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Conserved domains on  [gi|2048203248|ref|WP_214799695|]
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AmiS/UreI family transporter [Exiguobacterium sp. s50]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UreI_AmiS_like super family cl03519
UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family ...
 3-161 9.12e-46

UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and CO2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


The actual alignment was detected with superfamily member cd13429:

Pssm-ID: 446120  Cd Length: 165  Bit Score: 148.62  E-value: 9.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   3 NISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGA--SSAEMFGYASIYLFAFTYLYVGVTFLFNL 80
Cdd:cd13429     1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSdgDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  81 DGRGVGWFSLFVSISAIFYAIIGFTT-GDMMGAVTWLFWSLLWGLFFMGMGLGR-QIDGLTARVAFVLAWLTLIIPALFG 158
Cdd:cd13429    81 DGSGLGWYSLWVAIIALVYAIVSFGQfADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                  ...
gi 2048203248 159 LAN 161
Cdd:cd13429   161 LTG 163
 
Name Accession Description Interval E-value
UreI_AmiS_like_2 cd13429
UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and ...
 3-161 9.12e-46

UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259833  Cd Length: 165  Bit Score: 148.62  E-value: 9.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   3 NISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGA--SSAEMFGYASIYLFAFTYLYVGVTFLFNL 80
Cdd:cd13429     1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSdgDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  81 DGRGVGWFSLFVSISAIFYAIIGFTT-GDMMGAVTWLFWSLLWGLFFMGMGLGR-QIDGLTARVAFVLAWLTLIIPALFG 158
Cdd:cd13429    81 DGSGLGWYSLWVAIIALVYAIVSFGQfADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                  ...
gi 2048203248 159 LAN 161
Cdd:cd13429   161 LTG 163
AmiS_UreI pfam02293
AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well ...
 1-160 1.16e-41

AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well as putative amide transporters.


Pssm-ID: 426706  Cd Length: 165  Bit Score: 138.09  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   1 MGNISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGA--SSAEMFGYASIYLFAFTYLYVGVTFLF 78
Cdd:pfam02293   1 MLGVGLLYVGAVLFLNGLWLLGKIDDRSAAVINLFVGGLQLIINLVLIFGAgaDAASIYAAALGLLFGFTYLYVAINRLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  79 NLDGRGVGWFSLFVSISAIFYAIIGFTTG-DMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTARVAFVLAWLTLIIPALF 157
Cdd:pfam02293  81 GLDGRGLGWFSLFVAINAVPYALISFTAAgDPWFGVIWLAWAVLWLLFFLLLALKKPIGKFTGWLAIVEGIVTAWIPGFL 160


                  ...
gi 2048203248 158 GLA 160
Cdd:pfam02293 161 LLT 163
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
 28-159 3.58e-03

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 37.60  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   28 SAGVFSLFTGLLQTFIA---TWLVIGASSAEMFGYASIYLFAFTYLYVGVTFLFNLDGRGVgwfslfvsISAIFYAI-IG 103
Cdd:PLN02638   932 SAHLFAVFQGLLKVLAGidtNFTVTSKASDEDGDFAELYMFKWTTLLIPPTTLLIINLVGV--------VAGISYAInSG 1003

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2048203248  104 FTT-GDMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTarvaFVLAWLTLiIPALFGL 159
Cdd:PLN02638  1004 YQSwGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPT----IVVVWSIL-LASIFSL 1055
 
Name Accession Description Interval E-value
UreI_AmiS_like_2 cd13429
UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and ...
 3-161 9.12e-46

UreI/AmiS family, subgroup 2. Putative transporters related to proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259833  Cd Length: 165  Bit Score: 148.62  E-value: 9.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   3 NISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGA--SSAEMFGYASIYLFAFTYLYVGVTFLFNL 80
Cdd:cd13429     1 NVGLLFVGAVLFINGLVLLGRVDGKSAGVFNLFVGALQVVTPTYLIFQSdgDPWTIFAASGIFLFGFTYLYVGITNLFGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  81 DGRGVGWFSLFVSISAIFYAIIGFTT-GDMMGAVTWLFWSLLWGLFFMGMGLGR-QIDGLTARVAFVLAWLTLIIPALFG 158
Cdd:cd13429    81 DGSGLGWYSLWVAIIALVYAIVSFGQfADPVFGVIWLSWAYLWFLFFLLLGLGKeNLGPYTGWVAIVQSWITATVPALLI 160


                  ...
gi 2048203248 159 LAN 161
Cdd:cd13429   161 LTG 163
AmiS_UreI pfam02293
AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well ...
 1-160 1.16e-41

AmiS/UreI family transporter; This family includes UreI and proton gated urea channel as well as putative amide transporters.


Pssm-ID: 426706  Cd Length: 165  Bit Score: 138.09  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   1 MGNISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGA--SSAEMFGYASIYLFAFTYLYVGVTFLF 78
Cdd:pfam02293   1 MLGVGLLYVGAVLFLNGLWLLGKIDDRSAAVINLFVGGLQLIINLVLIFGAgaDAASIYAAALGLLFGFTYLYVAINRLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  79 NLDGRGVGWFSLFVSISAIFYAIIGFTTG-DMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTARVAFVLAWLTLIIPALF 157
Cdd:pfam02293  81 GLDGRGLGWFSLFVAINAVPYALISFTAAgDPWFGVIWLAWAVLWLLFFLLLALKKPIGKFTGWLAIVEGIVTAWIPGFL 160


                  ...
gi 2048203248 158 GLA 160
Cdd:pfam02293 161 LLT 163
UreI_AmiS cd13428
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily ...
 4-162 1.01e-30

UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259832  Cd Length: 162  Bit Score: 110.07  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   4 ISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVI-GASSAEMFGYASIYLFAFTYLYVGVTFLFNLDG 82
Cdd:cd13428     2 VVLLFVGIVLISNGIGGLGKIDPKSTAVMNFFTGGLSLIINIVVLVqGNENTAYYAAATGLLFAFTYLYVAINNIFGLDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  83 RGVGWFSLFVSISAIFYAIIGFTTGDMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTARVAFVLAWLTLIIPALFGLANL 162
Cdd:cd13428    82 RPYGWYCLFVAINTLPCAYISFSTGDMRFAIIWLLWGILWFTGFIELVLKKTLGKFVPYLTIFEGIVTCWIPGFLMLIGR 161
UreI_AmiS_like cd13404
UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family ...
 4-155 7.21e-22

UreI/AmiS family, proton-gated urea channel and putative amide transporters; This family includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and CO2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259831  Cd Length: 167  Bit Score: 87.19  E-value: 7.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   4 ISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVIGAS--SAEMFGYASIYLFAFTYLYVGVTFLFNLD 81
Cdd:cd13404     2 LGLLYVGAVLFVNGLMLLGKVPVKSASVLNLFVGALQCVVPTVMLIQAQgdSSSVLAAAGLLLFGFTYLYVAINNLAGFD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048203248  82 GRGVGWFSLFVSISAIFYAIIGF----TTGDMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTARVAFVLAWLTLIIPA 155
Cdd:cd13404    82 PRGIGWYSLFVACAAVPYAFLSFysltVSNGPWFGVIWLAWAVLWTLFFLVLGLKEPLSRFTGWLAILEGIPTCWIPA 159
UreI_AmiS_like_1 cd13747
UreI/Amis family, subgroup 1. Putative proton-gated urea channel and putative amide ...
 4-163 7.48e-22

UreI/Amis family, subgroup 1. Putative proton-gated urea channel and putative amide transporters; This subfamily includes putative UreI proton-gated urea channels and putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.


Pssm-ID: 259834  Cd Length: 167  Bit Score: 87.37  E-value: 7.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   4 ISLLFGGVALFINSLVLFGKVDVKSAGVFSLFTGLLQTFIATWLVI--GASSAEMFGYASIYLFAFTYLYVGVTFLFNLD 81
Cdd:cd13747     2 LVLLYVGAVLFLNGLWLLGKIDDKEVAVINLFVGILTFIVALYLAFvhGADAISIKAGALTLLFSFTYLWVAINRRVNVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248  82 GRGVGWFSLFVSISAIFYAIIGFTTGDMMG----AVTWLFWSLLWGLFFMGMGLGRQIDGLTARVAFVLAWLTLIIPALF 157
Cdd:cd13747    82 GRGLGWYCLFVALTAVPVAINALAGATGDWdiwlGFNWAAWAVLWFLYFLLLVLGRPIQRITGYFTILVGIFTGWIPGLL 161


                  ....*.
gi 2048203248 158 GLANLM 163
Cdd:cd13747   162 LLQGYW 167
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
 28-159 3.58e-03

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 37.60  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048203248   28 SAGVFSLFTGLLQTFIA---TWLVIGASSAEMFGYASIYLFAFTYLYVGVTFLFNLDGRGVgwfslfvsISAIFYAI-IG 103
Cdd:PLN02638   932 SAHLFAVFQGLLKVLAGidtNFTVTSKASDEDGDFAELYMFKWTTLLIPPTTLLIINLVGV--------VAGISYAInSG 1003

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2048203248  104 FTT-GDMMGAVTWLFWSLLWGLFFMGMGLGRQIDGLTarvaFVLAWLTLiIPALFGL 159
Cdd:PLN02638  1004 YQSwGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPT----IVVVWSIL-LASIFSL 1055
 
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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