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Conserved domains on  [gi|1934645|gb|AAB80896|]
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hypothetical protein YrdC [Bacillus subtilis subsp. subtilis str. 168]

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

 Zoom to residue level

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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 ...
 6-159 8.07e-51

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: 160.83  E-value: 8.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFDDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSlFHPKNEGFAIKEIVKPMDEEVIITK 85
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934645   86 TVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDQnDTYYDAATIH 159
Cdd:cd01014  80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDH-GGVLSAEEIH 152
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 6-159 8.07e-51

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: 160.83  E-value: 8.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFDDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSlFHPKNEGFAIKEIVKPMDEEVIITK 85
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934645   86 TVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDQnDTYYDAATIH 159
Cdd:cd01014  80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDH-GGVLSAEEIH 152
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-174 2.12e-47

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: 152.37  E-value: 2.12e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFDDK-KWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSLFH----------PKNEGFAIKEIV 74
Cdd:COG1335   1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTPGAELVPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645   75 KPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqndtyyd 154
Cdd:COG1335  81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASR----------- 149

                       170       180
                ....*....|....*....|
gi 1934645  155 AATIHNISLATLHDEFATIL 174
Cdd:COG1335 150 DPEAHEAALARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-177 1.94e-29

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 106.72  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645      6 ALIIVDVQKAF-DDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSLFHPK----------NEGFAIKEIV 74
Cdd:pfam00857   2 ALLVIDMQNDFvDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKdrpspafppgTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645     75 KPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqNDTYYD 154
Cdd:pfam00857  82 APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASL-----SPEAHD 156

                         170       180
                  ....*....|....*....|...
gi 1934645    155 AAtIHNISLAtlhdeFATILTTD 177
Cdd:pfam00857 157 AA-LERLAQR-----GAEVTTTE 173
PLN02621 PLN02621
nicotinamidase
 4-179 2.51e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 54.40  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645     4 KKALIIVDVQKAFddkkwgeRNNVKA-EENISKILELWREKGWTVIYIQHTSDKPHS------------LFHPKNEGFAI 70
Cdd:PLN02621  20 QAALLVIDMQNYF-------SSMAEPiLPALLTTIDLCRRASIPVFFTRHSHKSPSDygmlgewwdgdlILDGTTEAELM 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    71 KEIVKPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqnd 150
Cdd:PLN02621  93 PEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATA------- 165

                        170       180
                 ....*....|....*....|....*....
gi 1934645   151 tyydAATIHNISLATLHDEFATILTTDQL 179
Cdd:PLN02621 166 ----NEELHEATLKNLAYGFAYLVDCDRL 190
 
Name Accession Description Interval E-value
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 6-159 8.07e-51

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: 160.83  E-value: 8.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFDDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSlFHPKNEGFAIKEIVKPMDEEVIITK 85
Cdd:cd01014   1 ALLVIDVQNGYFDGGLPPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEGGS-FAPGSEGWEIHPELAPLEGETVIEK 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934645   86 TVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDQnDTYYDAATIH 159
Cdd:cd01014  80 TVPNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDH-GGVLSAEEIH 152
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 6-174 2.12e-47

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: 152.37  E-value: 2.12e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFDDK-KWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSLFH----------PKNEGFAIKEIV 74
Cdd:COG1335   1 ALLVIDVQNDFVPPgALAVPGADAVVANIARLLAAARAAGVPVIHTRDWHPPDGSEFAefdlwpphcvPGTPGAELVPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645   75 KPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqndtyyd 154
Cdd:COG1335  81 APLPGDPVVDKTRYSAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASR----------- 149

                       170       180
                ....*....|....*....|
gi 1934645  155 AATIHNISLATLHDEFATIL 174
Cdd:COG1335 150 DPEAHEAALARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 6-151 3.35e-38

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: 128.93  E-value: 3.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAF-DDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHS---------LFHPKNEGFAIKEIVK 75
Cdd:cd00431   1 ALLVVDMQNDFvPGGGLLLPGADELVPNINRLLAAARAAGIPVIFTRDWHPPDDPefaellwppHCVKGTEGAELVPELA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934645   76 PMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDQNDT 151
Cdd:cd00431  81 PLPDDLVIEKTRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAA 156
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 6-177 1.94e-29

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 106.72  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645      6 ALIIVDVQKAF-DDKKWGERNNVKAEENISKILELWREKGWTVIYIQHTSDKPHSLFHPK----------NEGFAIKEIV 74
Cdd:pfam00857   2 ALLVIDMQNDFvDSGGPKVEGIAAILENINRLLKAARKAGIPVIFTRQVPEPDDADFALKdrpspafppgTTGAELVPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645     75 KPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqNDTYYD 154
Cdd:pfam00857  82 APLPGDLVVDKTRFSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASL-----SPEAHD 156

                         170       180
                  ....*....|....*....|...
gi 1934645    155 AAtIHNISLAtlhdeFATILTTD 177
Cdd:pfam00857 157 AA-LERLAQR-----GAEVTTTE 173
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
6-180 1.23e-17

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


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 76.81  E-value: 1.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAF---DDKkwGERNNVKAEENISKILELWREKGWTVIYIQHT-----------SDKPHSLFHPKNEGFAIK 71
Cdd:COG1535  21 ALLIHDMQNYFlrpYDP--DEPPIRELVANIARLRDACRAAGIPVVYTAQPgdqtpedrgllNDFWGPGLTAGPEGQEIV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645   72 EIVKPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFGMRDqndt 151
Cdd:COG1535  99 DELAPAPGDTVLTKWRYSAFQRTDLEERLRELGRDQLIITGVYAHIGCLATAVDAFMRDIQPFVVADAVADFSREE---- 174

                       170       180
                ....*....|....*....|....*....
gi 1934645  152 yydaatiHNISLATLHDEFATILTTDQLI 180
Cdd:COG1535 175 -------HRMALEYVAGRCGVVVTTDEVL 196
CSHase cd01015
N-carbamoylsarcosine amidohydrolase (CSHase) hydrolyzes N-carbamoylsarcosine to sarcosine, ...
 6-139 1.24e-17

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: 76.29  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAF-DDKKWGERNNVKAEENISKILELWREKGWTVIY--IQHTSDKP-HSLFHPKNEGF----------AIK 71
Cdd:cd01015   1 ALLVIDLVEGYtQPGSYLAPGIAAALENVQRLLAAARAAGVPVIHttVVYDPDGAdGGLWARKVPAMsdlvegsplaAIC 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934645   72 EIVKPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDA 139
Cdd:cd01015  81 DELAPQEDEMVLVKKYASAFFGTSLAATLTARGVDTLIVAGCSTSGCIRATAVDAMQHGFRPIVVREC 148
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 4-142 1.05e-10

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: 58.04  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    4 KKALIIVDVQKAFDDKkwGERNNVKAEENISKILELWREKGW-TVIYIQHTSDKPHSLF---HPKN-------------- 65
Cdd:cd01011   1 TDALLVVDVQNDFCPG--GALAVPGGDAIVPLINALLSLFQYdLVVATQDWHPANHASFasnHPGQmpfitlppgpqvlw 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645   66 --------EGFAIKEIVKPMDEEVIITKTVN------SSFIG------TNLEEFLKLNEITTVVITGLTTPHCVSTTTRM 125
Cdd:cd01011  79 pdhcvqgtPGAELHPGLPVPDIDLIVRKGTNpdidsySAFFDndrrssTGLAEYLRERGIDRVDVVGLATDYCVKATALD 158

                       170
                ....*....|....*..
gi 1934645  126 SGNLGFDTYLISDATAA 142
Cdd:cd01011 159 ALKAGFEVRVLEDACRA 175
PLN02621 PLN02621
nicotinamidase
 4-179 2.51e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 54.40  E-value: 2.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645     4 KKALIIVDVQKAFddkkwgeRNNVKA-EENISKILELWREKGWTVIYIQHTSDKPHS------------LFHPKNEGFAI 70
Cdd:PLN02621  20 QAALLVIDMQNYF-------SSMAEPiLPALLTTIDLCRRASIPVFFTRHSHKSPSDygmlgewwdgdlILDGTTEAELM 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    71 KEIVKPMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAAFgmrdqnd 150
Cdd:PLN02621  93 PEIGRVTGPDEVVEKSTYSAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATA------- 165

                        170       180
                 ....*....|....*....|....*....
gi 1934645   151 tyydAATIHNISLATLHDEFATILTTDQL 179
Cdd:PLN02621 166 ----NEELHEATLKNLAYGFAYLVDCDRL 190
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 1-142 6.98e-09

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 53.15  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645     1 MEEKKALIIVDVQK---------------------------AFD----DKKWGERNNV--KAEENISKILELWREKG-WT 46
Cdd:PTZ00331   9 SSTNDALIIVDVQNdfckggslavpdaeevipvinqvrqshHFDlvvaTQDWHPPNHIsfASNHGKPKILPDGTTQGlWP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    47 VIYIQHTsdkPHSLFHPKnegfaikEIVKPMDeeVIITKTVN------SSFIG-----TNLEEFLKLNEITTVVITGLTT 115
Cdd:PTZ00331  89 PHCVQGT---KGAQLHKD-------LVVERID--IIIRKGTNrdvdsySAFDNdkgskTGLAQILKAHGVRRVFICGLAF 156

                        170       180
                 ....*....|....*....|....*..
gi 1934645   116 PHCVSTTTRMSGNLGFDTYLISDATAA 142
Cdd:PTZ00331 157 DFCVLFTALDAVKLGFKVVVLEDATRA 183
PRK11440 PRK11440
putative hydrolase; Provisional
 76-142 3.95e-04

putative hydrolase; Provisional


Pssm-ID: 183137  Cd Length: 188  Bit Score: 39.33  E-value: 3.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934645    76 PMDEEVIITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATAA 142
Cdd:PRK11440  92 KTDSDIEVTKRQWGAFYGTDLELQLRRRGIDTIVLCGISTNIGVESTARNAWELGFNLVIAEDACSA 158
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 6-180 2.79e-03

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: 36.80  E-value: 2.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645    6 ALIIVDVQKAFddkkwgeRNNVKAE----ENISKILELWREKGWTVIYIQHtsdkphslfHPKNEGFAIKEIVKPMDEEV 81
Cdd:cd01012   1 ALLLVDVQEKL-------APAIKSFdeliNNTVKLAKAAKLLDVPVILTEQ---------YPKGLGPTVPELREVFPDAP 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934645   82 IITKTVNSSFIGTNLEEFLKLNEITTVVITGLTTPHCVSTTTRMSGNLGFDTYLISDATaafGMRDQNDtyydaatiHNI 161
Cdd:cd01012  65 VIEKTSFSCWEDEAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADAC---GSRSKED--------HEL 133

                       170
                ....*....|....*....
gi 1934645  162 SLATLHDEFATILTTDQLI 180
Cdd:cd01012 134 ALARMRQAGAVLTTSESVL 152
 
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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