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Conserved domains on  [gi|446334881|ref|WP_000412736|]
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MULTISPECIES: ring-cleaving dioxygenase [Bacillus]

Protein Classification

ring-cleaving dioxygenase( domain architecture ID 10170053)

ring-cleaving dioxygenase is a vicinal oxygen chelate (VOC) family protein similar to Sphingomonas paucimobilis chlorohydroquinone/hydroquinone 1,2-dioxygenase LinE, which cleaves aromatic rings with two hydroxyl groups at para positions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-129 1.44e-65

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


:

Pssm-ID: 319934  Cd Length: 124  Bit Score: 201.75  E-value: 1.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881   7 GIHHITAIVGHPQENVDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKPGTIITFFPWAGARQGIIGDGQVGITSYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446334881  87 PKGAMKFWENRLEKFDISYTKM-TRFGEQYLEFDDPHGLHIELV 129
Cdd:cd08346   81 PKGSLSFWAERLEKFGVPHSEVvTRFGEKYLRFEDPDGTRLFLV 124
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 152-306 4.56e-64

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


:

Pssm-ID: 319935  Cd Length: 157  Bit Score: 199.01  E-value: 4.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 152 GFGGAVLLSAHPQKTAELLEHVMGLEKIGEEGEFVRFRSSA-DIGNIIDLKLS-TIGRGQMGVGTVHHIAWRASDDADQL 229
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLFAGGnGSGGVVDVLDDpDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446334881 230 DWKEHVSRFGYHVTPVQDRNYFNAIYFREHGEILFEIATDPPGFAHDESLETMGEELKLPEQYEQHRKQMEQTLLPF 306
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
 
Name Accession Description Interval E-value
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-129 1.44e-65

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 201.75  E-value: 1.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881   7 GIHHITAIVGHPQENVDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKPGTIITFFPWAGARQGIIGDGQVGITSYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446334881  87 PKGAMKFWENRLEKFDISYTKM-TRFGEQYLEFDDPHGLHIELV 129
Cdd:cd08346   81 PKGSLSFWAERLEKFGVPHSEVvTRFGEKYLRFEDPDGTRLFLV 124
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 152-306 4.56e-64

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 199.01  E-value: 4.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 152 GFGGAVLLSAHPQKTAELLEHVMGLEKIGEEGEFVRFRSSA-DIGNIIDLKLS-TIGRGQMGVGTVHHIAWRASDDADQL 229
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLFAGGnGSGGVVDVLDDpDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446334881 230 DWKEHVSRFGYHVTPVQDRNYFNAIYFREHGEILFEIATDPPGFAHDESLETMGEELKLPEQYEQHRKQMEQTLLPF 306
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-289 1.12e-24

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 96.95  E-value: 1.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 150 IKGFGGAVLLSAHPQKTAELLEHVMGLEKIGEEGEFVRFRSSADIGnIIDLKLSTIGRGQMGVGTVHHIAWRASDDADQL 229
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEH-LLVLEEAPGAPPRPGAAGLDHVAFRVPSRADLD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446334881 230 DWKEHVSRFGYHVTPVQDRNYFNAIYFREHGEILFEIATDPPGFAH--DESLETMGEELKLP 289
Cdd:COG2514   80 AALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHvgDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-134 1.73e-17

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 76.95  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881   6 MGIHHITAIVGHPQENVDFYAGVLGLRLVKQTvNFDDPGTYHLYFGNEGgkpGTIITFFPWAGArQGIIGDGQVGITSYV 85
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGA-APAPGGGGLHHLAFR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446334881  86 VPkgAMKFWENRLEKFDISYTKMTR---FGEQYLEFDDPHGLHIELVEREEG 134
Cdd:COG0346   76 VD--DLDAAYARLRAAGVEIEGEPRdraYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-128 2.60e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.60  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881    7 GIHHITAIVGHPQENVDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKpgtiITFFPWAGARQGIIGDGQVGITSYVV 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRV----LELLLNETPPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446334881   87 PKGAMKFWENRLEKFDISYTK-MTR--FGEQYLEFDDPHGLHIEL 128
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVRePGRhgWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-129 1.44e-65

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 201.75  E-value: 1.44e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881   7 GIHHITAIVGHPQENVDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKPGTIITFFPWAGARQGIIGDGQVGITSYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446334881  87 PKGAMKFWENRLEKFDISYTKM-TRFGEQYLEFDDPHGLHIELV 129
Cdd:cd08346   81 PKGSLSFWAERLEKFGVPHSEVvTRFGEKYLRFEDPDGTRLFLV 124
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 152-306 4.56e-64

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 199.01  E-value: 4.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 152 GFGGAVLLSAHPQKTAELLEHVMGLEKIGEEGEFVRFRSSA-DIGNIIDLKLS-TIGRGQMGVGTVHHIAWRASDDADQL 229
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLFAGGnGSGGVVDVLDDpDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446334881 230 DWKEHVSRFGYHVTPVQDRNYFNAIYFREHGEILFEIATDPPGFAHDESLETMGEELKLPEQYEQHRKQMEQTLLPF 306
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-289 1.12e-24

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 96.95  E-value: 1.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 150 IKGFGGAVLLSAHPQKTAELLEHVMGLEKIGEEGEFVRFRSSADIGnIIDLKLSTIGRGQMGVGTVHHIAWRASDDADQL 229
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEH-LLVLEEAPGAPPRPGAAGLDHVAFRVPSRADLD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446334881 230 DWKEHVSRFGYHVTPVQDRNYFNAIYFREHGEILFEIATDPPGFAH--DESLETMGEELKLP 289
Cdd:COG2514   80 AALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHvgDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-134 1.73e-17

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 76.95  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881   6 MGIHHITAIVGHPQENVDFYAGVLGLRLVKQTvNFDDPGTYHLYFGNEGgkpGTIITFFPWAGArQGIIGDGQVGITSYV 85
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGA-APAPGGGGLHHLAFR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446334881  86 VPkgAMKFWENRLEKFDISYTKMTR---FGEQYLEFDDPHGLHIELVEREEG 134
Cdd:COG0346   76 VD--DLDAAYARLRAAGVEIEGEPRdraYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-128 2.60e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.60  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881    7 GIHHITAIVGHPQENVDFYAGVLGLRLVKQTVNFDDPGTYHLYFGNEGGKpgtiITFFPWAGARQGIIGDGQVGITSYVV 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRV----LELLLNETPPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446334881   87 PKGAMKFWENRLEKFDISYTK-MTR--FGEQYLEFDDPHGLHIEL 128
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVRePGRhgWGGRYSYFRDPDGNLIEL 121
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-131 1.50e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319942  Cd Length: 122  Bit Score: 37.73  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881  24 FYAGVLGLRLVKQT---VNFD-DPGTYHLYFGNEGGKPGTIITffpwaGARQGIIGDGQVgitSYVVPKGAMKFWENRLE 99
Cdd:cd08354   17 FYEDVLGLKPMLRSgrhAFFRlGPQVLLVFDPGATSKDVRTGE-----VPGHGASGHGHF---AFAVPTEELAAWEARLE 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446334881 100 KFDISYTKMTRFGE--QYLEFDDPHGLHIELVER 131
Cdd:cd08354   89 AKGVPIESYTQWPEggKSLYFRDPAGNLVELASA 122
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 157-266 3.51e-03

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 36.73  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334881 157 VLLSAHPQKTAELLEHVMGLEKIG--EEGEFVRFRSSADIgnIIDLkLSTIGRGQMGVGTVHHIAWRASDDADQLDWKEH 234
Cdd:cd06587    3 ALRVPDLDASVAFYEEVLGFEVVSrnEGGGFAFLRLGPGL--RLAL-LEGPEPERPGGGGLFHLAFEVDDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446334881 235 VSRFGY-HVTPVQDRNYFNAIYFREHGEILFEI 266
Cdd:cd06587   80 AGAEGElVAPPVDDPWGGRSFYFRDPDGNLIEF 112
 
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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