|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
4-686 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 702.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 4 SQLLHPASIVVVGASNNVHKPGGAILKNLLSGGYTGELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAV 82
Cdd:COG1042 7 DALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPpDLAVIAVPAETVPDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 83 EMLAaEKQVKAFIILSAGFGEETHEGAVLEDRILETVNRYGASLIGPNCIGFMNSWH--HSVFSQPIPQlhPQGVDLISS 160
Cdd:COG1042 87 EECG-EKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATglNATFAPVPPL--PGNIALVSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 161 SGATAVFILESAVTKGLQFNSVWSVGNAKQIGVEDVLQYMDEHfnpeADSRIKLLYIESIGDPDRLLFHASSLIKkGCKI 240
Cdd:COG1042 164 SGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADD----PDTRVILLYLEGIRDGRRFLSAARAAAR-GKPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 241 AAIKAGSSESGSRAASSHTGAIASSDSAVEALFRKAGIVRCYSREELTTVGCIFT-LPELKGKNFAIITHAGGPGVMLTD 319
Cdd:COG1042 239 VVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALArQPPPRGRRLAIVTNSGGPGVLAAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 320 ALSKGGLNVPKLEGPVAEELKGKLFPGAAVGNPIDILATGTPEHLCLCLEYCEEKfDNIDAVMAIFGTPGLVTMFEMYDV 399
Cdd:COG1042 319 ALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLAD-PNVDAVLVILTPTAMTDPEEVAEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 400 LHEKMLHCKKPIFPILPSINTAGAEVAAFLAKGHVNFADEVTLGTALS----------RIMNAPRPanneiELFGVDVPR 469
Cdd:COG1042 398 LIEAAKGSGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAalvryrrnqeRLMETPAS-----EDFDPDRER 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 470 IRRIIDSIPADG--YIAPHYVQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKVVGP--VHKSDVGGVVLNIKSE 545
Cdd:COG1042 473 ARAIIEAALAEGrgVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPdiLHKSDVGGVRLNLRDA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 546 QHLALEFDRMMQI-----PEASA--IMVQPMLK-GTELFIGAKYEEKFGHVVLCGLGGIFVEVLKDISSGLAPLSYEEAY 617
Cdd:COG1042 553 EAVRAAFEEILARvraarPDARIdgVLVQPMVPgGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALAR 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492395500 618 SMIHSLRAYKIIKGTRGQKGVNEDKFAEIIVRLSTLLRFATEIKEMDINPLLATEKQVIAVDARIRIEK 686
Cdd:COG1042 633 EMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAP 701
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-395 |
3.66e-101 |
|
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.
Pssm-ID: 131764 [Multi-domain] Cd Length: 447 Bit Score: 316.94 E-value: 3.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 6 LLHPASIVVVGASNNVHKPGGAILKNLLSGGYTGELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAVEM 84
Cdd:TIGR02717 4 LFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPvDLAVIVVPAKYVPQVVEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 85 lAAEKQVKAFIILSAGFGEETHEGAVLEDRILETVNRYGASLIGPNCIGFMNSwHHSV---FSQPIPQlhPQGVDLISSS 161
Cdd:TIGR02717 84 -CGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINT-HIKLnatFAPTMPK--KGGIAFISQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 162 GATAVFILESAVTKGLQFNSVWSVGNAKQIGVEDVLQYMDEhfnpEADSRIKLLYIESIGDPDRLLFHASSLIKKGcKIA 241
Cdd:TIGR02717 160 GALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLAD----DPDTKVILLYLEGIKDGRKFLKTAREISKKK-PIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 242 AIKAGSSESGSRAASSHTGAIASSDSAVEALFRKAGIVRCYSREELTTVGCIF-TLPELKGKNFAIITHAGGPGVMLTDA 320
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLsNQPLPKGNRVAIITNAGGPGVIATDA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492395500 321 LSKGGLNVPKLEGPVAEELKGKLFPGAAVGNPIDILATGTPEHLCLCLEYCEEKfDNIDAVMAIFgTPGLVTMFE 395
Cdd:TIGR02717 315 CEENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAED-ENVDGVVVVL-TPTAMTDPE 387
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
480-684 |
4.97e-67 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 219.27 E-value: 4.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 480 DGYIAPHYVQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKVVGP--VHKSDVGGVVLNIKSEQHLALEFDRMMQ 557
Cdd:pfam13549 7 RTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPdiLHKSDVGGVRLNLRSAEAVRAAYEEILE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 558 I-----PEA--SAIMVQPMLK-GTELFIGAKYEEKFGHVVLCGLGGIFVEVLKDISSGLAPLSYEEAYSMIHSLRAYKII 629
Cdd:pfam13549 87 RvrryrPDAriEGVLVQPMAPgGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492395500 630 KGTRGQKGVNEDKFAEIIVRLSTLLRFATEIKEMDINPLLATEKQVIAVDARIRI 684
Cdd:pfam13549 167 KGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
6-101 |
1.47e-15 |
|
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: 72.54 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 6 LLHPA-SIVVVGASNNVHKPGGAILKNLLSGGYTGELRaVNPKE--TEVQGVAAFADVKDIPDT---DLAILAIPAALCP 79
Cdd:smart00881 1 LLNPNtSVAVVGASGNLGSFGLAVMRNLLEYGTKFVGG-VYPGKvgPKVDGVPVYDSVAEAPEEtgvDVAVIFVPAEAAP 79
|
90 100
....*....|....*....|..
gi 492395500 80 DAVEMlAAEKQVKAFIILSAGF 101
Cdd:smart00881 80 DAIDE-AIEAGIKGIVVITEGI 100
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
491-580 |
1.02e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.53 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 491 LLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKvvgPVHKSDVGGVVLNIKSEQHLALEFDRMMQipEASAIMVQPML 570
Cdd:PRK14016 221 LLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK---PLDGNHGRGVTVNITTREEIEAAYAVASK--ESSDVIVERYI 295
|
90
....*....|...
gi 492395500 571 KGTE---LFIGAK 580
Cdd:PRK14016 296 PGKDhrlLVVGGK 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
4-686 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 702.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 4 SQLLHPASIVVVGASNNVHKPGGAILKNLLSGGYTGELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAV 82
Cdd:COG1042 7 DALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPpDLAVIAVPAETVPDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 83 EMLAaEKQVKAFIILSAGFGEETHEGAVLEDRILETVNRYGASLIGPNCIGFMNSWH--HSVFSQPIPQlhPQGVDLISS 160
Cdd:COG1042 87 EECG-EKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATglNATFAPVPPL--PGNIALVSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 161 SGATAVFILESAVTKGLQFNSVWSVGNAKQIGVEDVLQYMDEHfnpeADSRIKLLYIESIGDPDRLLFHASSLIKkGCKI 240
Cdd:COG1042 164 SGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADD----PDTRVILLYLEGIRDGRRFLSAARAAAR-GKPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 241 AAIKAGSSESGSRAASSHTGAIASSDSAVEALFRKAGIVRCYSREELTTVGCIFT-LPELKGKNFAIITHAGGPGVMLTD 319
Cdd:COG1042 239 VVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALArQPPPRGRRLAIVTNSGGPGVLAAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 320 ALSKGGLNVPKLEGPVAEELKGKLFPGAAVGNPIDILATGTPEHLCLCLEYCEEKfDNIDAVMAIFGTPGLVTMFEMYDV 399
Cdd:COG1042 319 ALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLAD-PNVDAVLVILTPTAMTDPEEVAEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 400 LHEKMLHCKKPIFPILPSINTAGAEVAAFLAKGHVNFADEVTLGTALS----------RIMNAPRPanneiELFGVDVPR 469
Cdd:COG1042 398 LIEAAKGSGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAalvryrrnqeRLMETPAS-----EDFDPDRER 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 470 IRRIIDSIPADG--YIAPHYVQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKVVGP--VHKSDVGGVVLNIKSE 545
Cdd:COG1042 473 ARAIIEAALAEGrgVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPdiLHKSDVGGVRLNLRDA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 546 QHLALEFDRMMQI-----PEASA--IMVQPMLK-GTELFIGAKYEEKFGHVVLCGLGGIFVEVLKDISSGLAPLSYEEAY 617
Cdd:COG1042 553 EAVRAAFEEILARvraarPDARIdgVLVQPMVPgGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALAR 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492395500 618 SMIHSLRAYKIIKGTRGQKGVNEDKFAEIIVRLSTLLRFATEIKEMDINPLLATEKQVIAVDARIRIEK 686
Cdd:COG1042 633 EMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAP 701
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-395 |
3.66e-101 |
|
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.
Pssm-ID: 131764 [Multi-domain] Cd Length: 447 Bit Score: 316.94 E-value: 3.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 6 LLHPASIVVVGASNNVHKPGGAILKNLLSGGYTGELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAVEM 84
Cdd:TIGR02717 4 LFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPvDLAVIVVPAKYVPQVVEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 85 lAAEKQVKAFIILSAGFGEETHEGAVLEDRILETVNRYGASLIGPNCIGFMNSwHHSV---FSQPIPQlhPQGVDLISSS 161
Cdd:TIGR02717 84 -CGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINT-HIKLnatFAPTMPK--KGGIAFISQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 162 GATAVFILESAVTKGLQFNSVWSVGNAKQIGVEDVLQYMDEhfnpEADSRIKLLYIESIGDPDRLLFHASSLIKKGcKIA 241
Cdd:TIGR02717 160 GALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLAD----DPDTKVILLYLEGIKDGRKFLKTAREISKKK-PIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 242 AIKAGSSESGSRAASSHTGAIASSDSAVEALFRKAGIVRCYSREELTTVGCIF-TLPELKGKNFAIITHAGGPGVMLTDA 320
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLsNQPLPKGNRVAIITNAGGPGVIATDA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492395500 321 LSKGGLNVPKLEGPVAEELKGKLFPGAAVGNPIDILATGTPEHLCLCLEYCEEKfDNIDAVMAIFgTPGLVTMFE 395
Cdd:TIGR02717 315 CEENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAED-ENVDGVVVVL-TPTAMTDPE 387
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
480-684 |
4.97e-67 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 219.27 E-value: 4.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 480 DGYIAPHYVQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKVVGP--VHKSDVGGVVLNIKSEQHLALEFDRMMQ 557
Cdd:pfam13549 7 RTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPdiLHKSDVGGVRLNLRSAEAVRAAYEEILE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 558 I-----PEA--SAIMVQPMLK-GTELFIGAKYEEKFGHVVLCGLGGIFVEVLKDISSGLAPLSYEEAYSMIHSLRAYKII 629
Cdd:pfam13549 87 RvrryrPDAriEGVLVQPMAPgGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492395500 630 KGTRGQKGVNEDKFAEIIVRLSTLLRFATEIKEMDINPLLATEKQVIAVDARIRI 684
Cdd:pfam13549 167 KGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
152-294 |
5.98e-34 |
|
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: 126.43 E-value: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 152 PQGVDLISSSGATAVFILESAVTKGLQFNSVWSVGNAKQIGVEDVLQYMDEHfnpeADSRIKLLYIESIGDPDRLLFHAS 231
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADD----PETRVILLYLEGIRDGRRFLRAAR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492395500 232 SLIKKgCKIAAIKAGSSESGSRAASSHTGAIASSDSAVEALFRKAGIVRCYSREELTTVGCIF 294
Cdd:pfam13607 77 RAARR-KPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
|
|
| CoA_binding_2 |
pfam13380 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
11-136 |
1.43e-20 |
|
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: 433162 [Multi-domain] Cd Length: 116 Bit Score: 87.59 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 11 SIVVVGASNNVHKPGGAILKNLLSGGYtgELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAVEmLAAEK 89
Cdd:pfam13380 2 TIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPvDLVDVFRPPEAVPEIVE-EALAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 492395500 90 QVKAFIILSagfgeethegAVLEDRILETVNRYGASLIGPNCIGFMN 136
Cdd:pfam13380 79 GAKAVWLQP----------GIENEEAAAIARAAGIRVVGDRCLGVEH 115
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
6-101 |
1.47e-15 |
|
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: 72.54 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 6 LLHPA-SIVVVGASNNVHKPGGAILKNLLSGGYTGELRaVNPKE--TEVQGVAAFADVKDIPDT---DLAILAIPAALCP 79
Cdd:smart00881 1 LLNPNtSVAVVGASGNLGSFGLAVMRNLLEYGTKFVGG-VYPGKvgPKVDGVPVYDSVAEAPEEtgvDVAVIFVPAEAAP 79
|
90 100
....*....|....*....|..
gi 492395500 80 DAVEMlAAEKQVKAFIILSAGF 101
Cdd:smart00881 80 DAIDE-AIEAGIKGIVVITEGI 100
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
9-100 |
2.03e-09 |
|
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: 54.91 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 9 PASIVVVGASNNVHKPGGAILKNLLSGGyTGELRAVNPKE--TEVQGVAAFADVKDIPDT---DLAILAIPAALCPDAVE 83
Cdd:pfam02629 3 DTKVIVIGAGGLGIQGLNYHFIQMLGYG-IKMVFGVNPGKggTEILGIPVYNSVDELEEKtgvDVAVITVPAPFAQEAID 81
|
90
....*....|....*..
gi 492395500 84 MLaAEKQVKAFIILSAG 100
Cdd:pfam02629 82 EL-VDAGIKGIVNITPG 97
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
11-94 |
2.96e-06 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 47.04 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 11 SIVVVGASNNVHKPGGAILKNLLSGGYtgELRAVNPKETEVQGVAAFADVKDIPDT-DLAILAIPAALCPDAVEmLAAEK 89
Cdd:COG1832 18 TIAVVGLSPNPERPSYYVAKYLQRHGY--RVIPVNPGAKEILGEKVYASLADIPEPvDIVDVFRRSEAVPEIVD-EAIAI 94
|
....*
gi 492395500 90 QVKAF 94
Cdd:COG1832 95 GAKVV 99
|
|
| Ligase_CoA_2 |
pfam19045 |
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold. |
306-361 |
1.81e-05 |
|
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold.
Pssm-ID: 408815 Cd Length: 162 Bit Score: 45.33 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 492395500 306 IITHAGGPGVMLTDALSKGGLNVPKLEGPVAEELKGKLFPGAAVGNPIDILATGTP 361
Cdd:pfam19045 3 IITGAGGSGVLLSDACVDNGLTLMAIPPDLDAAFRKFIPPFGAAGNPVDITGGEPP 58
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
491-580 |
1.02e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.53 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 491 LLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKvvgPVHKSDVGGVVLNIKSEQHLALEFDRMMQipEASAIMVQPML 570
Cdd:PRK14016 221 LLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK---PLDGNHGRGVTVNITTREEIEAAYAVASK--ESSDVIVERYI 295
|
90
....*....|...
gi 492395500 571 KGTE---LFIGAK 580
Cdd:PRK14016 296 PGKDhrlLVVGGK 308
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
487-568 |
1.38e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.16 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 487 YVQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKvvgPVHKSDVGGVVLnIKSEQHLALEFDRMMQIPEASaIMV 566
Cdd:COG0189 99 FTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLK---PLDGSGGRGVFL-VEDEDALESILEALTELGSEP-VLV 173
|
..
gi 492395500 567 QP 568
Cdd:COG0189 174 QE 175
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
488-532 |
6.02e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 39.95 E-value: 6.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 492395500 488 VQALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVvakVVGPVHK 532
Cdd:PRK12815 674 FYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPV---LIRPSYV 715
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
490-631 |
6.15e-03 |
|
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: 39.09 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395500 490 ALLRSAGIPIVEEFVSDNKEEVLAFARRTGFPVVAKvvgPVhkSDVG--GVVLnIKSEQHLALEFDRMMQIPEA----SA 563
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVK---PA--DGAGsrGVRV-VRDEEELEAALAEARAEAKAgspnGE 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492395500 564 IMVQPMLKGTEL---FIGAKyeekfGHVVLCGL------GGIFVEVLKDISSGLAPLSYEEAYSMIHS-LRAYKIIKG 631
Cdd:COG0439 134 VLVEEFLEGREYsveGLVRD-----GEVVVCSItrkhqkPPYFVELGHEAPSPLPEELRAEIGELVARaLRALGYRRG 206
|
|
| |
