NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490215525|ref|WP_004113905|]
View 

MULTISPECIES: Gfo/Idh/MocA family protein [Klebsiella]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-330 7.10e-64

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 204.39  E-value: 7.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   1 MTVNIGLIGLGMIGRDHLQRFQTViQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIQSDDVDAIFICSIGPVHKEQ 80
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAAL-PGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  81 ILAAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGFMRRFDPGYNQLKATLDSGELGEILLIHCAHRNAS--V 158
Cdd:COG0673   81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVV-LMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpaG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 159 PESYTLEM------AINDSATHEIDIIRYLLNENIVSVRVDkpQKKTRRACAHLQDPLIVIFETESGVRIDDELFVNCDY 232
Cdd:COG0673  160 PADWRFDPelagggALLDLGIHDIDLARWLLGSEPESVSAT--GGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 233 G-YDIRCEVIGENAisalteqaltTVrsaqgysraipktcmerfataydrevqnFVDRVNLGAEMSgPSSWDGFVVAMVC 311
Cdd:COG0673  238 GeRDERLEVYGTKG----------TL----------------------------FVDAIRGGEPPP-VSLEDGLRALELA 278
                        330
                 ....*....|....*....
gi 490215525 312 DAGLASLKDGEKhaVSLPE 330
Cdd:COG0673  279 EAAYESARTGRR--VELPD 295
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-330 7.10e-64

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 204.39  E-value: 7.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   1 MTVNIGLIGLGMIGRDHLQRFQTViQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIQSDDVDAIFICSIGPVHKEQ 80
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAAL-PGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  81 ILAAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGFMRRFDPGYNQLKATLDSGELGEILLIHCAHRNAS--V 158
Cdd:COG0673   81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVV-LMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpaG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 159 PESYTLEM------AINDSATHEIDIIRYLLNENIVSVRVDkpQKKTRRACAHLQDPLIVIFETESGVRIDDELFVNCDY 232
Cdd:COG0673  160 PADWRFDPelagggALLDLGIHDIDLARWLLGSEPESVSAT--GGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 233 G-YDIRCEVIGENAisalteqaltTVrsaqgysraipktcmerfataydrevqnFVDRVNLGAEMSgPSSWDGFVVAMVC 311
Cdd:COG0673  238 GeRDERLEVYGTKG----------TL----------------------------FVDAIRGGEPPP-VSLEDGLRALELA 278
                        330
                 ....*....|....*....
gi 490215525 312 DAGLASLKDGEKhaVSLPE 330
Cdd:COG0673  279 EAAYESARTGRR--VELPD 295
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
2-321 4.87e-60

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 195.52  E-value: 4.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525    2 TVNIGLIGLGMIGRDHLQRFQTVIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVE-MIQSDDVDAIFICSIGPVHKEQ 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEaALADPEIDAVLIASPTDTHADL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   81 ILAAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGFMRRFDPGYNQLKATLDSGELGEILLIHCAHRN-ASVP 159
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVK-LQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDpAPPP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  160 ESYT-------LEMAIndsatHEIDIIRYLLNENIVSV------RVDKPQKKtrracAHLQDPLIVIFETESGV--RIDD 224
Cdd:TIGR04380 160 VAYVkvsgglfLDMTI-----HDFDMARFLLGSEVEEVyaqgsvLVDPAIGE-----AGDVDTAVITLKFENGAiaVIDN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  225 ELfvNCDYGYDIRCEVIGENAISALTEQALTTVR--SAQGYSRAIPKTC-MERFATAYDREVQNFVDRVNLGAEMSgPSS 301
Cdd:TIGR04380 230 SR--RAAYGYDQRVEVFGSKGMLRAENDTESTVIlyDAEGVRGDKPLNFfLERYRDAYRAEIQAFVDAILEGRPPP-VTG 306
                         330       340
                  ....*....|....*....|
gi 490215525  302 WDGFVVAMVCDAGLASLKDG 321
Cdd:TIGR04380 307 EDGLKALLLALAAKRSLEEG 326
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
3-123 1.15e-28

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 107.29  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525    3 VNIGLIGLGMIGRDHLQRFQTVIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIQSDDVDAIFICSIGPVHKEQIL 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 490215525   83 AAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGF 123
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVR-VSVGF 120
PRK10206 PRK10206
putative oxidoreductase; Provisional
50-163 2.29e-09

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 57.91  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  50 AQPYY-------DAVEMIQSDDVDAIFICSIGPVHKEQILAAIKAGKPVFCEKPLTPTADEAKAIIDaeVAYGKRMLQLG 122
Cdd:PRK10206  43 QAPIYshihftsDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFA--LAKSKGLTVTP 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490215525 123 FM-RRFDPGYNQLKATLDSGELGEILLIHcAHRNASVPESYT 163
Cdd:PRK10206 121 YQnRRFDSCFLTAKKAIESGKLGEIVEVE-SHFDYYRPVAET 161
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-330 7.10e-64

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 204.39  E-value: 7.10e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   1 MTVNIGLIGLGMIGRDHLQRFQTViQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIQSDDVDAIFICSIGPVHKEQ 80
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAAL-PGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  81 ILAAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGFMRRFDPGYNQLKATLDSGELGEILLIHCAHRNAS--V 158
Cdd:COG0673   81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVV-LMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRpaG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 159 PESYTLEM------AINDSATHEIDIIRYLLNENIVSVRVDkpQKKTRRACAHLQDPLIVIFETESGVRIDDELFVNCDY 232
Cdd:COG0673  160 PADWRFDPelagggALLDLGIHDIDLARWLLGSEPESVSAT--GGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525 233 G-YDIRCEVIGENAisalteqaltTVrsaqgysraipktcmerfataydrevqnFVDRVNLGAEMSgPSSWDGFVVAMVC 311
Cdd:COG0673  238 GeRDERLEVYGTKG----------TL----------------------------FVDAIRGGEPPP-VSLEDGLRALELA 278
                        330
                 ....*....|....*....
gi 490215525 312 DAGLASLKDGEKhaVSLPE 330
Cdd:COG0673  279 EAAYESARTGRR--VELPD 295
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
2-321 4.87e-60

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 195.52  E-value: 4.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525    2 TVNIGLIGLGMIGRDHLQRFQTVIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVE-MIQSDDVDAIFICSIGPVHKEQ 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEaALADPEIDAVLIASPTDTHADL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   81 ILAAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGFMRRFDPGYNQLKATLDSGELGEILLIHCAHRN-ASVP 159
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVK-LQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRITSRDpAPPP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  160 ESYT-------LEMAIndsatHEIDIIRYLLNENIVSV------RVDKPQKKtrracAHLQDPLIVIFETESGV--RIDD 224
Cdd:TIGR04380 160 VAYVkvsgglfLDMTI-----HDFDMARFLLGSEVEEVyaqgsvLVDPAIGE-----AGDVDTAVITLKFENGAiaVIDN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  225 ELfvNCDYGYDIRCEVIGENAISALTEQALTTVR--SAQGYSRAIPKTC-MERFATAYDREVQNFVDRVNLGAEMSgPSS 301
Cdd:TIGR04380 230 SR--RAAYGYDQRVEVFGSKGMLRAENDTESTVIlyDAEGVRGDKPLNFfLERYRDAYRAEIQAFVDAILEGRPPP-VTG 306
                         330       340
                  ....*....|....*....|
gi 490215525  302 WDGFVVAMVCDAGLASLKDG 321
Cdd:TIGR04380 307 EDGLKALLLALAAKRSLEEG 326
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
3-123 1.15e-28

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 107.29  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525    3 VNIGLIGLGMIGRDHLQRFQTVIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIQSDDVDAIFICSIGPVHKEQIL 82
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 490215525   83 AAIKAGKPVFCEKPLTPTADEAKAIIDAEVAYGKRmLQLGF 123
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVR-VSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
135-321 1.13e-11

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 63.21  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  135 KATLDSGELGEILLIHCAHRNASVPESYTLE---------MAINDSATHEIDIIRYLLNENIVSVRVdkpqkktrraCAH 205
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHTRDPFRPPQEFKRwrvdpeksgGALYDLGIHTIDLLIYLFGEPPSVVAV----------YAS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  206 lQDPLIVIFETESGVRIDdelfVNCDYGY-----DIRCEVIGENA-------------ISALTEQALTTVRSAQGYSRAI 267
Cdd:pfam02894  71 -EDTAFATLEFKNGAVGT----LETSGGSiveanGHRISIHGTKGsieldgiddgllsVTVVGEPGWATDDPMVRKGGDE 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490215525  268 PKTCMERFATAYDREVQNFVDRVNLGAEMsGPSSWDGFVVAMVCDAGLASLKDG 321
Cdd:pfam02894 146 VPEFLGSFAGGYLLEYDAFLEAVRGGKVV-LVDAEDGLYALAVIEAAYESAEEG 198
PRK10206 PRK10206
putative oxidoreductase; Provisional
50-163 2.29e-09

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 57.91  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  50 AQPYY-------DAVEMIQSDDVDAIFICSIGPVHKEQILAAIKAGKPVFCEKPLTPTADEAKAIIDaeVAYGKRMLQLG 122
Cdd:PRK10206  43 QAPIYshihftsDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFA--LAKSKGLTVTP 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490215525 123 FM-RRFDPGYNQLKATLDSGELGEILLIHcAHRNASVPESYT 163
Cdd:PRK10206 121 YQnRRFDSCFLTAKKAIESGKLGEIVEVE-SHFDYYRPVAET 161
PRK11579 PRK11579
putative oxidoreductase; Provisional
64-146 2.46e-05

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 45.48  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525  64 DVDAIFICSIGPVHKEQILAAIKAGKPVFCEKPLTPTADEAKAiIDAEVAYGKRMLQLGFMRRFDPGYNQLKATLDSGEL 143
Cdd:PRK11579  64 NIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARE-LDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVL 142

                 ...
gi 490215525 144 GEI 146
Cdd:PRK11579 143 GEV 145
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
1-91 5.44e-05

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 44.68  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   1 MTVNIGLIGLGMIG-----------RDHLQRFQTVIQNARVsAVCDINRnvtdtiAREYGAQPYY---DAVEMIQSDDVD 66
Cdd:PRK06349   2 KPLKVGLLGLGTVGsgvvrileenaEEIAARAGRPIEIKKV-AVRDLEK------DRGVDLPGILlttDPEELVNDPDID 74
                         90       100
                 ....*....|....*....|....*..
gi 490215525  67 aIFICSIGPVH--KEQILAAIKAGKPV 91
Cdd:PRK06349  75 -IVVELMGGIEpaRELILKALEAGKHV 100
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
4-91 1.72e-03

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 39.40  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   4 NIGLIGLGMIGR---DHLQrfqtvIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIqSDDVDAIFIC-SIGPVhKE 79
Cdd:COG1712    2 RIGLIGCGAIGSevaEALA-----DAGVELVAVYDRDPERAEALLASLGARVVSDVDELL-AADPDLVVEAaSQAAV-RE 74
                         90
                 ....*....|..
gi 490215525  80 QILAAIKAGKPV 91
Cdd:COG1712   75 HGPAVLEAGKDL 86
PRK13304 PRK13304
aspartate dehydrogenase;
5-91 9.72e-03

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 37.28  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490215525   5 IGLIGLGMIGRDHLQRFQTVIQNARVSAVCDINRNVTDTIAREYGAQPYYDAVEMIqsDDVDAIFIC-SIGPVhKEQILA 83
Cdd:PRK13304   4 IGIVGCGAIASLITKAILSGRINAELYAFYDRNLEKAENLASKTGAKACLSIDELV--EDVDLVVECaSVNAV-EEVVPK 80

                 ....*...
gi 490215525  84 AIKAGKPV 91
Cdd:PRK13304  81 SLENGKDV 88
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH