|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
2-696 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 2 SLEKLIRPKSIAIVGVTDKLG-FGRSAALSIVKSKDTDRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVVCTPRNVVPS 80
Cdd:COG1042 5 SLDALFRPRSVAVIGASDRPGkVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETVPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 81 VLKDSAELGTKAAVVYASGFAEEGtEEGTDLENQLIEISNTYDMKILGPNCMGLLNCIDKVNLWAGGskwdLDTKKPGIG 160
Cdd:COG1042 85 VVEECGEKGVKAAVVISAGFAETG-EEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAP----VPPLPGNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 161 IVGQSGFITAEIVssDYFN-----ISYGFSTGNGNIVTLEDAVDFLVDDNYASVIAIYLEGLKNPQKFIDALkRAAQKRK 235
Cdd:COG1042 160 LVSQSGALGTAIL--DWAAargigFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAA-RAAARGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 236 PVIILKSGRSEKGAISAASHTGNLAGSSKAFESIFEKYGVISVENLEQFMCLAQAFSVldGNLPTNSNFAAINFSGGENT 315
Cdd:COG1042 237 PVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALAR--QPPPRGRRLAIVTNSGGPGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 316 ICADLAEENGVELAEISSETKEEMKKYLPGFATPKNPLD----ATTALFHEkdmivgLLHTFEKDSSVG-----FTMVGA 386
Cdd:COG1042 315 LAADALEDLGLELAELSEETQAALRAVLPPFASVGNPVDitgdADPERYAA------ALEALLADPNVDavlviLTPTAM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 387 nirdeenEMHETLCQAVSEAReQGLKKPVFAVpTLEGNRYLDYRNRLEYNQVPIMSSVGTTFTCFNKMAKF--------- 457
Cdd:COG1042 389 -------TDPEEVAEALIEAA-KGSGKPVLAS-WMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYrrnqerlme 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 458 ------IDYDYSKRTLEFKAVKKRESNnvvALSELDSKIEMKKYGVPVPGQGNAKSIDELDEILKYIKYPVVLKINSSEI 531
Cdd:COG1042 460 tpasedFDPDRERARAIIEAALAEGRG---VLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDI 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 532 LHKSDVGGVKIGIKNRDEAVDAYNEILTNVKKAKPDANIDGILVQEMVESGIEIIIGITNDDQFGPMLLVGLGGVFVEVF 611
Cdd:COG1042 537 LHKSDVGGVRLNLRDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVL 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 612 KDTTLYPLPINHDEAIMMLKKLKSFKLLNGYRGSEPCDIDALADMMVKLGKYAYENKdEVKEIDLNPVFVYPkgKGVCAV 691
Cdd:COG1042 617 KDVALRLPPLNEALAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLP-EILELDINPLLVVP--EGVVAV 693
|
....*
gi 489518605 692 DALIV 696
Cdd:COG1042 694 DARIR 698
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
3-415 |
2.29e-96 |
|
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: 304.62 E-value: 2.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 3 LEKLIRPKSIAIVGVTDKLG-FGRSAALSIVKSKDTDRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVVCTPRNVVPSV 81
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGkVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 82 LKDSAELGTKAAVVYASGFAEEGtEEGTDLENQLIEISNTYDMKILGPNCMGLLNCIDKVNLWAGGSkwdlDTKKPGIGI 161
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVG-EEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPT----MPKKGGIAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 162 VGQSG-FITA--EIVSSDYFNISYGFSTGNGNIVTLEDAVDFLVDDNYASVIAIYLEGLKNPQKFIDALKRAAqKRKPVI 238
Cdd:TIGR02717 156 ISQSGaLLTAllDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREIS-KKKPIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 239 ILKSGRSEKGAISAASHTGNLAGSSKAFESIFEKYGVISVENLEQFMCLAQAFSVLdgNLPTNSNFAAINFSGGENTICA 318
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQ--PLPKGNRVAIITNAGGPGVIAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 319 DLAEENGVELAEISSETKEEMKKYLPGFATPKNPLD----ATTALFhekdmiVGLLHTFEKDSSVGFTMV----GANIRD 390
Cdd:TIGR02717 313 DACEENGLELAELSEATKNKLRNILPPEASIKNPVDvlgdATPERY------AKALKTVAEDENVDGVVVvltpTAMTDP 386
|
410 420
....*....|....*....|....*
gi 489518605 391 EEnemhetLCQAVSEAREQGLKKPV 415
Cdd:TIGR02717 387 EE------VAKGIIEGAKKSNEKPV 405
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
483-696 |
4.15e-64 |
|
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: 211.95 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 483 LSELDSKIEMKKYGVPVPGQGNAKSIDELDEILKYIKYPVVLKINSSEILHKSDVGGVKIGIKNRDEAVDAYNEILTNVK 562
Cdd:pfam13549 10 LTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAAYEEILERVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 563 KAKPDANIDGILVQEMVESGIEIIIGITNDDQFGPMLLVGLGGVFVEVFKDTTLYPLPINHDEAIMMLKKLKSFKLLNGY 642
Cdd:pfam13549 90 RYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLLKGY 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489518605 643 RGSEPCDIDALADMMVKLGKYAYENKdEVKEIDLNPVFVYPkgKGVCAVDALIV 696
Cdd:pfam13549 170 RGEPPADLDALEDVLVRVSQLVIDFP-EIRELDINPLLADE--DGVVALDARIR 220
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
8-100 |
7.24e-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: 70.62 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 8 RPKSIAIVGVTDKLGfgrSAALSIVKSKDTD------RVY--YVNPKREELfgrKCYKTIQEVPE--IVDCVVVCTPRNV 77
Cdd:smart00881 4 PNTSVAVVGASGNLG---SFGLAVMRNLLEYgtkfvgGVYpgKVGPKVDGV---PVYDSVAEAPEetGVDVAVIFVPAEA 77
|
90 100
....*....|....*....|...
gi 489518605 78 VPSVLKDSAELGTKAAVVYASGF 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEGI 100
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
496-556 |
1.27e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489518605 496 GVPVPGQGNAKSIDELDEILKYIKYPVVLKinsseilhKSDvG----GVKIGIKNRDEAVDAYNE 556
Cdd:PRK14016 226 GVPVPEGRVVTSAEDAWEAAEEIGYPVVVK--------PLD-GnhgrGVTVNITTREEIEAAYAV 281
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
2-696 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 2 SLEKLIRPKSIAIVGVTDKLG-FGRSAALSIVKSKDTDRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVVCTPRNVVPS 80
Cdd:COG1042 5 SLDALFRPRSVAVIGASDRPGkVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETVPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 81 VLKDSAELGTKAAVVYASGFAEEGtEEGTDLENQLIEISNTYDMKILGPNCMGLLNCIDKVNLWAGGskwdLDTKKPGIG 160
Cdd:COG1042 85 VVEECGEKGVKAAVVISAGFAETG-EEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAP----VPPLPGNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 161 IVGQSGFITAEIVssDYFN-----ISYGFSTGNGNIVTLEDAVDFLVDDNYASVIAIYLEGLKNPQKFIDALkRAAQKRK 235
Cdd:COG1042 160 LVSQSGALGTAIL--DWAAargigFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAA-RAAARGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 236 PVIILKSGRSEKGAISAASHTGNLAGSSKAFESIFEKYGVISVENLEQFMCLAQAFSVldGNLPTNSNFAAINFSGGENT 315
Cdd:COG1042 237 PVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALAR--QPPPRGRRLAIVTNSGGPGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 316 ICADLAEENGVELAEISSETKEEMKKYLPGFATPKNPLD----ATTALFHEkdmivgLLHTFEKDSSVG-----FTMVGA 386
Cdd:COG1042 315 LAADALEDLGLELAELSEETQAALRAVLPPFASVGNPVDitgdADPERYAA------ALEALLADPNVDavlviLTPTAM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 387 nirdeenEMHETLCQAVSEAReQGLKKPVFAVpTLEGNRYLDYRNRLEYNQVPIMSSVGTTFTCFNKMAKF--------- 457
Cdd:COG1042 389 -------TDPEEVAEALIEAA-KGSGKPVLAS-WMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYrrnqerlme 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 458 ------IDYDYSKRTLEFKAVKKRESNnvvALSELDSKIEMKKYGVPVPGQGNAKSIDELDEILKYIKYPVVLKINSSEI 531
Cdd:COG1042 460 tpasedFDPDRERARAIIEAALAEGRG---VLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDI 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 532 LHKSDVGGVKIGIKNRDEAVDAYNEILTNVKKAKPDANIDGILVQEMVESGIEIIIGITNDDQFGPMLLVGLGGVFVEVF 611
Cdd:COG1042 537 LHKSDVGGVRLNLRDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVL 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 612 KDTTLYPLPINHDEAIMMLKKLKSFKLLNGYRGSEPCDIDALADMMVKLGKYAYENKdEVKEIDLNPVFVYPkgKGVCAV 691
Cdd:COG1042 617 KDVALRLPPLNEALAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLP-EILELDINPLLVVP--EGVVAV 693
|
....*
gi 489518605 692 DALIV 696
Cdd:COG1042 694 DARIR 698
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
3-415 |
2.29e-96 |
|
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: 304.62 E-value: 2.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 3 LEKLIRPKSIAIVGVTDKLG-FGRSAALSIVKSKDTDRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVVCTPRNVVPSV 81
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGkVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 82 LKDSAELGTKAAVVYASGFAEEGtEEGTDLENQLIEISNTYDMKILGPNCMGLLNCIDKVNLWAGGSkwdlDTKKPGIGI 161
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVG-EEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPT----MPKKGGIAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 162 VGQSG-FITA--EIVSSDYFNISYGFSTGNGNIVTLEDAVDFLVDDNYASVIAIYLEGLKNPQKFIDALKRAAqKRKPVI 238
Cdd:TIGR02717 156 ISQSGaLLTAllDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREIS-KKKPIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 239 ILKSGRSEKGAISAASHTGNLAGSSKAFESIFEKYGVISVENLEQFMCLAQAFSVLdgNLPTNSNFAAINFSGGENTICA 318
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQ--PLPKGNRVAIITNAGGPGVIAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 319 DLAEENGVELAEISSETKEEMKKYLPGFATPKNPLD----ATTALFhekdmiVGLLHTFEKDSSVGFTMV----GANIRD 390
Cdd:TIGR02717 313 DACEENGLELAELSEATKNKLRNILPPEASIKNPVDvlgdATPERY------AKALKTVAEDENVDGVVVvltpTAMTDP 386
|
410 420
....*....|....*....|....*
gi 489518605 391 EEnemhetLCQAVSEAREQGLKKPV 415
Cdd:TIGR02717 387 EE------VAKGIIEGAKKSNEKPV 405
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
483-696 |
4.15e-64 |
|
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: 211.95 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 483 LSELDSKIEMKKYGVPVPGQGNAKSIDELDEILKYIKYPVVLKINSSEILHKSDVGGVKIGIKNRDEAVDAYNEILTNVK 562
Cdd:pfam13549 10 LTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAAYEEILERVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 563 KAKPDANIDGILVQEMVESGIEIIIGITNDDQFGPMLLVGLGGVFVEVFKDTTLYPLPINHDEAIMMLKKLKSFKLLNGY 642
Cdd:pfam13549 90 RYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLLKGY 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489518605 643 RGSEPCDIDALADMMVKLGKYAYENKdEVKEIDLNPVFVYPkgKGVCAVDALIV 696
Cdd:pfam13549 170 RGEPPADLDALEDVLVRVSQLVIDFP-EIRELDINPLLADE--DGVVALDARIR 220
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
158-291 |
1.53e-44 |
|
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: 156.09 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 158 GIGIVGQSGFITAEIVS---SDYFNISYGFSTGNGNIVTLEDAVDFLVDDNYASVIAIYLEGLKNPQKFIDALKRAAQkR 234
Cdd:pfam13607 3 NIALVSQSGALGAALLDwarSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR-R 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489518605 235 KPVIILKSGRSEKGAISAASHTGNLAGSSKAFESIFEKYGVISVENLEQFMCLAQAF 291
Cdd:pfam13607 82 KPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
|
|
| CoA_binding_2 |
pfam13380 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
10-136 |
9.07e-21 |
|
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: 87.98 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 10 KSIAIVGVTDKLG-FGRsAALSIVKSKDTdRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVVCTPRNVVPSVLKDSAEL 88
Cdd:pfam13380 1 KTIAVVGASPNPGrPGY-KVARYLLEHGY-PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489518605 89 GTKAAVVYASGFAEEgteegtdlenqLIEISNTYDMKILGPNCMGLLN 136
Cdd:pfam13380 79 GAKAVWLQPGIENEE-----------AAAIARAAGIRVVGDRCLGVEH 115
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
8-100 |
7.24e-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: 70.62 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 8 RPKSIAIVGVTDKLGfgrSAALSIVKSKDTD------RVY--YVNPKREELfgrKCYKTIQEVPE--IVDCVVVCTPRNV 77
Cdd:smart00881 4 PNTSVAVVGASGNLG---SFGLAVMRNLLEYgtkfvgGVYpgKVGPKVDGV---PVYDSVAEAPEetGVDVAVIFVPAEA 77
|
90 100
....*....|....*....|...
gi 489518605 78 VPSVLKDSAELGTKAAVVYASGF 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEGI 100
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
6-92 |
3.49e-11 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 61.30 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 6 LIRPKSIAIVGVTDK--------------LGFgrsaalsivkskdtdRVYYVNPKREELFGRKCYKTIQEVPEIVDCVVV 71
Cdd:COG1832 13 LKSAKTIAVVGLSPNperpsyyvakylqrHGY---------------RVIPVNPGAKEILGEKVYASLADIPEPVDIVDV 77
|
90 100
....*....|....*....|.
gi 489518605 72 CTPRNVVPSVLKDSAELGTKA 92
Cdd:COG1832 78 FRRSEAVPEIVDEAIAIGAKV 98
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
486-579 |
3.26e-07 |
|
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: 52.18 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 486 LDSKIEMK----KYGVPVPGQGNAKSIDELDEILKYIKYPVVLK-INSSeilhksdvG--GVKIgIKNRDEAVDAYNEIL 558
Cdd:COG0439 52 MRDKVLMRealaAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKpADGA--------GsrGVRV-VRDEEELEAALAEAR 122
|
90 100
....*....|....*....|.
gi 489518605 559 TNVKKAKPDaniDGILVQEMV 579
Cdd:COG0439 123 AEAKAGSPN---GEVLVEEFL 140
|
|
| Ligase_CoA_2 |
pfam19045 |
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold. |
307-424 |
2.81e-05 |
|
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold.
Pssm-ID: 408815 Cd Length: 162 Bit Score: 44.95 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 307 INFSGGENTICADLAEENGVELAEISSETKEEMKKYLPGFATPKNPLDAT----------TALFHEKD-----MIVGLLH 371
Cdd:pfam19045 4 ITGAGGSGVLLSDACVDNGLTLMAIPPDLDAAFRKFIPPFGAAGNPVDITggeppstyeaTIRLGLEDprihaLILGYWH 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489518605 372 TFekdssVGFTMVGAnirdeenemhETLCQAVSEAREQGLKKPVfaVPTLEGN 424
Cdd:pfam19045 84 TI-----VTPPMVFA----------ELMVRVVEEMRAKGIDKPV--VASLAGD 119
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
494-579 |
7.49e-05 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 45.69 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 494 KYGVPVPGQGNAKSIDELDEILKYIKYPVVLK-INSSEILHKSDVGGVKIG-IKNRDEAVDAYNEILtnvkkakpDANID 571
Cdd:COG3919 127 ELGVPVPKTVVLDSADDLDALAEDLGFPVVVKpADSVGYDELSFPGKKKVFyVDDREELLALLRRIA--------AAGYE 198
|
....*...
gi 489518605 572 gILVQEMV 579
Cdd:COG3919 199 -LIVQEYI 205
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
496-556 |
1.27e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489518605 496 GVPVPGQGNAKSIDELDEILKYIKYPVVLKinsseilhKSDvG----GVKIGIKNRDEAVDAYNE 556
Cdd:PRK14016 226 GVPVPEGRVVTSAEDAWEAAEEIGYPVVVK--------PLD-GnhgrGVTVNITTREEIEAAYAV 281
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
484-553 |
2.76e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 44.20 E-value: 2.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489518605 484 SELDSKIEMKKYGVPV-PG-QGNAKSIDELDEILKYIKYPVVLkinsseilhKSDVGGVKIGIK---NRDEAVDA 553
Cdd:PRK08654 115 SKINAKKLMKKAGVPVlPGtEEGIEDIEEAKEIAEEIGYPVII---------KASAGGGGIGMRvvySEEELEDA 180
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
492-560 |
1.60e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 41.54 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489518605 492 MKKYGVPVPGqgnAKSIDELDEILKYIK---YPVVLKinsseilhksDVG-----GVKIgIKNRDEAVDAYNEILTN 560
Cdd:COG0151 110 MARYGIPTAA---YRVFTDLEEALAYLEeqgAPIVVK----------ADGlaagkGVVV-AETLEEALAAVDDMLAD 172
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
483-579 |
3.56e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 483 LSELDSKIEMKKYGVPVPGQGNAKSIDELDEILKyikypvvlKINSSEILHKSDV--------GGVKIgIKNRDEAVDAY 554
Cdd:pfam08442 2 LHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAK--------KLGGKVYVVKAQVlaggrgkaGGVKL-AKSPEEAKEVA 72
|
90 100
....*....|....*....|....*....
gi 489518605 555 NEIL-TNVKKAKPDAN---IDGILVQEMV 579
Cdd:pfam08442 73 KEMLgKNLVTKQTGPDgqpVNKVLVEEAL 101
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
10-95 |
4.10e-03 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 39.72 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489518605 10 KSIAIVGvtdkLGF-GRSAALSIVKSKDTDRVYYVNPKREELF-------GRKCYKTIQEVPEIVDCVVVCTPRNVVPSV 81
Cdd:COG0287 2 MRIAIIG----LGLiGGSLALALKRAGLAHEVVGVDRSPETLEralelgvIDRAATDLEEAVADADLVVLAVPVGATIEV 77
|
90
....*....|....
gi 489518605 82 LKDSAELGTKAAVV 95
Cdd:COG0287 78 LAELAPHLKPGAIV 91
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
493-558 |
6.93e-03 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 39.26 E-value: 6.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489518605 493 KKYGVPVPGQGNAKSIDELDEILKYI-KYPVVLKinsSEILH----KSdvGGVKIgIKNRDEAVDAYNEIL 558
Cdd:COG0045 13 AKYGVPVPRGIVATTPEEAVAAAEELgGPPVVVK---AQVHAggrgKA--GGVKL-AKSPEEAREAAEEIL 77
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
488-525 |
7.31e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 39.34 E-value: 7.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489518605 488 SKIEMKKYGVPV-PG-QGNAKSIDELDEILKYIKYPVVLK 525
Cdd:PRK08462 121 AKEVMKRAGVPViPGsDGALKSYEEAKKIAKEIGYPVILK 160
|
|
|