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Conserved domains on  [gi|217035502|pdb|3FCD|A]
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Chain A, Lyase

Protein Classification

bleomycin resistance protein( domain architecture ID 10170075)

bleomycin resistance protein (BRP) is a binding protein with a strong affinity to the bleomycin family of antibiotics

CATH:  3.10.180.10
Gene Ontology:  GO:0046677
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-123 2.03e-33

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: 113.09  E-value: 2.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       10 TPFLHIPD*QEALTLFCDTLGFELKYRHSN--YAYLELSGCGLRLLEEPARKIIPDGiarVAICIDVSDIDSLHTKLSPA 87
Cdd:cd08349   1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPpgYAILSRGGVELHLFEHPGLDPAGSG---VAAYIRVEDIDALHAELKAA 77

                        90       100       110
                ....*....|....*....|....*....|....*..
3FCD_A       88 LENLPA-DQVEPLKN*PYGQREFQVR*PDGDWLNFTA 123
Cdd:cd08349  78 GLPLFGiPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-123 2.03e-33

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: 113.09  E-value: 2.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       10 TPFLHIPD*QEALTLFCDTLGFELKYRHSN--YAYLELSGCGLRLLEEPARKIIPDGiarVAICIDVSDIDSLHTKLSPA 87
Cdd:cd08349   1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPpgYAILSRGGVELHLFEHPGLDPAGSG---VAAYIRVEDIDALHAELKAA 77

                        90       100       110
                ....*....|....*....|....*....|....*..
3FCD_A       88 LENLPA-DQVEPLKN*PYGQREFQVR*PDGDWLNFTA 123
Cdd:cd08349  78 GLPLFGiPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
8-116 1.54e-16

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 69.88  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        8 QITPFLHIPD*QEALTLFCDTLGFELKYRHSN------YAYLELSGCGLRLLEEPARKIIPDGiARVAICIDVSDIDSLH 81
Cdd:COG2764   1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAEG-NGVSLSLYVDDVDALF 79

                        90       100       110
                ....*....|....*....|....*....|....*
3FCD_A       82 TKLSPAlenlPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:COG2764  80 ARLVAA----GATVVMPLQDTFWGDRFGMVRDPFG 110
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
16-121 9.44e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 44.75  E-value: 9.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A         16 PD*QEALTLFCDTLGFELKYRHSN-------YAYLELSGCGLRLLEEPA---RKIIPDGIARVAICIDVSDIDSLHTKLS 85
Cdd:pfam00903  10 GDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELLLNETpppAAAGFGGHHIAFIAFSVDDVDAAYDRLK 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
3FCD_A         86 palenlpADQVE---PLKN*PYGQREFQVR*PDGDWLNF 121
Cdd:pfam00903  90 -------AAGVEivrEPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-123 2.03e-33

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: 113.09  E-value: 2.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       10 TPFLHIPD*QEALTLFCDTLGFELKYRHSN--YAYLELSGCGLRLLEEPARKIIPDGiarVAICIDVSDIDSLHTKLSPA 87
Cdd:cd08349   1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPpgYAILSRGGVELHLFEHPGLDPAGSG---VAAYIRVEDIDALHAELKAA 77

                        90       100       110
                ....*....|....*....|....*....|....*..
3FCD_A       88 LENLPA-DQVEPLKN*PYGQREFQVR*PDGDWLNFTA 123
Cdd:cd08349  78 GLPLFGiPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
8-116 1.54e-16

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 69.88  E-value: 1.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        8 QITPFLHIPD*QEALTLFCDTLGFELKYRHSN------YAYLELSGCGLRLLEEPARKIIPDGiARVAICIDVSDIDSLH 81
Cdd:COG2764   1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAEG-NGVSLSLYVDDVDALF 79

                        90       100       110
                ....*....|....*....|....*....|....*
3FCD_A       82 TKLSPAlenlPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:COG2764  80 ARLVAA----GATVVMPLQDTFWGDRFGMVRDPFG 110
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-127 1.27e-08

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: 49.61  E-value: 1.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        6 IHQITpfLHIPD*QEALTLFCDTLGFELKYRH------SNYAYLEL-SGCGLRLLEEPARKIIPDGIARVAICIDVSDID 78
Cdd:COG0346   3 LHHVT--LRVSDLEASLAFYTDVLGLELVKRTdfgdggFGHAFLRLgDGTELELFEAPGAAPAPGGGGLHHLAFRVDDLD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
3FCD_A       79 SLHTKlspaLENLPADQVEPLKN*PYGQREFQVR*PDGDWLNFTAPLAE 127
Cdd:COG0346  81 AAYAR----LRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 13-121 2.31e-07

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: 45.98  E-value: 2.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       13 LHIPD*QEALTLFCDTLGFELKYRHSNYAYLELS---GCGLRLLEEP-ARKIIPDGIARvaICIDVSDIDSLHTKLSPAL 88
Cdd:cd06587   4 LRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRlgpGLRLALLEGPePERPGGGGLFH--LAFEVDDVDEVDERLREAG 81

                        90       100       110
                ....*....|....*....|....*....|...
3FCD_A       89 ENLpaDQVEPLKN*PYGQREFQVR*PDGDWLNF 121
Cdd:cd06587  82 AEG--ELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 9-116 2.56e-07

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: 46.33  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        9 ITPFLHIPD*QEALTLFCDTLGFELKYRHS--------------NYAYLELSGCGLRLLEEPArKIIPDGiarVAICIDV 74
Cdd:cd16355   1 LTPVLNVSDIPASFAWFEKVLGFQKDWDWGdpptfgsvgsgeceIFLCQGGQGGSLRLGPCGD-ALPSYG---AWMSVWV 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3FCD_A       75 SDIDSLHTKLSPAlenlPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:cd16355  77 DDVDALHRECRAR----GADIRQPPTDMPWGMREMHVRHPDG 114
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
16-121 9.44e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 44.75  E-value: 9.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A         16 PD*QEALTLFCDTLGFELKYRHSN-------YAYLELSGCGLRLLEEPA---RKIIPDGIARVAICIDVSDIDSLHTKLS 85
Cdd:pfam00903  10 GDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELLLNETpppAAAGFGGHHIAFIAFSVDDVDAAYDRLK 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
3FCD_A         86 palenlpADQVE---PLKN*PYGQREFQVR*PDGDWLNF 121
Cdd:pfam00903  90 -------AAGVEivrEPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-119 3.06e-06

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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 43.16  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       16 PD*QEALTLFCDTLGFELKYRHSNYAYLELS-GCGLRL-LEEPARKIIPDGIA----RVAICIDVSDIDSLHTKLSPALE 89
Cdd:cd08359  10 EDVAATAAFYVKHFGFRVIFDSDWYVSLRRAeRHGFELaIMDGQHGAVPAASQtqssGLIINFEVDDADAEYERLTQAGL 89

                        90       100       110
                ....*....|....*....|....*....|
3FCD_A       90 NLpadqVEPLKN*PYGQREFQVR*PDGDWL 119
Cdd:cd08359  90 EF----LEPPRDEPWGQRRFIVRDPNGVLI 115
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-116 3.95e-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: 40.39  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       13 LHIPD*QEALTLFCDTLGFELKYRH--SNYAYLELSGCGLRLL--EEPARKIIPDG-IARVAICIDVSDIDslhtKLSPA 87
Cdd:cd07264   6 LYVDDFAASLRFYRDVLGLPPRFLHeeGEYAEFDTGETKLALFsrKEMARSGGPDRrGSAFELGFEVDDVE----ATVEE 81

                        90       100
                ....*....|....*....|....*....
3FCD_A       88 LENLPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:cd07264  82 LVERGAEFVREPANKPWGQTVAYVRDPDG 110
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 9-116 2.20e-04

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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: 319943  Cd Length: 123  Bit Score: 38.17  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        9 ITPFLHIPD*QEALTLFCDTLGFELKYRHSN------YAYLELSGCGLRLLEE-----PARKIIPDGIARVAICIDVSDI 77
Cdd:cd08355   1 VVPTLRYRDAVAAIDWLVEAFGFEERMVVPGdegtihHAELTFGGGGVMVGSVrdearPDRPADAGGHGTQSVYVAVADP 80

                        90       100       110
                ....*....|....*....|....*....|....*....
3FCD_A       78 DSLHTKLSPAlenlPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:cd08355  81 DAHYERARAA----GAEIVMEPTDTDYGSRDYSARDPEG 115
BAT cd16354
Bleomycin N-Acetyltransferase and similar proteins; BlmB, encodes a bleomycin ...
 9-123 8.86e-04

Bleomycin N-Acetyltransferase and similar proteins; BlmB, encodes a bleomycin N-acetyltransferase, designated BAT, which inactivates Bm using acetyl-coenzyme A (AcCoA). BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. The N-terminal domain of BAT has a tunnel with two entrances: a wide entrance that accommodates the metal-binding domain of Bm and a narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains forms the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel and ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. BAT belongs to vicinal oxygen chelate (VOC) superfamily that 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 thiocoraline, 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: 319961  Cd Length: 114  Bit Score: 36.66  E-value: 8.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        9 ITPFLHIPD*QEALTLFCDTLGFELKYR---HSNYAYLELS----GCGLRLLEEParkiiPDGIARVAICIDVS-DIDSL 80
Cdd:cd16354   1 VEPVLPVRDVAATLDLLEAVLGARVGFEvgdPPEFAGAVLGpwsvGPGLRLVATP-----GGPIAPVTLHLDAGvEFDSL 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
3FCD_A       81 HTKLSPAlenlPADQVEPLKN*PYGQREFQVR*PDGDWLNFTA 123
Cdd:cd16354  76 HRRALAA----GARVDGPPVRQPWGRREFVLRLPEGHRLVVSG 114
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 17-116 1.20e-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: 36.12  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       17 D*QEALTLFCDTLGFELKYRHSN--YAYLELS---GCGLRLLEEPARKIIPDGI------ARVAICIDVSDIDSLHTKLS 85
Cdd:cd07263   8 DQDKALDFYVEKLGFEVVEDVPMggMRWVTVAppgSPGTSLLLEPKAHPAQMPQspeaagGTPGILLATDDIDATYERLT 87

                        90       100       110
                ....*....|....*....|....*....|...
3FCD_A       86 palenlpADQVEPLK--N*PYGQREFQVR*PDG 116
Cdd:cd07263  88 -------AAGVTFVQepTQMGGGRVANFRDPDG 113
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-116 1.32e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 36.12  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A        7 HQITPFLHIPD*QEALTLFCDTLGFELKYRHSNY------AYLELSGCGLRLLEE-PAR-KIIPDGI--ARVAICIDVSD 76
Cdd:cd07246   1 TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTTQEdgrvghAELRIGGTVVMVADEnPERgALSPTKLggTPVIFHLYVED 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
3FCD_A       77 IDSLHTKlspALENlPADQVEPLKN*PYGQREFQVR*PDG 116
Cdd:cd07246  81 VDATFAR---AVAA-GAVVVEPVEDQFWGDRVGKVKDPFG 116
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 25-116 6.96e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The 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: 319944  Cd Length: 113  Bit Score: 34.20  E-value: 6.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FCD_A       25 FCDTLGFELKYRHSNYAYLELSGCG--LRLLEEparkiiPDGIARVAICIDVSDIDSLHTKLSPALENLPAD-QVEPLKN 101
Cdd:cd08356  18 FYQALGFELASEEGGVAYFRLGDCSflLQDFYE------KEHAENFMMHLLVEDVDAWHQHVKTLGLAERYGvKVTDPTD 91

                        90
                ....*....|....*
3FCD_A      102 *PYGQREFQVR*PDG 116
Cdd:cd08356  92 QPWGMRDFVLTDPSG 106
 
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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