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Conserved domains on  [gi|636787711|ref|WP_024323880|]
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glyoxalase superfamily protein [Rhizobium ruizarguesonis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyoxalase_7 super family cl44988
Glyoxalase superfamily protein;
50-178 1.14e-56

Glyoxalase superfamily protein;


The actual alignment was detected with superfamily member pfam19581:

Pssm-ID: 437413  Cd Length: 133  Bit Score: 174.40  E-value: 1.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711   50 IDAAGASPSAIGIEPPMPIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDASPGAKAFV 129
Cdd:pfam19581   1 SDAETQTFGEIGFEQIFPILRIFDEAKAKAFYGDFLGFEADWEHHFDDHFPAYIQVSRAGLGLHLSEHHGDACPGSNIFV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 636787711  130 RVANIRAYHAELSAKDYRYMKPGVEEAPWGLE-MTVTDPFSNRIAFCEQK 178
Cdd:pfam19581  81 TMRGIDAFHKEITGKKYKFLNPGIEELFWGADcMEVIDPFGNHIRFCEQK 130
Glyoxalase_8 super family cl45445
Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This ...
 6-61 5.63e-14

Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 80 amino acids in length. This domain is part of the Glyoxalase superfamily.


The actual alignment was detected with superfamily member pfam20066:

Pssm-ID: 437898  Cd Length: 143  Bit Score: 65.22  E-value: 5.63e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636787711    6 DAKLMAKTLRQALADRDISLTHSETLEIVARQFGLDQWNILSAKIDAAGASPSAIG 61
Cdd:pfam20066  10 ELKAQAKRLRAALAAAGTPISHSQALELVAHQHGFRDWNTLHAAAGNRPPPPLQVG 65
 
Name Accession Description Interval E-value
Glyoxalase_7 pfam19581
Glyoxalase superfamily protein;
50-178 1.14e-56

Glyoxalase superfamily protein;


Pssm-ID: 437413  Cd Length: 133  Bit Score: 174.40  E-value: 1.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711   50 IDAAGASPSAIGIEPPMPIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDASPGAKAFV 129
Cdd:pfam19581   1 SDAETQTFGEIGFEQIFPILRIFDEAKAKAFYGDFLGFEADWEHHFDDHFPAYIQVSRAGLGLHLSEHHGDACPGSNIFV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 636787711  130 RVANIRAYHAELSAKDYRYMKPGVEEAPWGLE-MTVTDPFSNRIAFCEQK 178
Cdd:pfam19581  81 TMRGIDAFHKEITGKKYKFLNPGIEELFWGADcMEVIDPFGNHIRFCEQK 130
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 67-176 1.34e-31

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA 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. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 110.01  E-value: 1.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  67 PIFRIFSVEKAMEFYCRFLGFHLDWEHRfgenFPLYCQVSRDGMALHLSEHSGD--ASPGAKAFVRVANIRAYHAELSAK 144
Cdd:cd08349    2 PILPVRDIDKTLAFYVDVLGFEVDYERP----PPGYAILSRGGVELHLFEHPGLdpAGSGVAAYIRVEDIDALHAELKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 636787711 145 DYRYMK----PGVEEAPWGL-EMTVTDPFSNRIAFCE 176
Cdd:cd08349   78 GLPLFGipriTPIEDKPWGMrEFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
67-176 4.33e-18

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 75.28  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  67 PIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDaSPGAKA-----FVRVANIRAYHAEL 141
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPPD-SPAAEGngvslSLYVDDVDALFARL 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 636787711 142 SAKDYRYMKPgVEEAPWG-LEMTVTDPFSNRIAFCE 176
Cdd:COG2764   83 VAAGATVVMP-LQDTFWGdRFGMVRDPFGVLWMINT 117
Glyoxalase_8 pfam20066
Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This ...
 6-61 5.63e-14

Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 80 amino acids in length. This domain is part of the Glyoxalase superfamily.


Pssm-ID: 437898  Cd Length: 143  Bit Score: 65.22  E-value: 5.63e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636787711    6 DAKLMAKTLRQALADRDISLTHSETLEIVARQFGLDQWNILSAKIDAAGASPSAIG 61
Cdd:pfam20066  10 ELKAQAKRLRAALAAAGTPISHSQALELVAHQHGFRDWNTLHAAAGNRPPPPLQVG 65
 
Name Accession Description Interval E-value
Glyoxalase_7 pfam19581
Glyoxalase superfamily protein;
50-178 1.14e-56

Glyoxalase superfamily protein;


Pssm-ID: 437413  Cd Length: 133  Bit Score: 174.40  E-value: 1.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711   50 IDAAGASPSAIGIEPPMPIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDASPGAKAFV 129
Cdd:pfam19581   1 SDAETQTFGEIGFEQIFPILRIFDEAKAKAFYGDFLGFEADWEHHFDDHFPAYIQVSRAGLGLHLSEHHGDACPGSNIFV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 636787711  130 RVANIRAYHAELSAKDYRYMKPGVEEAPWGLE-MTVTDPFSNRIAFCEQK 178
Cdd:pfam19581  81 TMRGIDAFHKEITGKKYKFLNPGIEELFWGADcMEVIDPFGNHIRFCEQK 130
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 67-176 1.34e-31

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA 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. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 110.01  E-value: 1.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  67 PIFRIFSVEKAMEFYCRFLGFHLDWEHRfgenFPLYCQVSRDGMALHLSEHSGD--ASPGAKAFVRVANIRAYHAELSAK 144
Cdd:cd08349    2 PILPVRDIDKTLAFYVDVLGFEVDYERP----PPGYAILSRGGVELHLFEHPGLdpAGSGVAAYIRVEDIDALHAELKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 636787711 145 DYRYMK----PGVEEAPWGL-EMTVTDPFSNRIAFCE 176
Cdd:cd08349   78 GLPLFGipriTPIEDKPWGMrEFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
67-176 4.33e-18

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 75.28  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  67 PIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDaSPGAKA-----FVRVANIRAYHAEL 141
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPPD-SPAAEGngvslSLYVDDVDALFARL 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 636787711 142 SAKDYRYMKPgVEEAPWG-LEMTVTDPFSNRIAFCE 176
Cdd:COG2764   83 VAAGATVVMP-LQDTFWGdRFGMVRDPFGVLWMINT 117
Glyoxalase_8 pfam20066
Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This ...
 6-61 5.63e-14

Glyoxalase superfamily protein; This presumed domain is functionally uncharacterized. This domain family is found in bacteria, and is approximately 80 amino acids in length. This domain is part of the Glyoxalase superfamily.


Pssm-ID: 437898  Cd Length: 143  Bit Score: 65.22  E-value: 5.63e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 636787711    6 DAKLMAKTLRQALADRDISLTHSETLEIVARQFGLDQWNILSAKIDAAGASPSAIG 61
Cdd:pfam20066  10 ELKAQAKRLRAALAAAGTPISHSQALELVAHQHGFRDWNTLHAAAGNRPPPPLQVG 65
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 74-178 1.49e-10

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 55.80  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHLDWEHRFGENfplYCQVSRD-GMALHLSEHSGD-ASPGAKAFVRVANIRAYHAELSAKDYRYMKP 151
Cdd:COG3324   15 LERAKAFYEEVFGWTFEDDAGPGGD---YAEFDTDgGQVGGLMPGAEEpGGPGWLLYFAVDDLDAAVARVEAAGGTVLRP 91

                         90       100
                 ....*....|....*....|....*..
gi 636787711 152 GVEEAPWGLEMTVTDPFSNRIAFCEQK 178
Cdd:COG3324   92 PTDIPPWGRFAVFRDPEGNRFGLWQPA 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 74-176 1.39e-07

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: 48.06  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSR-DGMALHLSEHSGDASPGAK------AFvRVANIRAYHAELSAKDY 146
Cdd:COG0346   13 LEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLgDGTELELFEAPGAAPAPGGgglhhlAF-RVDDLDAAYARLRAAGV 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 636787711 147 RYMKpGVEEAPWGLEMT-VTDPFSNRIAFCE 176
Cdd:COG0346   92 EIEG-EPRDRAYGYRSAyFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
74-174 6.35e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 46.29  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711   74 VEKAMEFYCRFLGFHLDWEHRFGENFPLYCQVSRDGMALHLSEHSGDASPGAKAF---------VRVANIRAYHAELSAK 144
Cdd:pfam00903  12 LEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFgghhiafiaFSVDDVDAAYDRLKAA 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 636787711  145 DYRYMKPGVEEAPWGLEMTVTDPFSNRIAF 174
Cdd:pfam00903  92 GVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 67-167 1.97e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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: 319962  Cd Length: 121  Bit Score: 42.09  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  67 PIFRIFSVEKAMEFYCRFLGFHLDWEHRFGENFPLYCQ--------VSRDGMALHLSeHSGDASPGAKAF--VRVANIRA 136
Cdd:cd16355    3 PVLNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSVGSgeceiflcQGGQGGSLRLG-PCGDALPSYGAWmsVWVDDVDA 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 636787711 137 YHAELSAKDYRYMKPGvEEAPWGL-EMTVTDP 167
Cdd:cd16355   82 LHRECRARGADIRQPP-TDMPWGMrEMHVRHP 112
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 74-176 3.80e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 41.16  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHLDWEHRFGEnfplYCQVSRDGMALHLSEHS------GDASPGAKAFV--RVANIRAYHAELSAKD 145
Cdd:cd07264   11 FAASLRFYRDVLGLPPRFLHEEGE----YAEFDTGETKLALFSRKemarsgGPDRRGSAFELgfEVDDVEATVEELVERG 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 636787711 146 YRyMKPGVEEAPWGLE-MTVTDPFSNRIAFCE 176
Cdd:cd07264   87 AE-FVREPANKPWGQTvAYVRDPDGNLIEICE 117
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 74-168 4.80e-04

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: 319903  Cd Length: 112  Bit Score: 38.23  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHL----DWEHRFGENFPLYCQVSrdgmalhLSEHSGDASPGAKAFVRVANIRAYHAELSAKDYRYM 149
Cdd:cd07238   11 PERAAAFYGDHLGLPLvmdhGWIVTFASPGNAHAQIS-------LAREGGSGTVVPDLSIEVDDVDAVHARVVAAGLRIE 83

                         90       100
                 ....*....|....*....|
gi 636787711 150 KPGVEEaPWGLE-MTVTDPF 168
Cdd:cd07238   84 YGPTTE-AWGVRrFFVRDPF 102
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 74-174 3.20e-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: 35.58  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHLDWEHRFGENFPLYCQvsrDGMALHLSEHSGDASPGAKAF----VRVANIRAYHAELSAKDYRYM 149
Cdd:cd06587    9 LDASVAFYEEVLGFEVVSRNEGGGFAFLRLG---PGLRLALLEGPEPERPGGGGLfhlaFEVDDVDEVDERLREAGAEGE 85

                         90       100
                 ....*....|....*....|....*..
gi 636787711 150 K-PGVEEAPWGLEM-TVTDPFSNRIAF 174
Cdd:cd06587   86 LvAPPVDDPWGGRSfYFRDPDGNLIEF 112
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 74-176 7.37e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 34.97  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787711  74 VEKAMEFYCRFLGFHLDWEHRFGENF------PLYCQVSrdgMALHLSEHSGDAS-----PGAKAFVR--VANIRAYHAE 140
Cdd:cd07263    9 QDKALDFYVEKLGFEVVEDVPMGGMRwvtvapPGSPGTS---LLLEPKAHPAQMPqspeaAGGTPGILlaTDDIDATYER 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 636787711 141 LSAKDYRYMKPgVEEAPWGLEMTVTDPFSNRIAFCE 176
Cdd:cd07263   86 LTAAGVTFVQE-PTQMGGGRVANFRDPDGNLFALME 120
 
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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