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Conserved domains on  [gi|187609229|pdb|2Z0B|E]
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Chain E, Putative glycerophosphodiester phosphodiesterase 5

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 10-125 2.36e-54

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


:

Pssm-ID: 99888  Cd Length: 120  Bit Score: 165.96  E-value: 2.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E       10 QVAFEIRG-TLLPGEVFAICGSCDALGNWNPQNAVALLPENDtgES*LWKATIVLSRGVSVQYRYFKGYFLepkTIGGPC 88
Cdd:cd05814   2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                        90       100       110
                ....*....|....*....|....*....|....*..
2Z0B_E       89 QVIVHKWETHLQPRSITPLESEIIIDDGQFGIHNGVE 125
Cdd:cd05814  77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVE 113
 
Name Accession Description Interval E-value
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 10-125 2.36e-54

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 165.96  E-value: 2.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E       10 QVAFEIRG-TLLPGEVFAICGSCDALGNWNPQNAVALLPENDtgES*LWKATIVLSRGVSVQYRYFKGYFLepkTIGGPC 88
Cdd:cd05814   2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                        90       100       110
                ....*....|....*....|....*....|....*..
2Z0B_E       89 QVIVHKWETHLQPRSITPLESEIIIDDGQFGIHNGVE 125
Cdd:cd05814  77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVE 113
CBM_2 smart01065
Starch binding domain;
10-106 2.55e-24

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 88.94  E-value: 2.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E          10 QVAFEIRGTLL-PGEVFAICGSCDALGNWNPQNAVALlpENDTGES*LWKATI-VLSRGVSVQYRYFKGYFLEpktiggp 87
Cdd:smart01065   2 SVTFKVRNGYTqPGESVYVVGSVPELGNWNPKKAVPL--SPDTDGYPLWKGTVsLPPAGTTIEYKYVKVDEDG------- 72

                           90
                   ....*....|....*....
2Z0B_E          88 cqviVHKWETHLQPRSITP 106
Cdd:smart01065  73 ----SVTWESGPNRRLTVP 87
CBM_20 pfam00686
Starch binding domain;
10-75 4.44e-13

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 60.38  E-value: 4.44e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2Z0B_E         10 QVAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALLPENDTGES*LWKATIVLSRGVSVQYRYFK 75
Cdd:pfam00686   2 SVTFNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSYP-LWSGTVSLPAGTTIEYKYIK 66
PLN02950 PLN02950
4-alpha-glucanotransferase
 22-74 3.52e-06

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 44.71  E-value: 3.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
2Z0B_E        22 GEVFAICGSCDALGNWNPQNAVALLPENDtGES*LWKATIVLSRGVSVQYRYF 74
Cdd:PLN02950  22 GQSLLVCGSEPLLGSWNVKKGLLLSPVHQ-GDELVWEGSVSVPEGFSCEYSYY 73
 
Name Accession Description Interval E-value
CBM20_Prei4 cd05814
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ...
 10-125 2.36e-54

Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99888  Cd Length: 120  Bit Score: 165.96  E-value: 2.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E       10 QVAFEIRG-TLLPGEVFAICGSCDALGNWNPQNAVALLPENDtgES*LWKATIVLSRGVSVQYRYFKGYFLepkTIGGPC 88
Cdd:cd05814   2 RVTFRVFAsELAPGEVVAVVGSLPVLGNWQPEKAVPLEKEDD--DCNLWKASIELPRGVDFQYRYFVAVVL---NDSGPC 76

                        90       100       110
                ....*....|....*....|....*....|....*..
2Z0B_E       89 QVIVHKWETHLQPRSITPLESEIIIDDGQFGIHNGVE 125
Cdd:cd05814  77 QVIVRKWETHLQPRSIKPLEEERLNDDDKFGIYDGVE 113
CBM_2 smart01065
Starch binding domain;
10-106 2.55e-24

Starch binding domain;


Pssm-ID: 215006 [Multi-domain]  Cd Length: 88  Bit Score: 88.94  E-value: 2.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E          10 QVAFEIRGTLL-PGEVFAICGSCDALGNWNPQNAVALlpENDTGES*LWKATI-VLSRGVSVQYRYFKGYFLEpktiggp 87
Cdd:smart01065   2 SVTFKVRNGYTqPGESVYVVGSVPELGNWNPKKAVPL--SPDTDGYPLWKGTVsLPPAGTTIEYKYVKVDEDG------- 72

                           90
                   ....*....|....*....
2Z0B_E          88 cqviVHKWETHLQPRSITP 106
Cdd:smart01065  73 ----SVTWESGPNRRLTVP 87
CBM20 cd05467
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ...
 10-116 4.01e-19

The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 119437  Cd Length: 96  Bit Score: 75.80  E-value: 4.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0B_E       10 QVAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALLPENdtgES*LWKATIVL--SRGVSVQYRYFKGYflepktiggp 87
Cdd:cd05467   1 QVRFQVRCTTQFGQSVYVVGSHPELGNWDPAKALRLNTSN---SYPLWTGEIPLpaPEGQVIEYKYVIVD---------- 67

                        90       100       110
                ....*....|....*....|....*....|.
2Z0B_E       88 cQVIVHKWETHlQPRSI-TP-LESEIIIDDG 116
Cdd:cd05467  68 -DDGNVQWESG-SNRVLtVPsTSSLIVVDDW 96
CBM20_DSP cd05817
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 10-84 5.39e-14

Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99891  Cd Length: 100  Bit Score: 62.88  E-value: 5.39e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2Z0B_E       10 QVAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVAL-LPENDtges*LWKATIVLSRGVSVQYRYFKGYFLEPKTI 84
Cdd:cd05817   1 MVTFKIHYPTQFGEAVYISGNCNQLGNWNPSKAKRMqWNEGD-----LWTVDVGIPESVYIEYKYFVSNYDDPNTV 71
CBM20_glucoamylase cd05811
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ...
 11-75 1.64e-13

Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99886 [Multi-domain]  Cd Length: 106  Bit Score: 61.90  E-value: 1.64e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2Z0B_E       11 VAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALLPENDTGES*LWKATIVLSRGVSVQYRYFK 75
Cdd:cd05811   9 VTFNERVTTSYGENIKIVGSIPQLGNWDTSSAVALSASQYTSSNPLWSVTIPLPAGTSFEYKFIR 73
CBM_20 pfam00686
Starch binding domain;
10-75 4.44e-13

Starch binding domain;


Pssm-ID: 425821 [Multi-domain]  Cd Length: 95  Bit Score: 60.38  E-value: 4.44e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2Z0B_E         10 QVAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALLPENDTGES*LWKATIVLSRGVSVQYRYFK 75
Cdd:pfam00686   2 SVTFNVNATTQYGQSVYIVGSIPELGNWNPKKAIALSASEYSSYP-LWSGTVSLPAGTTIEYKYIK 66
CBM20_alpha_amylase cd05808
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ...
 11-75 3.83e-11

Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99883  Cd Length: 95  Bit Score: 55.45  E-value: 3.83e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2Z0B_E       11 VAFEIRGTLLPGEVFAICGSCDALGNWNPQNAVALlpenDTGES*LWKATIVLSRGVSVQYRYFK 75
Cdd:cd05808   3 VTFNVTATTVWGQNVYVVGNVPELGNWSPANAVAL----SAATYPVWSGTVDLPAGTAIEYKYIK 63
CBM20_DPE2_repeat2 cd05816
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 10-75 2.99e-09

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99890  Cd Length: 99  Bit Score: 50.79  E-value: 2.99e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z0B_E       10 QVAFEIRGTLLP-GEVFAICGSCDALGNWNPQNAVALlpeNDTGES*LWKATIVLSR-GVSVQYRYFK 75
Cdd:cd05816   1 VVQFKILCPYVPkGQSVYVTGSSPELGNWDPQKALKL---SDVGFP-IWEADIDISKdSFPFEYKYII 64
PLN02950 PLN02950
4-alpha-glucanotransferase
 22-74 3.52e-06

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 44.71  E-value: 3.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
2Z0B_E        22 GEVFAICGSCDALGNWNPQNAVALLPENDtGES*LWKATIVLSRGVSVQYRYF 74
Cdd:PLN02950  22 GQSLLVCGSEPLLGSWNVKKGLLLSPVHQ-GDELVWEGSVSVPEGFSCEYSYY 73
CBM20_DPE2_repeat1 cd05815
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ...
 22-74 3.56e-06

Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 starch binding domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal carbohydrate-binding domains. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99889  Cd Length: 101  Bit Score: 42.82  E-value: 3.56e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
2Z0B_E       22 GEVFAICGSCDALGNWNPQNAVALLPENDtGES*LWKATIVLSRGVSVQYRYF 74
Cdd:cd05815  13 GQSLLICGSDPLLGSWNVKKGLLLKPSHQ-GDVLVWSGSISVPPGFSSEYNYY 64
PLN02950 PLN02950
4-alpha-glucanotransferase
 11-75 1.42e-05

4-alpha-glucanotransferase


Pssm-ID: 215512 [Multi-domain]  Cd Length: 909  Bit Score: 43.17  E-value: 1.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2Z0B_E        11 VAFEIRGT-LLPGEVFAICGSCDALGNWNPQNAVALlpeNDTGES*LWKATIVLSRG-VSVQYRYFK 75
Cdd:PLN02950 155 VRFKIACPrLEEGTSVYVTGSIAQLGNWQVDDGLKL---NYTGDS-IWEADCLVPKSdFPIKYKYAL 217
CBM20_alpha_MTH cd05810
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ...
 24-75 1.20e-03

Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.


Pssm-ID: 99885  Cd Length: 97  Bit Score: 35.85  E-value: 1.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
2Z0B_E       24 VFAIcGSCDALGNWNPQNAVALLPENDTges*LWKATIVLSRGVSVQYRYFK 75
Cdd:cd05810  18 VYVV-GNVPQLGNWSPADAVKLDPTAYP----TWSGSISLPASTNVEWKCLK 64
 
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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