|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
49-346 |
0e+00 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 589.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 49 PPAAVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFA 128
Cdd:PLN00125 3 PPPAVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTEHLGLPVFNTVAEAKAETKANASVIYVPPPFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 129 AAAIMEGIQAELDLVVCITEGIPQHDMVRVKHALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTL 208
Cdd:PLN00125 83 AAAILEAMEAELDLVVCITEGIPQHDMVRVKAALNRQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 209 TYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTEKPVVAFIAG 288
Cdd:PLN00125 163 TYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072932338 289 LTAPPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFKERGLL 346
Cdd:PLN00125 243 LTAPPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGVAMLEVFKERGLL 300
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
52-341 |
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: 539.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 52 AVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAA 131
Cdd:COG0074 1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 132 IMEGIQAELDLVVCITEGIPQHDMVRVKHALNsQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYE 211
Cdd:COG0074 81 ILEAIDAGIKLIVCITEGIPVLDMVRVKRYAK-AKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSGTLTYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 212 AVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTeKPVVAFIAGLTA 291
Cdd:COG0074 160 AVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKENMT-KPVVAYIAGRTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1072932338 292 PPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFK 341
Cdd:COG0074 239 PPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
53-339 |
1.85e-176 |
|
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: 490.78 E-value: 1.85e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 53 VFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAAI 132
Cdd:TIGR01019 1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFDSVKEAVEETGANASVIFVPAPFAADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 133 MEGIQAELDLVVCITEGIPQHDMVRVKhALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYEA 212
Cdd:TIGR01019 81 FEAIDAGIELIVCITEGIPVHDMLKVK-RYMEESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGTLTYEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 213 VFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTeKPVVAFIAGLTAP 292
Cdd:TIGR01019 160 VHQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQNMS-KPVVGFIAGATAP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1072932338 293 PGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDL 339
Cdd:TIGR01019 239 PGKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEI 285
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
56-149 |
1.67e-35 |
|
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: 124.63 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 56 DKNTRVMCQGITGKNG---TFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAAI 132
Cdd:pfam02629 1 DKDTKVIVIGAGGLGIqglNYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSVDELEEKTGVDVAVITVPAPFAQEAI 80
|
90
....*....|....*..
gi 1072932338 133 MEGIQAELDLVVCITEG 149
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 ... |
54-150 |
6.28e-32 |
|
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: 115.30 E-value: 6.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 54 FVDKNTRVMCQGITGKNGTFHTEQAI---EYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAA 130
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGSFGLAVMRnllEYGTKFVGGVYPGKVGPKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPD 80
|
90 100
....*....|....*....|
gi 1072932338 131 AIMEGIQAELDLVVCITEGI 150
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; ... |
249-325 |
1.04e-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: 39.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 249 DPQTEGIVLI-----GEIGGTAEedAAALIKASGTEKPVVAFIAGL---------------TAPPGRRMGHAGAIVSggk 308
Cdd:cd07022 40 DPDVRAIVLDidspgGEVAGVFE--LADAIRAARAGKPIVAFVNGLaasaaywiasaadriVVTPTAGVGSIGVVAS--- 114
|
90
....*....|....*..
gi 1072932338 309 gtAQDKIKSLNDAGVKV 325
Cdd:cd07022 115 --HVDQSKALEKAGLKV 129
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
49-346 |
0e+00 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 589.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 49 PPAAVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFA 128
Cdd:PLN00125 3 PPPAVFVDKNTRVICQGITGKNGTFHTEQAIEYGTKMVGGVTPKKGGTEHLGLPVFNTVAEAKAETKANASVIYVPPPFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 129 AAAIMEGIQAELDLVVCITEGIPQHDMVRVKHALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTL 208
Cdd:PLN00125 83 AAAILEAMEAELDLVVCITEGIPQHDMVRVKAALNRQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 209 TYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTEKPVVAFIAG 288
Cdd:PLN00125 163 TYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072932338 289 LTAPPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFKERGLL 346
Cdd:PLN00125 243 LTAPPGRRMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGVAMLEVFKERGLL 300
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
35-344 |
0e+00 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 573.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 35 SSSLTQSRSFASSDPpaAVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHL--GLPVFNSVAEAKA 112
Cdd:PTZ00187 8 ILKVSFRARSSTSAP--RVWVNKNTKVICQGITGKQGTFHTEQAIEYGTKMVGGVNPKKAGTTHLkhGLPVFATVKEAKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 113 ETKANASVIYVPAPFAAAAIMEGIQAELDLVVCITEGIPQHDMVRVKHALNSQSKTRLIGPNCPGIIKPGECKIGIMPGY 192
Cdd:PTZ00187 86 ATGADASVIYVPPPHAASAIIEAIEAEIPLVVCITEGIPQHDMVKVKHALLSQNKTRLIGPNCPGIIKPGECKIGIMPGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 193 IHKPGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAAL 272
Cdd:PTZ00187 166 IHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEEAAEW 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072932338 273 IKASGTEKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFKERG 344
Cdd:PTZ00187 246 IKNNPIKKPVVSFIAGITAPPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMKKKG 317
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
52-341 |
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: 539.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 52 AVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAA 131
Cdd:COG0074 1 SILVNKNTRVIVQGITGKEGSFHTKQMLAYGTNVVAGVTPGKGGQTVLGVPVFDTVAEAVEETGADASVIFVPPPFAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 132 IMEGIQAELDLVVCITEGIPQHDMVRVKHALNsQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYE 211
Cdd:COG0074 81 ILEAIDAGIKLIVCITEGIPVLDMVRVKRYAK-AKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSGTLTYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 212 AVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTeKPVVAFIAGLTA 291
Cdd:COG0074 160 AVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKENMT-KPVVAYIAGRTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1072932338 292 PPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFK 341
Cdd:COG0074 239 PPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKALK 288
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
52-343 |
0e+00 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 530.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 52 AVFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAA 131
Cdd:PRK05678 2 SILINKDTKVIVQGITGKQGTFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFNTVAEAVEATGANASVIYVPPPFAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 132 IMEGIQAELDLVVCITEGIPQHDMVRVKHALNsQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYE 211
Cdd:PRK05678 82 ILEAIDAGIDLIVCITEGIPVLDMLEVKAYLE-RKKTRLIGPNCPGIITPGECKIGIMPGHIHKKGRVGVVSRSGTLTYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 212 AVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTeKPVVAFIAGLTA 291
Cdd:PRK05678 161 AVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKANVT-KPVVGYIAGVTA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1072932338 292 PPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDLFKER 343
Cdd:PRK05678 240 PPGKRMGHAGAIISGGKGTAEEKKEALEAAGVKVARTPSEIGELLKEVLKGL 291
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
53-339 |
1.85e-176 |
|
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: 490.78 E-value: 1.85e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 53 VFVDKNTRVMCQGITGKNGTFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAAI 132
Cdd:TIGR01019 1 ILLDKDTKVIVQGITGSQGSFHTEQMLAYGTNIVGGVTPGKGGTTVLGLPVFDSVKEAVEETGANASVIFVPAPFAADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 133 MEGIQAELDLVVCITEGIPQHDMVRVKhALNSQSKTRLIGPNCPGIIKPGECKIGIMPGYIHKPGKIGIVSRSGTLTYEA 212
Cdd:TIGR01019 81 FEAIDAGIELIVCITEGIPVHDMLKVK-RYMEESGTRLIGPNCPGIITPGECKIGIMPGHIHKPGNVGIVSRSGTLTYEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 213 VFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTeKPVVAFIAGLTAP 292
Cdd:TIGR01019 160 VHQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQNMS-KPVVGFIAGATAP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1072932338 293 PGRRMGHAGAIVSGGKGTAQDKIKSLNDAGVKVVESPAKIGAAMYDL 339
Cdd:TIGR01019 239 PGKRMGHAGAIISGGKGTAESKIEALEAAGVTVVKSPSDIGELLAEI 285
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
56-149 |
1.67e-35 |
|
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: 124.63 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 56 DKNTRVMCQGITGKNG---TFHTEQAIEYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAAAI 132
Cdd:pfam02629 1 DKDTKVIVIGAGGLGIqglNYHFIQMLGYGIKMVFGVNPGKGGTEILGIPVYNSVDELEEKTGVDVAVITVPAPFAQEAI 80
|
90
....*....|....*..
gi 1072932338 133 MEGIQAELDLVVCITEG 149
Cdd:pfam02629 81 DELVDAGIKGIVNITPG 97
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
202-323 |
2.19e-33 |
|
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: 120.06 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 202 VSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFFVDPQTEGIVLIGEIG-GTAEEDAAALIKA----S 276
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAikeaR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1072932338 277 GTEKPVVAFIAGLTAPPGRRMGHAGAIVSGGKGTAQDKIKSLNDAGV 323
Cdd:pfam00549 81 ARELPVVARVCGTEADPQGRSGQAKALAESGVLIASSNNQALRAAGA 127
|
|
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
95-341 |
1.63e-32 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 127.63 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 95 GTEHLGLPVFNSVAEA-KAETKANASVIYVPAPFAAAAIMEGI-QAELDLVVCITEGIPQHDMVRVKHALNSQSKTrLIG 172
Cdd:PLN02522 57 GQEEIAIPVHGSIEAAcKAHPTADVFINFASFRSAAASSMEALkQPTIRVVAIIAEGVPESDTKQLIAYARANNKV-VIG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 173 PNCPGIIKPGECKIGIMPGYI--------HKPGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLE 244
Cdd:PLN02522 136 PATVGGIQAGAFKIGDTAGTLdniiqcklYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 245 KFFVDPQTEGIVLIGEIGGTAEEDAAALIKASGTEKPVVAFIAGLTA---PPGRRMGHAGAIVSGGKGTAQDKIKSLNDA 321
Cdd:PLN02522 216 RFNNIPQIKMIVVLGELGGRDEYSLVEALKQGKVSKPVVAWVSGTCArlfKSEVQFGHAGAKSGGDMESAQAKNKALKDA 295
|
250 260
....*....|....*....|
gi 1072932338 322 GVKVVESPAKIGAAMYDLFK 341
Cdd:PLN02522 296 GAIVPTSFEALEAAIKETFE 315
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
54-150 |
6.28e-32 |
|
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: 115.30 E-value: 6.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 54 FVDKNTRVMCQGITGKNGTFHTEQAI---EYGTNMVAGVTPKKGGTEHLGLPVFNSVAEAKAETKANASVIYVPAPFAAA 130
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGSFGLAVMRnllEYGTKFVGGVYPGKVGPKVDGVPVYDSVAEAPEETGVDVAVIFVPAEAAPD 80
|
90 100
....*....|....*....|
gi 1072932338 131 AIMEGIQAELDLVVCITEGI 150
Cdd:smart00881 81 AIDEAIEAGIKGIVVITEGI 100
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
196-305 |
6.64e-10 |
|
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer.
Pssm-ID: 433345 [Multi-domain] Cd Length: 138 Bit Score: 56.71 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 196 PGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGgdpfNGT--NFVDCLEKFFVDPQTEGIVL-IGEIGgtaeeDAAAL 272
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLG----NEAdvDFADLLEYLADDPETRVILLyLEGIR-----DGRRF 71
|
90 100 110
....*....|....*....|....*....|....*...
gi 1072932338 273 IKA---SGTEKPVVAFIAGLTaPPGRRMG--HAGAIVS 305
Cdd:pfam13607 72 LRAarrAARRKPVVVLKAGRS-EAGARAAasHTGALAG 108
|
|
| PRK06091 |
PRK06091 |
membrane protein FdrA; Validated |
116-298 |
1.35e-07 |
|
membrane protein FdrA; Validated
Pssm-ID: 180395 [Multi-domain] Cd Length: 555 Bit Score: 53.13 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 116 ANASVIYVPAPFAAAAIMEGIQAELDlVVCITEGIPQHDMVRVKHALNSQsktRLI--GPNCpgiikpGECKIGIMP--- 190
Cdd:PRK06091 118 ANLALISVAGEYAAELAEQALDRNLN-VMMFSDNVTLEDEIRLKTRAREK---GLLvmGPDC------GTAMIAGTPlaf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 191 GYIHKPGKIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFN----GTNFVDCLEKFFVDPQTEGIVLIGEIGGTA- 265
Cdd:PRK06091 188 ANVMPEGNIGVIGASGTGIQELCSQIALAGEGITHAIGLGGRDLSaevgGISALTALEMLSADEKSEVIAFVSKPPAEAv 267
|
170 180 190
....*....|....*....|....*....|...
gi 1072932338 266 EEDAAALIKASGteKPVVAFIAGLTaPPGRRMG 298
Cdd:PRK06091 268 RLKIINAMKATG--KPVVALFLGYT-PAVARDE 297
|
|
| S49_Sppa_36K_type |
cd07022 |
Signal peptide peptidase A (SppA) 36K type, a serine protease, has catalytic Ser-Lys dyad; ... |
249-325 |
1.04e-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: 39.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072932338 249 DPQTEGIVLI-----GEIGGTAEedAAALIKASGTEKPVVAFIAGL---------------TAPPGRRMGHAGAIVSggk 308
Cdd:cd07022 40 DPDVRAIVLDidspgGEVAGVFE--LADAIRAARAGKPIVAFVNGLaasaaywiasaadriVVTPTAGVGSIGVVAS--- 114
|
90
....*....|....*..
gi 1072932338 309 gtAQDKIKSLNDAGVKV 325
Cdd:cd07022 115 --HVDQSKALEKAGLKV 129
|
|
| |
