|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
1-717 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 909.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 1 MSQRTLHTLFKPGSIAVIGASNSHKRAGNVVMKNLLSGGFAGPIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRAS 80
Cdd:COG1042 1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 81 SVPAIVETLAQFGCKVAIIMASGMAdELNEQGENLLELTQGNARRYGMRILGPNSLGMMLPPQGLNASLAHAGALPGKIA 160
Cdd:COG1042 81 TVPDVVEECGEKGVKAAVVISAGFA-ETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 161 FVSQSAAICTTVLDWANNKGIGFSSFISLGDATDIDFDELLDFLGRDSRTSAIMLYIDSVNEKRHFLSAARAAARHKPIL 240
Cdd:COG1042 160 LVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 241 VIKSGRSAEGGNAAKLHTGGIAGNDAVYEAAFRRAGMLRVTDLVELFAALESLAHLNPLNGERLCILSNGGGPAVLAVDE 320
Cdd:COG1042 240 VLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 321 LVLKGGKLAQLSEATLDKLSQLLPSTWSGQNPVDIIGDAGAERYSQALSVLMDSDELDAILVLHSPSALGESVTIADALI 400
Cdd:COG1042 320 LEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 401 ETVKQHSKrnrvSILTNWSGEDAAYRARKHFSKAGIPTYRTPEGAVRAFMHMVEYRRNQKLLQEVPQsiPDSIPTDSATA 480
Cdd:COG1042 400 EAAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA--SEDFDPDRERA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 481 RSLLQQAIAKGKRVLETHDARNILNAYGLDTIDTWYAKDAAEAVAIADKAGYPVALKVQSPDILHKSDVHGVMLNLTSAN 560
Cdd:COG1042 474 RAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 561 EVNQAAAAIVERVHASNPAASVEGMIVQKMAltAGAQELRVAVISDPVFGPAIMLGEGGSEWEPTRDAAVALPPLNMALA 640
Cdd:COG1042 554 AVRAAFEEILARVRAARPDARIDGVLVQPMV--PGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALA 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2178847744 641 RYMVIQALKTQKIRDRHLPQGLDMRALCLMLTQISQLIIDCPEIESLDLNPVLAAGEKITLLDVNLRLNPEVTDNAG 717
Cdd:COG1042 632 REMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-456 |
3.34e-162 |
|
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: 481.04 E-value: 3.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 6 LHTLFKPGSIAVIGASNSHKRAGNVVMKNLLSGGFAGPIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRASSVPAI 85
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 86 VETLAQFGCKVAIIMASGMAdELNEQGENLLELTQGNARRYGMRILGPNSLGMMLPPQGLNASLAHAGALPGKIAFVSQS 165
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFK-EVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 166 AAICTTVLDWANNKGIGFSSFISLGDATDIDFDELLDFLGRDSRTSAIMLYIDSVNEKRHFLSAARAAARHKPILVIKSG 245
Cdd:TIGR02717 160 GALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 246 RSAEGGNAAKLHTGGIAGNDAVYEAAFRRAGMLRVTDLVELFAALESLAHLNPLNGERLCILSNGGGPAVLAVDELVLKG 325
Cdd:TIGR02717 240 TSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 326 GKLAQLSEATLDKLSQLLPSTWSGQNPVDIIGDAGAERYSQALSVLMDSDELDAILVLHSPSALGESVTIADALIETVKQ 405
Cdd:TIGR02717 320 LELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKK 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2178847744 406 HskrNRVSILTNWSGEDAAYRARKHFSKAGIPTYRTPEGAVRAFMHMVEYR 456
Cdd:TIGR02717 400 S---NEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
486-708 |
1.51e-91 |
|
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: 288.61 E-value: 1.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 486 QAIAKGKRVLETHDARNILNAYGLDTIDTWYAKDAAEAVAIADKAGYPVALKVQSPDILHKSDVHGVMLNLTSANEVNQA 565
Cdd:pfam13549 1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 566 AAAIVERVHASNPAASVEGMIVQKMALtaGAQELRVAVISDPVFGPAIMLGEGGSEWEPTRDAAVALPPLNMALARYMvI 645
Cdd:pfam13549 81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2178847744 646 QALKTQKIRDRHLPQ-GLDMRALCLMLTQISQLIIDCPEIESLDLNPVLAAGEKITLLDVNLRL 708
Cdd:pfam13549 158 RRTRAYKLLKGYRGEpPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
9-103 |
3.50e-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: 214881 [Multi-domain] Cd Length: 100 Bit Score: 86.02 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 9 LFKPG-SIAVIGASNSHKRAGNVVMKNLLSGG--FAGPIMP--VTPKYHavmGVLAYPNIESLPIK--PDLAIICTRASS 81
Cdd:smart00881 1 LLNPNtSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGPKVD---GVPVYDSVAEAPEEtgVDVAVIFVPAEA 77
|
90 100
....*....|....*....|..
gi 2178847744 82 VPAIVETLAQFGCKVAIIMASG 103
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEG 99
|
|
| RimL |
COG1670 |
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ... |
740-889 |
1.26e-12 |
|
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441276 [Multi-domain] Cd Length: 173 Bit Score: 66.95 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 740 VMLRPILPEDEPKHLDFDNsltDED--RYKRYFGVRSRMTHEEMAVLTQIDYAREMAFIATIRDENGEeeTLGAVRAS-I 816
Cdd:COG1670 8 LRLRPLRPEDAEALAELLN---DPEvaRYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGE--LIGVVGLYdI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2178847744 817 DPDNTEAEFAMAVRSSHQGIGIGKLLLEKLINYYRTT-GTQVLTGFTMFENRNMASLAKSLGFTVTFDMEEHLI 889
Cdd:COG1670 83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
777-878 |
1.67e-07 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 50.59 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 777 THEEMAVLTQIDYAREMAFIATIRDEngeeETLGAVRASIDPDNTE--AEFAMAVRSSHQGIGIGKLLLEKLINYYRTTG 854
Cdd:pfam00583 17 PDEPLDLLEDWDEDASEGFFVAEEDG----ELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92
|
90 100
....*....|....*....|....
gi 2178847744 855 TQVLTGFTMFENRNMASLAKSLGF 878
Cdd:pfam00583 93 CERIFLEVAADNLAAIALYEKLGF 116
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
1-717 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 909.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 1 MSQRTLHTLFKPGSIAVIGASNSHKRAGNVVMKNLLSGGFAGPIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRAS 80
Cdd:COG1042 1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 81 SVPAIVETLAQFGCKVAIIMASGMAdELNEQGENLLELTQGNARRYGMRILGPNSLGMMLPPQGLNASLAHAGALPGKIA 160
Cdd:COG1042 81 TVPDVVEECGEKGVKAAVVISAGFA-ETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 161 FVSQSAAICTTVLDWANNKGIGFSSFISLGDATDIDFDELLDFLGRDSRTSAIMLYIDSVNEKRHFLSAARAAARHKPIL 240
Cdd:COG1042 160 LVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 241 VIKSGRSAEGGNAAKLHTGGIAGNDAVYEAAFRRAGMLRVTDLVELFAALESLAHLNPLNGERLCILSNGGGPAVLAVDE 320
Cdd:COG1042 240 VLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 321 LVLKGGKLAQLSEATLDKLSQLLPSTWSGQNPVDIIGDAGAERYSQALSVLMDSDELDAILVLHSPSALGESVTIADALI 400
Cdd:COG1042 320 LEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 401 ETVKQHSKrnrvSILTNWSGEDAAYRARKHFSKAGIPTYRTPEGAVRAFMHMVEYRRNQKLLQEVPQsiPDSIPTDSATA 480
Cdd:COG1042 400 EAAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA--SEDFDPDRERA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 481 RSLLQQAIAKGKRVLETHDARNILNAYGLDTIDTWYAKDAAEAVAIADKAGYPVALKVQSPDILHKSDVHGVMLNLTSAN 560
Cdd:COG1042 474 RAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 561 EVNQAAAAIVERVHASNPAASVEGMIVQKMAltAGAQELRVAVISDPVFGPAIMLGEGGSEWEPTRDAAVALPPLNMALA 640
Cdd:COG1042 554 AVRAAFEEILARVRAARPDARIDGVLVQPMV--PGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALA 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2178847744 641 RYMVIQALKTQKIRDRHLPQGLDMRALCLMLTQISQLIIDCPEIESLDLNPVLAAGEKITLLDVNLRLNPEVTDNAG 717
Cdd:COG1042 632 REMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-456 |
3.34e-162 |
|
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: 481.04 E-value: 3.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 6 LHTLFKPGSIAVIGASNSHKRAGNVVMKNLLSGGFAGPIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRASSVPAI 85
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 86 VETLAQFGCKVAIIMASGMAdELNEQGENLLELTQGNARRYGMRILGPNSLGMMLPPQGLNASLAHAGALPGKIAFVSQS 165
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFK-EVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 166 AAICTTVLDWANNKGIGFSSFISLGDATDIDFDELLDFLGRDSRTSAIMLYIDSVNEKRHFLSAARAAARHKPILVIKSG 245
Cdd:TIGR02717 160 GALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 246 RSAEGGNAAKLHTGGIAGNDAVYEAAFRRAGMLRVTDLVELFAALESLAHLNPLNGERLCILSNGGGPAVLAVDELVLKG 325
Cdd:TIGR02717 240 TSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 326 GKLAQLSEATLDKLSQLLPSTWSGQNPVDIIGDAGAERYSQALSVLMDSDELDAILVLHSPSALGESVTIADALIETVKQ 405
Cdd:TIGR02717 320 LELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKK 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2178847744 406 HskrNRVSILTNWSGEDAAYRARKHFSKAGIPTYRTPEGAVRAFMHMVEYR 456
Cdd:TIGR02717 400 S---NEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
486-708 |
1.51e-91 |
|
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: 288.61 E-value: 1.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 486 QAIAKGKRVLETHDARNILNAYGLDTIDTWYAKDAAEAVAIADKAGYPVALKVQSPDILHKSDVHGVMLNLTSANEVNQA 565
Cdd:pfam13549 1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 566 AAAIVERVHASNPAASVEGMIVQKMALtaGAQELRVAVISDPVFGPAIMLGEGGSEWEPTRDAAVALPPLNMALARYMvI 645
Cdd:pfam13549 81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2178847744 646 QALKTQKIRDRHLPQ-GLDMRALCLMLTQISQLIIDCPEIESLDLNPVLAAGEKITLLDVNLRL 708
Cdd:pfam13549 158 RRTRAYKLLKGYRGEpPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
156-293 |
1.06e-60 |
|
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: 202.31 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 156 PGKIAFVSQSAAICTTVLDWANNKGIGFSSFISLGDATDIDFDELLDFLGRDSRTSAIMLYIDSVNEKRHFLSAARAAAR 235
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2178847744 236 HKPILVIKSGRSAEGGNAAKLHTGGIAGNDAVYEAAFRRAGMLRVTDLVELFAALESL 293
Cdd:pfam13607 81 RKPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
|
|
| CoA_binding_2 |
pfam13380 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
14-141 |
9.02e-28 |
|
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: 108.40 E-value: 9.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 14 SIAVIGASNSHKRAGNVVMKNLLSGGFagPIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRASSVPAIVETLAQFG 93
Cdd:pfam13380 2 TIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2178847744 94 CKVAIIMASGMADELNEQgenlleltqgnARRYGMRILGPNSLGMMLP 141
Cdd:pfam13380 80 AKAVWLQPGIENEEAAAI-----------ARAAGIRVVGDRCLGVEHP 116
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
9-103 |
3.50e-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: 214881 [Multi-domain] Cd Length: 100 Bit Score: 86.02 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 9 LFKPG-SIAVIGASNSHKRAGNVVMKNLLSGG--FAGPIMP--VTPKYHavmGVLAYPNIESLPIK--PDLAIICTRASS 81
Cdd:smart00881 1 LLNPNtSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGPKVD---GVPVYDSVAEAPEEtgVDVAVIFVPAEA 77
|
90 100
....*....|....*....|..
gi 2178847744 82 VPAIVETLAQFGCKVAIIMASG 103
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEG 99
|
|
| RimL |
COG1670 |
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ... |
740-889 |
1.26e-12 |
|
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441276 [Multi-domain] Cd Length: 173 Bit Score: 66.95 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 740 VMLRPILPEDEPKHLDFDNsltDED--RYKRYFGVRSRMTHEEMAVLTQIDYAREMAFIATIRDENGEeeTLGAVRAS-I 816
Cdd:COG1670 8 LRLRPLRPEDAEALAELLN---DPEvaRYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGE--LIGVVGLYdI 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2178847744 817 DPDNTEAEFAMAVRSSHQGIGIGKLLLEKLINYYRTT-GTQVLTGFTMFENRNMASLAKSLGFTVTFDMEEHLI 889
Cdd:COG1670 83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
739-890 |
2.97e-11 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 62.70 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 739 EVMLRPILPEDEPKHLDFDNSLTDEdRYKRYFGVRsrMTHEEMAV-LTQIDYAREMAFIAtirDENGEeeTLGAVRASI- 816
Cdd:COG1247 1 EMTIRPATPEDAPAIAAIYNEAIAE-GTATFETEP--PSEEEREAwFAAILAPGRPVLVA---EEDGE--VVGFASLGPf 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2178847744 817 ---DPDNTEAEFAMAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTMFENRNMASLAKSLGFTVTFDMEEHLIK 890
Cdd:COG1247 73 rprPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFK 149
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
14-96 |
1.58e-10 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 59.76 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 14 SIAVIGASNSHKRAGNVVMKNLLSGGFAgpIMPVTPKYHAVMGVLAYPNIESLPIKPDLAIICTRASSVPAIVETLAQFG 93
Cdd:COG1832 18 TIAVVGLSPNPERPSYYVAKYLQRHGYR--VIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVPEIVDEAIAIG 95
|
...
gi 2178847744 94 CKV 96
Cdd:COG1832 96 AKV 98
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
123-276 |
1.87e-10 |
|
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: 62.77 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 123 ARRYGMRILGPNSLGMMLPPQ---GLNASLAHAgalPGKIAFVSQSAAICTTVLDWANNKGIGFSSFISLGdaTD----I 195
Cdd:COG0074 111 AKAKGTRLIGPNCPGIITPGEcklGIMPGHIFK---PGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIG--GDpiigT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 196 DFDELLDFLGRDSRTSAIMLY--IDSVNEKRhflsAAR--AAARHKPILVIKSGRSA-EG---GNAAKLHTGGiAGNDAV 267
Cdd:COG0074 186 SFIDVLELFEEDPETEAIVMIgeIGGSAEEE----AAEyiKENMTKPVVAYIAGRTApPGkrmGHAGAIISGG-KGTAES 260
|
....*....
gi 2178847744 268 YEAAFRRAG 276
Cdd:COG0074 261 KIEALEAAG 269
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
10-103 |
4.41e-10 |
|
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: 57.22 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 10 FKPGSIAVIGASNSHKRAGNVVMKNLLSGGFAGpIMPVTPK--YHAVMGVLAYPNIESLP--IKPDLAIICTRASSVPAI 85
Cdd:pfam02629 1 DKDTKVIVIGAGGLGIQGLNYHFIQMLGYGIKM-VFGVNPGkgGTEILGIPVYNSVDELEekTGVDVAVITVPAPFAQEA 79
|
90
....*....|....*...
gi 2178847744 86 VETLAQFGCKVAIIMASG 103
Cdd:pfam02629 80 IDELVDAGIKGIVNITPG 97
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
777-878 |
1.67e-07 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 50.59 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 777 THEEMAVLTQIDYAREMAFIATIRDEngeeETLGAVRASIDPDNTE--AEFAMAVRSSHQGIGIGKLLLEKLINYYRTTG 854
Cdd:pfam00583 17 PDEPLDLLEDWDEDASEGFFVAEEDG----ELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92
|
90 100
....*....|....*....|....
gi 2178847744 855 TQVLTGFTMFENRNMASLAKSLGF 878
Cdd:pfam00583 93 CERIFLEVAADNLAAIALYEKLGF 116
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
810-896 |
1.68e-06 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 46.96 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 810 GAVRASIDPDNTEAE-FAMAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTMFENRNMASLAKSLGFTVT--FDMEE 886
Cdd:COG0456 1 GFALLGLVDGGDEAEiEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVgeRPNYY 80
|
90
....*....|
gi 2178847744 887 HLIKMHMELP 896
Cdd:COG0456 81 GDDALVMEKE 90
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
805-895 |
6.06e-06 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 46.59 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 805 EEETLGAVRASIDPDNTeAEFA-MAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTMFENRNMASLAKSLGFTVTFD 883
Cdd:COG0454 42 KGEPIGFAGLRRLDDKV-LELKrLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIER 120
|
90
....*....|...
gi 2178847744 884 MEEHLI-KMHMEL 895
Cdd:COG0454 121 YVAYVGgEFEKEL 133
|
|
| Acetyltransf_3 |
pfam13302 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
740-879 |
2.06e-05 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 379112 [Multi-domain] Cd Length: 139 Bit Score: 45.03 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 740 VMLRPILPEDEPkhlDFDNSLTDEDRykRYFGVRSRMTHEE-----MAVLTQIDYAREMAFIATIRDENgeeeTLGAVR- 813
Cdd:pfam13302 2 LLLRPLTEEDAE---ALFELLSDPEV--MRYGVPWPLTLEEarewlARIWAADEAERGYGWAIELKDTG----FIGSIGl 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2178847744 814 ASIDPDNTEAEFAMAVRSSHQGIGIGKLLLEKLINY-YRTTGTQVLTGFTMFENRNMASLAKSLGFT 879
Cdd:pfam13302 73 YDIDGEPERAELGYWLGPDYWGKGYATEAVRALLEYaFEELGLPRLVARIDPENTASRRVLEKLGFK 139
|
|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
805-880 |
4.28e-05 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 42.83 E-value: 4.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2178847744 805 EEETLGAVRASIDPDNTE-AEFAMAVRSSHQGIGIGKLLLEKLINYYRTTGtqvLTGFTMFENRNMASLAKSLGFTV 880
Cdd:pfam13508 11 DGKIVGFAALLPLDDEGAlAELRLAVHPEYRGQGIGRALLEAAEAAAKEGG---IKLLELETTNRAAAFYEKLGFEE 84
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
788-881 |
2.76e-03 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 38.91 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178847744 788 DYAREMAFIATIrdengEEETLGAVRASIDPDNTEAEFA----MAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTm 863
Cdd:COG3153 35 DPAAGLSLVAED-----DGEIVGHVALSPVDIDGEGPALllgpLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG- 108
|
90
....*....|....*...
gi 2178847744 864 feNRNMASLAKSLGFTVT 881
Cdd:COG3153 109 --DPSLLPFYERFGFRPA 124
|
|
| COG3393 |
COG3393 |
Predicted acetyltransferase, GNAT family [General function prediction only]; |
826-890 |
2.90e-03 |
|
Predicted acetyltransferase, GNAT family [General function prediction only];
Pssm-ID: 442620 [Multi-domain] Cd Length: 86 Bit Score: 37.58 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2178847744 826 AMAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTMFENRNMASLAKSLGFTVTFDMEEHLIK 890
Cdd:COG3393 20 GVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
805-881 |
7.47e-03 |
|
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440859 [Multi-domain] Cd Length: 132 Bit Score: 37.66 E-value: 7.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2178847744 805 EEETLGAVRASIDPDNTeAEFA-MAVRSSHQGIGIGKLLLEKLINYYRTTGTQVLTGFTmfeNRNMASLAKSLGFTVT 881
Cdd:COG1246 36 DGEIVGCAALHPLDEDL-AELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEEI 109
|
|
|