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Conserved domains on  [gi|355433155|gb|AER92609|]
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dextransucrase, partial [Leuconostoc mesenteroides]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_70 super family cl27864
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ...
 229-592 6.45e-161

Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.


The actual alignment was detected with superfamily member pfam02324:

Pssm-ID: 426720 [Multi-domain]  Cd Length: 831  Bit Score: 480.71  E-value: 6.45e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  229 LLMTWWPDKATQVNYLNAMKYlDATETETVYTSDDSQDALNKAAQNIQVKIEEKISQEGQTQWLKDDISKFVDSQSNWNI 308
Cdd:pfam02324   1 LLMSWWPDKETQIAYLNYMNA-QGGGNGENYDADSNQEQLNIAAATIQAKIEAKISQLKNTDWLRDIINAFVKTQPAWNS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  309 ASESKGT----DHLQGGALLYVN-SDKTPDANSDYRLLNRTPTNQTG--TPLYT---TDPTQGGYDFLLANDVDNSNPVV 378
Cdd:pfam02324  80 DSEKDTSagedDHLQGGALLYDNeGDKTAYANSDYRILNRTPTNQTGkkDPKYFadnSDNTIGGYDFLLANDIDNSNPVV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  379 QAEQLNWMYYLLNFGSITNNDAEANFDSIRVDAVDNVDADLLQIAADYFKAAYGVDKSDAISNQHVSILEDWSDNDAEYV 458
Cdd:pfam02324 160 QAEQLNWLHFLMNFGNIVANDPDANFDGIRVDAVDNVDADLLQIAGDYLKAAKGIDKNDKAAIDHLSILEAWSDNDPPYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  459 KDNGDNQLSMDNKLRLSLKYSLTMPAVDQYGNK---RSGLEPFLTNSLVDRTNDSTDNTAQPNYSFVRAHDSEVQTVIAE 535
Cdd:pfam02324 240 HDDGDAMINIDNKLRLSLLFALAKPLEKDASNKleiRSGLEPLITNSLNNRSADGAESAAMANYIFIRAHDSEVQDLIAD 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 355433155  536 IIKQRIDPDSDGLSPTMDQLTEAFKIYNADQLKTDKEFTQYNIPSTYATILTNKDTV 592
Cdd:pfam02324 320 IIKAEINPKTDGLSFTLDEIKKAFEIYNEDLLAAEKKYTHSNIALAYALLLSNKDSI 376
glucan_65_rpt super family cl37372
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ...
 122-166 9.67e-07

glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.


The actual alignment was detected with superfamily member TIGR04035:

Pssm-ID: 274933 [Multi-domain]  Cd Length: 62  Bit Score: 45.97  E-value: 9.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 355433155  122 LKTIDGKTYYYDDDD-QVKKNFATvIDGKVLYFDKETGALAdTNDY 166
Cdd:TIGR04035  13 AQTIDGVTYYFDENGkQVKGDFVT-NGGGTYYYDKDSGALV-TNRF 56
 
Name Accession Description Interval E-value
Glyco_hydro_70 pfam02324
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ...
 229-592 6.45e-161

Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.


Pssm-ID: 426720 [Multi-domain]  Cd Length: 831  Bit Score: 480.71  E-value: 6.45e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  229 LLMTWWPDKATQVNYLNAMKYlDATETETVYTSDDSQDALNKAAQNIQVKIEEKISQEGQTQWLKDDISKFVDSQSNWNI 308
Cdd:pfam02324   1 LLMSWWPDKETQIAYLNYMNA-QGGGNGENYDADSNQEQLNIAAATIQAKIEAKISQLKNTDWLRDIINAFVKTQPAWNS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  309 ASESKGT----DHLQGGALLYVN-SDKTPDANSDYRLLNRTPTNQTG--TPLYT---TDPTQGGYDFLLANDVDNSNPVV 378
Cdd:pfam02324  80 DSEKDTSagedDHLQGGALLYDNeGDKTAYANSDYRILNRTPTNQTGkkDPKYFadnSDNTIGGYDFLLANDIDNSNPVV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  379 QAEQLNWMYYLLNFGSITNNDAEANFDSIRVDAVDNVDADLLQIAADYFKAAYGVDKSDAISNQHVSILEDWSDNDAEYV 458
Cdd:pfam02324 160 QAEQLNWLHFLMNFGNIVANDPDANFDGIRVDAVDNVDADLLQIAGDYLKAAKGIDKNDKAAIDHLSILEAWSDNDPPYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  459 KDNGDNQLSMDNKLRLSLKYSLTMPAVDQYGNK---RSGLEPFLTNSLVDRTNDSTDNTAQPNYSFVRAHDSEVQTVIAE 535
Cdd:pfam02324 240 HDDGDAMINIDNKLRLSLLFALAKPLEKDASNKleiRSGLEPLITNSLNNRSADGAESAAMANYIFIRAHDSEVQDLIAD 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 355433155  536 IIKQRIDPDSDGLSPTMDQLTEAFKIYNADQLKTDKEFTQYNIPSTYATILTNKDTV 592
Cdd:pfam02324 320 IIKAEINPKTDGLSFTLDEIKKAFEIYNEDLLAAEKKYTHSNIALAYALLLSNKDSI 376
glucan_65_rpt TIGR04035
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ...
 122-166 9.67e-07

glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.


Pssm-ID: 274933 [Multi-domain]  Cd Length: 62  Bit Score: 45.97  E-value: 9.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 355433155  122 LKTIDGKTYYYDDDD-QVKKNFATvIDGKVLYFDKETGALAdTNDY 166
Cdd:TIGR04035  13 AQTIDGVTYYFDENGkQVKGDFVT-NGGGTYYYDKDSGALV-TNRF 56
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 122-161 1.17e-05

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 42.53  E-value: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 355433155  122 LKTIDGKTYYYDDD-DQVKKNFATvIDGKVLYFDKETGALA 161
Cdd:pfam19127   4 WQTINGQTLYFDSDgKQVKGWVVT-IDGKWYYFDADSGEMV 43
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 361-418 1.55e-04

Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 44.43  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 355433155 361 GGYDFLLANDVDNSNPVVQAEQLNWMYYLLNfgsitnndaEANFDSIRVDAVDNVDAD 418
Cdd:cd11318  191 GNYDYLMGADIDYSNPEVREELKRWGKWYIN---------TTGLDGFRLDAVKHISAS 239
PLN00196 PLN00196
alpha-amylase; Provisional
 284-452 2.07e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 40.67  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155 284 SQEGQTQWLKDDISKFVDS--QSNWNIASESKGTDHLQGGALLYVNSDKTPDANSDY--RLLNRTPT---NQTGTPlytt 356
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKgvQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWgpHMICRDDTqysDGTGNL---- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155 357 dptQGGYDFLLANDVDNSNPVVQAEQLNWMYYLlnfgsitnnDAEANFDSIRVDAVDNVDADLLQIAAD----------- 425
Cdd:PLN00196 162 ---DTGADFAAAPDIDHLNKRVQRELIGWLLWL---------KSDIGFDAWRLDFAKGYSAEVAKVYIDgtepsfavaei 229

                        170       180
                 ....*....|....*....|....*...
gi 355433155 426 YFKAAYGVD-KSDAISNQHVSILEDWSD 452
Cdd:PLN00196 230 WTSMAYGGDgKPEYDQNAHRQELVNWVD 257
 
Name Accession Description Interval E-value
Glyco_hydro_70 pfam02324
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ...
 229-592 6.45e-161

Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.


Pssm-ID: 426720 [Multi-domain]  Cd Length: 831  Bit Score: 480.71  E-value: 6.45e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  229 LLMTWWPDKATQVNYLNAMKYlDATETETVYTSDDSQDALNKAAQNIQVKIEEKISQEGQTQWLKDDISKFVDSQSNWNI 308
Cdd:pfam02324   1 LLMSWWPDKETQIAYLNYMNA-QGGGNGENYDADSNQEQLNIAAATIQAKIEAKISQLKNTDWLRDIINAFVKTQPAWNS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  309 ASESKGT----DHLQGGALLYVN-SDKTPDANSDYRLLNRTPTNQTG--TPLYT---TDPTQGGYDFLLANDVDNSNPVV 378
Cdd:pfam02324  80 DSEKDTSagedDHLQGGALLYDNeGDKTAYANSDYRILNRTPTNQTGkkDPKYFadnSDNTIGGYDFLLANDIDNSNPVV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  379 QAEQLNWMYYLLNFGSITNNDAEANFDSIRVDAVDNVDADLLQIAADYFKAAYGVDKSDAISNQHVSILEDWSDNDAEYV 458
Cdd:pfam02324 160 QAEQLNWLHFLMNFGNIVANDPDANFDGIRVDAVDNVDADLLQIAGDYLKAAKGIDKNDKAAIDHLSILEAWSDNDPPYL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155  459 KDNGDNQLSMDNKLRLSLKYSLTMPAVDQYGNK---RSGLEPFLTNSLVDRTNDSTDNTAQPNYSFVRAHDSEVQTVIAE 535
Cdd:pfam02324 240 HDDGDAMINIDNKLRLSLLFALAKPLEKDASNKleiRSGLEPLITNSLNNRSADGAESAAMANYIFIRAHDSEVQDLIAD 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 355433155  536 IIKQRIDPDSDGLSPTMDQLTEAFKIYNADQLKTDKEFTQYNIPSTYATILTNKDTV 592
Cdd:pfam02324 320 IIKAEINPKTDGLSFTLDEIKKAFEIYNEDLLAAEKKYTHSNIALAYALLLSNKDSI 376
glucan_65_rpt TIGR04035
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ...
 122-166 9.67e-07

glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.


Pssm-ID: 274933 [Multi-domain]  Cd Length: 62  Bit Score: 45.97  E-value: 9.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 355433155  122 LKTIDGKTYYYDDDD-QVKKNFATvIDGKVLYFDKETGALAdTNDY 166
Cdd:TIGR04035  13 AQTIDGVTYYFDENGkQVKGDFVT-NGGGTYYYDKDSGALV-TNRF 56
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 122-161 1.17e-05

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 42.53  E-value: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 355433155  122 LKTIDGKTYYYDDD-DQVKKNFATvIDGKVLYFDKETGALA 161
Cdd:pfam19127   4 WQTINGQTLYFDSDgKQVKGWVVT-IDGKWYYFDADSGEMV 43
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 361-418 1.55e-04

Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.


Pssm-ID: 200457 [Multi-domain]  Cd Length: 391  Bit Score: 44.43  E-value: 1.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 355433155 361 GGYDFLLANDVDNSNPVVQAEQLNWMYYLLNfgsitnndaEANFDSIRVDAVDNVDAD 418
Cdd:cd11318  191 GNYDYLMGADIDYSNPEVREELKRWGKWYIN---------TTGLDGFRLDAVKHISAS 239
PLN00196 PLN00196
alpha-amylase; Provisional
 284-452 2.07e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 40.67  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155 284 SQEGQTQWLKDDISKFVDS--QSNWNIASESKGTDHLQGGALLYVNSDKTPDANSDY--RLLNRTPT---NQTGTPlytt 356
Cdd:PLN00196  86 SKYGNEAQLKSLIEAFHGKgvQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWgpHMICRDDTqysDGTGNL---- 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 355433155 357 dptQGGYDFLLANDVDNSNPVVQAEQLNWMYYLlnfgsitnnDAEANFDSIRVDAVDNVDADLLQIAAD----------- 425
Cdd:PLN00196 162 ---DTGADFAAAPDIDHLNKRVQRELIGWLLWL---------KSDIGFDAWRLDFAKGYSAEVAKVYIDgtepsfavaei 229

                        170       180
                 ....*....|....*....|....*...
gi 355433155 426 YFKAAYGVD-KSDAISNQHVSILEDWSD 452
Cdd:PLN00196 230 WTSMAYGGDgKPEYDQNAHRQELVNWVD 257
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 357-418 3.44e-03

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 40.26  E-value: 3.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 355433155 357 DPTQGGYDFLLANDVDNSNPVVQAEQLNWMYYLLNfgsitnndaEANFDSIRVDAVDNVDAD 418
Cdd:PRK09441 189 DDENGNFDYLMGADIDFRHPEVREELKYWAKWYME---------TTGFDGFRLDAVKHIDAW 241
 
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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