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Conserved domains on  [gi|3860989|emb|CAA14889|]
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SUCCINYL-COA LIGASE (sucD) [Rickettsia prowazekii str. Madrid E]

Protein Classification

succinate--CoA ligase subunit alpha( domain architecture ID 11481473)

ADP-forming/GDP-forming succinate--CoA ligase subunit alpha is the coenzyme A and phosphate binding subunit of the succinyl-CoA synthetase that couples the hydrolysis of succinyl-CoA to the synthesis of ATP/GTP, as part of the citric acid cycle (TCA)

CATH:  3.40.50.261
EC:  6.2.1.-
Gene Ontology:  GO:0000166|GO:0016874|GO:0003824
SCOP:  4000071

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-291 0e+00

succinyl-CoA synthetase subunit alpha; Validated


:

Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 531.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     1 MAILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:PRK05678   1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFNTVAEAVEATGANASVIYVPPPFAAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    81 SILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYE 160
Cdd:PRK05678  81 AILEAIDAGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRSGTLTYE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   161 AVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSkIKKPIVSFIAGITA 240
Cdd:PRK05678 161 AVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKAN-VTKPVVGYIAGVTA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 3860989   241 PADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLLNK 291
Cdd:PRK05678 240 PPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
 
Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-291 0e+00

succinyl-CoA synthetase subunit alpha; Validated


Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 531.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     1 MAILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:PRK05678   1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFNTVAEAVEATGANASVIYVPPPFAAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    81 SILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYE 160
Cdd:PRK05678  81 AILEAIDAGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRSGTLTYE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   161 AVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSkIKKPIVSFIAGITA 240
Cdd:PRK05678 161 AVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKAN-VTKPVVGYIAGVTA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 3860989   241 PADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLLNK 291
Cdd:PRK05678 240 PPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 2-289 0e+00

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


Pssm-ID: 439844 [Multi-domain]  Cd Length: 288  Bit Score: 529.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    2 AILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADS 81
Cdd:COG0074   1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   82 ILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYEA 161
Cdd:COG0074  81 ILEAIDAGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSGTLTYEA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989  162 VAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKqSKIKKPIVSFIAGITAP 241
Cdd:COG0074 161 VWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIK-ENMTKPVVAYIAGRTAP 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3860989  242 ADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLL 289
Cdd:COG0074 240 PGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
sucCoAalpha TIGR01019
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ...
 3-289 0e+00

succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]


Pssm-ID: 130091 [Multi-domain]  Cd Length: 286  Bit Score: 510.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989      3 ILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADSI 82
Cdd:TIGR01019   1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFDSVKEAVEETGANASVIFVPAPFAADAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     83 LEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYEAV 162
Cdd:TIGR01019  81 FEAIDAGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGTLTYEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    163 AQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSkIKKPIVSFIAGITAPA 242
Cdd:TIGR01019 161 HQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQN-MSKPVVGFIAGATAPP 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 3860989    243 DKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLL 289
Cdd:TIGR01019 240 GKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEIL 286
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-99 7.37e-31

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 111.15  E-value: 7.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989      6 NKKTKVICQGFT--GSQGT-FHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADSI 82
Cdd:pfam02629   1 DKDTKVIVIGAGglGIQGLnYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSVDELEEKTGVDVAVITVPAPFAQEAI 80

                          90
                  ....*....|....*..
gi 3860989     83 LEAIDAKIEVVVCITEG 99
Cdd:pfam02629  81 DELVDAGIKGIVNITPG 97
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 4-100 4.25e-30

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 109.14  E-value: 4.25e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989       4 LINKKTKVICQGFTGSQGTFHSEQAIA---YGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNlleYGTKFVGGVYPGKVGPKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPD 80

                           90       100
                   ....*....|....*....|
gi 3860989      81 SILEAIDAKIEVVVCITEGI 100
Cdd:smart00881  81 AIDEAIEAGIKGIVVITEGI 100
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
 196-275 4.27e-03

Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.


Pssm-ID: 132933 [Multi-domain]  Cd Length: 214  Bit Score: 37.54  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989  196 LQDDETKAIIMI-----GEIGGSAEedAADFIKQSKIKKPIVSFIAG--------ITAPADK----RMGHAGAIisGGKG 258
Cdd:cd07022  38 LADPDVRAIVLDidspgGEVAGVFE--LADAIRAARAGKPIVAFVNGlaasaaywIASAADRivvtPTAGVGSI--GVVA 113

                        90
                ....*....|....*..
gi 3860989  259 SAEDKVEVLQSAGVIIT 275
Cdd:cd07022 114 SHVDQSKALEKAGLKVT 130
 
Name Accession Description Interval E-value
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-291 0e+00

succinyl-CoA synthetase subunit alpha; Validated


Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 531.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     1 MAILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:PRK05678   1 MSILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFNTVAEAVEATGANASVIYVPPPFAAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    81 SILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYE 160
Cdd:PRK05678  81 AILEAIDAGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRSGTLTYE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   161 AVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSkIKKPIVSFIAGITA 240
Cdd:PRK05678 161 AVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKAN-VTKPVVGYIAGVTA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 3860989   241 PADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLLNK 291
Cdd:PRK05678 240 PPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKG 290
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 2-289 0e+00

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


Pssm-ID: 439844 [Multi-domain]  Cd Length: 288  Bit Score: 529.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    2 AILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADS 81
Cdd:COG0074   1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   82 ILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYEA 161
Cdd:COG0074  81 ILEAIDAGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSGTLTYEA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989  162 VAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKqSKIKKPIVSFIAGITAP 241
Cdd:COG0074 161 VWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIK-ENMTKPVVAYIAGRTAP 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3860989  242 ADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLL 289
Cdd:COG0074 240 PGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
sucCoAalpha TIGR01019
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ...
 3-289 0e+00

succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]


Pssm-ID: 130091 [Multi-domain]  Cd Length: 286  Bit Score: 510.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989      3 ILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADSI 82
Cdd:TIGR01019   1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFDSVKEAVEETGANASVIFVPAPFAADAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     83 LEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYEAV 162
Cdd:TIGR01019  81 FEAIDAGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGTLTYEAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    163 AQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSkIKKPIVSFIAGITAPA 242
Cdd:TIGR01019 161 HQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQN-MSKPVVGFIAGATAPP 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 3860989    243 DKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLL 289
Cdd:TIGR01019 240 GKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEIL 286
PTZ00187 PTZ00187
succinyl-CoA synthetase alpha subunit; Provisional
 3-291 0e+00

succinyl-CoA synthetase alpha subunit; Provisional


Pssm-ID: 240307 [Multi-domain]  Cd Length: 317  Bit Score: 502.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     3 ILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHL--NLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:PTZ00187  24 VWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGTTHLkhGLPVFATVKEAKKATGADASVIYVPPPHAAS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    81 SILEAIDAKIEVVVCITEGIPVLDMIKVKRALI-GSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTY 159
Cdd:PTZ00187 104 AIIEAIEAEIPLVVCITEGIPQHDMVKVKHALLsQNKTRLIGPNCPGIIKPGECKIGIMPGHIHKKGKIGIVSRSGTLTY 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   160 EAVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSKIKKPIVSFIAGIT 239
Cdd:PTZ00187 184 EAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGIT 263

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 3860989   240 APADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLLNK 291
Cdd:PTZ00187 264 APPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMKK 315
PLN00125 PLN00125
Succinyl-CoA ligase [GDP-forming] subunit alpha
 2-289 1.27e-163

Succinyl-CoA ligase [GDP-forming] subunit alpha


Pssm-ID: 215066 [Multi-domain]  Cd Length: 300  Bit Score: 456.35  E-value: 1.27e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989     2 AILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADS 81
Cdd:PLN00125   6 AVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTEHLGLPVFNTVAEAKAETKANASVIYVPPPFAAAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    82 ILEAIDAKIEVVVCITEGIPVLDMIKVKRALIG-SKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYE 160
Cdd:PLN00125  86 ILEAMEAELDLVVCITEGIPQHDMVRVKAALNRqSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTLTYE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   161 AVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSKIKKPIVSFIAGITA 240
Cdd:PLN00125 166 AVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 3860989   241 PADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLL 289
Cdd:PLN00125 246 PPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGVAMLEVF 294
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-99 7.37e-31

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 111.15  E-value: 7.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989      6 NKKTKVICQGFT--GSQGT-FHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADSI 82
Cdd:pfam02629   1 DKDTKVIVIGAGglGIQGLnYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSVDELEEKTGVDVAVITVPAPFAQEAI 80

                          90
                  ....*....|....*..
gi 3860989     83 LEAIDAKIEVVVCITEG 99
Cdd:pfam02629  81 DELVDAGIKGIVNITPG 97
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 4-100 4.25e-30

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 109.14  E-value: 4.25e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989       4 LINKKTKVICQGFTGSQGTFHSEQAIA---YGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAAD 80
Cdd:smart00881   1 LLNPNTSVAVVGASGNLGSFGLAVMRNlleYGTKFVGGVYPGKVGPKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPD 80

                           90       100
                   ....*....|....*....|
gi 3860989      81 SILEAIDAKIEVVVCITEGI 100
Cdd:smart00881  81 AIDEAIEAGIKGIVVITEGI 100
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 151-273 7.60e-30

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: 109.66  E-value: 7.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    151 VSRSGTLTYEAVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIG-GSAEEDAADFIKQSK--- 226
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIKear 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 3860989    227 -IKKPIVSFIAGITAPADKRMGHAGAIISGGKGSAEDKVEVLQSAGVI 273
Cdd:pfam00549  81 aRELPVVARVCGTEADPQGRSGQAKALAESGVLIASSNNQALRAAGAV 128
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
 37-277 3.27e-26

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 107.98  E-value: 3.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    37 GGVTPGKGGHTHL-------NLPVYNTVHEA-KAKTGANASVIYVPPGFAADSILEAIDA-KIEVVVCITEGIPVLDMIK 107
Cdd:PLN02522  42 GIINPGSEGFQKLffgqeeiAIPVHGSIEAAcKAHPTADVFINFASFRSAAASSMEALKQpTIRVVAIIAEGVPESDTKQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   108 VKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKI--------GDIGIVSRSGTLT---YEAVAQTTAaglGQSTCV 176
Cdd:PLN02522 122 LIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIiqcklyrpGSVGFVSKSGGMSnemYNVIARVTD---GIYEGI 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   177 GIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSKIKKPIVSFIAGITA---PADKRMGHAGAII 253
Cdd:PLN02522 199 AIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEALKQGKVSKPVVAWVSGTCArlfKSEVQFGHAGAKS 278

                        250       260
                 ....*....|....*....|....
gi 3860989   254 SGGKGSAEDKVEVLQSAGVIITRS 277
Cdd:PLN02522 279 GGDMESAQAKNKALKDAGAIVPTS 302
PRK06091 PRK06091
membrane protein FdrA; Validated
 66-241 2.97e-08

membrane protein FdrA; Validated


Pssm-ID: 180395 [Multi-domain]  Cd Length: 555  Bit Score: 54.28  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989    66 ANASVIYVPPGFAADSILEAIDAKIEVVVcITEGIPVLDMIKVK-----RALIgsktrLIGPNCpgvitpGECKIGIMP- 139
Cdd:PRK06091 118 ANLALISVAGEYAAELAEQALDRNLNVMM-FSDNVTLEDEIRLKtrareKGLL-----VMGPDC------GTAMIAGTPl 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989   140 --GHIHKIGDIGIVSRSGTLTYEAVAQTTAAGLGQSTCVGIGG----DPVNGTSFVDCIEMFLQDDETKAIIMIGEigGS 213
Cdd:PRK06091 186 afANVMPEGNIGVIGASGTGIQELCSQIALAGEGITHAIGLGGrdlsAEVGGISALTALEMLSADEKSEVIAFVSK--PP 263

                        170       180
                 ....*....|....*....|....*....
gi 3860989   214 AEEDAADFIKQSK-IKKPIVSFIAGITAP 241
Cdd:PRK06091 264 AEAVRLKIINAMKaTGKPVVALFLGYTPA 292
S49_Sppa_36K_type cd07022
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ...
 196-275 4.27e-03

Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; Signal peptide peptidase A (SppA; Peptidase S49; Protease IV) 36K type: SppA is found in all three domains of life and is involved in the cleavage of signal peptides after their removal from the precursor proteins by signal peptidases. Members in this subfamily are all bacterial and include sohB peptidase and protein C. These are sometimes referred to as 36K type since they contain only one domain, unlike E. coli SppA that also contains an amino-terminal domain. Site-directed mutagenesis and sequence analysis have shown these SppAs to be serine proteases. The predicted active site serine for members in this family occurs in a transmembrane domain. Mutagenesis studies also suggest that the catalytic center comprises a Ser-Lys dyad and not the usual Ser-His-Asp catalytic triad found in the majority of serine proteases.


Pssm-ID: 132933 [Multi-domain]  Cd Length: 214  Bit Score: 37.54  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860989  196 LQDDETKAIIMI-----GEIGGSAEedAADFIKQSKIKKPIVSFIAG--------ITAPADK----RMGHAGAIisGGKG 258
Cdd:cd07022  38 LADPDVRAIVLDidspgGEVAGVFE--LADAIRAARAGKPIVAFVNGlaasaaywIASAADRivvtPTAGVGSI--GVVA 113

                        90
                ....*....|....*..
gi 3860989  259 SAEDKVEVLQSAGVIIT 275
Cdd:cd07022 114 SHVDQSKALEKAGLKVT 130
 
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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