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Conserved domains on  [gi|505962498|ref|WP_015729555|]
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VOC family protein [Staphylococcus pseudintermedius]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-121 2.80e-40

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.


The actual alignment was detected with superfamily member cd08346:

Pssm-ID: 472697  Cd Length: 124  Bit Score: 135.88  E-value: 2.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   5 GHHHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDHGMVHIFYGDQQNSPGTLLTFFEIPNAGAMRKGTNMIARIGLLV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505962498  85 PNEaALDFFEARLQEKATNISR-GTYMEQPALYFDDPD 121
Cdd:cd08346   81 PKG-SLSFWAERLEKFGVPHSEvVTRFGEKYLRFEDPD 117
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 155-276 2.13e-23

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.


The actual alignment was detected with superfamily member cd08347:

Pssm-ID: 472697  Cd Length: 157  Bit Score: 93.08  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498 155 GLGPIEIHVADAQKTLDYLRDTLDFKDKAQFGEQ-SVVAIDDQGYYSDLVIIEKDGPNVRPGRGYVHHHALATENDDTLN 233
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLvRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505962498 234 QLVSLHDHLAGKHSGVIDRIWFKSLYYRQ-NKIMYEFATLAPGF 276
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREpGGVLFEIATDGPGF 124
 
Name Accession Description Interval E-value
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 5-121 2.80e-40

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: 135.88  E-value: 2.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   5 GHHHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDHGMVHIFYGDQQNSPGTLLTFFEIPNAGAMRKGTNMIARIGLLV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505962498  85 PNEaALDFFEARLQEKATNISR-GTYMEQPALYFDDPD 121
Cdd:cd08346   81 PKG-SLSFWAERLEKFGVPHSEvVTRFGEKYLRFEDPD 117
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 155-276 2.13e-23

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: 93.08  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498 155 GLGPIEIHVADAQKTLDYLRDTLDFKDKAQFGEQ-SVVAIDDQGYYSDLVIIEKDGPNVRPGRGYVHHHALATENDDTLN 233
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLvRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505962498 234 QLVSLHDHLAGKHSGVIDRIWFKSLYYRQ-NKIMYEFATLAPGF 276
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREpGGVLFEIATDGPGF 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-121 4.28e-16

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: 72.72  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   4 TGHHHISMYTKDLDQNKAFYTETLGLHLTKETvNQDDHGMVHIFYGDQQnspGTLLTFFEIPNAGAMRKGTNmIARIGLL 83
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGG-LHHLAFR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505962498  84 VPNeaaLDFFEARLQEKATNISRG---TYMEQPALYFDDPD 121
Cdd:COG0346   76 VDD---LDAAYARLRAAGVEIEGEprdRAYGYRSAYFRDPD 113
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-121 7.10e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 58.23  E-value: 7.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498    7 HHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDHGMVHIFYGDqqnsPGTLLTFFEIPNAGAMRKGTNMIArIGLLVPN 86
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLA----GGRVLELLLNETPPPAAAGFGGHH-IAFIAFS 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 505962498   87 EAALDFFEARLQEKATNISRG---TYMEQPALYFDDPD 121
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREpgrHGWGGRYSYFRDPD 115
 
Name Accession Description Interval E-value
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 5-121 2.80e-40

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: 135.88  E-value: 2.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   5 GHHHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDHGMVHIFYGDQQNSPGTLLTFFEIPNAGAMRKGTNMIARIGLLV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505962498  85 PNEaALDFFEARLQEKATNISR-GTYMEQPALYFDDPD 121
Cdd:cd08346   81 PKG-SLSFWAERLEKFGVPHSEvVTRFGEKYLRFEDPD 117
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 155-276 2.13e-23

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: 93.08  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498 155 GLGPIEIHVADAQKTLDYLRDTLDFKDKAQFGEQ-SVVAIDDQGYYSDLVIIEKDGPNVRPGRGYVHHHALATENDDTLN 233
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLvRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505962498 234 QLVSLHDHLAGKHSGVIDRIWFKSLYYRQ-NKIMYEFATLAPGF 276
Cdd:cd08347   81 AWKERLEELGFDNSGIVDRFYFESLYFREpGGVLFEIATDGPGF 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-121 4.28e-16

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: 72.72  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   4 TGHHHISMYTKDLDQNKAFYTETLGLHLTKETvNQDDHGMVHIFYGDQQnspGTLLTFFEIPNAGAMRKGTNmIARIGLL 83
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGG-LHHLAFR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505962498  84 VPNeaaLDFFEARLQEKATNISRG---TYMEQPALYFDDPD 121
Cdd:COG0346   76 VDD---LDAAYARLRAAGVEIEGEprdRAYGYRSAYFRDPD 113
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-121 2.69e-13

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 65.36  E-value: 2.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   3 ITGHHHISMYTKDLDQNKAFYTETLGLHLTKEtvnqdDHGMVHiFYGDQQNspgTLLTFFEIPNAGAmRKGTNMIARIGL 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVER-----EGGRVY-LRADGGE---HLLVLEEAPGAPP-RPGAAGLDHVAF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505962498  83 LVPNEAALDFFEARLQEKATNISRGT-YMEQPALYFDDPD 121
Cdd:COG2514   71 RVPSRADLDAALARLAAAGVPVEGAVdHGVGESLYFRDPD 110
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-121 7.10e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 58.23  E-value: 7.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498    7 HHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDHGMVHIFYGDqqnsPGTLLTFFEIPNAGAMRKGTNMIArIGLLVPN 86
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLA----GGRVLELLLNETPPPAAAGFGGHH-IAFIAFS 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 505962498   87 EAALDFFEARLQEKATNISRG---TYMEQPALYFDDPD 121
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREpgrHGWGGRYSYFRDPD 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-121 7.05e-09

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: 52.53  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   8 HISMYTKDLDQNKAFYTETLGLHLTKEtvnqdDHGMVHIFYGDqqnSPGTLLTFFEIPNAGAMRKGTnmIARIGLLVPNE 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSR-----NEGGGFAFLRL---GPGLRLALLEGPEPERPGGGG--LFHLAFEVDDV 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505962498  88 AALDFFEARLQEKATNISRG--TYMEQPALYFDDPD 121
Cdd:cd06587   71 DEVDERLREAGAEGELVAPPvdDPWGGRSFYFRDPD 106
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 8-121 2.32e-07

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC 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: 319918  Cd Length: 124  Bit Score: 48.46  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498   8 HISMYTKDLDQNKAFYTETLGLHLTKETVNQddhgmVHIFYGDQQNspgtLLTFFEIPNAGAMRKGTNMIARIGLLVPNE 87
Cdd:cd07255    5 RVTLKVADLERQSAFYQNVIGLSVLKQNASR-----AYLGVDGKQV----LLVLEAIPDAVLAPRSTTGLYHFAILLPDR 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 505962498  88 AALDFFEARLQEKATNISRGTYMEQPALYFDDPD 121
Cdd:cd07255   76 KALGRALAHLAEHGPLIGAADHGVSEAIYLSDPE 109
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-121 2.10e-05

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: 43.12  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505962498  10 SMYTKDLDQNKAFYTETLGLHLTKETVN----QDDHGMVHIFYGDQQNSPGTLLtffEIPNAGAMRKGtnmiaRIGLLVP 85
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRhaffRLGPQVLLVFDPGATSKDVRTG---EVPGHGASGHG-----HFAFAVP 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505962498  86 NEaALDFFEARLQEKATNISRGTYME--QPALYFDDPD 121
Cdd:cd08354   77 TE-ELAAWEARLEAKGVPIESYTQWPegGKSLYFRDPA 113
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 7-41 5.04e-03

vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD and similar proteins. 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: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 35.98  E-value: 5.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 505962498   7 HHISMYTKDLDQNKAFYTETLGLHLTKETVNQDDH 41
Cdd:cd08352    4 HHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERN 38
 
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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