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Conserved domains on  [gi|1420808876|gb|AXB22641|]
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alpha-amylase, partial [Amphilophus trimaculatus]

Protein Classification

alpha-amylase family protein( domain architecture ID 1562432)

alpha-amylase family protein may catalyze the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmyAc_family super family cl38930
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
 2-156 1.13e-63

Alpha amylase catalytic domain family; 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; and 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 this 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.


The actual alignment was detected with superfamily member cd11317:

Pssm-ID: 476817 [Multi-domain]  Cd Length: 329  Bit Score: 197.79  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876   2 AAECERFLGPKGFGGVQISPPNDHILvnSPWRPWWQRYQPISYDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMCg 81
Cdd:cd11317    16 AKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMA- 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420808876  82 sgggsgthsscgnwfnagseefpsvpfskldfndqkcktgsgeienyGDIYQVRDCRLVGLLDLALEKDYVRGKV 156
Cdd:cd11317    93 -----------------------------------------------GDANEVRNCELVGLADLNTESDYVRDKI 120
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 2-156 1.13e-63

Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 197.79  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876   2 AAECERFLGPKGFGGVQISPPNDHILvnSPWRPWWQRYQPISYDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMCg 81
Cdd:cd11317    16 AKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMA- 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420808876  82 sgggsgthsscgnwfnagseefpsvpfskldfndqkcktgsgeienyGDIYQVRDCRLVGLLDLALEKDYVRGKV 156
Cdd:cd11317    93 -----------------------------------------------GDANEVRNCELVGLADLNTESDYVRDKI 120
Aamy smart00642
Alpha-amylase domain;
2-80 9.20e-24

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 90.85  E-value: 9.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876    2 AAECErFLGPKGFGGVQISPPNDHILVnspwRPWWQRYQPISYDLC-SRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:smart00642  22 IEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVDAAHARGIKVILDVVINHTS 96
PLN02784 PLN02784
alpha-amylase
 13-80 2.39e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 48.85  E-value: 2.39e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1420808876  13 GFGGVQISPPNDHIlvnSPwrpwwQRYQPIS-YDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:PLN02784  534 GFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRC 594
 
Name Accession Description Interval E-value
AmyAc_bac_euk_AmyA cd11317
Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ...
 2-156 1.13e-63

Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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: 200456 [Multi-domain]  Cd Length: 329  Bit Score: 197.79  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876   2 AAECERFLGPKGFGGVQISPPNDHILvnSPWRPWWQRYQPISYDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMCg 81
Cdd:cd11317    16 AKECERFLGPAGYGGVQVSPPQEHIV--GPGRPWWERYQPVSYKLNSRSGTEAEFRDMVNRCNAAGVRVYVDAVINHMA- 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420808876  82 sgggsgthsscgnwfnagseefpsvpfskldfndqkcktgsgeienyGDIYQVRDCRLVGLLDLALEKDYVRGKV 156
Cdd:cd11317    93 -----------------------------------------------GDANEVRNCELVGLADLNTESDYVRDKI 120
AmyAc_bac1_AmyA cd11315
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ...
 13-155 1.31e-25

Alpha amylase catalytic domain found in bacterial 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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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: 200454 [Multi-domain]  Cd Length: 352  Bit Score: 99.66  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876  13 GFGGVQISPPNdHILVNSPWRP-WWQRYQPISYDLC-SRSGSEAELKDMITRCNNVGVNIYVDAVINHMcgsggGSGTHS 90
Cdd:cd11315    26 GYTAIQTSPPQ-KSKEGGNEGGnWWYRYQPTDYRIGnNQLGTEDDFKALCAAAHKYGIKIIVDVVFNHM-----ANEGSA 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420808876  91 SCGNWFNAGSEEFpsvpFSKLDFNDQKCktgsgeIENYGDIYQVRDCRLVGLLDLALEKDYVRGK 155
Cdd:cd11315   100 IEDLWYPSADIEL----FSPEDFHGNGG------ISNWNDRWQVTQGRLGGLPDLNTENPAVQQQ 154
Aamy smart00642
Alpha-amylase domain;
2-80 9.20e-24

Alpha-amylase domain;


Pssm-ID: 214758 [Multi-domain]  Cd Length: 166  Bit Score: 90.85  E-value: 9.20e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876    2 AAECErFLGPKGFGGVQISPPNDHILVnspwRPWWQRYQPISYDLC-SRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:smart00642  22 IEKLD-YLKDLGVTAIWLSPIFESPQG----YPSYHGYDISDYKQIdPRFGTMEDFKELVDAAHARGIKVILDVVINHTS 96
AmyAc_euk_AmyA cd11319
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ...
 13-153 2.18e-12

Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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: 200458 [Multi-domain]  Cd Length: 375  Bit Score: 63.35  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1420808876  13 GFGGVQISPPNDHILVNSPW----RPWWQryQPIsYDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMcgsgggsgt 88
Cdd:cd11319    56 GFDAIWISPIVKNIEGNTAYgeayHGYWA--QDL-YSLNPHFGTADDLKALSKALHKRGMYLMVDVVVNHM--------- 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1420808876  89 hsscgnwfnAGSEEFPSVPFSKLD-FNDQK-----CKtgsgeIENYGDIYQVRDCRL----VGLLDLALEKDYVR 153
Cdd:cd11319   124 ---------ASAGPGSDVDYSSFVpFNDSSyyhpyCW-----ITDYNNQTSVEDCWLgddvVALPDLNTENPFVV 184
AmyAc_arch_bac_plant_AmyA cd11314
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ...
 44-80 2.22e-08

Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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: 200453 [Multi-domain]  Cd Length: 302  Bit Score: 51.45  E-value: 2.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1420808876  44 YDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:cd11314    57 YDLNSRYGSEAELRSLIAALHAKGIKVIADIVINHRS 93
PLN02784 PLN02784
alpha-amylase
 13-80 2.39e-07

alpha-amylase


Pssm-ID: 215419 [Multi-domain]  Cd Length: 894  Bit Score: 48.85  E-value: 2.39e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1420808876  13 GFGGVQISPPNDHIlvnSPwrpwwQRYQPIS-YDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:PLN02784  534 GFTVVWLPPPTESV---SP-----EGYMPKDlYNLNSRYGTIDELKDLVKSFHEVGIKVLGDAVLNHRC 594
PRK09441 PRK09441
cytoplasmic alpha-amylase; Reviewed
 51-79 1.70e-04

cytoplasmic alpha-amylase; Reviewed


Pssm-ID: 236518 [Multi-domain]  Cd Length: 479  Bit Score: 40.64  E-value: 1.70e-04
                          10        20
                  ....*....|....*....|....*....
gi 1420808876  51 GSEAELKDMITRCNNVGVNIYVDAVINHM 79
Cdd:PRK09441   78 GTKEELLNAIDALHENGIKVYADVVLNHK 106
PLN00196 PLN00196
alpha-amylase; Provisional
 21-80 1.04e-03

alpha-amylase; Provisional


Pssm-ID: 165762 [Multi-domain]  Cd Length: 428  Bit Score: 38.36  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1420808876  21 PPNDHILVNspwrpwwQRYQPIS-YDL-CSRSGSEAELKDMITRCNNVGVNIYVDAVINHMC 80
Cdd:PLN00196   64 PPPSHSVSE-------QGYMPGRlYDLdASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRT 118
AmyAc_bac_fung_AmyA cd11318
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ...
 51-79 2.38e-03

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: 37.11  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|....*....
gi 1420808876  51 GSEAELKDMITRCNNVGVNIYVDAVINHM 79
Cdd:cd11318    76 GTKEELLEAIKALHENGIQVYADAVLNHK 104
PLN02361 PLN02361
alpha-amylase
 13-78 9.85e-03

alpha-amylase


Pssm-ID: 177990 [Multi-domain]  Cd Length: 401  Bit Score: 35.18  E-value: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1420808876  13 GFGGVQISPPNDHIlvnSPwrpwwQRYQPIS-YDLCSRSGSEAELKDMITRCNNVGVNIYVDAVINH 78
Cdd:PLN02361   42 GFTSAWLPPPSQSL---AP-----EGYLPQNlYSLNSAYGSEHLLKSLLRKMKQYNVRAMADIVINH 100
 
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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