|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
1-609 |
6.60e-140 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 429.16 E-value: 6.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 1 MTVRNLDALFHPTAVAVVGASPRPGSVGAMVWACVLDGRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPA 80
Cdd:COG1042 1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 81 TWPGIVRKLGGLGVRAAIIV--GETRSGADRAALERA-LAAAKPYLLRVVGPGSLGVVSPALG--AHFGAPAciVKAGGV 155
Cdd:COG1042 81 TVPDVVEECGEKGVKAAVVIsaGFAETGEEGAALEQElLEIARRYGMRLLGPNCLGLINPATGlnATFAPVP--PLPGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 156 AWVSQSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAARNKPV 235
Cdd:COG1042 159 ALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 236 LALRAGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEALGVGRAAAtSGGVTLVTSDRGVAKLAV 301
Cdd:COG1042 239 VVLKSGRSEAGaraaashtgalagsDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPR-GRRLAIVTNSGGPGVLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 302 DALAAAGETLAQWPRAAVDEVGGALPAGIVAGNPLLLGDDARPEYFGAALKALAQHPPTGTVFVVHATSHSAPAVDVARV 381
Cdd:COG1042 318 DALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 382 LIESRKFARRGMLACFFGGVDAAT-RDALHVHGIPVHTTPQRLARAHARLVDYQLGRELLMQTPEgtPPQPAASISAARH 460
Cdd:COG1042 398 LIEAAKGSGKPVLASWMGGDSVAEaRRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA--SEDFDPDRERARA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 461 TARAALAQGRDGFEGDAALEWLAGFGIEC-----ATDAD------------V-------------DMGDTIVDIT----- 505
Cdd:COG1042 476 IIEAALAEGRGVLTEAEAKALLAAYGIPVvptrlARSAEeavaaaeeigypVvlkivspdilhksDVGGVRLNLRdaeav 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 506 ------------------------------------VGMYDDPNFGPV------------FRysvppaDgvsapfVVYGL 537
Cdd:COG1042 556 raafeeilarvraarpdaridgvlvqpmvpggveliVGVKRDPVFGPVimfglggifvevLK------D------VALRL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 538 PPFNTVLARAVVARS-------PYAHRAPP--EPLLQALTALSQAVCDVREIVEMSLV-LRVRPTRVVALGPHIRLATGR 607
Cdd:COG1042 624 PPLNEALAREMIRELraakllrGYRGRPPAdlDALADVLVRLSQLAADLPEILELDINpLLVVPEGVVAVDARIRLAPPA 703
|
..
gi 685730662 608 SR 609
Cdd:COG1042 704 PP 705
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-434 |
3.60e-88 |
|
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: 285.74 E-value: 3.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 6 LDALFHPTAVAVVGASPRPGSVGAMVWACVLDGRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPATWPGI 85
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 86 VRKLGGLGVRAAIIV----GETrSGADRAALERALAAAKPYLLRVVGPGSLGVVSPALG--AHFGAPAciVKAGGVAWVS 159
Cdd:TIGR02717 81 VEECGEKGVKGAVVItagfKEV-GEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKlnATFAPTM--PKKGGIAFIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 160 QSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAARNKPVLALR 239
Cdd:TIGR02717 158 QSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 240 AGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEALGVGRaAATSGGVTLVTSDRGVAKLAVDALA 305
Cdd:TIGR02717 238 SGTSEAGakaasshtgalagsDEAYDAAFKQAGVIRADSIEELFDLARLLSNQP-LPKGNRVAIITNAGGPGVIATDACE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 306 AAGETLAQWPRAAVDEVGGALPAGIVAGNPLLLGDDARPEYFGAALKALAQHPPTGTVFVVHATSHSAPAVDVARVLIES 385
Cdd:TIGR02717 317 ENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 685730662 386 RKFA-RRGMLACFFGGVDAAT-RDALHVHGIPVHTTPQRLARAHARLVDYQ 434
Cdd:TIGR02717 397 AKKSnEKPVVAGFMGGKSVDPaKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
152-275 |
8.99e-43 |
|
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: 151.46 E-value: 8.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 152 AGGVAWVSQSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAAR 231
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 685730662 232 NKPVLALRAGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEAL 275
Cdd:pfam13607 81 RKPVVVLKAGRSEAGaraaashtgalagsDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
630-775 |
2.62e-14 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 71.18 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 630 ITVRPIRPEDEAAHRELLSAMTPDDLRMrfFGAIRNFDHSQIARMTQIDYDREMALIAtldDADGRAH---TLGAVRAVT 706
Cdd:COG1247 2 MTIRPATPEDAPAIAAIYNEAIAEGTAT--FETEPPSEEEREAWFAAILAPGRPVLVA---EEDGEVVgfaSLGPFRPRP 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685730662 707 DPDNEAtEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAVSSTEE 775
Cdd:COG1247 77 AYRGTA-EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLP 144
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
9-100 |
3.44e-14 |
|
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: 69.08 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 9 LFHP-TAVAVVGASPRPGSVGAMVWACVLDG--RFGGAIWP--VNPKYGELnghKVYPYVDQLPSA--PSVALVCTPPAT 81
Cdd:smart00881 1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYgtKFVGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77
|
90
....*....|....*....
gi 685730662 82 WPGIVRKLGGLGVRAAIIV 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVI 96
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
711-770 |
1.92e-08 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 53.49 E-value: 1.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 711 EATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAV 770
Cdd:TIGR01575 54 EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNE 113
|
|
| rimI |
PRK09491 |
ribosomal-protein-alanine N-acetyltransferase; Provisional |
711-768 |
6.48e-08 |
|
ribosomal-protein-alanine N-acetyltransferase; Provisional
Pssm-ID: 181904 [Multi-domain] Cd Length: 146 Bit Score: 52.24 E-value: 6.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 711 EATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG--TAWMigEALRENTAMISLAKDSGF 768
Cdd:PRK09491 63 EATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGvaTLWL--EVRASNAAAIALYESLGF 120
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
654-768 |
7.28e-08 |
|
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: 51.36 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 654 DLRMRFFGAIRNFDHSQIarmtQIDYDREMALIATLDDADGRAhtLGAVRAVTDPD--NEATEFAIAVRPDQKGKGLGRM 731
Cdd:pfam00583 6 ELLSEEFPEPWPDEPLDL----LEDWDEDASEGFFVAEEDGEL--VGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTA 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 685730662 732 LMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGF 768
Cdd:pfam00583 80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
125-241 |
1.72e-04 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 44.19 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 125 RVVGPGSLGVVSPALGAHFGAPACIVKAGGVAWVSQSNALTNAVLGWAHARGLGFSHAVALGGEA--DVDAADVLDYLAS 202
Cdd:PLN00125 123 RLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPfnGTNFVDCLEKFVK 202
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 685730662 203 DAETRAILLELDTVKSARKfmSAA---RAAARNKPVLALRAG 241
Cdd:PLN00125 203 DPQTEGIILIGEIGGTAEE--DAAafiKESGTEKPVVAFIAG 242
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
693-744 |
9.68e-04 |
|
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 38.03 E-value: 9.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 685730662 693 DGRAHTLGAVRAVTDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:cd04301 7 DGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
1-609 |
6.60e-140 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 429.16 E-value: 6.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 1 MTVRNLDALFHPTAVAVVGASPRPGSVGAMVWACVLDGRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPA 80
Cdd:COG1042 1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 81 TWPGIVRKLGGLGVRAAIIV--GETRSGADRAALERA-LAAAKPYLLRVVGPGSLGVVSPALG--AHFGAPAciVKAGGV 155
Cdd:COG1042 81 TVPDVVEECGEKGVKAAVVIsaGFAETGEEGAALEQElLEIARRYGMRLLGPNCLGLINPATGlnATFAPVP--PLPGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 156 AWVSQSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAARNKPV 235
Cdd:COG1042 159 ALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 236 LALRAGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEALGVGRAAAtSGGVTLVTSDRGVAKLAV 301
Cdd:COG1042 239 VVLKSGRSEAGaraaashtgalagsDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPR-GRRLAIVTNSGGPGVLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 302 DALAAAGETLAQWPRAAVDEVGGALPAGIVAGNPLLLGDDARPEYFGAALKALAQHPPTGTVFVVHATSHSAPAVDVARV 381
Cdd:COG1042 318 DALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 382 LIESRKFARRGMLACFFGGVDAAT-RDALHVHGIPVHTTPQRLARAHARLVDYQLGRELLMQTPEgtPPQPAASISAARH 460
Cdd:COG1042 398 LIEAAKGSGKPVLASWMGGDSVAEaRRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA--SEDFDPDRERARA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 461 TARAALAQGRDGFEGDAALEWLAGFGIEC-----ATDAD------------V-------------DMGDTIVDIT----- 505
Cdd:COG1042 476 IIEAALAEGRGVLTEAEAKALLAAYGIPVvptrlARSAEeavaaaeeigypVvlkivspdilhksDVGGVRLNLRdaeav 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 506 ------------------------------------VGMYDDPNFGPV------------FRysvppaDgvsapfVVYGL 537
Cdd:COG1042 556 raafeeilarvraarpdaridgvlvqpmvpggveliVGVKRDPVFGPVimfglggifvevLK------D------VALRL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 538 PPFNTVLARAVVARS-------PYAHRAPP--EPLLQALTALSQAVCDVREIVEMSLV-LRVRPTRVVALGPHIRLATGR 607
Cdd:COG1042 624 PPLNEALAREMIRELraakllrGYRGRPPAdlDALADVLVRLSQLAADLPEILELDINpLLVVPEGVVAVDARIRLAPPA 703
|
..
gi 685730662 608 SR 609
Cdd:COG1042 704 PP 705
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
6-434 |
3.60e-88 |
|
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: 285.74 E-value: 3.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 6 LDALFHPTAVAVVGASPRPGSVGAMVWACVLDGRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPATWPGI 85
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 86 VRKLGGLGVRAAIIV----GETrSGADRAALERALAAAKPYLLRVVGPGSLGVVSPALG--AHFGAPAciVKAGGVAWVS 159
Cdd:TIGR02717 81 VEECGEKGVKGAVVItagfKEV-GEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKlnATFAPTM--PKKGGIAFIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 160 QSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAARNKPVLALR 239
Cdd:TIGR02717 158 QSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 240 AGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEALGVGRaAATSGGVTLVTSDRGVAKLAVDALA 305
Cdd:TIGR02717 238 SGTSEAGakaasshtgalagsDEAYDAAFKQAGVIRADSIEELFDLARLLSNQP-LPKGNRVAIITNAGGPGVIATDACE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 306 AAGETLAQWPRAAVDEVGGALPAGIVAGNPLLLGDDARPEYFGAALKALAQHPPTGTVFVVHATSHSAPAVDVARVLIES 385
Cdd:TIGR02717 317 ENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 685730662 386 RKFA-RRGMLACFFGGVDAAT-RDALHVHGIPVHTTPQRLARAHARLVDYQ 434
Cdd:TIGR02717 397 AKKSnEKPVVAGFMGGKSVDPaKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
152-275 |
8.99e-43 |
|
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: 151.46 E-value: 8.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 152 AGGVAWVSQSNALTNAVLGWAHARGLGFSHAVALGGEADVDAADVLDYLASDAETRAILLELDTVKSARKFMSAARAAAR 231
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 685730662 232 NKPVLALRAGRGDSG--------------DLLYTAAFQRAGMVRVDALDDLLDEIEAL 275
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 ... |
15-137 |
1.78e-22 |
|
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: 92.99 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 15 VAVVGASPRPGSVGAMVWACVLdgRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPATWPGIVRKLGGLGV 94
Cdd:pfam13380 3 IAVVGASPNPGRPGYKVARYLL--EHGYPVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 685730662 95 RAAIIVGETRSGAdraalerALAAAKPYLLRVVGPGSLGVVSP 137
Cdd:pfam13380 81 KAVWLQPGIENEE-------AAAIARAAGIRVVGDRCLGVEHP 116
|
|
| MnaT |
COG1247 |
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism]; |
630-775 |
2.62e-14 |
|
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
Pssm-ID: 440860 [Multi-domain] Cd Length: 163 Bit Score: 71.18 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 630 ITVRPIRPEDEAAHRELLSAMTPDDLRMrfFGAIRNFDHSQIARMTQIDYDREMALIAtldDADGRAH---TLGAVRAVT 706
Cdd:COG1247 2 MTIRPATPEDAPAIAAIYNEAIAEGTAT--FETEPPSEEEREAWFAAILAPGRPVLVA---EEDGEVVgfaSLGPFRPRP 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685730662 707 DPDNEAtEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAVSSTEE 775
Cdd:COG1247 77 AYRGTA-EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLP 144
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
9-100 |
3.44e-14 |
|
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: 69.08 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 9 LFHP-TAVAVVGASPRPGSVGAMVWACVLDG--RFGGAIWP--VNPKYGELnghKVYPYVDQLPSA--PSVALVCTPPAT 81
Cdd:smart00881 1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYgtKFVGGVYPgkVGPKVDGV---PVYDSVAEAPEEtgVDVAVIFVPAEA 77
|
90
....*....|....*....
gi 685730662 82 WPGIVRKLGGLGVRAAIIV 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVI 96
|
|
| RimL |
COG1670 |
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ... |
626-768 |
1.41e-13 |
|
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: 69.26 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 626 RGERITVRPIRPEDEAAHRELLSamtpDDLRMRFF-GAIRNFDHSQ--IARMTQIDYDREMALIATLDDADGRAhtLGAV 702
Cdd:COG1670 4 ETERLRLRPLRPEDAEALAELLN----DPEVARYLpGPPYSLEEARawLERLLADWADGGALPFAIEDKEDGEL--IGVV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685730662 703 RAV-TDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYA-RSRGTAWMIGEALRENTAMISLAKDSGF 768
Cdd:COG1670 78 GLYdIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGF 145
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
15-96 |
8.07e-09 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 54.75 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 15 VAVVGASPRPGSVGAMVWACVLdgRFGGAIWPVNPKYGELNGHKVYPYVDQLPSAPSVALVCTPPATWPGIVRKLGGLGV 94
Cdd:COG1832 19 IAVVGLSPNPERPSYYVAKYLQ--RHGYRVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVPEIVDEAIAIGA 96
|
..
gi 685730662 95 RA 96
Cdd:COG1832 97 KV 98
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
125-242 |
1.33e-08 |
|
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: 56.99 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 125 RVVGPGSLGVVSPA---LGAHfgaPACIVKAGGVAWVSQSNALTNAVlgwAH---ARGLGFSHAVALGGEADV--DAADV 196
Cdd:COG0074 117 RLIGPNCPGIITPGeckLGIM---PGHIFKPGRVGIVSRSGTLTYEA---VWqltQAGLGQSTCVGIGGDPIIgtSFIDV 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 685730662 197 LDYLASDAETRAILL--------EldtvksarkfMSAAR--AAARNKPVLALRAGR 242
Cdd:COG0074 191 LELFEEDPETEAIVMigeiggsaE----------EEAAEyiKENMTKPVVAYIAGR 236
|
|
| rimI |
TIGR01575 |
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ... |
711-770 |
1.92e-08 |
|
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273701 [Multi-domain] Cd Length: 131 Bit Score: 53.49 E-value: 1.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 711 EATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAV 770
Cdd:TIGR01575 54 EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNE 113
|
|
| RimI |
COG0456 |
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ... |
705-786 |
2.38e-08 |
|
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440224 [Multi-domain] Cd Length: 92 Bit Score: 51.97 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 705 VTDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAVSSTEEPGVVAFRLK 784
Cdd:COG0456 7 LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALV 86
|
..
gi 685730662 785 LQ 786
Cdd:COG0456 87 ME 88
|
|
| rimI |
PRK09491 |
ribosomal-protein-alanine N-acetyltransferase; Provisional |
711-768 |
6.48e-08 |
|
ribosomal-protein-alanine N-acetyltransferase; Provisional
Pssm-ID: 181904 [Multi-domain] Cd Length: 146 Bit Score: 52.24 E-value: 6.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 711 EATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG--TAWMigEALRENTAMISLAKDSGF 768
Cdd:PRK09491 63 EATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGvaTLWL--EVRASNAAAIALYESLGF 120
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
654-768 |
7.28e-08 |
|
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: 51.36 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 654 DLRMRFFGAIRNFDHSQIarmtQIDYDREMALIATLDDADGRAhtLGAVRAVTDPD--NEATEFAIAVRPDQKGKGLGRM 731
Cdd:pfam00583 6 ELLSEEFPEPWPDEPLDL----LEDWDEDASEGFFVAEEDGEL--VGFASLSIIDDepPVGEIEGLAVAPEYRGKGIGTA 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 685730662 732 LMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGF 768
Cdd:pfam00583 80 LLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
|
|
| Acetyltransf_3 |
pfam13302 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
629-768 |
2.64e-07 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 379112 [Multi-domain] Cd Length: 139 Bit Score: 50.42 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 629 RITVRPIRPEDeaahRELLSAMTPDDLRMRF-FGAIRNFDHSQ--IARMTQIDYDREMALIATLDDADGRahtLGAVRAV 705
Cdd:pfam13302 1 RLLLRPLTEED----AEALFELLSDPEVMRYgVPWPLTLEEARewLARIWAADEAERGYGWAIELKDTGF---IGSIGLY 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685730662 706 -TDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSR-GTAWMIGEALRENTAMISLAKDSGF 768
Cdd:pfam13302 74 dIDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGF 138
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
506-603 |
5.21e-07 |
|
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: 51.32 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 506 VGMYDDPNFGPVFRYSvppADGVSA---PFVVYGLPPFNTVLARAVVARSP-------YAHRAPP--EPLLQALTALSQA 573
Cdd:pfam13549 114 VGVTRDPQFGPVIMFG---LGGIAVevlKDVAFRLPPLNMTLAREMIRRTRaykllkgYRGEPPAdlDALEDVLVRVSQL 190
|
90 100 110
....*....|....*....|....*....|.
gi 685730662 574 VCDVREIVEMSL-VLRVRPTRVVALGPHIRL 603
Cdd:pfam13549 191 VIDFPEIRELDInPLLADEDGVVALDARIRL 221
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
197-723 |
2.87e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.03 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 197 LDYLASDAETRAILLELDTVKSARKFMSAARAAARNKPVLALRAGRGDSGDLLYTAAFQRAGMVRVDALDDLLDEIEALG 276
Cdd:COG3321 847 VDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAAL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 277 VGRAAATSGGVTLVTSDRGVAKLAVDALAAAGETLAQWPRAAVDEVGGALPAGIVAGNPLLLGDDARPEYFGAALKALAQ 356
Cdd:COG3321 927 AALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLA 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 357 HPPTGTVFVVHATSHSAPAVDVARVLIESRKFARRG-MLACFFGGVDAATRDALHVHGIPVHTTPQRLARAHARLVDYQL 435
Cdd:COG3321 1007 AAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAaAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALAL 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 436 GRELLMQTPEGTPPQPAASISAARHTARAALAQGRDGFEGDAALEWLAGFGIECATDADVDMGDTIVDITVGMYDDPNFG 515
Cdd:COG3321 1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAA 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 516 PVFRYSVPPADGVSAPFVVYGLPPFNTVLARAVVARSPYAHRAPPEPLLQALTALSQAVCDVREIVEMSLVLRVRPTRVV 595
Cdd:COG3321 1167 LLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVA 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 596 ALGPHIRLATGRSRLAIVPYPRYLEQQLDWRGERITVRPIRPEDEAAHRELLSAMTPDDLRMRFFGAIRNFDHSQIARMT 675
Cdd:COG3321 1247 ALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 685730662 676 QIDYDREMALIATLDDADGRAHTLGAVRAVTDPDNEATEFAIAVRPDQ 723
Cdd:COG3321 1327 AAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAA 1374
|
|
| PhnO |
COG0454 |
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ... |
717-785 |
2.94e-06 |
|
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];
Pssm-ID: 440222 [Multi-domain] Cd Length: 136 Bit Score: 47.36 E-value: 2.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 717 IAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGFAVSSTEEPGV-VAFRLKL 785
Cdd:COG0454 64 LYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVgGEFEKEL 133
|
|
| yhbS |
COG3153 |
Predicted N-acetyltransferase YhbS [General function prediction only]; |
632-744 |
1.45e-05 |
|
Predicted N-acetyltransferase YhbS [General function prediction only];
Pssm-ID: 442387 [Multi-domain] Cd Length: 142 Bit Score: 45.46 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 632 VRPIRPEDEAAHRELLSAMTPDDLRMRFFGAIRNfdhsqiarmtqiDYDREMALIATlddADGR--AHTLGAVRAVTDPD 709
Cdd:COG3153 1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLRE------------DPAAGLSLVAE---DDGEivGHVALSPVDIDGEG 65
|
90 100 110
....*....|....*....|....*....|....*
gi 685730662 710 NEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:COG3153 66 PALLLGPLAVDPEYRGQGIGRALMRAALEAARERG 100
|
|
| ArgA |
COG1246 |
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ... |
630-744 |
1.62e-05 |
|
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: 44.98 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 630 ITVRPIRPEDEAAHRELLSAMTPDDLRMRFFGAirnfdhsqiarmtqidydremaliatldDADGRAhtLGAVRAVTDPD 709
Cdd:COG1246 1 MTIRPATPDDVPAILELIRPYALEEEIGEFWVA----------------------------EEDGEI--VGCAALHPLDE 50
|
90 100 110
....*....|....*....|....*....|....*
gi 685730662 710 NEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:COG1246 51 DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG 85
|
|
| ElaA |
COG2153 |
Predicted N-acyltransferase, GNAT family [General function prediction only]; |
689-744 |
4.19e-05 |
|
Predicted N-acyltransferase, GNAT family [General function prediction only];
Pssm-ID: 441756 [Multi-domain] Cd Length: 134 Bit Score: 44.02 E-value: 4.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685730662 689 LDDADGRAHTLGA---------VRAVTDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:COG2153 27 LDGKDEDARHLLAyddgelvatARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERG 91
|
|
| COG3393 |
COG3393 |
Predicted acetyltransferase, GNAT family [General function prediction only]; |
700-768 |
1.24e-04 |
|
Predicted acetyltransferase, GNAT family [General function prediction only];
Pssm-ID: 442620 [Multi-domain] Cd Length: 86 Bit Score: 41.43 E-value: 1.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685730662 700 GAVRAVTDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRGTAWMIGEALRENTAMISLAKDSGF 768
Cdd:COG3393 4 AMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
125-241 |
1.72e-04 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 44.19 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 125 RVVGPGSLGVVSPALGAHFGAPACIVKAGGVAWVSQSNALTNAVLGWAHARGLGFSHAVALGGEA--DVDAADVLDYLAS 202
Cdd:PLN00125 123 RLIGPNCPGIIKPGECKIGIMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPfnGTNFVDCLEKFVK 202
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 685730662 203 DAETRAILLELDTVKSARKfmSAA---RAAARNKPVLALRAG 241
Cdd:PLN00125 203 DPQTEGIILIGEIGGTAEE--DAAafiKESGTEKPVVAFIAG 242
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
693-744 |
9.68e-04 |
|
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 38.03 E-value: 9.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 685730662 693 DGRAHTLGAVRAVTDPDNEATEFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:cd04301 7 DGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERG 58
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|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
125-241 |
1.73e-03 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 41.24 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685730662 125 RVVGPGSLGVVSPA---LGAhfgAPACIVKAGGVAWVSQSNALTNAVLGWAHARGLGFSHAVALGGEA--DVDAADVLDY 199
Cdd:PTZ00187 142 RLIGPNCPGIIKPGeckIGI---MPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPfnGTNFIDCLKL 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 685730662 200 LASDAETRAILL--EL--DTVKSARKFMSAARaaaRNKPVLALRAG 241
Cdd:PTZ00187 219 FLNDPETEGIILigEIggTAEEEAAEWIKNNP---IKKPVVSFIAG 261
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|
| Acetyltransf_7 |
pfam13508 |
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions. |
699-744 |
8.12e-03 |
|
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
Pssm-ID: 463905 [Multi-domain] Cd Length: 84 Bit Score: 36.28 E-value: 8.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 685730662 699 LGAVRAVTDPDNEAT-EFAIAVRPDQKGKGLGRMLMTRIIDYARSRG 744
Cdd:pfam13508 15 VGFAALLPLDDEGALaELRLAVHPEYRGQGIGRALLEAAEAAAKEGG 61
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