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Conserved domains on  [gi|251836808|pdb|2KJZ|A]
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Chain A, ATC0852

Protein Classification

VOC family protein( domain architecture ID 10163551)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Enterobacter agglomerans phenazine resistance protein, EhpR

Gene Ontology:  GO:0046872
PubMed:  11076500|21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 28-141 5.87e-68

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


:

Pssm-ID: 319922  Cd Length: 114  Bit Score: 201.09  E-value: 5.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       28 FTILYVDNPPASTQFYKALLGVDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTGGGGELAFRVENDAQVDETFAGW 107
Cdd:cd07261   1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                        90       100       110
                ....*....|....*....|....*....|....
2KJZ_A      108 KASGVAMLQQPAKMEFGYTFTAADPDSHRLRVYA 141
Cdd:cd07261  81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVCC 114
 
Name Accession Description Interval E-value
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 28-141 5.87e-68

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 201.09  E-value: 5.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       28 FTILYVDNPPASTQFYKALLGVDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTGGGGELAFRVENDAQVDETFAGW 107
Cdd:cd07261   1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                        90       100       110
                ....*....|....*....|....*....|....
2KJZ_A      108 KASGVAMLQQPAKMEFGYTFTAADPDSHRLRVYA 141
Cdd:cd07261  81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVCC 114
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 23-139 2.62e-22

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 85.27  E-value: 2.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       23 MTHPDFTILYVDNPPASTQFYKAL-LGVDPVESSPTFSLFVLANGMKLGLWSRH------TVEPKASVTGGGGELAFRVE 95
Cdd:COG3607   1 MPRIIFVNLPVADLERSRAFYEALgFTFNPQFSDEGAACFVLGEGIVLMLLPREkfatftGKPIADATGFTEVLLALNVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
2KJZ_A       96 NDAQVDETFAGWKASGVAMLQQPAKMEFGYTFTAADPDSHRLRV 139
Cdd:COG3607  81 SREEVDALVAKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEV 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
27-139 3.00e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A         27 DFTILYVDNPPASTQFYKALLG------VDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTGGGGeLAFRVENDAQV 100
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGfklveeTDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHH-IAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
2KJZ_A        101 DETFAGWKASGVAMLQQPAKMEFGYTFT-AADPDSHRLRV 139
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 28-141 5.87e-68

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 201.09  E-value: 5.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       28 FTILYVDNPPASTQFYKALLGVDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTGGGGELAFRVENDAQVDETFAGW 107
Cdd:cd07261   1 LVILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLWSSEEVEPKVAVTGGGAELSFMVPSGEQVDEVYAEW 80

                        90       100       110
                ....*....|....*....|....*....|....
2KJZ_A      108 KASGVAMLQQPAKMEFGYTFTAADPDSHRLRVYA 141
Cdd:cd07261  81 KAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVCC 114
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 23-139 2.62e-22

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 85.27  E-value: 2.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       23 MTHPDFTILYVDNPPASTQFYKAL-LGVDPVESSPTFSLFVLANGMKLGLWSRH------TVEPKASVTGGGGELAFRVE 95
Cdd:COG3607   1 MPRIIFVNLPVADLERSRAFYEALgFTFNPQFSDEGAACFVLGEGIVLMLLPREkfatftGKPIADATGFTEVLLALNVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
2KJZ_A       96 NDAQVDETFAGWKASGVAMLQQPAKMEFGYTFTAADPDSHRLRV 139
Cdd:COG3607  81 SREEVDALVAKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEV 124
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 28-137 9.21e-16

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: 68.51  E-value: 9.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       28 FTILYVDNPPASTQFYKALLGVDP---VESSPtFSLFVLaNGMKLGLWSRHTVEP--KASVTGGGGELAFRVENdaqVDE 102
Cdd:cd07264   3 YIVLYVDDFAASLRFYRDVLGLPPrflHEEGE-YAEFDT-GETKLALFSRKEMARsgGPDRRGSAFELGFEVDD---VEA 77

                        90       100       110
                ....*....|....*....|....*....|....*
2KJZ_A      103 TFAGWKASGVAMLQQPAKMEFGYTFTAADPDSHRL 137
Cdd:cd07264  78 TVEELVERGAEFVREPANKPWGQTVAYVRDPDGNL 112
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 29-139 3.48e-15

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: 66.78  E-value: 3.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       29 TILYVDNPPASTQFYKALLGVDPVE--SSPTFSLFVLANGMKLGLWSRHTVEPKASvtGGGGELAFRVENDAQVDETFAG 106
Cdd:cd06587   2 VALRVPDLDASVAFYEEVLGFEVVSrnEGGGFAFLRLGPGLRLALLEGPEPERPGG--GGLFHLAFEVDDVDEVDERLRE 79

                        90       100       110
                ....*....|....*....|....*....|...
2KJZ_A      107 WKASGVAMLQQPAKMEFGYTFTAADPDSHRLRV 139
Cdd:cd06587  80 AGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 24-140 1.27e-13

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: 63.09  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       24 THPDFTILYVDNPPASTQFYKALLGVDPVESSP------TFSLFVLANGMKLGLWSRHTVEPkASVTGGGGELAFRVENd 97
Cdd:COG0346   1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGTELELFEAPGAAP-APGGGGLHHLAFRVDD- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
2KJZ_A       98 aqVDETFAGWKASGVAMLQQPAKMEFGYTFTA-ADPDSHRLRVY 140
Cdd:COG0346  79 --LDAAYARLRAAGVEIEGEPRDRAYGYRSAYfRDPDGNLIELV 120
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 23-140 1.77e-11

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 57.34  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       23 MTHPDFTILYVDNPPASTQFYKALLGVDPVESSP---TFSLFVLANGMKLGLWSRHTVEPKASVTggggeLAFRVENdaq 99
Cdd:COG3324   2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGGQVGGLMPGAEEPGGPGWL-----LYFAVDD--- 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
2KJZ_A      100 VDETFAGWKASGVAMLQQPAKM-EFGYTFTAADPDSHRLRVY 140
Cdd:COG3324  74 LDAAVARVEAAGGTVLRPPTDIpPWGRFAVFRDPEGNRFGLW 115
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
27-139 3.00e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A         27 DFTILYVDNPPASTQFYKALLG------VDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTGGGGeLAFRVENDAQV 100
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGfklveeTDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHH-IAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
2KJZ_A        101 DETFAGWKASGVAMLQQPAKMEFGYTFT-AADPDSHRLRV 139
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 29-135 3.60e-08

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319942  Cd Length: 122  Bit Score: 48.90  E-value: 3.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       29 TILYVDNPPASTQFYKALLGVDPVESSPTFSLFVLANGMKLGLWSRHTVEPKASVTG------GGGELAFRVENDaQVDE 102
Cdd:cd08354   4 TCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTGEVpghgasGHGHFAFAVPTE-ELAA 82

                        90       100       110
                ....*....|....*....|....*....|...
2KJZ_A      103 TFAGWKASGVAMLQQPAKMEFGYTFTAADPDSH 135
Cdd:cd08354  83 WEARLEAKGVPIESYTQWPEGGKSLYFRDPAGN 115
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
24-141 3.19e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 46.49  E-value: 3.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       24 THPDFTILYVDNPPASTQFYKALLGVDPVESSPTFSLFVLANGM-KLGLWSRHTVEPKASvTGGGGELAFRVENDAQVDE 102
Cdd:COG2514   2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEhLLVLEEAPGAPPRPG-AAGLDHVAFRVPSRADLDA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
2KJZ_A      103 TFAGWKASGVAmLQQPAKMEFGYTFTAADPDSHRLRVYA 141
Cdd:COG2514  81 ALARLAAAGVP-VEGAVDHGVGESLYFRDPDGNLIELYT 118
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 30-141 4.37e-05

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: 40.29  E-value: 4.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       30 ILYVDNPPASTQFYKALLG--VDPVESSPTFsLFVLANGMKLGLWSRHTVEPkasvTGGGGELAFRVENdaqVDETFAGW 107
Cdd:cd08349   3 ILPVRDIDKTLAFYVDVLGfeVDYERPPPGY-AILSRGGVELHLFEHPGLDP----AGSGVAAYIRVED---IDALHAEL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
2KJZ_A      108 KASGVAMLQQPAKMEFGYT------FTAADPDSHRLRVYA 141
Cdd:cd08349  75 KAAGLPLFGIPRITPIEDKpwgmreFAVVDPDGNLLRFGQ 114
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 29-139 1.88e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 38.82  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2KJZ_A       29 TILYVDNPPASTQFYKALLGVDPVESSP-----------------TFSLFVLANGMKLGlwsrhtvePKASVTGGGGELA 91
Cdd:cd07263   2 VMLYVDDQDKALDFYVEKLGFEVVEDVPmggmrwvtvappgspgtSLLLEPKAHPAQMP--------QSPEAAGGTPGIL 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
2KJZ_A       92 FRVENdaqVDETFAGWKASGVAMLQQPAKMEFGYTFTAADPDSHRLRV 139
Cdd:cd07263  74 LATDD---IDATYERLTAAGVTFVQEPTQMGGGRVANFRDPDGNLFAL 118
 
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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