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Conserved domains on  [gi|16130509|ref|NP_417079|]
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peptidyl-lysine N-acetyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

bifunctional acetate--CoA ligase family protein/GNAT family N-acetyltransferase( domain architecture ID 11437151)

bifunctional acetate--CoA ligase family protein/GNAT family N-acetyltransferase containing an N-terminal domain similar to ADP-forming acetate--CoA ligase that catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate, and a C-terminal domain that may catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-700 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


:

Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 869.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   1 MSQRGLEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNAS 80
Cdd:COG1042   1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509  81 RNLALLEELGEKGCKTCIILSAP--------ASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAF 152
Cdd:COG1042  81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 153 ISQSAAVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042 161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 233 IKSGRSPAAQRLLNT-T---AGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDAL 308
Cdd:COG1042 241 LKSGRSEAGARAAAShTgalAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 309 WSRNGKLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIE 388
Cdd:COG1042 321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 389 AVKHHPRskyvSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTAEAHL 468
Cdd:COG1042 401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 469 LLQQAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEV 548
Cdd:COG1042 476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 549 QQAANAIFDRVKMAWPQARVHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARY 628
Cdd:COG1042 556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509 629 LVIQGIKSKKIRARSALRPLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDVTLDISPFEGD 700
Cdd:COG1042 634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 2.76e-17

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: 80.43  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 722 NGERCLFRPILPEDEPQLQQFISRvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRIDqTEEILGVTRAI 800
Cdd:COG1670   4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKE-DGELIGVVGLY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130509 801 S-DPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDH-GLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG1670  81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-700 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 869.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   1 MSQRGLEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNAS 80
Cdd:COG1042   1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509  81 RNLALLEELGEKGCKTCIILSAP--------ASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAF 152
Cdd:COG1042  81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 153 ISQSAAVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042 161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 233 IKSGRSPAAQRLLNT-T---AGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDAL 308
Cdd:COG1042 241 LKSGRSEAGARAAAShTgalAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 309 WSRNGKLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIE 388
Cdd:COG1042 321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 389 AVKHHPRskyvSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTAEAHL 468
Cdd:COG1042 401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 469 LLQQAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEV 548
Cdd:COG1042 476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 549 QQAANAIFDRVKMAWPQARVHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARY 628
Cdd:COG1042 556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509 629 LVIQGIKSKKIRARSALRPLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDVTLDISPFEGD 700
Cdd:COG1042 634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 4.58e-131

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: 400.15  E-value: 4.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509     6 LEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNASRNLAL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509    86 LEELGEKGCKTCIILSA--------PASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAgfkevgeeGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   158 AVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   238 SP----AAQRLLNTTAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDALWSRNG 313
Cdd:TIGR02717 241 SEagakAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   314 KLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIEAVKHH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 16130509   394 PRskyVSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYR 443
Cdd:TIGR02717 401 NE---KPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 472-690 9.85e-90

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: 283.60  E-value: 9.85e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   472 QAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   552 ANAIFDRVKMAWPQARVHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARYLvI 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   632 QGIKSKKIRARSALR-PLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDV 690
Cdd:pfam13549 158 RRTRAYKLLKGYRGEpPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDA 217
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 2.76e-17

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: 80.43  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 722 NGERCLFRPILPEDEPQLQQFISRvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRIDqTEEILGVTRAI 800
Cdd:COG1670   4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKE-DGELIGVVGLY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130509 801 S-DPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDH-GLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG1670  81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 4.18e-16

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: 74.47  E-value: 4.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509      9 LLRP-KSIAVIGASMKPNRAGYLMMRNLLAGG--FNGPVLP--VTPAwkaVLGVLAWPDIASLP--FTPDLAVLCTNASR 81
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGPK---VDGVPVYDSVAEAPeeTGVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|.
gi 16130509     82 NLALLEELGEKGCKTCIILSA 102
Cdd:smart00881  78 APDAIDEAIEAGIKGIVVITE 98
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 3.54e-11

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: 60.99  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   750 DLYYRYFSEinEFTHEDLANMTQIDYDREMAFVAVRRidqTEEILGVTRAISDPDNID--AEFAVLVRSDLKGLGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEE---DGELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16130509   828 MEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-700 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 869.06  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   1 MSQRGLEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNAS 80
Cdd:COG1042   1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509  81 RNLALLEELGEKGCKTCIILSAP--------ASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAF 152
Cdd:COG1042  81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 153 ISQSAAVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042 161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 233 IKSGRSPAAQRLLNT-T---AGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDAL 308
Cdd:COG1042 241 LKSGRSEAGARAAAShTgalAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 309 WSRNGKLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIE 388
Cdd:COG1042 321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 389 AVKHHPRskyvSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTAEAHL 468
Cdd:COG1042 401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 469 LLQQAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEV 548
Cdd:COG1042 476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 549 QQAANAIFDRVKMAWPQARVHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARY 628
Cdd:COG1042 556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509 629 LVIQGIKSKKIRARSALRPLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDVTLDISPFEGD 700
Cdd:COG1042 634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 4.58e-131

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: 400.15  E-value: 4.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509     6 LEALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNASRNLAL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509    86 LEELGEKGCKTCIILSA--------PASQHEDLRACALRHNMRLLGPNSLGLLAPWQGLNASFSPVPIKRGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAgfkevgeeGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   158 AVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   238 SP----AAQRLLNTTAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDALWSRNG 313
Cdd:TIGR02717 241 SEagakAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   314 KLATLSEETCQKLRDALPEHVAISNPLDLRDDASSEHYIKTLDILLHSQDFDALMVIHSPSAAAPATESAQVLIEAVKHH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 16130509   394 PRskyVSLLTNWCGEHSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYR 443
Cdd:TIGR02717 401 NE---KPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 472-690 9.85e-90

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: 283.60  E-value: 9.85e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   472 QAIAEGATSLDTHEVQPILQAYGMNTLPTWIASDSTEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTANEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   552 ANAIFDRVKMAWPQARVHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEDQAVVALPPLNMNLARYLvI 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   632 QGIKSKKIRARSALR-PLDVAGLSQLLVQVSNLIVDCPEIQRLDIHPLLASGSEFTALDV 690
Cdd:pfam13549 158 RRTRAYKLLKGYRGEpPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDA 217
Succ_CoA_lig pfam13607
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ...
 147-280 2.39e-54

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: 184.59  E-value: 2.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   147 RGKLAFISQSAAVSNTILDWAQQRKMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASR 226
Cdd:pfam13607   1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130509   227 NKPILVIKSGRSPAAQRLLNT----TAGMDPAWDAAIQRAGLLRVQDTHELFSAVETL 280
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 ...
 13-132 2.43e-31

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: 118.41  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509    13 KSIAVIGASMKPNRAGYLMMRNLLAGGFngPVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNASRNLALLEELGEK 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALAL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 16130509    93 GCKTCIILsaPASQHEDLRACALRHNMRLLGPNSLGLLAP 132
Cdd:pfam13380  79 GAKAVWLQ--PGIENEEAAAIARAAGIRVVGDRCLGVEHP 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 2.76e-17

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: 80.43  E-value: 2.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 722 NGERCLFRPILPEDEPQLQQFISRvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRIDqTEEILGVTRAI 800
Cdd:COG1670   4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKE-DGELIGVVGLY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130509 801 S-DPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDH-GLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG1670  81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 4.18e-16

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: 74.47  E-value: 4.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509      9 LLRP-KSIAVIGASMKPNRAGYLMMRNLLAGG--FNGPVLP--VTPAwkaVLGVLAWPDIASLP--FTPDLAVLCTNASR 81
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGPK---VDGVPVYDSVAEAPeeTGVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|.
gi 16130509     82 NLALLEELGEKGCKTCIILSA 102
Cdd:smart00881  78 APDAIDEAIEAGIKGIVVITE 98
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
728-863 4.09e-15

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.88  E-value: 4.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 728 FRPILPEDEPQLQQFISRVTKEDLYyRYFSEinEFTHEDLAN-MTQIDYDREMAFVAVRRidqtEEILGVTRAIS----D 802
Cdd:COG1247   4 IRPATPEDAPAIAAIYNEAIAEGTA-TFETE--PPSEEEREAwFAAILAPGRPVLVAEED----GEVVGFASLGPfrprP 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130509 803 PDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG1247  77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
7-96 2.48e-12

Predicted CoA-binding protein [General function prediction only];


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 65.15  E-value: 2.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   7 EALLRPKSIAVIGASMKPNRAGYLMMRNLLAGGFNgpVLPVTPAWKAVLGVLAWPDIASLPFTPDLAVLCTNASRNLALL 86
Cdd:COG1832  11 EILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYR--VIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVPEIV 88

                        90
                ....*....|
gi 16130509  87 EELGEKGCKT 96
Cdd:COG1832  89 DEAIAIGAKV 98
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 3.54e-11

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: 60.99  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   750 DLYYRYFSEinEFTHEDLANMTQIDYDREMAFVAVRRidqTEEILGVTRAISDPDNID--AEFAVLVRSDLKGLGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEE---DGELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 16130509   828 MEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 814-863 9.22e-07

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 9.22e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 16130509 814 VRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG0456  21 VDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGF 70
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 725-863 3.02e-06

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 47.73  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   725 RCLFRPILPEDEPQLQQFISRvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVrrIDQTEEILGVTRAIS-D 802
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD--PEVMRYGVPWPLTlEEAREWLARIWAADEAERGYGWAI--ELKDTGFIGSIGLYDiD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509   803 PDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYT-RDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGF 138
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
728-863 2.05e-05

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 45.08  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 728 FRPILPEDEPQLqqfisrvtkEDLYYRYFSEINEfthEDLANMTQIDYDREMAFVAVRRidqtEEILGVTRAISDPDNID 807
Cdd:COG3153   1 IRPATPEDAEAI---------AALLRAAFGPGRE---AELVDRLREDPAAGLSLVAEDD----GEIVGHVALSPVDIDGE 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 808 AEFAVL----VRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRgmvALARKLGF 863
Cdd:COG3153  65 GPALLLgplaVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLL---PFYERFGF 121
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 728-863 8.01e-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: 43.44  E-value: 8.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 728 FRPILPEDEPQLQQFISrvtkedlYYRYFSEINEFthedlanmtqidydremaFVAvrriDQTEEILGVTRAISDPDNId 807
Cdd:COG1246   3 IRPATPDDVPAILELIR-------PYALEEEIGEF------------------WVA----EEDGEIVGCAALHPLDEDL- 52

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130509 808 AEFA-VLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITmpnNRGMVALARKLGF 863
Cdd:COG1246  53 AELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGF 106
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 743-865 9.66e-05

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 43.12  E-value: 9.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 743 ISRVTKEDlyyryFSEIN--EFTHEDLANMTQIDYDREmaFVAVrriDQTEEILGVT--RAISDPDnidAEFAVL-VRSD 817
Cdd:COG0454   3 IRKATPED-----INFILliEALDAELKAMEGSLAGAE--FIAV---DDKGEPIGFAglRRLDDKV---LELKRLyVLPE 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 16130509 818 LKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGFNV 865
Cdd:COG0454  70 YRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
792-863 2.98e-04

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.28  E-value: 2.98e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509 792 EILGVTRAISDPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGF 863
Cdd:COG3393   1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 110-207 7.81e-04

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: 42.35  E-value: 7.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 110 LRACALRHNMRLLGPNSLGLLAPWQgLNASFSPVPI-KRGKLAFISQSAAVSNTILDWAQQRKMGFSYFIALG-DSL-DI 186
Cdd:COG0074 107 VKRYAKAKGTRLIGPNCPGIITPGE-CKLGIMPGHIfKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGgDPIiGT 185

                        90       100
                ....*....|....*....|.
gi 16130509 187 DVDELLDYLARDSKTSAILLY 207
Cdd:COG0074 186 SFIDVLELFEEDPETEAIVMI 206
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
791-873 1.02e-03

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.17  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 791 EEILGVTRaISDPDNIDAEFA-VLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLngitmpnnrgmVALAR--------KL 861
Cdd:COG2153  43 GELVATAR-LLPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARERGARRI-----------VLSAQahavgfyeKL 110

                        90
                ....*....|....
gi 16130509 862 GFNV--DIQLEEGI 873
Cdd:COG2153 111 GFVPvgEEFLEAGI 124
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 776-863 4.86e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509   776 DREMAFVAVRRidqtEEILGVTRAISDPDNID-AEFAVLVRSDLKGLGLGRRLMEKLITYTRDHGLQRlngITMPNNRGM 854
Cdd:pfam13508   1 PGGRFFVAEDD----GKIVGFAALLPLDDEGAlAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKL---LELETTNRA 73


                  ....*....
gi 16130509   855 VALARKLGF 863
Cdd:pfam13508  74 AAFYEKLGF 82
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 484-607 7.83e-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: 39.65  E-value: 7.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130509 484 HEVQ--PILQAYGMNTLPTWIASDSTEAVHIAEQIGY-PVALklrspdiphKSEVQ--------GVMLyLRTANEVQQAA 552
Cdd:COG0045   4 HEYQakELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVV---------KAQVHaggrgkagGVKL-AKSPEEAREAA 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130509 553 NAIFDRvKMAWPQA-----RVHGLLVQSMANraGAQELRVVVEHDPVFG-PLIML-GEGGVE 607
Cdd:COG0045  74 EEILGM-TLVTHQTgpkgkPVNKVLVEEGVD--IAKELYLSILLDRATRrPVIMAsTEGGMD 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
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