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Conserved domains on  [gi|1176773517|gb|OQY91393|]
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MAG: succinate--CoA ligase subunit beta [Anaerolineae bacterium UTCFX1]

Protein Classification

succinate--CoA ligase subunit beta( domain architecture ID 11414565)

ADP/GDP-forming succinate--CoA ligase subunit beta provides nucleotide specificity and binds the succinate substrate for the succinate--CoA ligase enzyme, which functions in the citric acid cycle (TCA) by coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP

CATH:  3.40.50.261
EC:  6.2.1.-
Gene Ontology:  GO:0004774|GO:0000287|GO:0000166|GO:0006099|GO:0042709
PubMed:  3332988

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-364 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


:

Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 620.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:COG0045     1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:COG0045    81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:COG0045   161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:COG0045   241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:COG0045   321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLniIAADTL 374
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-364 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 620.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:COG0045     1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:COG0045    81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:COG0045   161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:COG0045   241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:COG0045   321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLniIAADTL 374
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-364 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 599.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:PRK00696    1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGgVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:PRK00696   81 LvthqtgpKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:PRK00696  161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:PRK00696  241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:PRK00696  321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLniIAADTL 374
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-364 3.04e-177

succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]


Pssm-ID: 273396 [Multi-domain]  Cd Length: 386  Bit Score: 498.06  E-value: 3.04e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELG-GRVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGaGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 IK-------GLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:TIGR01016  81 LVtnqtdplGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENA--KMITAETL 364
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESglNIIFATSM 374
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-195 5.22e-87

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 261.81  E-value: 5.22e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   2 KLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGGRV-VIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSMEI 80
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVyVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  81 K-------GLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQAR 153
Cdd:pfam08442  81 VtkqtgpdGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1176773517 154 DIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVI 195
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-364 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 620.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:COG0045     1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:COG0045    81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:COG0045   161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:COG0045   241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:COG0045   321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLniIAADTL 374
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-364 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 599.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:PRK00696    1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGgVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:PRK00696   81 LvthqtgpKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:PRK00696  161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:PRK00696  241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:PRK00696  321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLniIAADTL 374
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-364 3.04e-177

succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]


Pssm-ID: 273396 [Multi-domain]  Cd Length: 386  Bit Score: 498.06  E-value: 3.04e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELG-GRVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGaGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 IK-------GLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:TIGR01016  81 LVtnqtdplGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENA--KMITAETL 364
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESglNIIFATSM 374
PRK14046 PRK14046
malate--CoA ligase subunit beta; Provisional
 1-364 2.18e-146

malate--CoA ligase subunit beta; Provisional


Pssm-ID: 237594 [Multi-domain]  Cd Length: 392  Bit Score: 419.89  E-value: 2.18e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   1 MKLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGG-RVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSME 79
Cdd:PRK14046    1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGwHWVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  80 I-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQA 152
Cdd:PRK14046   81 LvthqtgpEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 153 RDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMRDTDEEAP 232
Cdd:PRK14046  161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 233 AEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKAVLFNIFG 312
Cdd:PRK14046  241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 313 GITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENA--KMITAETL 364
Cdd:PRK14046  321 GINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESglPIITADTL 374
PLN00124 PLN00124
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
 3-364 5.17e-124

succinyl-CoA ligase [GDP-forming] subunit beta; Provisional


Pssm-ID: 177736 [Multi-domain]  Cd Length: 422  Bit Score: 364.07  E-value: 5.17e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   3 LHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEEL---GGRVVIKSQVLVGGRGKA-------GGIKVAKnAAEAEQLA 72
Cdd:PLN00124   30 IHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpdEGEVVVKSQILAGGRGLGtfknglkGGVHIVK-KDKAEELA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  73 QQILSMEI-------KGLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLL 145
Cdd:PLN00124  109 GKMLGQILvtkqtgpAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDIFK 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 146 GLRDYQARDIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLIALDGKMLIDDNAMFRQSDLNEMR 225
Cdd:PLN00124  189 GITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFALR 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 226 DTDEEAPAEIEARKYGLSYIKLDGNIGCMVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGADKVAAAMRIILSDSNVKA 305
Cdd:PLN00124  269 DTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKVKA 348

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176773517 306 VLFNIFGGITRCDEVARGILVAMDEVKPKVPMVVRLVGTNAEEGRKLLENAKM--ITAETL 364
Cdd:PLN00124  349 ILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMtlITAEDL 409
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-195 5.22e-87

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 261.81  E-value: 5.22e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   2 KLHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGGRV-VIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQILSMEI 80
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVyVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  81 K-------GLPVRKILVDEAAAIEKEIYFSITNDRAAKKPVMIASAAGGVDIEEVAATNPEKIIKVHIDPLLGLRDYQAR 153
Cdd:pfam08442  81 VtkqtgpdGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1176773517 154 DIAASINLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVI 195
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 254-363 2.88e-23

CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.


Pssm-ID: 395434 [Multi-domain]  Cd Length: 128  Bit Score: 93.86  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 254 MVNGAGLAMTSMDIVKLFNGEPANFLDIGGGAGA-DKVAAAMRIILSDSNVKAVLFNIFGGITRCDEVARGILVAMDEVK 332
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTpTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAR 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1176773517 333 P-KVPMVVRLVGTNAE-----EGRKLLENAKMITAET 363
Cdd:pfam00549  81 ArELPVVARVCGTEADpqgrsGQAKALAESGVLIASS 117
PLN02235 PLN02235
ATP citrate (pro-S)-lyase
 2-349 2.40e-10

ATP citrate (pro-S)-lyase


Pssm-ID: 177879 [Multi-domain]  Cd Length: 423  Bit Score: 61.71  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   2 KLHEYQSKTIF-------AKYGVPIPKGRVAATAlEARHIAEE----LGGRVVIKSQVLVGGRGKAGGIKVAKNAAEAEQ 70
Cdd:PLN02235    5 KIREYDSKRLLkehlkrlAGIDLPIRSAQVTEST-DFNELANKepwlSSTKLVVKPDMLFGKRGKSGLVALNLDLAQVAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  71 LAQQILSMEI-----KGlPVRKILVDEAAAIEKEIYFSITNDRAAkkpVMIA-SAAGGVDIEEvaatNPEKIIKVHIDPL 144
Cdd:PLN02235   84 FVKERLGKEVemggcKG-PITTFIVEPFVPHDQEFYLSIVSDRLG---CSISfSECGGIEIEE----NWDKVKTIFLPTE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 145 LGLRDYQARDIAASinLPREYWRDFSKIAEGLWQAYRKTDATLAEINPLVITEDKRLiALDGKMLIDDNAMFRQ----SD 220
Cdd:PLN02235  156 APLTSEICAPLIAT--LPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPY-PLDMRGELDDTAAFKNfkkwGN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517 221 LN-------EMRDTDEEAPAEIEARKYGLSYIKLD--GNIGCMVNGAGLAMTSMDIVKL--FNGEPANFLDIGGGAGADK 289
Cdd:PLN02235  233 IEfplpfgrVMSPTESFIHGLDEKTSASLKFTVLNpkGRIWTMVAGGGASVIYADTVGDlgYASELGNYAEYSGAPNEEE 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1176773517 290 VAAAMRIILS------DSNVKAVLfnIFGGITRCDEVA---RGILVAMDEVKPK-----VPMVVRLVGTNAEEG 349
Cdd:PLN02235  313 VLQYARVVIDcatanpDGRKRALL--IGGGIANFTDVAatfNGIIRALREKESKlkaarMHIFVRRGGPNYQKG 384
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 3-210 8.25e-09

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 55.17  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   3 LHEYQSKTIFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKS---QVLvgGRGKAGGIKVA-KNAAEAEQLAQQILSM 78
Cdd:pfam13549  10 LTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIvspDIL--HKSDVGGVRLNlRSAEAVRAAYEEILER 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  79 EIKGLP---VRKILVDEAAAIEKEIYFSITNDraakkPV---MIASAAGGVDIE---EVAATNP--------EKIIKVHI 141
Cdd:pfam13549  88 VRRYRPdarIEGVLVQPMAPGGRELIVGVTRD-----PQfgpVIMFGLGGIAVEvlkDVAFRLPplnmtlarEMIRRTRA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176773517 142 DPLL-GLRDYQARDIAASIN-LPR--EYWRDFSKIAEglwqayrktdatlAEINPLVITEDKrLIALDGKMLI 210
Cdd:pfam13549 163 YKLLkGYRGEPPADLDALEDvLVRvsQLVIDFPEIRE-------------LDINPLLADEDG-VVALDARIRL 221
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 6-92 3.74e-08

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 53.72  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   6 YQSKTIFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLVGGRgkagGIKVAKNAAEAEQLAQQILSMEIKGLPV 85
Cdd:COG0439    56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSR----GVRVVRDEEELEAALAEARAEAKAGSPN 131


                  ....*..
gi 1176773517  86 RKILVDE 92
Cdd:COG0439   132 GEVLVEE 138
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 14-109 1.39e-06

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 50.38  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   14 KYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLVGGRGkaGGIkvAKNAAEAEQLAQQILSMEikglPVRKILVDEA 93
Cdd:TIGR01369  137 EIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTG--GGI--AYNREELKEIAERALSAS----PINQVLVEKS 208

                           90
                   ....*....|....*.
gi 1176773517   94 AAIEKEIYFSITNDRA 109
Cdd:TIGR01369  209 LAGWKEIEYEVMRDSN 224
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 11-79 6.01e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 44.16  E-value: 6.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176773517  11 IFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKSqvLVGGRGKagGIKVAKNAAEAEQLAQQILSME 79
Cdd:COG0189   103 LLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKP--LDGSGGR--GVFLVEDEDALESILEALTELG 167
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 9-75 6.65e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 44.76  E-value: 6.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176773517   9 KTIFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLVGGRGKAGGIKVAKNAAEAEQLAQQI 75
Cdd:PRK14016  219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVNITTREEIEAAYAVASKE 285
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 16-100 4.87e-04

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 42.17  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  16 GVPIPKGRVAATALEARHIAEELGGRVVIK-SQVLvGGRGkaGGIkvAKNAAEAEQLAQQILSMEikglPVRKILVDE-- 92
Cdd:COG0458   126 GIPQPKSGTATSVEEALAIAEEIGYPVIVRpSYVL-GGRG--MGI--VYNEEELEEYLERALKVS----PDHPVLIDEsl 196


                  ....*...
gi 1176773517  93 AAAIEKEI 100
Cdd:COG0458   197 LGAKEIEV 204
carB PRK05294
carbamoyl-phosphate synthase large subunit;
9-100 6.44e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 42.01  E-value: 6.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517    9 KTIFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLVGGRGkaGGIkvAKNAAEAEQLAQqilsmeiKGL---PV 85
Cdd:PRK05294   133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVIIRPSFTLGGTG--GGI--AYNEEELEEIVE-------RGLdlsPV 201

                           90
                   ....*....|....*
gi 1176773517   86 RKILVDEAAAIEKEI 100
Cdd:PRK05294   202 TEVLIEESLLGWKEY 216
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 8-92 9.72e-04

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 40.77  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   8 SKTIFAKYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLVGGRgkagGIKVAKNAAEAEQLAQQILSMEIKGLPVRK 87
Cdd:COG0151   106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGK----GVVVAETLEEALAAVDDMLADGKFGDAGAR 181


                  ....*
gi 1176773517  88 ILVDE 92
Cdd:COG0151   182 VVIEE 186
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 13-100 1.39e-03

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 39.16  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517  13 AKYGVPIPKGRVAATALEARHIAEELGGRVVIKSQVLvGGRGKagGIKVAKNAAEAEQLAqqilsmeiKGLPVRKILVDE 92
Cdd:pfam02222   1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKARRG-GYDGK--GQYVVRSEADLPQAW--------EELGDGPVIVEE 69


                  ....*...
gi 1176773517  93 AAAIEKEI 100
Cdd:pfam02222  70 FVPFDREL 77
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 16-108 3.75e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 39.57  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176773517   16 GVPIPKGRVAATALEARHIAEELGGRVVI-KSQVLVGgrgkAGGIkVAKNAAEAEQLAQQILSMEikglPVRKILVDEAA 94
Cdd:PRK12815   140 GEPVPESEIVTSVEEALAFAEKIGFPIIVrPAYTLGG----TGGG-IAENLEELEQLFKQGLQAS----PIHQCLLEESI 210

                           90
                   ....*....|....
gi 1176773517   95 AIEKEIYFSITNDR 108
Cdd:PRK12815   211 AGWKEIEYEVMRDR 224
 
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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