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Conserved domains on  [gi|1028844058|ref|WP_064013187|]
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protein lysine acetyltransferase [Salmonella enterica]

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: 872.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   1 MSQQGLEALLRPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNAS 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  81 RNLALLDALGAKGCKTCIILSAPTSQ--------HEELLACARHYKMRLLGPNSLGLLAPWQGLNASFSPVPIKQGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGFAEtgeegaalEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 233 IKSGRSPAAQRLLNT----SAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAAShtgaLAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 309 WSRNGKLATLSEETCLQLRQALPAHIDIANPLDLCDDASSEHYVKTLDILLASQDFDALMVIHSPSAAAPGTESAHALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 389 TIKRHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTTEAHN 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 469 LLQRAIAEGATSLDTHEVQPILHAYGLHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTASEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 549 QQAANAIFDRVKMAWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028844058 629 LVIQGIKQRKIRARSALRPLDIVGLSQLLVQVSNLIVDCPEIQRLDIHPLLASASEFTALDVTLDIAPFDGD 700
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-866 2.41e-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: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 722 NGDRCLFRPILPEDEPQLQQFIAQvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRMDNaEEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKED-GELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028844058 801 S-DPDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYTRDH-GLKRLNGITMPNNRGMVALARKLGFQVD 866
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
 
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: 872.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   1 MSQQGLEALLRPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNAS 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  81 RNLALLDALGAKGCKTCIILSAPTSQ--------HEELLACARHYKMRLLGPNSLGLLAPWQGLNASFSPVPIKQGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGFAEtgeegaalEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 233 IKSGRSPAAQRLLNT----SAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAAShtgaLAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 309 WSRNGKLATLSEETCLQLRQALPAHIDIANPLDLCDDASSEHYVKTLDILLASQDFDALMVIHSPSAAAPGTESAHALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 389 TIKRHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTTEAHN 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 469 LLQRAIAEGATSLDTHEVQPILHAYGLHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTASEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 549 QQAANAIFDRVKMAWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028844058 629 LVIQGIKQRKIRARSALRPLDIVGLSQLLVQVSNLIVDCPEIQRLDIHPLLASASEFTALDVTLDIAPFDGD 700
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 3.86e-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: 400.53  E-value: 3.86e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   6 LEALLRPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNASRNLAL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  86 LDALGAKGCKTCIILSAPTSQ--------HEELLACARHYKMRLLGPNSLGLLAPWQGLNASFSPVPIKQGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAGFKEvgeegaelEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 158 AVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 238 SPAAQRLLNTS----AGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDELWSRNG 313
Cdd:TIGR02717 241 SEAGAKAASSHtgalAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 314 KLATLSEETCLQLRQALPAHIDIANPLDLCDDASSEHYVKTLDILLASQDFDALMVIHSPSAAAPGTESAHALIETIKRH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1028844058 394 PRgkfVTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYR 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 4.94e-88

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: 278.98  E-value: 4.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 472 RAIAEGATSLDTHEVQPILHAYGLHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTASEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 552 ANAIFDRVKMAWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARYLVi 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMI- 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028844058 632 qgikqRKIRARSALR------PLDIVGLSQLLVQVSNLIVDCPEIQRLDIHPLLASASEFTALDV 690
Cdd:pfam13549 158 -----RRTRAYKLLKgyrgepPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDA 217
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-866 2.41e-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: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 722 NGDRCLFRPILPEDEPQLQQFIAQvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRMDNaEEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKED-GELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028844058 801 S-DPDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYTRDH-GLKRLNGITMPNNRGMVALARKLGFQVD 866
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 4.40e-15

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 71.77  E-value: 4.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058    9 LLRP-KSIAVIGASMKPHRAGYLMMRNLLAGG--FNGPVLP--VTPawkAVLGVMAWPDIASLP--FTPDLAILCTNASR 81
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGP---KVDGVPVYDSVAEAPeeTGVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|.
gi 1028844058   82 NLALLDALGAKGCKTCIILSA 102
Cdd:smart00881  78 APDAIDEAIEAGIKGIVVITE 98
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 2.67e-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: 61.38  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 750 DLYYRYFSEinEFTHEDLANMTQIDYDREMAFVAVRRMDnaeEILGVTRA--ISDPDNVDAEFAVLVRSDLKGLGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEEDG---ELVGFASLsiIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1028844058 828 MEKLIAYTRDHGLKRLNGITMPNNRGMVALARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 781-843 8.22e-03

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: 35.71  E-value: 8.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028844058 781 FVAVrrmdNAEEILGVTRAISDPDNVD-AE-FAVLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRL 843
Cdd:cd04301     2 LVAE----DDGEIVGFASLSPDGSGGDtAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
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: 872.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   1 MSQQGLEALLRPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNAS 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  81 RNLALLDALGAKGCKTCIILSAPTSQ--------HEELLACARHYKMRLLGPNSLGLLAPWQGLNASFSPVPIKQGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGFAEtgeegaalEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 233 IKSGRSPAAQRLLNT----SAGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAAShtgaLAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 309 WSRNGKLATLSEETCLQLRQALPAHIDIANPLDLCDDASSEHYVKTLDILLASQDFDALMVIHSPSAAAPGTESAHALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 389 TIKRHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPSNLTSNTTEAHN 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 469 LLQRAIAEGATSLDTHEVQPILHAYGLHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTASEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 549 QQAANAIFDRVKMAWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028844058 629 LVIQGIKQRKIRARSALRPLDIVGLSQLLVQVSNLIVDCPEIQRLDIHPLLASASEFTALDVTLDIAPFDGD 700
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPP 705
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 3.86e-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: 400.53  E-value: 3.86e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   6 LEALLRPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNASRNLAL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  86 LDALGAKGCKTCIILSAPTSQ--------HEELLACARHYKMRLLGPNSLGLLAPWQGLNASFSPVPIKQGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAGFKEvgeegaelEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 158 AVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 238 SPAAQRLLNTS----AGMDPAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGDRLMIISNGAAPAALALDELWSRNG 313
Cdd:TIGR02717 241 SEAGAKAASSHtgalAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 314 KLATLSEETCLQLRQALPAHIDIANPLDLCDDASSEHYVKTLDILLASQDFDALMVIHSPSAAAPGTESAHALIETIKRH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1028844058 394 PRgkfVTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYR 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 4.94e-88

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: 278.98  E-value: 4.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 472 RAIAEGATSLDTHEVQPILHAYGLHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSEVQGVMLYLRTASEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 552 ANAIFDRVKMAWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARYLVi 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMI- 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028844058 632 qgikqRKIRARSALR------PLDIVGLSQLLVQVSNLIVDCPEIQRLDIHPLLASASEFTALDV 690
Cdd:pfam13549 158 -----RRTRAYKLLKgyrgepPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDA 217
Succ_CoA_lig pfam13607
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ...
 148-280 2.30e-53

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: 181.90  E-value: 2.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 148 GKLAFISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDVDELLDYLARDSKTSAILLYLEQLSDARRFVSAARSASRN 227
Cdd:pfam13607   2 GNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAARR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1028844058 228 KPILVIKSGRSPAAQRLLNT----SAGMDPAWDAAIQRAGLLRVQDTHELFSAVETL 280
Cdd:pfam13607  82 KPVVVLKAGRSEAGARAAAShtgaLAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 13-132 2.95e-30

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: 115.33  E-value: 2.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  13 KSIAVIGASMKPHRAGYLMMRNLLAGGFngPVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNASRNLALLDALGAK 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALAL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1028844058  93 GCKTCIILSAptSQHEELLACARHYKMRLLGPNSLGLLAP 132
Cdd:pfam13380  79 GAKAVWLQPG--IENEEAAAIARAAGIRVVGDRCLGVEHP 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-866 2.41e-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: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 722 NGDRCLFRPILPEDEPQLQQFIAQvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDREMAFVAVRRMDNaEEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKED-GELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028844058 801 S-DPDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYTRDH-GLKRLNGITMPNNRGMVALARKLGFQVD 866
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
728-871 5.10e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 79.27  E-value: 5.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 728 FRPILPEDEPQLQQFIAQVTKEDLYyRYFSEinEFTHEDLAN-MTQIDYDREMAFVAVRrmdnAEEILGVTRAIS----D 802
Cdd:COG1247     4 IRPATPEDAPAIAAIYNEAIAEGTA-TFETE--PPSEEEREAwFAAILAPGRPVLVAEE----DGEVVGFASLGPfrprP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028844058 803 PDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRLNGITMPNNRGMVALARKLGFQVDIQLEE 871
Cdd:COG1247    77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPE 145
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 4.40e-15

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 71.77  E-value: 4.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058    9 LLRP-KSIAVIGASMKPHRAGYLMMRNLLAGG--FNGPVLP--VTPawkAVLGVMAWPDIASLP--FTPDLAILCTNASR 81
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGP---KVDGVPVYDSVAEAPeeTGVDVAVIFVPAEA 77

                           90       100
                   ....*....|....*....|.
gi 1028844058   82 NLALLDALGAKGCKTCIILSA 102
Cdd:smart00881  78 APDAIDEAIEAGIKGIVVITE 98
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
1-96 2.06e-12

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 65.15  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058   1 MSQQGLEALLR-PKSIAVIGASMKPHRAGYLMMRNLLAGGFNgpVLPVTPAWKAVLGVMAWPDIASLPFTPDLAILCTNA 79
Cdd:COG1832     4 PDDEEIREILKsAKTIAVVGLSPNPERPSYYVAKYLQRHGYR--VIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRS 81

                          90
                  ....*....|....*..
gi 1028844058  80 SRNLALLDALGAKGCKT 96
Cdd:COG1832    82 EAVPEIVDEAIAIGAKV 98
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 2.67e-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: 61.38  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 750 DLYYRYFSEinEFTHEDLANMTQIDYDREMAFVAVRRMDnaeEILGVTRA--ISDPDNVDAEFAVLVRSDLKGLGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEEDG---ELVGFASLsiIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1028844058 828 MEKLIAYTRDHGLKRLNGITMPNNRGMVALARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 814-865 9.77e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 50.42  E-value: 9.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028844058 814 VRSDLKGLGLGRRLMEKLIAYTRDHGLKRLNGITMPNNRGMVALARKLGFQV 865
Cdd:COG0456    21 VDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 725-864 2.58e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 50.81  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 725 RCLFRPILPEDEPQLQQFIAQvtKEDLYYRYFSEIN-EFTHEDLANMTQIDYDRE-MAFVAVRRmdnAEEILGVTRAIS- 801
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD--PEVMRYGVPWPLTlEEAREWLARIWAADEAERgYGWAIELK---DTGFIGSIGLYDi 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028844058 802 DPDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYT-RDHGLKRLNGITMPNNRGMVALARKLGFQ 864
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
728-865 1.36e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.54  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 728 FRPILPEDEPQLqqfiaqvtkEDLYYRYFSEINEfthEDLANMTQIDYDREMAFVAVRrmdnAEEILGVTRAISDPDNVD 807
Cdd:COG3153     1 IRPATPEDAEAI---------AALLRAAFGPGRE---AELVDRLREDPAAGLSLVAED----DGEIVGHVALSPVDIDGE 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028844058 808 AEFAVL----VRSDLKGLGLGRRLMEKLIAYTRDHGLKRLNGITMPNNRgmvALARKLGFQV 865
Cdd:COG3153    65 GPALLLgplaVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLL---PFYERFGFRP 123
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 761-865 2.58e-06

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 47.74  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 761 EFTHEDLANMTQIDYDREmaFVAVrrmDNAEEILGVTRAISDPDNVdAEFAVL-VRSDLKGLGLGRRLMEKLIAYTRDHG 839
Cdd:COG0454    18 EALDAELKAMEGSLAGAE--FIAV---DDKGEPIGFAGLRRLDDKV-LELKRLyVLPEYRGKGIGKALLEALLEWARERG 91

                          90       100
                  ....*....|....*....|....*.
gi 1028844058 840 LKRLNGITMPNNRGMVALARKLGFQV 865
Cdd:COG0454    92 CTALELDTLDGNPAAIRFYERLGFKE 117
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 728-865 5.74e-06

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: 46.52  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 728 FRPILPEDEPQLQQFIAQvtkedlyYRYFSEINEFthedlanmtqidydremaFVAVRrmdnAEEILGVTRAISDPDNVd 807
Cdd:COG1246     3 IRPATPDDVPAILELIRP-------YALEEEIGEF------------------WVAEE----DGEIVGCAALHPLDEDL- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1028844058 808 AEFA-VLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRLNGITMPNNRGmvaLARKLGFQV 865
Cdd:COG1246    53 AELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIH---FYEKLGFEE 108
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
792-864 6.07e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 45.28  E-value: 6.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028844058 792 EILGVTRAISDPDNVDAEFAVLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRLNGITMPNNRGMVALARKLGFQ 864
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 84-207 7.61e-05

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: 45.44  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  84 ALLDALGAkGCKTCIILSAPTSQHE--ELLACARHYKMRLLGPNSLGLLAPWQgLNASFSPVPI-KQGKLAFISQSAAVS 160
Cdd:COG0074    80 AILEAIDA-GIKLIVCITEGIPVLDmvRVKRYAKAKGTRLIGPNCPGIITPGE-CKLGIMPGHIfKPGRVGIVSRSGTLT 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1028844058 161 NTILDWAQQREMGFSYFIALG-DSL-DIDVDELLDYLARDSKTSAILLY 207
Cdd:COG0074   158 YEAVWQLTQAGLGQSTCVGIGgDPIiGTSFIDVLELFEEDPETEAIVMI 206
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
789-873 1.03e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.86  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 789 NAEEILGVTRaISDPDNVDAEFA-VLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRLngitmpnnrgmVALAR-------- 859
Cdd:COG2153    41 DDGELVATAR-LLPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARERGARRI-----------VLSAQahavgfye 108

                          90
                  ....*....|....*.
gi 1028844058 860 KLGFQV--DIQLEEGI 873
Cdd:COG2153   109 KLGFVPvgEEFLEAGI 124
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 776-865 2.50e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.52  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058 776 DREMAFVAvrrmDNAEEILGVTRAISDPDNVD-AEFAVLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRlngITMPNNRGM 854
Cdd:pfam13508   1 PGGRFFVA----EDDGKIVGFAALLPLDDEGAlAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKL---LELETTNRA 73

                          90
                  ....*....|.
gi 1028844058 855 VALARKLGFQV 865
Cdd:pfam13508  74 AAFYEKLGFEE 84
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 11-102 1.57e-03

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: 38.73  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028844058  11 RPKSIAVIGASMKPHRAGYLMMRNLLAGGFNGpVLPVTPAwKA---VLGVMAWPDIASLP--FTPDLAILCTNASRNLAL 85
Cdd:pfam02629   2 KDTKVIVIGAGGLGIQGLNYHFIQMLGYGIKM-VFGVNPG-KGgteILGIPVYNSVDELEekTGVDVAVITVPAPFAQEA 79

                          90
                  ....*....|....*..
gi 1028844058  86 LDALGAKGCKTCIILSA 102
Cdd:pfam02629  80 IDELVDAGIKGIVNITP 96
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 781-843 8.22e-03

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: 35.71  E-value: 8.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028844058 781 FVAVrrmdNAEEILGVTRAISDPDNVD-AE-FAVLVRSDLKGLGLGRRLMEKLIAYTRDHGLKRL 843
Cdd:cd04301     2 LVAE----DDGEIVGFASLSPDGSGGDtAYiGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
 
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.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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