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Conserved domains on  [gi|2265605998|ref|WP_253382586|]
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protein lysine acetyltransferase [unidentified bacterial endosymbiont]

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];
1-702 0e+00

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


:

Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 877.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   1 MSQRGLEALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHGPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAK 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  81 RNPELLASLGEKGCKTCIILSSP--------PEQHSELLACASRYQMRLLGPNSLGLLAPWQGLNASFSPVPIRKGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 233 IKSGRSPAAQRLLHSHSGM----DAAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGEKLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAASHTGAlagsDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 309 WRRNGKLAALGEETLQRLQEALPDSVTPDNPLDLRDDASSERYIKAISILLDSRDFDALMIIHSPSAAAPGSESGRALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 389 TVRDHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPNNLTANSVDVHR 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 469 QLQQAIEEGATSLDTHEVRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSDIQGVMLYLRTAAEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 549 QQAADAIIDRVKMTWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265605998 629 LVIQAIKSKKIRGRSALRPLDIAGLSQFLVQVSNLIVDCAQIQRLDIHPLLASGNEFTALDVTLEIAPFVGDKE 702
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAP 707
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 7.04e-14

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: 70.41  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 722 NGERALFRPILPEDEPQLRVFIAQvtKEDLYYRYFSEIN-EFTHDDLANMTQIDYDREMAFVAVRRSDQGdEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKEDG-ELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265605998 801 S-DPDNIDAEFAVLVRSDLKGFGLGRRLLEKLISYTRDH-GLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-702 0e+00

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 877.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   1 MSQRGLEALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHGPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAK 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  81 RNPELLASLGEKGCKTCIILSSP--------PEQHSELLACASRYQMRLLGPNSLGLLAPWQGLNASFSPVPIRKGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 233 IKSGRSPAAQRLLHSHSGM----DAAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGEKLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAASHTGAlagsDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 309 WRRNGKLAALGEETLQRLQEALPDSVTPDNPLDLRDDASSERYIKAISILLDSRDFDALMIIHSPSAAAPGSESGRALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 389 TVRDHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPNNLTANSVDVHR 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 469 QLQQAIEEGATSLDTHEVRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSDIQGVMLYLRTAAEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 549 QQAADAIIDRVKMTWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265605998 629 LVIQAIKSKKIRGRSALRPLDIAGLSQFLVQVSNLIVDCAQIQRLDIHPLLASGNEFTALDVTLEIAPFVGDKE 702
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAP 707
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 9.89e-135

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: 409.78  E-value: 9.89e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   6 LEALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHGPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAKRNPEL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  86 LASLGEKGCKTCIILSS--------PPEQHSELLACASRYQMRLLGPNSLGLLAPWQGLNASFSPVPIRKGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAgfkevgeeGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 158 AVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 238 SPAAQRLLHSHSGM----DAAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGEKLMIISNGAAPAALALDELWRRNG 313
Cdd:TIGR02717 241 SEAGAKAASSHTGAlagsDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 314 KLAALGEETLQRLQEALPDSVTPDNPLDLRDDASSERYIKAISILLDSRDFDALMIIHSPSAAAPGSESGRALIETVRDH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265605998 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 ...
 472-694 2.49e-89

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: 282.44  E-value: 2.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 472 QAIEEGATSLDTHEVRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSDIQGVMLYLRTAAEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 552 ADAIIDRVKMTWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARYLvI 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265605998 632 QAIKSKKI-RGRSALRPLDIAGLSQFLVQVSNLIVDCAQIQRLDIHPLLASGNEFTALDVTLEI 694
Cdd:pfam13549 158 RRTRAYKLlKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 2.44e-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: 72.16  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998    9 LLRP-KSIAVIGASMKPDRAGYLMMRNLLAGG--FHGPVIPVtPAYKAVQGVLAWPDVQSLPFV--PDLAVLCTHAKRNP 83
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPG-KVGPKVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAP 79

                           90
                   ....*....|....*....
gi 2265605998   84 ELLASLGEKGCKTCIILSS 102
Cdd:smart00881  80 DAIDEAIEAGIKGIVVITE 98
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 7.04e-14

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: 70.41  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 722 NGERALFRPILPEDEPQLRVFIAQvtKEDLYYRYFSEIN-EFTHDDLANMTQIDYDREMAFVAVRRSDQGdEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKEDG-ELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265605998 801 S-DPDNIDAEFAVLVRSDLKGFGLGRRLLEKLISYTRDH-GLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 1.35e-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: 53.68  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 750 DLYYRYFSEinEFTHDDLANMTQIDYDREMAFVAVRRsdqGDEILGVTRAISDPDNID--AEFAVLVRSDLKGFGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEE---DGELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2265605998 828 LEKLISYTRDHGLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-702 0e+00

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


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 877.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   1 MSQRGLEALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHGPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAK 80
Cdd:COG1042     1 MSTRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  81 RNPELLASLGEKGCKTCIILSSP--------PEQHSELLACASRYQMRLLGPNSLGLLAPWQGLNASFSPVPIRKGKLAF 152
Cdd:COG1042    81 TVPDVVEECGEKGVKAAVVISAGfaetgeegAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 153 ISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASRNKPILV 232
Cdd:COG1042   161 VSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 233 IKSGRSPAAQRLLHSHSGM----DAAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGEKLMIISNGAAPAALALDEL 308
Cdd:COG1042   241 LKSGRSEAGARAAASHTGAlagsDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADAL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 309 WRRNGKLAALGEETLQRLQEALPDSVTPDNPLDLRDDASSERYIKAISILLDSRDFDALMIIHSPSAAAPGSESGRALIE 388
Cdd:COG1042   321 EDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIE 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 389 TVRDHPRgkfvTLLTNWCGEFSSQEARRLFSEAGLPTYRTPEGTITAFMHMVEYRRNQKQLRETPAlPNNLTANSVDVHR 468
Cdd:COG1042   401 AAKGSGK----PVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPA-SEDFDPDRERARA 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 469 QLQQAIEEGATSLDTHEVRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSDIQGVMLYLRTAAEV 548
Cdd:COG1042   476 IIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEAV 555

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 549 QQAADAIIDRVKMTWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARY 628
Cdd:COG1042   556 RAAFEEILARVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALARE 633

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265605998 629 LVIQAIKSKKIRGRSALRPLDIAGLSQFLVQVSNLIVDCAQIQRLDIHPLLASGNEFTALDVTLEIAPFVGDKE 702
Cdd:COG1042   634 MIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAP 707
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 6-443 9.89e-135

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: 409.78  E-value: 9.89e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   6 LEALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHGPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAKRNPEL 85
Cdd:TIGR02717   1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  86 LASLGEKGCKTCIILSS--------PPEQHSELLACASRYQMRLLGPNSLGLLAPWQGLNASFSPVPIRKGKLAFISQSA 157
Cdd:TIGR02717  81 VEECGEKGVKGAVVITAgfkevgeeGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 158 AVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASRNKPILVIKSGR 237
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 238 SPAAQRLLHSHSGM----DAAWDAAIQRAGLLRVQDTHELFSAVETLSHMRPLRGEKLMIISNGAAPAALALDELWRRNG 313
Cdd:TIGR02717 241 SEAGAKAASSHTGAlagsDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 314 KLAALGEETLQRLQEALPDSVTPDNPLDLRDDASSERYIKAISILLDSRDFDALMIIHSPSAAAPGSESGRALIETVRDH 393
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEGAKKS 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265605998 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 ...
 472-694 2.49e-89

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: 282.44  E-value: 2.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 472 QAIEEGATSLDTHEVRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGYPVALKLRSPDIPHKSDIQGVMLYLRTAAEVQQA 551
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 552 ADAIIDRVKMTWPQARIHGLLVQSMANraGAQELRVVVEHDPVFGPLIMLGEGGVEWRPEEQAVVALPPLNMNLARYLvI 631
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAP--GGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREM-I 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265605998 632 QAIKSKKI-RGRSALRPLDIAGLSQFLVQVSNLIVDCAQIQRLDIHPLLASGNEFTALDVTLEI 694
Cdd:pfam13549 158 RRTRAYKLlKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
Succ_CoA_lig pfam13607
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ...
 147-280 1.71e-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: 184.98  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 147 KGKLAFISQSAAVSNTILDWAQQREMGFSYFIALGDSLDIDADELLDFLARDSKTSAILLYLEHLSDARRFVSASRSASR 226
Cdd:pfam13607   1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2265605998 227 NKPILVIKSGRSPAAQRLLHSH----SGMDAAWDAAIQRAGLLRVQDTHELFSAVETL 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 3.67e-28

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


Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 109.55  E-value: 3.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998  13 KSIAVIGASMKPDRAGYLMMRNLLAGGFhgPVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCTHAKRNPELLASLGEK 92
Cdd:pfam13380   1 KTIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALAL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2265605998  93 GCKTCIILSSppEQHSELLACASRYQMRLLGPNSLGLLAP 132
Cdd:pfam13380  79 GAKAVWLQPG--IENEEAAAIARAAGIRVVGDRCLGVEHP 116
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 9-102 2.44e-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: 72.16  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998    9 LLRP-KSIAVIGASMKPDRAGYLMMRNLLAGG--FHGPVIPVtPAYKAVQGVLAWPDVQSLPFV--PDLAVLCTHAKRNP 83
Cdd:smart00881   1 LLNPnTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPG-KVGPKVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAP 79

                           90
                   ....*....|....*....
gi 2265605998   84 ELLASLGEKGCKTCIILSS 102
Cdd:smart00881  80 DAIDEAIEAGIKGIVVITE 98
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 722-863 7.04e-14

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: 70.41  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 722 NGERALFRPILPEDEPQLRVFIAQvtKEDLYYRYFSEIN-EFTHDDLANMTQIDYDREMAFVAVRRSDQGdEILGVTRAI 800
Cdd:COG1670     4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPYSlEEARAWLERLLADWADGGALPFAIEDKEDG-ELIGVVGLY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265605998 801 S-DPDNIDAEFAVLVRSDLKGFGLGRRLLEKLISYTRDH-GLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:COG1670    81 DiDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGF 145
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
728-863 1.01e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 69.64  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 728 FRPILPEDEPQLRVFIAQVTKEDLYyRYFSEinEFTHDDLAN-MTQIDYDREMAFVAVRrsdqGDEILGVTRAIS----D 802
Cdd:COG1247     4 IRPATPEDAPAIAAIYNEAIAEGTA-TFETE--PPSEEEREAwFAAILAPGRPVLVAEE----DGEVVGFASLGPfrprP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265605998 803 PDNIDAEFAVLVRSDLKGFGLGRRLLEKLISYTRDHGLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:COG1247    77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGF 137
YccU COG1832
Predicted CoA-binding protein [General function prediction only];
7-87 3.90e-11

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


Pssm-ID: 441437 [Multi-domain]  Cd Length: 138  Bit Score: 61.68  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998   7 EALLRPKSIAVIGASMKPDRAGYLMMRNLLAGGFHgpVIPVTPAYKAVQGVLAWPDVQSLPFVPDLAVLCthakRNPELL 86
Cdd:COG1832    11 EILKSAKTIAVVGLSPNPERPSYYVAKYLQRHGYR--VIPVNPGAKEILGEKVYASLADIPEPVDIVDVF----RRSEAV 84


                  .
gi 2265605998  87 A 87
Cdd:COG1832    85 P 85
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 750-863 1.35e-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: 53.68  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 750 DLYYRYFSEinEFTHDDLANMTQIDYDREMAFVAVRRsdqGDEILGVTRAISDPDNID--AEFAVLVRSDLKGFGLGRRL 827
Cdd:pfam00583   6 ELLSEEFPE--PWPDEPLDLLEDWDEDASEGFFVAEE---DGELVGFASLSIIDDEPPvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2265605998 828 LEKLISYTRDHGLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
728-880 7.93e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.54  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 728 FRPILPEDEPQLrvfiaqvtkEDLYYRYFSEINEfthDDLANMTQIDYDREMAFVAVRrsdqGDEILGVTRAISDPDNID 807
Cdd:COG3153     1 IRPATPEDAEAI---------AALLRAAFGPGRE---AELVDRLREDPAAGLSLVAED----DGEIVGHVALSPVDIDGE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 808 AEFAVL----VRSDLKGFGLGRRLLEKLISYTRDHG--LLRLNGitmpdNRGMVTLARKLGF----DVDIQLDEGIVALS 877
Cdd:COG3153    65 GPALLLgplaVDPEYRGQGIGRALMRAALEAARERGarAVVLLG-----DPSLLPFYERFGFrpagELGLTLGPDEVFLA 139


                  ...
gi 2265605998 878 LSL 880
Cdd:COG3153   140 KEL 142
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 725-863 8.45e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 43.49  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 725 RALFRPILPEDEPQLRVFIAQvtKEDLYYRYFSEIN-EFTHDDLANMTQIDYDREMAFVAVRRSDQGdeILGVTRAIS-D 802
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD--PEVMRYGVPWPLTlEEAREWLARIWAADEAERGYGWAIELKDTG--FIGSIGLYDiD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265605998 803 PDNIDAEFAVLVRSDLKGFGLGRRLLEKLISYT-RDHGLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGF 138
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 814-863 1.06e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 41.95  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265605998 814 VRSDLKGFGLGRRLLEKLISYTRDHGLLRLNGITMPDNRGMVTLARKLGF 863
Cdd:COG0456    21 VDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGF 70
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 761-865 2.97e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 41.58  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 761 EFTHDDLANMTQIDYDREmaFVAVrrsDQGDEILGVT--RAISDPDnidAEFAVL-VRSDLKGFGLGRRLLEKLISYTRD 837
Cdd:COG0454    18 EALDAELKAMEGSLAGAE--FIAV---DDKGEPIGFAglRRLDDKV---LELKRLyVLPEYRGKGIGKALLEALLEWARE 89

                          90       100       110
                  ....*....|....*....|....*....|
gi 2265605998 838 HGL--LRLNgiTMPDNRGMVTLARKLGFDV 865
Cdd:COG0454    90 RGCtaLELD--TLDGNPAAIRFYERLGFKE 117
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 484-689 1.50e-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: 41.96  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 484 HE--VRPVLGSYGIHTLPTWIASDSAEAVHIAEQIGY-PVALklrspdiphKSDIQ--------GVMLyLRTAAEVQQAA 552
Cdd:COG0045     4 HEyqAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGpPVVV---------KAQVHaggrgkagGVKL-AKSPEEAREAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 553 DAIIDRV---KMTWPQAR-IHGLLVQSMANraGAQELRVVVEHDPVFG-PLIML-GEGGVEW------RPEEQAVVALPP 620
Cdd:COG0045    74 EEILGMTlvtHQTGPKGKpVNKVLVEEGVD--IAKELYLSILLDRATRrPVIMAsTEGGMDIeevaeeTPEKIIKVPIDP 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265605998 621 LnMNLARYlviQAiksKKIRGRSALRPLDIAGLSQFLVQVSNLIV--DCAQIQrldIHPL-LASGNEFTALD 689
Cdd:COG0045   152 L-VGLQPY---QA---RELAFALGLPGKQVKQFAKILKKLYRAFVekDASLVE---INPLvVTKDGRLVALD 213
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 766-863 3.39e-03

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 38.43  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 766 DLANMTQIDYDREMAFVAvrrsDQGDEILGVTRAISDPDNIdAEFA-VLVRSDLKGFGLGRRLLEKLISYTRDHGLLRLN 844
Cdd:COG1246    16 ELIRPYALEEEIGEFWVA----EEDGEIVGCAALHPLDEDL-AELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF 90

                          90
                  ....*....|....*....
gi 2265605998 845 GITMPDNRGmvtLARKLGF 863
Cdd:COG1246    91 LLTTSAAIH---FYEKLGF 106
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 109-207 3.95e-03

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: 40.04  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265605998 109 ELLACASRYQMRLLGPNSLGLLAPWQgLNASFSPVPI-RKGKLAFISQSAAVSNTILDWAQQREMGFSYFIALG-DSL-D 185
Cdd:COG0074   106 RVKRYAKAKGTRLIGPNCPGIITPGE-CKLGIMPGHIfKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGgDPIiG 184

                          90       100
                  ....*....|....*....|..
gi 2265605998 186 IDADELLDFLARDSKTSAILLY 207
Cdd:COG0074   185 TSFIDVLELFEEDPETEAIVMI 206
 
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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