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Conserved domains on  [gi|6980734|pdb|1CQJ|E]
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Chain E, Crystal Structure Of Dephosphorylated E. Coli Succinyl-coa Synthetase

Protein Classification

succinate--CoA ligase subunit beta (domain architecture ID 11479099)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sucC PRK00696
succinyl-CoA synthetase subunit beta; Provisional
1-385 0e+00

succinyl-CoA synthetase subunit beta; Provisional


:

Pssm-ID: 234813  Cd Length: 388  Bit Score: 696.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK00696  81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E       321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAA 385
 
Name Accession Description Interval E-value
sucC PRK00696
succinyl-CoA synthetase subunit beta; Provisional
1-385 0e+00

succinyl-CoA synthetase subunit beta; Provisional


Pssm-ID: 234813  Cd Length: 388  Bit Score: 696.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK00696  81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E       321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAA 385
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
1-385 0e+00

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: 639.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:TIGR01016  81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E        321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAA 385
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion];
1-385 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion];


Pssm-ID: 223123 [Multi-domain]  Cd Length: 387  Bit Score: 592.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKr 80
Cdd:COG0045   1 MNLHEYQAKELFAKYGIPVPPGYVATSPEEAEEAAKELGGGPVVVKAQVHAGGRGKAGGVKLAKSPEEAKEAAEEILGK- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       81 lvTYQTDANGQPVNQILVEAATD-IAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQ 159
Cdd:COG0045  80 --NYQTDIKGEPVNKVLVEEAVDiIKKEYYLSIVLDRSSRRPVLMASTEGGMDIEEVAEKTPEKIVKVSVDPLTGLRPYQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E      160 GRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITK-QGDLICLDGKLGADGNALFRQPDLREMRDQSQE 238
Cdd:COG0045 158 ARELAFKLGLEGELVKQVADIIKKLYKLFVEKDATLVEINPLVVTPdGGDVLALDAKITLDDNALFRHPDLAELRDESEE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E      239 DPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNI 318
Cdd:COG0045 238 DPREAEASGYGLNYVELDGNIGCIVNGAGLAMATMDIVKLYGGKPANFLDVGGGATAERVKEAFKLILSDPNVKAIFVNI 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CQJ_E      319 FGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:COG0045 318 FGGITRCDEVAEGIIAALKEVGVNVPLVVRLEGTNVEEGKRILAESGLNIIAADDLDEAAEKAVELA 384
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-203 1.20e-112

ATP-grasp domain;


Pssm-ID: 285620 [Multi-domain]  Cd Length: 202  Bit Score: 326.90  E-value: 1.20e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          2 NLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRL 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVAFSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEAAKEMLGKNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         82 VTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGR 161
Cdd:pfam08442  81 VTKQTGPEGKPVNKVLVEEALDIKREYYLSIVLDRASKGPVVIASTEGGVDIEEVAAKNPEAIIKVPIDPAKGLQPYQAR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1CQJ_E        162 ELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVI 203
Cdd:pfam08442 161 EIAFKLGLPGELVKQAADIIKKLYKLFVEYDATLVEINPLVE 202
 
Name Accession Description Interval E-value
sucC PRK00696
succinyl-CoA synthetase subunit beta; Provisional
1-385 0e+00

succinyl-CoA synthetase subunit beta; Provisional


Pssm-ID: 234813  Cd Length: 388  Bit Score: 696.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK00696  81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E       321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAA 385
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
1-385 0e+00

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: 639.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:TIGR01016  81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E        321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAA 385
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion];
1-385 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion];


Pssm-ID: 223123 [Multi-domain]  Cd Length: 387  Bit Score: 592.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKr 80
Cdd:COG0045   1 MNLHEYQAKELFAKYGIPVPPGYVATSPEEAEEAAKELGGGPVVVKAQVHAGGRGKAGGVKLAKSPEEAKEAAEEILGK- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       81 lvTYQTDANGQPVNQILVEAATD-IAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQ 159
Cdd:COG0045  80 --NYQTDIKGEPVNKVLVEEAVDiIKKEYYLSIVLDRSSRRPVLMASTEGGMDIEEVAEKTPEKIVKVSVDPLTGLRPYQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E      160 GRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITK-QGDLICLDGKLGADGNALFRQPDLREMRDQSQE 238
Cdd:COG0045 158 ARELAFKLGLEGELVKQVADIIKKLYKLFVEKDATLVEINPLVVTPdGGDVLALDAKITLDDNALFRHPDLAELRDESEE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E      239 DPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNI 318
Cdd:COG0045 238 DPREAEASGYGLNYVELDGNIGCIVNGAGLAMATMDIVKLYGGKPANFLDVGGGATAERVKEAFKLILSDPNVKAIFVNI 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CQJ_E      319 FGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAV 385
Cdd:COG0045 318 FGGITRCDEVAEGIIAALKEVGVNVPLVVRLEGTNVEEGKRILAESGLNIIAADDLDEAAEKAVELA 384
PRK14046 PRK14046
malate--CoA ligase subunit beta; Provisional
1-384 3.60e-174

malate--CoA ligase subunit beta; Provisional


Pssm-ID: 237594  Cd Length: 392  Bit Score: 490.38  E-value: 3.60e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK14046   1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK14046  81 LVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK14046 161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK14046 241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
1CQJ_E       321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAA 384
Cdd:PRK14046 321 GINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAVEA 384
PLN00124 PLN00124
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
1-384 2.75e-134

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


Pssm-ID: 177736 [Multi-domain]  Cd Length: 422  Bit Score: 390.26  E-value: 2.75e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKI--GAGPWVVKCQVHAGGRGKA-------GGVKVVnSKEDIRA 71
Cdd:PLN00124  28 LNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpDEGEVVVKSQILAGGRGLGtfknglkGGVHIV-KKDKAEE 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        72 FAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDP 151
Cdd:PLN00124 107 LAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDI 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       152 LTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLRE 231
Cdd:PLN00124 187 FKGITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFA 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       232 MRDQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKV 311
Cdd:PLN00124 267 LRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKV 346
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1CQJ_E       312 KAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAA 384
Cdd:PLN00124 347 KAILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKA 419
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-203 1.20e-112

ATP-grasp domain;


Pssm-ID: 285620 [Multi-domain]  Cd Length: 202  Bit Score: 326.90  E-value: 1.20e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          2 NLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRL 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVAFSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEAAKEMLGKNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         82 VTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGR 161
Cdd:pfam08442  81 VTKQTGPEGKPVNKVLVEEALDIKREYYLSIVLDRASKGPVVIASTEGGVDIEEVAAKNPEAIIKVPIDPAKGLQPYQAR 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1CQJ_E        162 ELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVI 203
Cdd:pfam08442 161 EIAFKLGLPGELVKQAADIIKKLYKLFVEYDATLVEINPLVE 202
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
262-382 3.94e-29

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: 334139 [Multi-domain]  Cd Length: 128  Bit Score: 109.27  E-value: 3.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        262 MVNGAGLAMGTMDIVKLHGGEPANFLDVGGGA-TKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVG 340
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1CQJ_E        341 VNVPVV-VRLEGNNA-----ELGAKKLADSGLNIIAAKGLTDAAQQVV 382
Cdd:pfam00549  81 ARELPVvARVCGTEAdpqgrEEQAKALAESGVLIASSNNQALRAAGAV 128
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
3-115 5.23e-09

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


Pssm-ID: 338812  Cd Length: 221  Bit Score: 55.93  E-value: 5.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          3 LHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGaGPWVVKCqVHAGGRGK--AGGVKV-VNSKEDIRAfAENWLGK 79
Cdd:pfam13549  10 LTEHEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIG-YPVVLKI-VSPDILHKsdVGGVRLnLRSAEEVRA-AYEAILA 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
1CQJ_E         80 RLVTYQTDANgqpVNQILVEAATDIAKELYLGAVVD 115
Cdd:pfam13549  87 RVRRYRPDAR---IEGVLVQPMAPRGRELIVGVTRD 119
PLN02235 PLN02235
ATP citrate (pro-S)-lyase
3-338 1.12e-06

ATP citrate (pro-S)-lyase


Pssm-ID: 177879  Cd Length: 423  Bit Score: 50.15  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         3 LHEYQAKQLFARY-----GLPAPVGYACTTprEAEEAASKIGAGPW------VVKCQVHAGGRGKAGGVKVVNSKEDIRA 71
Cdd:PLN02235   6 IREYDSKRLLKEHlkrlaGIDLPIRSAQVT--ESTDFNELANKEPWlsstklVVKPDMLFGKRGKSGLVALNLDLAQVAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        72 FAENWLGKrlvTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFmaSTEGGVEIEK-------VAEETPHLI 144
Cdd:PLN02235  84 FVKERLGK---EVEMGGCKGPITTFIVEPFVPHDQEFYLSIVSDRLGCSISF--SECGGIEIEEnwdkvktIFLPTEAPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       145 HKVALDPLTGPMPyqgrelafkLGLEGKLvQQFTKifmGLATIFLERDLALIEINPLVITkQGDLICLDGKLGADGNALF 224
Cdd:PLN02235 159 TSEICAPLIATLP---------LEIRGKI-EEFIK---GVFAVFQDLDFTFLEMNPFTLV-DGEPYPLDMRGELDDTAAF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E       225 RQ-----------PDLREMR--DQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG--GEPANFLDV 289
Cdd:PLN02235 225 KNfkkwgniefplPFGRVMSptESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGyaSELGNYAEY 304
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
1CQJ_E       290 GGGATKERVTEAFKIILS------DDKVKAVLvnIFGGIVR-CDLIA--DGIIGAVAE 338
Cdd:PLN02235 305 SGAPNEEEVLQYARVVIDcatanpDGRKRALL--IGGGIANfTDVAAtfNGIIRALRE 360
purD TIGR00877
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ...
8-125 2.93e-05

phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273315 [Multi-domain]  Cd Length: 422  Bit Score: 45.76  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          8 AKQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAENWLGKRLvtyqtd 87
Cdd:TIGR00877 108 AKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGA-PIVVKADGLAAGK----GVIVAKTNEEAIKAVEDILEQKF------ 176
                          90       100       110
                  ....*....|....*....|....*....|....*...
1CQJ_E         88 anGQPVNQILVEAATDiAKELYLGAVVDRssRRVVFMA 125
Cdd:TIGR00877 177 --GDAGERVVIEEFLD-GEEFSLLAFVDG--KTVIPMP 209
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism];
8-126 5.17e-05

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism];


Pssm-ID: 223229 [Multi-domain]  Cd Length: 428  Bit Score: 44.86  E-value: 5.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        8 AKQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAENWLGKrlvtyqtD 87
Cdd:COG0151 107 AKDFMKKYGIPTAEYEVFTDPEEAKAYIDEKGA-PIVVKADGLAAGK----GVIVAMTLEEAEAAVDEMLEG-------N 174
                        90       100       110
                ....*....|....*....|....*....|....*....
1CQJ_E       88 ANGQPVNQILVEAATDiAKELYLGAVVDrsSRRVVFMAS 126
Cdd:COG0151 175 AFGSAGARVVIEEFLD-GEEFSLQAFVD--GKTVIPMPT 210
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism];
8-123 2.94e-04

Biotin carboxylase [Lipid transport and metabolism];


Pssm-ID: 223516 [Multi-domain]  Cd Length: 449  Bit Score: 42.64  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        8 AKQLFARYGLPAPVG--YACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKVVNSKED-------IRAFAENWLG 78
Cdd:COG0439 119 ARRLMAKAGVPVVPGsdGAVADNEEALAIAEEIGY-PVIVKAAAGGGGR----GMRVVRNEEEleaafeaARGEAEAAFG 193
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1CQJ_E       79 K------------RLVTYQTDANG--------------QPVNQILVE--AATDIAKEL--YLGAVVDRSSRRVVF 123
Cdd:COG0439 194 NprvylekfiegpRHIEVQVLGDGhgnvihlgerdcsiQRRHQKVIEeaPSPLLTEELreKIGEAAVRAAKLIGY 268
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
9-99 1.23e-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: 40.75  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E           9 KQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGvkVVNSKEDIRAFAENWLgkrlvtyqtda 88
Cdd:TIGR01369  132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGY-PVIVRPAFTLGGTG--GG--IAYNREELKEIAERAL----------- 195
                           90
                   ....*....|.
1CQJ_E          89 NGQPVNQILVE 99
Cdd:TIGR01369  196 SASPINQVLVE 206
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
8-99 1.30e-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: 307287 [Multi-domain]  Cd Length: 194  Bit Score: 39.19  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          8 AKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAENWLgkrlvtyQTD 87
Cdd:pfam01071   6 AKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK----GVIVASSNEEAIKAVDEIL-------EQK 74
                          90
                  ....*....|..
1CQJ_E         88 ANGQPVNQILVE 99
Cdd:pfam01071  75 KFGEAGETVVIE 86
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
9-99 1.70e-03

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism];


Pssm-ID: 223534 [Multi-domain]  Cd Length: 400  Bit Score: 39.99  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E        9 KQLFARYGLPAPvGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAENWLGKrlvtyqtda 88
Cdd:COG0458 121 KEAMREIGIPVP-SRIAHSVEEADEIADEIGY-PVIVKPSFGLGGS----GGGIAYNEEELEEIIEEGLRA--------- 185
                        90
                ....*....|.
1CQJ_E       89 ngQPVNQILVE 99
Cdd:COG0458 186 --SPVEEVLIE 194
RTC pfam01137
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
29-145 2.27e-03

RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organisms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.


Pssm-ID: 334399  Cd Length: 325  Bit Score: 39.43  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E         29 REAEEAASK-IGAGPWVVKCQVH-----AGGRGKAGGVKVVNSKEDIRAFAENwLGKRlvtyqtdanGQPVNQILVEAAT 102
Cdd:pfam01137 197 RMVAAARGLlLKFLPDVYIETDVykgeeSGAGGGGGITLVAETTEGCLLGASA-LGER---------GKPAEDVGEEAAE 266
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
1CQJ_E        103 DIAKELYLGAVVDRSSRR--VVFMASTEGGVEIeKVAEETPHLIH 145
Cdd:pfam01137 267 ELLEELESGGCVDEHLQDqlILFMALAKGGSRI-RTGPLTLHTIT 310
PRK14016 PRK14016
cyanophycin synthetase; Provisional
9-74 2.53e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 39.75  E-value: 2.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CQJ_E         9 KQLFARYGLPAPVGYACTTPREAEEAASKIGaGPWVVKCQvhAGGRGKagGVKV-VNSKEDIR-AFAE 74
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIG-YPVVVKPL--DGNHGR--GVTVnITTREEIEaAYAV 281
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
16-82 2.64e-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: 280399 [Multi-domain]  Cd Length: 169  Bit Score: 37.99  E-value: 2.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CQJ_E         16 GLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHaGGRGKagGVKVVNSKEDIRAFAENWLGKRLV 82
Cdd:pfam02222   4 GLPTPRFMFAESLEELIKAGQELGF-PCVVKARRG-GYDGK--GQYVIRSEADIQQAWEELGGGPVI 66
carB PRK05294
carbamoyl phosphate synthase large subunit; Reviewed
9-99 4.77e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 38.92  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CQJ_E          9 KQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGvkVVNSKEDIRAFAENWLgkrlvtyqtDA 88
Cdd:PRK05294  133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGY-PVIIRPSFTLGGTG--GG--IAYNEEELEEIVERGL---------DL 198
                          90
                  ....*....|.
1CQJ_E         89 NgqPVNQILVE 99
Cdd:PRK05294  199 S--PVTEVLIE 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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