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Conserved domains on  [gi|74139919|dbj|BAE31798|]
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unnamed protein product, partial [Mus musculus]

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

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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 ...
 62-450 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: 578.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:COG0045   3 LHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKA-------GGVKLAKSPEEAREAAEE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:COG0045  76 ILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:COG0045 156 QPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDL 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:COG0045 236 SEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139919 382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKL 450
Cdd:COG0045 316 VNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVEL 384
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 62-450 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: 578.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:COG0045   3 LHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKA-------GGVKLAKSPEEAREAAEE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:COG0045  76 ILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:COG0045 156 QPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDL 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:COG0045 236 SEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139919 382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKL 450
Cdd:COG0045 316 VNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVEL 384
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
62-452 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 545.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:PRK00696   3 LHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKA-------GGVKLAKSPEEAREFAKQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:PRK00696  76 ILGMTLVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:PRK00696 156 QPFQAREIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:PRK00696 236 SEEDPLEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74139919  382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSE 452
Cdd:PRK00696 316 VNIFGGITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAK 386
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 62-452 3.39e-162

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: 463.39  E-value: 3.39e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919    62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:TIGR01016   3 LHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKA-------GGVKVAKSKEEARAAAEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:TIGR01016  76 LLGKELVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:TIGR01016 156 LPYQAREIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:TIGR01016 236 SQEDPREVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVF 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74139919   382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSE 452
Cdd:TIGR01016 316 INIFGGITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
ATP-grasp_2 pfam08442
ATP-grasp domain;
61-269 9.42e-92

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 276.83  E-value: 9.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919    61 SLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSS 140
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKA-------GGVKLAKSPEEAKEVAK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   141 QMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEG 220
Cdd:pfam08442  74 EMLGKNLVTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 74139919   221 IKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVE 269
Cdd:pfam08442 154 LTPYQAREIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 62-450 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: 578.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:COG0045   3 LHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKA-------GGVKLAKSPEEAREAAEE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:COG0045  76 ILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:COG0045 156 QPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDL 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919 302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:COG0045 236 SEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139919 382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKL 450
Cdd:COG0045 316 VNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVEL 384
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
62-452 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 545.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:PRK00696   3 LHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKA-------GGVKLAKSPEEAREFAKQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:PRK00696  76 ILGMTLVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:PRK00696 156 QPFQAREIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:PRK00696 236 SEEDPLEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74139919  382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSE 452
Cdd:PRK00696 316 VNIFGGITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAK 386
PLN00124 PLN00124
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
 58-453 0e+00

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


Pssm-ID: 177736 [Multi-domain]  Cd Length: 422  Bit Score: 538.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   58 RTLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKL--GSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVfSPEEA 135
Cdd:PLN00124  26 RRLNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpDEGEVVVKSQILAGGRGLGTFKNGLKGGVHIV-KKDKA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  136 KAVSSQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPI 215
Cdd:PLN00124 105 EELAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPI 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  216 DIVEGIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKI 295
Cdd:PLN00124 185 DIFKGITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEI 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  296 FDLQDWSQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDK 375
Cdd:PLN00124 265 FALRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDD 344

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74139919  376 KVQAILVNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEI 453
Cdd:PLN00124 345 KVKAILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKALAI 422
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 62-452 3.39e-162

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: 463.39  E-value: 3.39e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919    62 LHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSSQ 141
Cdd:TIGR01016   3 LHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKA-------GGVKVAKSKEEARAAAEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   142 MIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEGI 221
Cdd:TIGR01016  76 LLGKELVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   222 KKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQDW 301
Cdd:TIGR01016 156 LPYQAREIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   302 SQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQAIL 381
Cdd:TIGR01016 236 SQEDPREVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVF 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74139919   382 VNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSE 452
Cdd:TIGR01016 316 INIFGGITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
PRK14046 PRK14046
malate--CoA ligase subunit beta; Provisional
 60-448 5.45e-140

malate--CoA ligase subunit beta; Provisional


Pssm-ID: 237594 [Multi-domain]  Cd Length: 392  Bit Score: 407.17  E-value: 5.45e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   60 LSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVS 139
Cdd:PRK14046   1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKA-------GGIKLCRTYNEVRDAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  140 SQMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVE 219
Cdd:PRK14046  74 EDLLGKKLVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  220 GIKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDSDGKVLCMDAKINFDSNSAYRQKKIFDLQ 299
Cdd:PRK14046 154 GLQQFQAREIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMR 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  300 DWSQEDERDKEAANADINYIGLDGSIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVQQVTEAFKLITSDKKVQA 379
Cdd:PRK14046 234 DPSQEDPREAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKA 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139919  380 ILVNIFGGIMRCDVIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVV 448
Cdd:PRK14046 314 ILVNIFAGINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAV 382
ATP-grasp_2 pfam08442
ATP-grasp domain;
61-269 9.42e-92

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 276.83  E-value: 9.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919    61 SLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGtftsglkGGVKIVFSPEEAKAVSS 140
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKA-------GGVKLAKSPEEAKEVAK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   141 QMIGQKLITKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSAQGGVNIEDVAAENPEAIVKEPIDIVEG 220
Cdd:pfam08442  74 EMLGKNLVTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 74139919   221 IKKEQAVTLAQKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVE 269
Cdd:pfam08442 154 LTPYQAREIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 328-448 2.90e-36

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: 130.07  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   328 LVNGAGLAMATMDIIKLHGGTPANFLDVGGGA-TVQQVTEAFKLITSDKKVQAILVNIFGGIMRCDVIAQGIVMAVKDLE 406
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 74139919   407 -IRIPVVVRLQGTRVD-----DAKALIADSGLKILACDDLDEAAKMVV 448
Cdd:pfam00549  81 aRELPVVARVCGTEADpqgrsGQAKALAESGVLIASSNNQALRAAGAV 128
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 69-137 3.34e-05

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: 45.25  E-value: 3.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74139919  69 ELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSkDVVIKAQVLAGGRgkgtftsglkgGVKIVFSPEEAKA 137
Cdd:COG0439  60 EALAAAGVPVPGFALVDSPEEALAFAEEIGY-PVVVKPADGAGSR-----------GVRVVRDEEELEA 116
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 66-119 7.17e-04

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 42.07  E-value: 7.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74139919   66 LSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKdVVIKAQvlAGGRGKGTFT 119
Cdd:PRK14016 217 LTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYP-VVVKPL--DGNHGRGVTV 267
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 65-118 1.44e-03

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: 40.31  E-value: 1.44e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 74139919  65 YLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGsKDVVIKaqVLAGGRGKGTF 118
Cdd:COG0189  98 LFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELG-GPVVLK--PLDGSGGRGVF 148
PLN02735 PLN02735
carbamoyl-phosphate synthase
 68-113 1.70e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 40.92  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74139919    68 MELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLaGGR 113
Cdd:PLN02735  707 NAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVL-GGR 751
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 69-167 2.94e-03

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).


Pssm-ID: 395851 [Multi-domain]  Cd Length: 194  Bit Score: 38.80  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919    69 ELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRgkgtftsglkgGVKIVFSPEEAKAVSSQMIGQkli 148
Cdd:pfam01071   8 DFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK-----------GVIVASSNEEAIKAVDEILEQ--- 73

                          90
                  ....*....|....*....
gi 74139919   149 tKQTGEKGricNQVLVCER 167
Cdd:pfam01071  74 -KKFGEAG---ETVVIEEF 88
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 69-150 3.27e-03

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: 39.86  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  69 ELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKdVVIK-AQVLaGGRGKGtftsglkggvkIVFSPEE-----AKAVSSQM 142
Cdd:COG0458 120 ELLDKLGIPQPKSGTATSVEEALAIAEEIGYP-VIVRpSYVL-GGRGMG-----------IVYNEEEleeylERALKVSP 186


                ....*...
gi 74139919 143 IGQKLITK 150
Cdd:COG0458 187 DHPVLIDE 194
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 29-150 7.22e-03

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: 38.83  E-value: 7.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919     29 QTTLRAAAQvLGNSGLFNKHGLQVQQQQQRTLSLHE--YLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKdVVIKA 106
Cdd:TIGR01369   92 QTALNLAVE-LEESGVLEKYGVEVLGTPVEAIKKAEdrELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYP-VIVRP 169

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 74139919    107 QVLAGGRGKGtftsglkggvkIVFSPEE-----AKAVSSQMIGQKLITK 150
Cdd:TIGR01369  170 AFTLGGTGGG-----------IAYNREElkeiaERALSASPINQVLVEK 207
PLN02235 PLN02235
ATP citrate (pro-S)-lyase
 62-294 7.32e-03

ATP citrate (pro-S)-lyase


Pssm-ID: 177879 [Multi-domain]  Cd Length: 423  Bit Score: 38.60  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919   62 LHEYLSMELLQE-----AGVSVP--KGFVAKSSDEAYAIAKK--LGSKDVVIKAQVLAGGRGKgtftSGLKgGVKIVFSp 132
Cdd:PLN02235   6 IREYDSKRLLKEhlkrlAGIDLPirSAQVTESTDFNELANKEpwLSSTKLVVKPDMLFGKRGK----SGLV-ALNLDLA- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  133 eEAKAVSSQMIGQKLitKQTGEKGRIcnQVLVCERKYP-RREYYFAITMER-----SFqgpvligSAQGGVNIEdvaaEN 206
Cdd:PLN02235  80 -QVATFVKERLGKEV--EMGGCKGPI--TTFIVEPFVPhDQEFYLSIVSDRlgcsiSF-------SECGGIEIE----EN 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139919  207 PEAIVKEPIDIVEGIKKEQAVTLAQkmGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEdSDGKVLCMDAKINFDS 286
Cdd:PLN02235 144 WDKVKTIFLPTEAPLTSEICAPLIA--TLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTL-VDGEPYPLDMRGELDD 220


                 ....*...
gi 74139919  287 NSAYRQKK 294
Cdd:PLN02235 221 TAAFKNFK 228
 
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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