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Conserved domains on  [gi|1371371789|gb|PSQ93700|]
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hypothetical protein BRD52_00425 [Bacteroidetes bacterium SW_4_67_19]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
208-326 1.70e-30

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


:

Pssm-ID: 441851  Cd Length: 121  Bit Score: 111.97  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789 208 FDKADRDRETMRLtqNADDPLPDVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTALIDECTPFDEAFEQLRDACERLNR 287
Cdd:COG2250     1 LRRAERDLEAAEL--LLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKTHDLRELLELLEKLLPEPEELRDLLRLLDK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1371371789 288 YAVDVRYPGDPG---YDPSADEARDARDPAERVCAFVREALE 326
Cdd:COG2250    79 AYIPARYPDALPegpEEYTREEAEEALELAEEVLEFVEKLLK 120
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
73-161 1.29e-18

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


:

Pssm-ID: 441314  Cd Length: 95  Bit Score: 79.30  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  73 PEIEDALLQRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADLDGPRRDRRAhlrqLLRPLIRKVDAPVDVLTY 152
Cdd:COG1708     2 STLLRELLEEIVEALRRGPEVAAVYLFGSYARGDARPDSDIDLLVVVDDPPLPDERLE----LLADLLRELGLPVDLVVL 77


                  ....*....
gi 1371371789 153 TPAEFAREK 161
Cdd:COG1708    78 TPAELELRL 86
 
Name Accession Description Interval E-value
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
208-326 1.70e-30

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 111.97  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789 208 FDKADRDRETMRLtqNADDPLPDVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTALIDECTPFDEAFEQLRDACERLNR 287
Cdd:COG2250     1 LRRAERDLEAAEL--LLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKTHDLRELLELLEKLLPEPEELRDLLRLLDK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1371371789 288 YAVDVRYPGDPG---YDPSADEARDARDPAERVCAFVREALE 326
Cdd:COG2250    79 AYIPARYPDALPegpEEYTREEAEEALELAEEVLEFVEKLLK 120
HEPN pfam05168
HEPN domain;
204-323 4.75e-26

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 100.00  E-value: 4.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789 204 VRSWFDKADRDRETMRLtqNADDPLPDVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTALIDECTPFDEAFEQLRDACE 283
Cdd:pfam05168   1 AEDWLRRAEEDLEAAEL--LLEEGDYDWACFHAQQAAEKALKALLLKLGGDPPKTHDLRELLGELKKGLGLPEELREILD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1371371789 284 RLNRYAVDVRYPgdPGYDPSADEARDARDPAERVCAFVRE 323
Cdd:pfam05168  79 ELEKAYIESRYP--DADEGTEEDAEEALKDAEEILELVEE 116
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
73-161 1.29e-18

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


Pssm-ID: 441314  Cd Length: 95  Bit Score: 79.30  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  73 PEIEDALLQRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADLDGPRRDRRAhlrqLLRPLIRKVDAPVDVLTY 152
Cdd:COG1708     2 STLLRELLEEIVEALRRGPEVAAVYLFGSYARGDARPDSDIDLLVVVDDPPLPDERLE----LLADLLRELGLPVDLVVL 77


                  ....*....
gi 1371371789 153 TPAEFAREK 161
Cdd:COG1708    78 TPAELELRL 86
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
 77-170 3.58e-13

Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.


Pssm-ID: 143393  Cd Length: 93  Bit Score: 64.36  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  77 DALLQRVVDRLVEAVD-PAAILLFGSRAKGTVRSDSDVDLCVIADLDGPRRDRRAHLRQLLRPLIRKVDapVDVLTYTPA 155
Cdd:cd05403     1 EEILEEILEILRELLGgVEKVYLFGSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVD--LVVLNALEL 78

                          90
                  ....*....|....*
gi 1371371789 156 EFAREKHLLNSVTYF 170
Cdd:cd05403    79 ELLLRILIEGEGIYL 93
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
230-317 1.37e-11

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 60.78  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  230 DVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTAL---IDECTPFDEAFEQLRDACERLNRYAVDVRYP--GDPGYDPSA 304
Cdd:smart00748  21 DLAAFLSQQAAELALKALLLALGGEPPKTHSLRELlseLEKLLRLPEFIDEIRECLNLLEEAYIKSRYPdaGEPLEWYTK 100

                           90
                   ....*....|...
gi 1371371789  305 DEARDARDPAERV 317
Cdd:smart00748 101 EDAEELLKCAEEI 113
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
 81-183 4.30e-11

Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in polymorphic toxins (NTox45) and polyvalent proteins.


Pssm-ID: 465859  Cd Length: 93  Bit Score: 58.69  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  81 QRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADlDGPRRDRRAHLRQLL--RPLIRKVDapVDVLTYTPAEFA 158
Cdd:pfam18765   1 EKIKEILKKNPEIEAAYLFGSRAKGDAREDSDIDLAVLYD-EKLDFEELLELASELedILLLRKVD--LVDLNKAPPVLA 77

                          90       100
                  ....*....|....*....|....*
gi 1371371789 159 REkhllnsvtyfIEKHGRTLYRRDD 183
Cdd:pfam18765  78 HQ----------ILKEGKLLYSRDE 92
 
Name Accession Description Interval E-value
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
208-326 1.70e-30

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 111.97  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789 208 FDKADRDRETMRLtqNADDPLPDVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTALIDECTPFDEAFEQLRDACERLNR 287
Cdd:COG2250     1 LRRAERDLEAAEL--LLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKTHDLRELLELLEKLLPEPEELRDLLRLLDK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1371371789 288 YAVDVRYPGDPG---YDPSADEARDARDPAERVCAFVREALE 326
Cdd:COG2250    79 AYIPARYPDALPegpEEYTREEAEEALELAEEVLEFVEKLLK 120
HEPN pfam05168
HEPN domain;
204-323 4.75e-26

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 100.00  E-value: 4.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789 204 VRSWFDKADRDRETMRLtqNADDPLPDVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTALIDECTPFDEAFEQLRDACE 283
Cdd:pfam05168   1 AEDWLRRAEEDLEAAEL--LLEEGDYDWACFHAQQAAEKALKALLLKLGGDPPKTHDLRELLGELKKGLGLPEELREILD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1371371789 284 RLNRYAVDVRYPgdPGYDPSADEARDARDPAERVCAFVRE 323
Cdd:pfam05168  79 ELEKAYIESRYP--DADEGTEEDAEEALKDAEEILELVEE 116
MJ0604 COG1708
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
73-161 1.29e-18

Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];


Pssm-ID: 441314  Cd Length: 95  Bit Score: 79.30  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  73 PEIEDALLQRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADLDGPRRDRRAhlrqLLRPLIRKVDAPVDVLTY 152
Cdd:COG1708     2 STLLRELLEEIVEALRRGPEVAAVYLFGSYARGDARPDSDIDLLVVVDDPPLPDERLE----LLADLLRELGLPVDLVVL 77


                  ....*....
gi 1371371789 153 TPAEFAREK 161
Cdd:COG1708    78 TPAELELRL 86
NT_KNTase_like cd05403
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ...
 77-170 3.58e-13

Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.


Pssm-ID: 143393  Cd Length: 93  Bit Score: 64.36  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  77 DALLQRVVDRLVEAVD-PAAILLFGSRAKGTVRSDSDVDLCVIADLDGPRRDRRAHLRQLLRPLIRKVDapVDVLTYTPA 155
Cdd:cd05403     1 EEILEEILEILRELLGgVEKVYLFGSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVD--LVVLNALEL 78

                          90
                  ....*....|....*
gi 1371371789 156 EFAREKHLLNSVTYF 170
Cdd:cd05403    79 ELLLRILIEGEGIYL 93
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
230-317 1.37e-11

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 60.78  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  230 DVTCYHAQQAAEKCLKGFLTARGREVEKTHDLTAL---IDECTPFDEAFEQLRDACERLNRYAVDVRYP--GDPGYDPSA 304
Cdd:smart00748  21 DLAAFLSQQAAELALKALLLALGGEPPKTHSLRELlseLEKLLRLPEFIDEIRECLNLLEEAYIKSRYPdaGEPLEWYTK 100

                           90
                   ....*....|...
gi 1371371789  305 DEARDARDPAERV 317
Cdd:smart00748 101 EDAEELLKCAEEI 113
MJ0435 COG1669
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
78-156 3.22e-11

Predicted nucleotidyltransferase MJ0435 [General function prediction only];


Pssm-ID: 441275  Cd Length: 96  Bit Score: 59.16  E-value: 3.22e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371371789  78 ALLQRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADlDGPRRDRRAHLRQLLRPLIrkvDAPVDVLTYTPAE 156
Cdd:COG1669     8 EILREVIEELAERYGVSRLGLFGSVARGEAREDSDIDLLVEFD-EPTSLFDLFELEEELEELL---GRKVDLVTLDGLS 82
Polbeta pfam18765
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ...
 81-183 4.30e-11

Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in polymorphic toxins (NTox45) and polyvalent proteins.


Pssm-ID: 465859  Cd Length: 93  Bit Score: 58.69  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  81 QRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIADlDGPRRDRRAHLRQLL--RPLIRKVDapVDVLTYTPAEFA 158
Cdd:pfam18765   1 EKIKEILKKNPEIEAAYLFGSRAKGDAREDSDIDLAVLYD-EKLDFEELLELASELedILLLRKVD--LVDLNKAPPVLA 77

                          90       100
                  ....*....|....*....|....*
gi 1371371789 159 REkhllnsvtyfIEKHGRTLYRRDD 183
Cdd:pfam18765  78 HQ----------ILKEGKLLYSRDE 92
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 80-161 2.23e-09

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 53.57  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371371789  80 LQRVVDRLVEAVDPAAILLFGSRAKGTVRSDSDVDLCVIadLDGPRRDRRAHLRQLLRPLIRKVDA-PVDVLTYTPAEFA 158
Cdd:pfam01909   1 LRKLREILKELFPVAEVVLFGSYARGTALPGSDIDLLVV--FPEPVEEERLLKLAKIIKELEELLGlEVDLVTREKIEFP 78


                  ...
gi 1371371789 159 REK 161
Cdd:pfam01909  79 LVK 81
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 81-149 6.86e-05

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 41.77  E-value: 6.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371371789  81 QRVVDRLVEAV---DPAA-ILLFGSRAKGTVRSDSDVDLCVIadLDGPRRDRRAHLRQLLRpLIRKVDAPVDV 149
Cdd:cd05402     3 EEVLDRLQELIkewFPGAkLYPFGSYVTGLGLPGSDIDLCLL--GPNHRVDREDFLRKLAK-LLKKSGEVVEV 72
NT_2-5OAS_ClassI-CCAase cd05400
Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class ...
 74-137 1.14e-03

Nucleotidyltransferase (NT) domain of 2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I CCA-adding enzyme; In vertebrates, 2-5OASs are induced by interferon during the innate immune response to protect against RNA virus infections. In the presence of an RNA activator, 2-5OASs catalyze the oligomerization of ATP into 2-5A. 2-5A activates endoribonuclease L, which leads to degradation of the viral RNA. 2-5OASs are also implicated in cell growth control, differentiation, and apoptosis. This family includes human OAS1, -2, -3, and OASL. CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This class I group includes the archaeal Sulfolobus shibatae and Archeoglobus fulgidus CCA-adding enzymes. It belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this family.


Pssm-ID: 143390 [Multi-domain]  Cd Length: 143  Bit Score: 38.53  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371371789  74 EIEDALLQRVVDRLVEAVDPAA-----ILLFGSRAKGT-VRSDSDVDL-CVIADLDGPRRDRRAHLRQLLR 137
Cdd:cd05400     3 EEAKERYREIREALKESLSELAgrvaeVFLQGSYARGTaLRGDSDIDLvVVLPDDTSFAEYGPAELLDELG 73
 
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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