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Conserved domains on  [gi|21361163|ref|NP_000812|]
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vitamin K-dependent gamma-carboxylase isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VKG_Carbox pfam05090
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
66-504 0e+00

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


:

Pssm-ID: 461546  Cd Length: 432  Bit Score: 599.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    66 VFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLP 145
Cdd:pfam05090   1 VFRILFGLLMLIDIIRERGTGWIDKRYIEPKFHFSFPGFEWVKPLPGDWMYLLYLIMGLGALGIMLGFKYRLSCLLFFLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   146 YWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVE 225
Cdd:pfam05090  81 FTYIFLMDKTTYNNHYYLYGLLSFLMIFLPANRYFSLDAWLNPKIRNSHVPRWNYFILKFQLFIVYFYAGLAKLNPDWLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   226 GYSMEYLsrhWLFSPFKLLLSEELTSLL----VVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSY 301
Cdd:pfam05090 161 GAMPLKL---WLFSPFDLPLIGPLLQELwvayIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   302 VMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSvscvykrsrgKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSH 381
Cdd:pfam05090 238 VMLATALIFFSPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRH 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   382 FLTQGYNNWTNGLYGYSWDMMVHSrSHQHVKITYRDGRTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSRLLPKY 458
Cdd:pfam05090 308 FLYPGYVFWTEEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKK 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 21361163   459 NVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQP 504
Cdd:pfam05090 387 GIKNPSVYADSWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
512-604 2.53e-04

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member cd02235:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 100  Bit Score: 40.64  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163 512 WRAKLQEIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLREGEKMQLPAGEY 586
Cdd:cd02235   3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75
                        90
                ....*....|....*...
gi 21361163 587 HKVYTTSPSPSCYMYVYV 604
Cdd:cd02235  76 HNAKNVGSGPAKLLATYI 93
 
Name Accession Description Interval E-value
VKG_Carbox pfam05090
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
66-504 0e+00

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


Pssm-ID: 461546  Cd Length: 432  Bit Score: 599.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    66 VFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLP 145
Cdd:pfam05090   1 VFRILFGLLMLIDIIRERGTGWIDKRYIEPKFHFSFPGFEWVKPLPGDWMYLLYLIMGLGALGIMLGFKYRLSCLLFFLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   146 YWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVE 225
Cdd:pfam05090  81 FTYIFLMDKTTYNNHYYLYGLLSFLMIFLPANRYFSLDAWLNPKIRNSHVPRWNYFILKFQLFIVYFYAGLAKLNPDWLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   226 GYSMEYLsrhWLFSPFKLLLSEELTSLL----VVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSY 301
Cdd:pfam05090 161 GAMPLKL---WLFSPFDLPLIGPLLQELwvayIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   302 VMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSvscvykrsrgKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSH 381
Cdd:pfam05090 238 VMLATALIFFSPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRH 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   382 FLTQGYNNWTNGLYGYSWDMMVHSrSHQHVKITYRDGRTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSRLLPKY 458
Cdd:pfam05090 308 FLYPGYVFWTEEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKK 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 21361163   459 NVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQP 504
Cdd:pfam05090 387 GIKNPSVYADSWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
HTTM smart00752
Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent ...
56-315 2.86e-101

Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane) in its N-terminus. In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal gene transfer than by early invention. The conservation of VKGC catalytic sites indicates an enzymatic function also for the other family members.


Pssm-ID: 214802  Cd Length: 271  Bit Score: 312.72  E-value: 2.86e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163     56 NRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCR--FPLLDALRPLP-------LDWMYLVYTIMFLGA 126
Cdd:smart00752   1 ERPVDPASLAVFRILFGLLMLLDILRERGLSDLDLRYGDPLFFCRlaFPLFDQMSPLPfhmlsdsLDWMYLLYALMIVGA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    127 LGMMLGLCYRISCVLFLLPYWYVFLLDKTSWN--NHSYLYGLLAFQLTfmDANHYWSVDGLLNAHRRNAHVPLWNYAVLR 204
Cdd:smart00752  81 LLLLLGYRTRLSSVLFWLLVWSIQLRDKTVWNggDHSYLVGLFLLLFL--PAGRYWSIDALRNRRRRDAIVPLWATFVLR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    205 GQIFIVYFIAGVKKLDAD-WVEGYSMEY-LSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFF 282
Cdd:smart00752 159 IQVFIIYFFAGLKKLDGDeWVDGTAMYYlLSLDWFFSPLDLVLLEFPPLLLAVTWGGLLFDLFFPFLLFNRRTRPIGLVV 238
                          250       260       270
                   ....*....|....*....|....*....|...
gi 21361163    283 VSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEW 315
Cdd:smart00752 239 FIAFHLGNAVLFGIGMFPFVMIGALPLFLPPEW 271
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
512-604 2.53e-04

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 40.64  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163 512 WRAKLQEIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLREGEKMQLPAGEY 586
Cdd:cd02235   3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75
                        90
                ....*....|....*...
gi 21361163 587 HKVYTTSPSPSCYMYVYV 604
Cdd:cd02235  76 HNAKNVGSGPAKLLATYI 93
DoxX COG2259
Uncharacterized membrane protein YphA, DoxX/SURF4 family [Function unknown];
55-191 3.28e-03

Uncharacterized membrane protein YphA, DoxX/SURF4 family [Function unknown];


Pssm-ID: 441860  Cd Length: 134  Bit Score: 38.27  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163  55 LNRPTDPASLAVFRFLFGFLMVLdipqeRGLSSLDR-----KYLDGLDVcrfplldalrPLPLDWMYLVYTIMFLGALGM 129
Cdd:COG2259   2 LLSTLADLGLLLLRLLLGLLFLA-----HGLQKLFGfdgtaGFFASLGL----------PLPALLAYLAGLAELVGGLLL 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361163 130 MLGLCYRISCVL---FLLPYWYVFLLDKTSWNNHSY----LYGLLAFQLTFMDANhYWSVDGLLNAHRR 191
Cdd:COG2259  67 ILGLFTRLAALLlagFMLVAIFVVHLPNGFWAMGGGeknlLLAGGLLALALLGPG-RYSLDALLGRRLR 134
 
Name Accession Description Interval E-value
VKG_Carbox pfam05090
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
66-504 0e+00

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


Pssm-ID: 461546  Cd Length: 432  Bit Score: 599.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    66 VFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLP 145
Cdd:pfam05090   1 VFRILFGLLMLIDIIRERGTGWIDKRYIEPKFHFSFPGFEWVKPLPGDWMYLLYLIMGLGALGIMLGFKYRLSCLLFFLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   146 YWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVE 225
Cdd:pfam05090  81 FTYIFLMDKTTYNNHYYLYGLLSFLMIFLPANRYFSLDAWLNPKIRNSHVPRWNYFILKFQLFIVYFYAGLAKLNPDWLF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   226 GYSMEYLsrhWLFSPFKLLLSEELTSLL----VVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSY 301
Cdd:pfam05090 161 GAMPLKL---WLFSPFDLPLIGPLLQELwvayIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPY 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   302 VMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSvscvykrsrgKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSH 381
Cdd:pfam05090 238 VMLATALIFFSPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRH 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163   382 FLTQGYNNWTNGLYGYSWDMMVHSrSHQHVKITYRDGRTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSRLLPKY 458
Cdd:pfam05090 308 FLYPGYVFWTEEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKK 386
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 21361163   459 NVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQP 504
Cdd:pfam05090 387 GIKNPSVYADSWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
HTTM smart00752
Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent ...
56-315 2.86e-101

Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane) in its N-terminus. In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal gene transfer than by early invention. The conservation of VKGC catalytic sites indicates an enzymatic function also for the other family members.


Pssm-ID: 214802  Cd Length: 271  Bit Score: 312.72  E-value: 2.86e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163     56 NRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCR--FPLLDALRPLP-------LDWMYLVYTIMFLGA 126
Cdd:smart00752   1 ERPVDPASLAVFRILFGLLMLLDILRERGLSDLDLRYGDPLFFCRlaFPLFDQMSPLPfhmlsdsLDWMYLLYALMIVGA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    127 LGMMLGLCYRISCVLFLLPYWYVFLLDKTSWN--NHSYLYGLLAFQLTfmDANHYWSVDGLLNAHRRNAHVPLWNYAVLR 204
Cdd:smart00752  81 LLLLLGYRTRLSSVLFWLLVWSIQLRDKTVWNggDHSYLVGLFLLLFL--PAGRYWSIDALRNRRRRDAIVPLWATFVLR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163    205 GQIFIVYFIAGVKKLDAD-WVEGYSMEY-LSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFF 282
Cdd:smart00752 159 IQVFIIYFFAGLKKLDGDeWVDGTAMYYlLSLDWFFSPLDLVLLEFPPLLLAVTWGGLLFDLFFPFLLFNRRTRPIGLVV 238
                          250       260       270
                   ....*....|....*....|....*....|...
gi 21361163    283 VSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEW 315
Cdd:smart00752 239 FIAFHLGNAVLFGIGMFPFVMIGALPLFLPPEW 271
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
512-604 2.53e-04

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 40.64  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163 512 WRAKLQEIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLREGEKMQLPAGEY 586
Cdd:cd02235   3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75
                        90
                ....*....|....*...
gi 21361163 587 HKVYTTSPSPSCYMYVYV 604
Cdd:cd02235  76 HNAKNVGSGPAKLLATYI 93
DoxX COG2259
Uncharacterized membrane protein YphA, DoxX/SURF4 family [Function unknown];
55-191 3.28e-03

Uncharacterized membrane protein YphA, DoxX/SURF4 family [Function unknown];


Pssm-ID: 441860  Cd Length: 134  Bit Score: 38.27  E-value: 3.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361163  55 LNRPTDPASLAVFRFLFGFLMVLdipqeRGLSSLDR-----KYLDGLDVcrfplldalrPLPLDWMYLVYTIMFLGALGM 129
Cdd:COG2259   2 LLSTLADLGLLLLRLLLGLLFLA-----HGLQKLFGfdgtaGFFASLGL----------PLPALLAYLAGLAELVGGLLL 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361163 130 MLGLCYRISCVL---FLLPYWYVFLLDKTSWNNHSY----LYGLLAFQLTFMDANhYWSVDGLLNAHRR 191
Cdd:COG2259  67 ILGLFTRLAALLlagFMLVAIFVVHLPNGFWAMGGGeknlLLAGGLLALALLGPG-RYSLDALLGRRLR 134
 
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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