 ....*....|....*....
gi 446767641 155 vyIHNTILASLNGVYANVM 173
Cdd:COG1335  153 --AHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 4-152 5.31e-46

Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function.


Pssm-ID: 238245 [Multi-domain]  Cd Length: 161  Bit Score: 148.57  E-value: 5.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQHVAIKEDATF--------FLPNTEGVHIHESVR 75
Cdd:cd00431    1 ALLVVDMQNDFVPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPEFaellwpphCVKGTEGAELVPELA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446767641  76 PLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNATI 152
Cdd:cd00431   81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAAL 157
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 3-176 4.78e-35

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 120.97  E-value: 4.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641    3 TALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQHV---------AIKEDATFFLPNTEGVHIHES 73
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVpepddadfaLKDRPSPAFPPGTTGAELVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   74 VRPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFknatip 153
Cdd:pfam00857  81 LAPLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEA------ 154

                         170       180
                  ....*....|....*....|...
gi 446767641  154 avyiHNTILASLNGVYANVMSTE 176
Cdd:pfam00857 155 ----HDAALERLAQRGAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
2-180 8.34e-21

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 84.90  E-value: 8.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   2 KTALLLVDIQNdYFphgkMELRNPAEASAYA-----SQLLQLFRKKNEPIFHIQH--VAIKEDATFFL--------PNTE 66
Cdd:COG1535   19 RAALLIHDMQN-YF----LRPYDPDEPPIRElvaniARLRDACRAAGIPVVYTAQpgDQTPEDRGLLNdfwgpgltAGPE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  67 GVHIHESVRPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACAtkDLS 146
Cdd:COG1535   94 GQEIVDELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVA--DFS 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446767641 147 FKNatipavyiHNTILASLNGVYANVMSTEEFLA 180
Cdd:COG1535  172 REE--------HRMALEYVAGRCGVVVTTDEVLE 197
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 4-180 2.03e-16

N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, carbon dioxide and ammonia. CSHase is involved in one of the two alternative pathways for creatinine degradation to glycine in microorganisms.This CSHase-containing pathway degrades creatinine via N-methylhydantoin N-carbamoylsarcosine and sarcosine to glycine. Enzymes of this pathway are used in the diagnosis for renal disfunction, for determining creatinine levels in urine and serum.


Pssm-ID: 238497 [Multi-domain]  Cd Length: 179  Bit Score: 72.82  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPIFHIQhVAIKEDATF----------FLPNTEGVH---I 70
Cdd:cd01015    1 ALLVIDLVEGYTQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHTT-VVYDPDGADgglwarkvpaMSDLVEGSPlaaI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  71 HESVRPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKdlsfkna 150
Cdd:cd01015   80 CDELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVRECVGDR------- 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 446767641 151 tipAVYIHNTILASLNGVYANVMSTEEFLA 180
Cdd:cd01015  153 ---APAPHEANLFDIDNKYGDVVSTDDALA 179
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
1-140 9.64e-10

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 55.77  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   1 MKTALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFRKKNEPI-------------FHIQHVAIKED-------ATF 60
Cdd:PRK11609   1 MKRALLLVDLQNDFCAGGALAVPEGDSTIDVANRLIDWCQSRGIPViasqdwhpanhgsFASNHGAEPGTqgeldglPQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  61 FLP-----NTEGVHIHesvrPLREESVI--LKH-------------YPNSFR-ETDLLKQLQRLAIEHVVICGMMTHMCI 119
Cdd:PRK11609  81 WWPdhcvqNSEGAALH----PLLNQKAIdaVFHkgenplidsysafFDNGHRqKTALDDWLREHGITELIVMGLATDYCV 156

                        170       180
                 ....*....|....*....|.
gi 446767641 120 DATVRAAFDFGLQCTVIHDAC 140
Cdd:PRK11609 157 KFTVLDALALGYQVNVITDGC 177
PLN02621 PLN02621
nicotinamidase
 2-152 1.03e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 55.17  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   2 KTALLLVDIQNDYFPHGKMELRNpaeasayASQLLQLFRKKNEPIFHIQHV--------AIKE--DATFFLPNT-EGVHI 70
Cdd:PLN02621  20 QAALLVIDMQNYFSSMAEPILPA-------LLTTIDLCRRASIPVFFTRHShkspsdygMLGEwwDGDLILDGTtEAELM 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  71 HESVRPLREESVILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNA 150
Cdd:PLN02621  93 PEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELHEA 172


                 ..
gi 446767641 151 TI 152
Cdd:PLN02621 173 TL 174
PRK11440 PRK11440
putative hydrolase; Provisional
 83-180 3.48e-08

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 50.88  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  83 ILKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACATKDLSFKNATIpavyihNTIL 162
Cdd:PRK11440  99 VTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSAASAEQHQNSM------NHIF 172

                         90
                 ....*....|....*...
gi 446767641 163 ASLngvyANVMSTEEFLA 180
Cdd:PRK11440 173 PRI----ARVRSVEEILN 186
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 2-141 4.84e-08

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 50.73  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   2 KTALLLVDIQNDYFPHGKMELRNPAEASAYASQLLQLFR-------KKNEPIFHIQHVAIKEDATFFL------------ 62
Cdd:cd01011    1 TDALLVVDVQNDFCPGGALAVPGGDAIVPLINALLSLFQydlvvatQDWHPANHASFASNHPGQMPFItlppgpqvlwpd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641  63 ---PNTEGVHIHESVRPLREESVILK------------HYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAF 127
Cdd:cd01011   81 hcvQGTPGAELHPGLPVPDIDLIVRKgtnpdidsysafFDNDRRSSTGLAEYLRERGIDRVDVVGLATDYCVKATALDAL 160

                        170
                 ....*....|....
gi 446767641 128 DFGLQCTVIHDACA 141
Cdd:cd01011  161 KAGFEVRVLEDACR 174
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 4-142 4.59e-06

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 44.51  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767641   4 ALLLVDIQNDYFPHgkmeLRNPAEASAYASQLLQLFRKKNEPIFHIQHVAIKEDATfflpntegvhIHESVRPLREESVI 83
Cdd:cd01012    1 ALLLVDVQEKLAPA----IKSFDELINNTVKLAKAAKLLDVPVILTEQYPKGLGPT----------VPELREVFPDAPVI 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446767641  84 LKHYPNSFRETDLLKQLQRLAIEHVVICGMMTHMCIDATVRAAFDFGLQCTVIHDACAT 142
Cdd:cd01012   67 EKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGS 125
 
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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