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Conserved domains on  [gi|489863325|ref|WP_003766938|]
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bis(5'-nucleosyl)-tetraphosphatase (symmetrical) YqeK [Listeria innocua]

Protein Classification

HD domain-containing protein( domain architecture ID 10004362)

HD domain-containing protein similar to Bacillus subtilis YqeK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeK COG1713
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ...
 1-183 4.20e-93

Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only];


:

Pssm-ID: 441319 [Multi-domain]  Cd Length: 184  Bit Score: 268.91  E-value: 4.20e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   1 MERNEVLKKVEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFD-PRLLQFHR 79
Cdd:COG1713    1 MDREEILEKLKERLSPKRYEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEELLELAKEYGLDlDELEEYNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  80 SLWHAPVGAYLAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLALKSLDAAMLFALSN 159
Cdd:COG1713   81 ELLHGPVGAYLAKEEFGITDEEILNAIRYHTTGRPNMSLLEKIIFLADYIEPGRDFPGVEELRKLAKQDLDEAVLEALDN 160

                        170       180
                 ....*....|....*....|....
gi 489863325 160 TITYLIKKQQSVFPDTLDAYNYFV 183
Cdd:COG1713  161 TIKYLIEKGRLIHPRTIEARNYLL 184
 
Name Accession Description Interval E-value
YqeK COG1713
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ...
 1-183 4.20e-93

Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441319 [Multi-domain]  Cd Length: 184  Bit Score: 268.91  E-value: 4.20e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   1 MERNEVLKKVEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFD-PRLLQFHR 79
Cdd:COG1713    1 MDREEILEKLKERLSPKRYEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEELLELAKEYGLDlDELEEYNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  80 SLWHAPVGAYLAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLALKSLDAAMLFALSN 159
Cdd:COG1713   81 ELLHGPVGAYLAKEEFGITDEEILNAIRYHTTGRPNMSLLEKIIFLADYIEPGRDFPGVEELRKLAKQDLDEAVLEALDN 160

                        170       180
                 ....*....|....*....|....
gi 489863325 160 TITYLIKKQQSVFPDTLDAYNYFV 183
Cdd:COG1713  161 TIKYLIEKGRLIHPRTIEARNYLL 184
TIGR00488 TIGR00488
putative HD superfamily hydrolase of NAD metabolism; The function of this protein family is ...
 10-166 3.58e-43

putative HD superfamily hydrolase of NAD metabolism; The function of this protein family is unknown. Members of this family of uncharacterized proteins from the Mycoplasmas are longer at the amino end, fused to a region of nicotinamide nucleotide adenylyltransferase, an NAD salvage biosynthesis enzyme. Members are putative metal-dependent phosphohydrolases for NAD metabolism. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273103 [Multi-domain]  Cd Length: 158  Bit Score: 141.47  E-value: 3.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   10 VEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFDPRLLQFHRSLWHAPVGAY 89
Cdd:TIGR00488   1 LKQQLDEHRYQHCLGVGQTAKQLAEANKLDSKKAEIAGAYHDLAKFLPKEQLKQIAKREKMPAHLLYPSPKLLHAYVGAY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489863325   90 LAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRT-FPGVYKARRLALKSLDAAMLFALSNTITYLIK 166
Cdd:TIGR00488  81 ILKREFGVQDEDILDAIRNHTSGPPGMSLLDMIIYVADKLEPNRGaGIEIDELRKLAKTDLKQAYIITLKYTMVLLKK 158
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
4-165 4.17e-39

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 136.23  E-value: 4.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   4 NEVLKKVeeaMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFDPRLLQFHrsLWH 83
Cdd:PRK07152 186 EDILKSF---LDEYRYKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDEEKHRKFLKKYLKDVKNLPWY--VLH 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  84 APVGAYLAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLALKSLDAAMLFALSNTITY 163
Cdd:PRK07152 261 QYVGALWLKHVYGIDDEEILNAIRNHTSLAEEMSTLDKIVYVADKIEPGRKYIGIQKLRKLAFKDLDEAFKEVLKYQYEL 340


                 ..
gi 489863325 164 LI 165
Cdd:PRK07152 341 IK 342
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 18-132 2.50e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 55.32  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   18 RFKHTLGVEKAAIELAEHY-HMDVEKARITALLHDYAKYYEDDKArkiiedegfdprlLQFHRSLWHAPVGAYLAEKEFG 96
Cdd:pfam01966   1 RLEHSLRVALLARELAEELgELDRELLLLAALLHDIGKGPFGDEK-------------PEFEIFLGHAVVGAEILRELEK 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489863325   97 ITDPE-ILEAIRLHTTGSGAM------SDFDKLIYLADYTEPG 132
Cdd:pfam01966  68 RLGLEdVLKLILEHHESWEGAgypeeiSLEARIVKLADRLDAL 110
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 17-146 1.88e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  17 SRFKHTLGVEKAAIELAEHYHM---DVEKARITALLHDYAKYYEDDKARKIIEDEGFDprllqfhrslwHAPVGAYLA-- 91
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLseeDIELLRLAALLHDIGKPGTPDAITEEESELEKD-----------HAIVGAEILre 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489863325  92 ---EKEFGITDPEILEAIRLHTT-----------GSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLAL 146
Cdd:cd00077   71 lllEEVIKLIDELILAVDASHHErldglgypdglKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 17-134 4.88e-06

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 44.21  E-value: 4.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325    17 SRFKHTLGVEKAAIELAEHY-HMDVEKARITALLHDYAKYYEDDKARKIIEDEgfdprllqfhrsLWHAPVGAYLAEKEF 95
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELgLLDIELLLLAALLHDIGKPGTPDSFLVKTSVL------------EDHHFIGAEILLEEE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 489863325    96 G--ITDPEILEAIRLHTTGSG-----AMSDFDKLIYLADYTEPGRT 134
Cdd:smart00471  72 EprILEEILRTAILSHHERPDglrgePITLEARIVKVADRLDALRA 117
 
Name Accession Description Interval E-value
YqeK COG1713
Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal ...
 1-183 4.20e-93

Diadenosine tetraphosphatase YqeK or a related HD superfamily phosphohydrolase [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441319 [Multi-domain]  Cd Length: 184  Bit Score: 268.91  E-value: 4.20e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   1 MERNEVLKKVEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFD-PRLLQFHR 79
Cdd:COG1713    1 MDREEILEKLKERLSPKRYEHTLGVAETAVELAERYGVDVEKAELAGLLHDYAKELPPEELLELAKEYGLDlDELEEYNP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  80 SLWHAPVGAYLAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLALKSLDAAMLFALSN 159
Cdd:COG1713   81 ELLHGPVGAYLAKEEFGITDEEILNAIRYHTTGRPNMSLLEKIIFLADYIEPGRDFPGVEELRKLAKQDLDEAVLEALDN 160

                        170       180
                 ....*....|....*....|....
gi 489863325 160 TITYLIKKQQSVFPDTLDAYNYFV 183
Cdd:COG1713  161 TIKYLIEKGRLIHPRTIEARNYLL 184
TIGR00488 TIGR00488
putative HD superfamily hydrolase of NAD metabolism; The function of this protein family is ...
 10-166 3.58e-43

putative HD superfamily hydrolase of NAD metabolism; The function of this protein family is unknown. Members of this family of uncharacterized proteins from the Mycoplasmas are longer at the amino end, fused to a region of nicotinamide nucleotide adenylyltransferase, an NAD salvage biosynthesis enzyme. Members are putative metal-dependent phosphohydrolases for NAD metabolism. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273103 [Multi-domain]  Cd Length: 158  Bit Score: 141.47  E-value: 3.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   10 VEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFDPRLLQFHRSLWHAPVGAY 89
Cdd:TIGR00488   1 LKQQLDEHRYQHCLGVGQTAKQLAEANKLDSKKAEIAGAYHDLAKFLPKEQLKQIAKREKMPAHLLYPSPKLLHAYVGAY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489863325   90 LAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRT-FPGVYKARRLALKSLDAAMLFALSNTITYLIK 166
Cdd:TIGR00488  81 ILKREFGVQDEDILDAIRNHTSGPPGMSLLDMIIYVADKLEPNRGaGIEIDELRKLAKTDLKQAYIITLKYTMVLLKK 158
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
4-165 4.17e-39

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 136.23  E-value: 4.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   4 NEVLKKVeeaMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDKARKIIEDEGFDPRLLQFHrsLWH 83
Cdd:PRK07152 186 EDILKSF---LDEYRYKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDEEKHRKFLKKYLKDVKNLPWY--VLH 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  84 APVGAYLAEKEFGITDPEILEAIRLHTTGSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLALKSLDAAMLFALSNTITY 163
Cdd:PRK07152 261 QYVGALWLKHVYGIDDEEILNAIRNHTSLAEEMSTLDKIVYVADKIEPGRKYIGIQKLRKLAFKDLDEAFKEVLKYQYEL 340


                 ..
gi 489863325 164 LI 165
Cdd:PRK07152 341 IK 342
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 18-132 2.50e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 55.32  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   18 RFKHTLGVEKAAIELAEHY-HMDVEKARITALLHDYAKYYEDDKArkiiedegfdprlLQFHRSLWHAPVGAYLAEKEFG 96
Cdd:pfam01966   1 RLEHSLRVALLARELAEELgELDRELLLLAALLHDIGKGPFGDEK-------------PEFEIFLGHAVVGAEILRELEK 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489863325   97 ITDPE-ILEAIRLHTTGSGAM------SDFDKLIYLADYTEPG 132
Cdd:pfam01966  68 RLGLEdVLKLILEHHESWEGAgypeeiSLEARIVKLADRLDAL 110
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 17-146 1.88e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  17 SRFKHTLGVEKAAIELAEHYHM---DVEKARITALLHDYAKYYEDDKARKIIEDEGFDprllqfhrslwHAPVGAYLA-- 91
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGLseeDIELLRLAALLHDIGKPGTPDAITEEESELEKD-----------HAIVGAEILre 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489863325  92 ---EKEFGITDPEILEAIRLHTT-----------GSGAMSDFDKLIYLADYTEPGRTFPGVYKARRLAL 146
Cdd:cd00077   71 lllEEVIKLIDELILAVDASHHErldglgypdglKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
20-128 2.99e-07

HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 48.81  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325  20 KHTLGVEKAAIELAEHYHM-DVEKARITALLHDYAK----YYEDDKARKIIED-EGFDPRLLQFHRSL---WHAPVGAYL 90
Cdd:COG1639  107 RHSLAVAAAARALARRLGLlDPEEAFLAGLLHDIGKlvllSLFPEEYAELLALaEADGLSLAEAEREVlgtDHAELGAAL 186

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489863325  91 AEK-EFgitDPEILEAIRLHTTGSGAMSDFD--KLIYLADY 128
Cdd:COG1639  187 ARKwGL---PEELVEAIRYHHDPEAAGEHRRlaALVHLANR 224
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 17-134 4.88e-06

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 44.21  E-value: 4.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325    17 SRFKHTLGVEKAAIELAEHY-HMDVEKARITALLHDYAKYYEDDKARKIIEDEgfdprllqfhrsLWHAPVGAYLAEKEF 95
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELgLLDIELLLLAALLHDIGKPGTPDSFLVKTSVL------------EDHHFIGAEILLEEE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 489863325    96 G--ITDPEILEAIRLHTTGSG-----AMSDFDKLIYLADYTEPGRT 134
Cdd:smart00471  72 EprILEEILRTAILSHHERPDglrgePITLEARIVKVADRLDALRA 117
HDOD pfam08668
HDOD domain;
21-109 9.11e-06

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 44.14  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   21 HTLGVEKAAIELAEHYHMDV-EKARITALLHD-----YAKYYEDD--KARKIIEDEGFdpRLLQFHRSLW---HAPVGAY 89
Cdd:pfam08668  98 HSLACALAARLLARRLGLDDpEEAFLAGLLHDigkliLLSLLPDKyeELLEKAAEEGI--SLLEAERELLgtdHAEVGAA 175

                          90       100
                  ....*....|....*....|.
gi 489863325   90 LAEK-EFgitDPEILEAIRLH 109
Cdd:pfam08668 176 LLERwNL---PEELVEAIAYH 193
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 5-72 3.35e-05

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 42.58  E-value: 3.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489863325   5 EVLKKVEEAMPTSRFKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYED-----------DKARKIIEDEGFDP 72
Cdd:COG1418    6 KLVKYLRTSYGQHDLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHevegshaeigaELARKYLESLGFPE 84
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 19-109 1.73e-03

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 35.77  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489863325   19 FKHTLGVEKAAIELAEHYHMDVEKARITALLHDYAKYYEDDkaRKIIEDegfdprllqfhrslwHAPVGAYLAEKeFGIt 98
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELGLDVELARRGALLHDIGKPITRE--GVIFES---------------HVVVGAEIARK-YGE- 66

                          90
                  ....*....|.
gi 489863325   99 DPEILEAIRLH 109
Cdd:TIGR00277  67 PLEVIDIIAEH 77
 
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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