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Conserved domains on  [gi|1600742754|gb|QBQ28316|]
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acyltransferase [Klebsiella pneumoniae]

Protein Classification

acyltransferase( domain architecture ID 10007154)

acyltransferase similar to Escherichia coli O-acetyltransferase WecH that catalyzes the acetylation of both cyclic ECA (ECA(CYC)) and phosphoglyceride-linked ECA (ECA(PG))

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
2-299 9.21e-42

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 148.21  E-value: 9.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   2 QEKIHWITNLRGIACMMVVMIHSTSWYITHPHAITLLQWDIANLLNSASRVSVPLFFMISGYLFFGERSAQPRHFW---- 77
Cdd:COG3274     6 KKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLLDRKKEDLKDFYkkrl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  78 -RIGLCIAFYSALSLLYITLFTHINVEL---SLKNLLQKPVFYHLWFFFAIAVIYLLSPLIQ--VKSTSSTMLLALMAIL 151
Cdd:COG3274    86 rRILIPLLFWSLIYLLFFTFLGGFSFNSlseFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRklVRKASKRELLYFLLLW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 152 GILANPNMVSVKAVGIEWLPVNLYINGdtfyYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHELRWRGD 231
Cdd:COG3274   166 LILSLLLPYLNTLLGIDLFFTLTLFLG----YLGYFLLGYYLARYKARLKKRRLIALLLFLVGLALTFLGTYLLSLQTGK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 232 FGDTWYLYCGPAVFVCAVTLLTLAKNWL--NARPLPGIACIARHSLGIYGFHALIVHALRASHLELSRWP 299
Cdd:COG3274   242 FNELFYSYLSPNVVLMSVALFLLLKNLSfrSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLGLNLLNIN 311
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
2-299 9.21e-42

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 148.21  E-value: 9.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   2 QEKIHWITNLRGIACMMVVMIHSTSWYITHPHAITLLQWDIANLLNSASRVSVPLFFMISGYLFFGERSAQPRHFW---- 77
Cdd:COG3274     6 KKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLLDRKKEDLKDFYkkrl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  78 -RIGLCIAFYSALSLLYITLFTHINVEL---SLKNLLQKPVFYHLWFFFAIAVIYLLSPLIQ--VKSTSSTMLLALMAIL 151
Cdd:COG3274    86 rRILIPLLFWSLIYLLFFTFLGGFSFNSlseFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRklVRKASKRELLYFLLLW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 152 GILANPNMVSVKAVGIEWLPVNLYINGdtfyYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHELRWRGD 231
Cdd:COG3274   166 LILSLLLPYLNTLLGIDLFFTLTLFLG----YLGYFLLGYYLARYKARLKKRRLIALLLFLVGLALTFLGTYLLSLQTGK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 232 FGDTWYLYCGPAVFVCAVTLLTLAKNWL--NARPLPGIACIARHSLGIYGFHALIVHALRASHLELSRWP 299
Cdd:COG3274   242 FNELFYSYLSPNVVLMSVALFLLLKNLSfrSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLGLNLLNIN 311
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
5-289 1.74e-17

Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyze the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans.


Pssm-ID: 426413 [Multi-domain]  Cd Length: 330  Bit Score: 81.83  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   5 IHWITNLRGIACMMVVMIHSTSWYITHPHAITLLQWDIanLLNSASRVSVPLFFMISGYLFFGERSAQP-------RHFW 77
Cdd:pfam01757   1 IAYLDLLRGIAILLVVIGHVLLAFGYGGFGLPLELALL--FLVFLGRFGVPLFFFISGYLLAALRRRRRslfkfikKRLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  78 RIGLCIAFYSALSLLYITLFTHINVELSLKNLLQ--------KPVFYHLWFFFAIAVIYLLSPLIQVKSTSSTMLLALMA 149
Cdd:pfam01757  79 RLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLlnngplffLGVNGHLWFLSALFVFYLLLPLLLRLLRKLKKSLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 150 ILGILANPNMVSVKAVGIEWLPVNLYINGDTFYYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHElrWR 229
Cdd:pfam01757 159 LLLLLLLFLLYILILLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIRSKRLKLLIIILLALALLALILLLLFLF--GL 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600742754 230 GDFGDTWYLYCGPAVFVCAVTLLTLAKNWLNARP--LPGIACIARHSLGIYGFHALIVHALR 289
Cdd:pfam01757 237 DPLALEFYGYPSLLLLLLGILLLLLLALLLANLRslRRLLSYLGKYSFGIYLIHPPILLLLG 298
 
Name Accession Description Interval E-value
WecH COG3274
Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];
2-299 9.21e-42

Surface polysaccharide O-acyltransferase WecH [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442505 [Multi-domain]  Cd Length: 345  Bit Score: 148.21  E-value: 9.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   2 QEKIHWITNLRGIACMMVVMIHSTSWYITHPHAITLLQWDIANLLNSASRVSVPLFFMISGYLFFGERSAQPRHFW---- 77
Cdd:COG3274     6 KKRIVYLDLLRVLAIFAVVLIHVTAPFVSSPGLIGSLNWWVANLLDSLSRFAVPLFFMISGALLLDRKKEDLKDFYkkrl 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  78 -RIGLCIAFYSALSLLYITLFTHINVEL---SLKNLLQKPVFYHLWFFFAIAVIYLLSPLIQ--VKSTSSTMLLALMAIL 151
Cdd:COG3274    86 rRILIPLLFWSLIYLLFFTFLGGFSFNSlseFLKNLLTGGVSYHLWFLYMIIGLYLFTPLLRklVRKASKRELLYFLLLW 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 152 GILANPNMVSVKAVGIEWLPVNLYINGdtfyYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHELRWRGD 231
Cdd:COG3274   166 LILSLLLPYLNTLLGIDLFFTLTLFLG----YLGYFLLGYYLARYKARLKKRRLIALLLFLVGLALTFLGTYLLSLQTGK 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 232 FGDTWYLYCGPAVFVCAVTLLTLAKNWL--NARPLPGIACIARHSLGIYGFHALIVHALRASHLELSRWP 299
Cdd:COG3274   242 FNELFYSYLSPNVVLMSVALFLLLKNLSfrSSKLSRLLSRLSKYSFGIYLIHPLVLDLLTKLGLNLLNIN 311
Acyl_transf_3 pfam01757
Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain ...
5-289 1.74e-17

Acyltransferase family; This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyze the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans.


Pssm-ID: 426413 [Multi-domain]  Cd Length: 330  Bit Score: 81.83  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   5 IHWITNLRGIACMMVVMIHSTSWYITHPHAITLLQWDIanLLNSASRVSVPLFFMISGYLFFGERSAQP-------RHFW 77
Cdd:pfam01757   1 IAYLDLLRGIAILLVVIGHVLLAFGYGGFGLPLELALL--FLVFLGRFGVPLFFFISGYLLAALRRRRRslfkfikKRLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  78 RIGLCIAFYSALSLLYITLFTHINVELSLKNLLQ--------KPVFYHLWFFFAIAVIYLLSPLIQVKSTSSTMLLALMA 149
Cdd:pfam01757  79 RLLIPYLLWSLLYALLLLLVAGLSVGGALLLLLLlnngplffLGVNGHLWFLSALFVFYLLLPLLLRLLRKLKKSLLLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 150 ILGILANPNMVSVKAVGIEWLPVNLYINGDTFYYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHElrWR 229
Cdd:pfam01757 159 LLLLLLLFLLYILILLVGVPFTVLVLFIFLYLPFFLLGALLARYRKRIRSKRLKLLIIILLALALLALILLLLFLF--GL 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600742754 230 GDFGDTWYLYCGPAVFVCAVTLLTLAKNWLNARP--LPGIACIARHSLGIYGFHALIVHALR 289
Cdd:pfam01757 237 DPLALEFYGYPSLLLLLLGILLLLLLALLLANLRslRRLLSYLGKYSFGIYLIHPPILLLLG 298
NolL COG3594
Fucose 4-O-acetylase or related acetyltransferase [Carbohydrate transport and metabolism];
1-283 2.00e-10

Fucose 4-O-acetylase or related acetyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 442813  Cd Length: 270  Bit Score: 60.37  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   1 MQEKIHWITNLRGIACMMVVMIHSTSWYITHPHAITLLqwdianlLNSASRVSVPLFFMISGYLFFGERSAQPRHFWRI- 79
Cdd:COG3594     4 AKKRDPWIDNAKGILIILVVLGHAIGPLIGDGDWLRAL-------YLFIYSFHMPLFFFISGYFSKPSRNGFKKFLKKKf 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  80 -GLCI---AFYSALSLLYITLFTHINVELSLKNLLQKPvFYHLWFFFAIAVIYLLSPLIQ-VKSTSSTMLLALMAILGIL 154
Cdd:COG3594    77 kRLLVpylIFQLIYSLFKFLVEGGEPLDLSLLLLLLDP-NGALWFLPALFVWRLLLPLLRrLRRWPLLIALAIGLLAGYL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 155 AnpnmvsvkavgIEWLPVNLyinGDTFYYVLY---GVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLheLRWRGD 231
Cdd:COG3594   156 P-----------SIGLPLSL---DRTLVFLPFfllGYLLRKYHLERLRRLRVLLLAVAVFLAAALLGFNRYL--LLGSRS 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1600742754 232 FGDTWYLYCGPAVFVCAVTLLTLAKNWLNARPLPgIACIARHSLGIYGFHAL 283
Cdd:COG3594   220 YGNWYGPLLRLLVALLGILLVLALLALLPRRRTW-LTYLGRNTLYIYLLHGF 270
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
1-290 7.99e-07

Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441440  Cd Length: 309  Bit Score: 50.03  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   1 MQEKIHWITNLRGIACMMVVMIHSTSWYITHPHAITLlqwdianllnSASRVSVPLFFMISGYLFFgeRSAQPRHFWRIG 80
Cdd:COG1835     4 SRRRLPSLDGLRGLAALLVVLYHAFLLFPPGPLGGLL----------SGGFLGVDVFFVLSGFLIT--RSLLRRLERGGF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  81 LCIAFYSA-----LSLLYITLFthinvelslknllqkpVFYHLWFFFAIAVIYLLSPLI-QVKSTSSTMLLALMAILGIL 154
Cdd:COG1835    72 SLRRFYLRrflriYPAYLVVLL----------------LTGHLWSLSVELQFYLLFPLLlLLLRRLRRRLLALLALLALA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 155 AnpnmVSVKAVGIEWLPVNLYINGDTFYYVLY--GVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHelrwrgdf 232
Cdd:COG1835   136 S----LLLLALLLTGDPSAAYFLTLTRLWEFLlgALLALLYRRLRRLRRLLALAGLALLLAALLLLDGAPFP-------- 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1600742754 233 GDTWYLYCGPAVFVCAVTLLTLAKNWLNARPLPGiacIARHSLGIYGFHALIVHALRA 290
Cdd:COG1835   204 GFGLLPLLAALLVLAAAAGSGLLSRLLSSRPLVF---LGDISYSLYLWHWPVLVLLLA 258
YfiQ COG3936
Membrane-bound acyltransferase YfiQ, involved in biofilm formation [Carbohydrate transport and ...
11-307 2.93e-05

Membrane-bound acyltransferase YfiQ, involved in biofilm formation [Carbohydrate transport and metabolism];


Pssm-ID: 443137  Cd Length: 334  Bit Score: 45.34  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  11 LRGIACMMVVMIHSTSWYITHpHAITLLQWDIANLLNSASRVSVPLFFMISGYLF-FGERSAQPRHFW--RIGLCIAFYS 87
Cdd:COG3936    11 LRGILCLSIVLHHIITMTTLK-SDVSLNQVEVLFIFRLLLMFATPVFIFLSEFLLaYSYKQNYPKGFLkkRLQYIFIPYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  88 ALSLLYITLFTHINVELSLKNLLQKPVF---YHLWFFFAIAVIYLLSPLIQ--VKSTSST--MLLALMAILGILANPNMV 160
Cdd:COG3936    90 IIALIYAIYESLIKTNADFVDSFLTNIFlgnWHGWFILVIFQFYLLFYLFFkfLKKYNPAvvVLLSLLINYVYLAYFNNF 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 161 SVKAVGIEWLpvnlyingdtFYYVLYGVLGRAIGTLDTD-KKWLTplcaalFIAAVWVISRGTLHELRWRGDFGDTWYLY 239
Cdd:COG3936   170 GAKTIFLGWL----------FYFVLGYYMGKNYERFLKFlEKYRI------FIVIFAILAFGFFIYGALSGNLTEVTSKR 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 240 CGPAVFVCAVTLLTLAknWLN-ARPLPG-IACIARHSLGIYGFHALIVHALRASHLELSRWPLLDIVWIF 307
Cdd:COG3936   234 FDLIPYTISVIFLVFL--LLMkVKLVPKfLNFISNYSFEIYLIHPLILILLGSFFVSLEDSPLLYVLLVF 301
YcfT COG4763
Uncharacterized membrane protein YcfT [Function unknown];
2-290 7.90e-05

Uncharacterized membrane protein YcfT [Function unknown];


Pssm-ID: 443795  Cd Length: 342  Bit Score: 43.77  E-value: 7.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754   2 QEKIHWITNLRGIACMMVVMIHSTswyITHPHAITLLQWDIAnLLNSASRVSVPLFFMISGYLF-----FGERSAQPRHF 76
Cdd:COG4763     6 KQRVDWIDTAKGICIILVVMMHSV---LGVYAAGGLAGFWHY-VNAFLKPFRMPLFFLISGLFAsrvidRPWREYLDRRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754  77 WRIGLciaFYSALSLLYITLFTHINVE------LSLKNLLQKPV--FYHLWFFFAIAVIYLLSpliqvKSTSSTMLLALM 148
Cdd:COG4763    82 VHFLY---FYVLWGVIQWLFKAPINAAanaayaGSLSEFLMGLIlpFGTLWYLYALAVYFVVT-----KLLRRVPPPLVL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1600742754 149 AILGILanpNMVSVKAVGIeWLPVNLYINGdtFYYVLYGVLGRAIGTLDTDKKWLTPLCAALFIAAVWVISRGTLHELRW 228
Cdd:COG4763   154 AAAAAL---EIAPVLPTGW-WGVDSFARYF--VYFYLGYFFAPQIFALADWARARRALALAGLALWAVANALLVFGLALL 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1600742754 229 RGdfgdtWYLYCGPAVFVCAVTLLTLAKNWLNARPLpgiACIARHSLGIYGFHALIVHALRA 290
Cdd:COG4763   228 PG-----VSLLLGLLGAVAIVALASLLARRRLMAPL---RYIGRNTLVIYLAHFIPMAALRL 281
 
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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