NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|283806485|dbj|BAI66366|]
View 

zeocin resistance protein [Moss transformation vector p35S-loxP-Zeo]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 8-118 4.63e-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: 111.55  E-value: 4.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   8 VPVLTARDVAGAVEFWTDRLGFSRDFV--EDDFAGVVRDDVTLFISAVQDQV-VPDNTLAWVLVRGLDELYAEWSEVVST 84
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYErpPPGYAILSRGGVELHLFEHPGLDpAGSGVAAYIRVEDIDALHAELKAAGLP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 283806485  85 NFRdasGPAMTEIGEQPWG-REFALRDPAGNCVHF 118
Cdd:cd08349   81 LFG---IPRITPIEDKPWGmREFAVVDPDGNLLRF 112
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-118 4.63e-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: 111.55  E-value: 4.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   8 VPVLTARDVAGAVEFWTDRLGFSRDFV--EDDFAGVVRDDVTLFISAVQDQV-VPDNTLAWVLVRGLDELYAEWSEVVST 84
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYErpPPGYAILSRGGVELHLFEHPGLDpAGSGVAAYIRVEDIDALHAELKAAGLP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 283806485  85 NFRdasGPAMTEIGEQPWG-REFALRDPAGNCVHF 118
Cdd:cd08349   81 LFG---IPRITPIEDKPWGmREFAVVDPDGNLLRF 112
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
6-121 7.09e-10

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 52.55  E-value: 7.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   6 SAVPVLTARDVAGAVEFWTDRLGFSRDFVEDD------FAGVVRDDVTLFISAV---QDQVVPDNTLAWVLVRGLDELYA 76
Cdd:COG2764    1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAppdSPAAEGNGVSLSLYVDDVDALFA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 283806485  77 EWSEvvstnfrdASGPAMTEIGEQPWG-REFALRDPAGNCVHFVAE 121
Cdd:COG2764   81 RLVA--------AGATVVMPLQDTFWGdRFGMVRDPFGVLWMINTP 118
Glyoxalase_7 pfam19581
Glyoxalase superfamily protein;
8-118 2.56e-05

Glyoxalase superfamily protein;


Pssm-ID: 437413  Cd Length: 133  Bit Score: 40.74  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485    8 VPVLTARDVAGAVEFWTDRLGFSRDF---VEDDFAG---VVRDDVTLFISAVQDQVVPDNTLaWVLVRGLDELYaewSEV 81
Cdd:pfam19581  17 FPILRIFDEAKAKAFYGDFLGFEADWehhFDDHFPAyiqVSRAGLGLHLSEHHGDACPGSNI-FVTMRGIDAFH---KEI 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 283806485   82 VSTNFRDASgPAMTEIgeqPWGRE-FALRDPAGNCVHF 118
Cdd:pfam19581  93 TGKKYKFLN-PGIEEL---FWGADcMEVIDPFGNHIRF 126
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-118 4.63e-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: 111.55  E-value: 4.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   8 VPVLTARDVAGAVEFWTDRLGFSRDFV--EDDFAGVVRDDVTLFISAVQDQV-VPDNTLAWVLVRGLDELYAEWSEVVST 84
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYErpPPGYAILSRGGVELHLFEHPGLDpAGSGVAAYIRVEDIDALHAELKAAGLP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 283806485  85 NFRdasGPAMTEIGEQPWG-REFALRDPAGNCVHF 118
Cdd:cd08349   81 LFG---IPRITPIEDKPWGmREFAVVDPDGNLLRF 112
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
6-121 7.09e-10

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 52.55  E-value: 7.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   6 SAVPVLTARDVAGAVEFWTDRLGFSRDFVEDD------FAGVVRDDVTLFISAV---QDQVVPDNTLAWVLVRGLDELYA 76
Cdd:COG2764    1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAppdSPAAEGNGVSLSLYVDDVDALFA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 283806485  77 EWSEvvstnfrdASGPAMTEIGEQPWG-REFALRDPAGNCVHFVAE 121
Cdd:COG2764   81 RLVA--------AGATVVMPLQDTFWGdRFGMVRDPFGVLWMINTP 118
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 7-119 1.68e-08

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: 48.81  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   7 AVPVLTARDVAGAVEFWTdRLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVL-VRGLDELYAEWSEVVSTN 85
Cdd:cd08350    4 ATPNLPSRDFDATAAFYA-RLGFQTVYRDDGWMILRRGDLTLEFFPHPDLDPAASWFSCCLrVDDLDALYAQWSAAGIPE 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 283806485  86 FrDASGPAMTEIGEQPWG-REFALRDPAGNCVHFV 119
Cdd:cd08350   83 D-TRGIPRLHPPQTQPWGiRMFALIDPDGSLLRLI 116
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-114 1.42e-05

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 41.16  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485  10 VLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVR----DDVTLFISAVQDQVVPDNTLAWVLVRGLDELYAEwsevvstn 85
Cdd:COG3324    9 ELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEfdtdGGQVGGLMPGAEEPGGPGWLLYFAVDDLDAAVAR-------- 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 283806485  86 FRDASGPAMTEIGEQP-WGREFALRDPAGN 114
Cdd:COG3324   81 VEAAGGTVLRPPTDIPpWGRFAVFRDPEGN 110
Glyoxalase_7 pfam19581
Glyoxalase superfamily protein;
8-118 2.56e-05

Glyoxalase superfamily protein;


Pssm-ID: 437413  Cd Length: 133  Bit Score: 40.74  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485    8 VPVLTARDVAGAVEFWTDRLGFSRDF---VEDDFAG---VVRDDVTLFISAVQDQVVPDNTLaWVLVRGLDELYaewSEV 81
Cdd:pfam19581  17 FPILRIFDEAKAKAFYGDFLGFEADWehhFDDHFPAyiqVSRAGLGLHLSEHHGDACPGSNI-FVTMRGIDAFH---KEI 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 283806485   82 VSTNFRDASgPAMTEIgeqPWGRE-FALRDPAGNCVHF 118
Cdd:pfam19581  93 TGKKYKFLN-PGIEEL---FWGADcMEVIDPFGNHIRF 126
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 10-118 6.57e-05

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: 39.43  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485  10 VLTARDVAGAVEFWTDRLGF--SRDFVEDDFAGVVR-DDVTLFISAVQDQ---VVPDNTLAWVLVRGLDELYAEWSEvvs 83
Cdd:cd06587    3 ALRVPDLDASVAFYEEVLGFevVSRNEGGGFAFLRLgPGLRLALLEGPEPerpGGGGLFHLAFEVDDVDEVDERLRE--- 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 283806485  84 tnfRDASGPAMTEIGEQPWG-REFALRDPAGNCVHF 118
Cdd:cd06587   80 ---AGAEGELVAPPVDDPWGgRSFYFRDPDGNLIEF 112
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 8-113 1.72e-04

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: 38.24  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   8 VPVLTARDVAGAVEFWTDRLGFSRDFVEDD---FAGVVRDDVTLFIsAVQDQVVP----------DNTLAW--VLVRGLD 72
Cdd:cd16355    2 TPVLNVSDIPASFAWFEKVLGFQKDWDWGDpptFGSVGSGECEIFL-CQGGQGGSlrlgpcgdalPSYGAWmsVWVDDVD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 283806485  73 ELYAEWSEVVSTNfrdASGPAmteigEQPWG-REFALRDPAG 113
Cdd:cd16355   81 ALHRECRARGADI---RQPPT-----DMPWGmREMHVRHPDG 114
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 8-113 1.98e-04

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: 38.05  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   8 VPvltARDVAGAVEFWTDrLGFSRDFVEDDFAGVVRDDVTLFISAVQDQVVPDNTLAWVLVRGLDelyAEWSEVVSTNFR 87
Cdd:cd08356    7 VP---AKDFELSKAFYQA-LGFELASEEGGVAYFRLGDCSFLLQDFYEKEHAENFMMHLLVEDVD---AWHQHVKTLGLA 79

                         90       100
                 ....*....|....*....|....*..
gi 283806485  88 DASGPAMTEIGEQPWG-REFALRDPAG 113
Cdd:cd08356   80 ERYGVKVTDPTDQPWGmRDFVLTDPSG 106
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-118 3.83e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 34.73  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   10 VLTARDVAGAVEFWTDRLGFSRDFVEDDFAGVVR---------DDVTLFISAVQDQVVPDNTLA--WVLVRGLDELYAEW 78
Cdd:pfam00903   6 ALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLrsafflaggRVLELLLNETPPPAAAGFGGHhiAFIAFSVDDVDAAY 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 283806485   79 SEVVSTNFRDASGPamteiGEQPWG-REFALRDPAGNCVHF 118
Cdd:pfam00903  86 DRLKAAGVEIVREP-----GRHGWGgRYSYFRDPDGNLIEL 121
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-114 5.46e-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: 34.19  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485   5 TSAVPVltaRDVAGAVEFWTDRLGFsrDFVEDDFAGVVR---------DDVTLFIS-------AVQDQVVPDNTLAWVL- 67
Cdd:cd07263    1 QVMLYV---DDQDKALDFYVEKLGF--EVVEDVPMGGMRwvtvappgsPGTSLLLEpkahpaqMPQSPEAAGGTPGILLa 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 283806485  68 VRGLDELYAEWsevvstnfRDASGPAMTEIGEQPWGREFALRDPAGN 114
Cdd:cd07263   76 TDDIDATYERL--------TAAGVTFVQEPTQMGGGRVANFRDPDGN 114
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
10-122 9.39e-03

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 33.78  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 283806485  10 VLTARDVAGAVEFWTDRLGFSRDFVEDDFA--GVVRDDVTLFISAVQDQVVPDNT-----LAWvLVRGLDELyAEWSEVV 82
Cdd:COG2514    8 TLRVRDLERSAAFYTDVLGLEVVEREGGRVylRADGGEHLLVLEEAPGAPPRPGAagldhVAF-RVPSRADL-DAALARL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 283806485  83 stnfrDASGPAMTEIGEQPWGREFALRDPAGNCVHFVAEE 122
Cdd:COG2514   86 -----AAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDR 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH