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Conserved domains on  [gi|221535464|gb|EEE38452|]
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bleomycin resistance family protein [Rhodobacteraceae bacterium KLH11]

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 ...
 8-121 1.64e-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: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   8 TPFVLCSSLERQIAFYCDRLGFTCTFQQ--DNYAFLRRDPVAIRLLECPARAdgrLLGDDQSFYIDVEGIDALYEKLRPR 85
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLD---PAGSGVAAYIRVEDIDALHAELKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 221535464  86 LQGLP-EGKVRPPFDQPYQQREFHVLDEDGTLVFFGE 121
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 ...
 8-121 1.64e-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: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   8 TPFVLCSSLERQIAFYCDRLGFTCTFQQ--DNYAFLRRDPVAIRLLECPARAdgrLLGDDQSFYIDVEGIDALYEKLRPR 85
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLD---PAGSGVAAYIRVEDIDALHAELKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 221535464  86 LQGLP-EGKVRPPFDQPYQQREFHVLDEDGTLVFFGE 121
Cdd:cd08349   78 GLPLFgIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-122 1.47e-12

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 59.48  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   7 LTPFVLCSSLERQIAFYCDRLGFTCTFQQDN------YAFLRRDPVAIRLLECPARADGRLlGDDQSFYIDVEGIDALYE 80
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAE-GNGVSLSLYVDDVDALFA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 221535464  81 KLRPRlqglpEGKV-RPPFDQPYQQREFHVLDEDGTLVFFGED 122
Cdd:COG2764   81 RLVAA-----GATVvMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
11-117 1.04e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 49.75  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   11 VLCSSLERQIAFYCDRLGFTCTFQQDN-------YAFLRRDPVAIRLLECPARADGRLLGDD---QSFYIDVEGIDALYE 80
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELLLNETPPPAAAGFGGhhiAFIAFSVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221535464   81 KLRPRlqGLPEgkVRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:pfam00903  87 RLKAA--GVEI--VREPGRHGWGGRYSYFRDPDGNLI 119
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-121 1.64e-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: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   8 TPFVLCSSLERQIAFYCDRLGFTCTFQQ--DNYAFLRRDPVAIRLLECPARAdgrLLGDDQSFYIDVEGIDALYEKLRPR 85
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERppPGYAILSRGGVELHLFEHPGLD---PAGSGVAAYIRVEDIDALHAELKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 221535464  86 LQGLP-EGKVRPPFDQPYQQREFHVLDEDGTLVFFGE 121
Cdd:cd08349   78 GLPLFgIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-122 1.47e-12

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 59.48  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   7 LTPFVLCSSLERQIAFYCDRLGFTCTFQQDN------YAFLRRDPVAIRLLECPARADGRLlGDDQSFYIDVEGIDALYE 80
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPPDSPAAE-GNGVSLSLYVDDVDALFA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 221535464  81 KLRPRlqglpEGKV-RPPFDQPYQQREFHVLDEDGTLVFFGED 122
Cdd:COG2764   81 RLVAA-----GATVvMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 13-119 1.98e-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: 51.37  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  13 CSSLERQIAFYCDRLGFTC--TFQQDNYAFLRRDPVAIRLLECPARADGRLLGDDQSFYIDVEGIDALYEKLrpRLQGLP 90
Cdd:cd06587    6 VPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERL--REAGAE 83

                         90       100
                 ....*....|....*....|....*....
gi 221535464  91 EGKVRPPFDQPYQQREFHVLDEDGTLVFF 119
Cdd:cd06587   84 GELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 7-120 2.01e-09

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: 51.72  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   7 LTPFVLCSSLERQIAFYCDRLGFTCTFQQ--------------DNYAFLRRDPVAIRLLECPARadgrLLGDDQSFYIDV 72
Cdd:cd16355    1 LTPVLNVSDIPASFAWFEKVLGFQKDWDWgdpptfgsvgsgecEIFLCQGGQGGSLRLGPCGDA----LPSYGAWMSVWV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 221535464  73 EGIDALYEKLRPRlqGLpegKVR-PPFDQPYQQREFHVLDEDGTLVFFG 120
Cdd:cd16355   77 DDVDALHRECRAR--GA---DIRqPPTDMPWGMREMHVRHPDGHRFRVG 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
11-117 1.04e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 49.75  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   11 VLCSSLERQIAFYCDRLGFTCTFQQDN-------YAFLRRDPVAIRLLECPARADGRLLGDD---QSFYIDVEGIDALYE 80
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELLLNETPPPAAAGFGGhhiAFIAFSVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 221535464   81 KLRPRlqGLPEgkVRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:pfam00903  87 RLKAA--GVEI--VREPGRHGWGGRYSYFRDPDGNLI 119
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-117 1.17e-07

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: 47.01  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   7 LTPFVLCSSLERQIAFYCDRLGFTCTFQQDNYAFLR---RDPVAIRLLEC---PARADGRLLGDDQSFYIDVEGIDALYE 80
Cdd:cd08359    3 LGPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRraeRHGFELAIMDGqhgAVPAASQTQSSGLIINFEVDDADAEYE 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 221535464  81 klrpRLQGLPEGKVRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:cd08359   83 ----RLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLI 115
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 13-117 3.06e-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: 45.75  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  13 CSSLERQIAFYCDRLGFTCTFQQDN------YAFLRR-DPVAIRLLECPARADGRLLGDDQSFYIDVEGIDALYEKLRPR 85
Cdd:COG0346   10 VSDLEASLAFYTDVLGLELVKRTDFgdggfgHAFLRLgDGTELELFEAPGAAPAPGGGGLHHLAFRVDDLDAAYARLRAA 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 221535464  86 lqGLPEgkVRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:COG0346   90 --GVEI--EGEPRDRAYGYRSAYFRDPDGNLI 117
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 5-116 5.42e-07

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: 44.98  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   5 LELTPFVLCSSLERQIAFYCDrLGFTCTFQQDNYAFLRRDPVAIRLlecparadgrllgddQSFY-----------IDVE 73
Cdd:cd08356    1 IEIKAFVPAKDFELSKAFYQA-LGFELASEEGGVAYFRLGDCSFLL---------------QDFYekehaenfmmhLLVE 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 221535464  74 GIDALYEKLRPRlqGLPEG---KVRPPFDQPYQQREFHVLDEDGTL 116
Cdd:cd08356   65 DVDAWHQHVKTL--GLAERygvKVTDPTDQPWGMRDFVLTDPSGVL 108
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-117 7.08e-07

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 44.63  E-value: 7.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  10 FVLCSSLERQIAFYCDRLGFTCTFQQD---NYAFLRRDPVAIRLLECPARADGrllGDDQSFYIDVEGIDALYEKLRPRl 86
Cdd:COG3324    9 ELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGGQVGGLMPGAEEPG---GPGWLLYFAVDDLDAAVARVEAA- 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 221535464  87 qGlpeGKV-RPPFDQPYQQREFHVLDEDGTLV 117
Cdd:COG3324   85 -G---GTVlRPPTDIPPWGRFAVFRDPEGNRF 112
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 16-117 2.18e-06

BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. 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. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface.


Pssm-ID: 319938  Cd Length: 118  Bit Score: 43.42  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  16 LERQIAFYcDRLGFTCTFQQDNYAFLRRDPVairLLECPARADGRLLGDDQSFYIDVEGIDALYEKLRPrlQGLPEG--- 92
Cdd:cd08350   13 FDATAAFY-ARLGFQTVYRDDGWMILRRGDL---TLEFFPHPDLDPAASWFSCCLRVDDLDALYAQWSA--AGIPEDtrg 86

                         90       100
                 ....*....|....*....|....*..
gi 221535464  93 --KVRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:cd08350   87 ipRLHPPQTQPWGIRMFALIDPDGSLL 113
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-44 1.45e-03

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 36.09  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 221535464   4 ILELTPFVL-CSSLERQIAFYCDRLGFTCTFQQDNYAFLRRD 44
Cdd:COG2514    1 ITRLGHVTLrVRDLERSAAFYTDVLGLEVVEREGGRVYLRAD 42
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 17-117 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: 319903  Cd Length: 112  Bit Score: 35.92  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  17 ERQIAFYCDRLGFTCTFQQD---NYAFLRRDPVAIRLLecparADGRLLGDDQSFYIDVEGIDALYEKLRPrlQGLPegK 93
Cdd:cd07238   12 ERAAAFYGDHLGLPLVMDHGwivTFASPGNAHAQISLA-----REGGSGTVVPDLSIEVDDVDAVHARVVA--AGLR--I 82

                         90       100
                 ....*....|....*....|....
gi 221535464  94 VRPPFDQPYQQREFHVLDEDGTLV 117
Cdd:cd07238   83 EYGPTTEAWGVRRFFVRDPFGRLI 106
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 14-121 1.56e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 35.77  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464  14 SSLERQIAFYCDRLGFTCTFQQDNYAFLRRDPVAIRLLECPARADGRLLGDDQ-----SFYIDVEGIDALYEKLRPRlqg 88
Cdd:cd07264    9 DDFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETKLALFSRKEMARSGGPDRrgsafELGFEVDDVEATVEELVER--- 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 221535464  89 lPEGKVRPPFDQPYQQREFHVLDEDGTLVFFGE 121
Cdd:cd07264   86 -GAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-121 1.63e-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: 319953  Cd Length: 122  Bit Score: 35.91  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221535464   9 PFVLCSSLERQIAFYCDRLG--FTCTFQ-----------QDNYAFLrrDPVAIRLLECPARADGRLLgddqsfYIDVEGI 75
Cdd:cd09011    6 PLLVVKDIEKSKKFYEDVLGqkILLDFGenvvfeggfalQEKKSWL--ETIIISDLSIKQQSNNFEL------YFEVDDF 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 221535464  76 DALYEKLRPRLQglpEGKVRPPFDQPYQQREFHVLDEDGTLVFFGE 121
Cdd:cd09011   78 DAFFEKLNPHKD---IEFIHPILEHPWGQRVFRFYDPDGHIIEIGE 120
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 14-57 9.91e-03

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: 33.82  E-value: 9.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 221535464  14 SSLERQIAFYCDRLGFTCTFQQDNYAFLRRD--PVAIRLLECPARA 57
Cdd:cd07255   11 ADLERQSAFYQNVIGLSVLKQNASRAYLGVDgkQVLLVLEAIPDAV 56
 
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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