NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1278273923|gb|PIY25615|]
View 

hypothetical protein COZ12_00010 [Deltaproteobacteria bacterium CG_4_10_14_3_um_filter_60_8]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG3246 COG3246
Uncharacterized conserved protein, DUF849 family [Function unknown];
21-295 5.69e-104

Uncharacterized conserved protein, DUF849 family [Function unknown];


:

Pssm-ID: 442477  Cd Length: 276  Bit Score: 310.52  E-value: 5.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923  21 TEPVIINACLSGNVPTKETSPHLPVSVDEIVNDAIAVLDSGASILHIHARAPDGTPAWQPEIYGRIFEGIRCHQPEAILV 100
Cdd:COG3246     1 MRKVIITCAITGAIHTKSMNPALPVTPEEIAEDAIAAAEAGAAIVHLHVRDPDGRPSQDPELFREIVERIREACPDVIIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 101 ASTSGRQHADLGKRSAVLTldgKAKPDMASLTLGSMNF--PAQSSVNSPETMQSLCLRMRERGITPELEAFDLGMLNYAF 178
Cdd:COG3246    81 LTTGGGGGMTVEERLAHLA---ELKPEMASLDMGSMNFglGDRVFENTPADIEELAREMQERGVKPEIECFDTGHLYNAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 179 YLQRKGFLPQTCYVNLLMGSLGTVPGRMLDLANLVREIPRDWIWAGAGIGRYQLAVNNAALLMGGHVRVGLEDNPCYDYV 258
Cdd:COG3246   158 RLIDRGLLKGPLHFQFVLGVPGGMPADPENLLAMVDRLPDGATWSVAGIGRHQLPLAAMAIALGGHVRVGLEDNLYLDKG 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278273923 259 ECeAATNKGLVERIVCLAHNLGRPIATCGEARHKLRL 295
Cdd:COG3246   238 VL-AKSNAELVERAVRIAEELGREVATPAEAREILGL 273
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 306-454 2.73e-17

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: 78.11  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 306 VIIRKISVEDVGLAMDLLSKWNMAPvqasaaitrperdhlEMDNTFVACIQDKVVGVASWLPIDPLRAETASLAVAPEFI 385
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYALEE---------------EIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYR 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278273923 386 GCGIGYKLQEARLAEMRSQGIRHVRTETdRPDVIRWYvSKFGYRITGTNPKKHAFSLAERDYWTVLELE 454
Cdd:COG1246    66 GRGIGRRLLEALLAEARELGLKRLFLLT-TSAAIHFY-EKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
 
Name Accession Description Interval E-value
COG3246 COG3246
Uncharacterized conserved protein, DUF849 family [Function unknown];
21-295 5.69e-104

Uncharacterized conserved protein, DUF849 family [Function unknown];


Pssm-ID: 442477  Cd Length: 276  Bit Score: 310.52  E-value: 5.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923  21 TEPVIINACLSGNVPTKETSPHLPVSVDEIVNDAIAVLDSGASILHIHARAPDGTPAWQPEIYGRIFEGIRCHQPEAILV 100
Cdd:COG3246     1 MRKVIITCAITGAIHTKSMNPALPVTPEEIAEDAIAAAEAGAAIVHLHVRDPDGRPSQDPELFREIVERIREACPDVIIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 101 ASTSGRQHADLGKRSAVLTldgKAKPDMASLTLGSMNF--PAQSSVNSPETMQSLCLRMRERGITPELEAFDLGMLNYAF 178
Cdd:COG3246    81 LTTGGGGGMTVEERLAHLA---ELKPEMASLDMGSMNFglGDRVFENTPADIEELAREMQERGVKPEIECFDTGHLYNAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 179 YLQRKGFLPQTCYVNLLMGSLGTVPGRMLDLANLVREIPRDWIWAGAGIGRYQLAVNNAALLMGGHVRVGLEDNPCYDYV 258
Cdd:COG3246   158 RLIDRGLLKGPLHFQFVLGVPGGMPADPENLLAMVDRLPDGATWSVAGIGRHQLPLAAMAIALGGHVRVGLEDNLYLDKG 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278273923 259 ECeAATNKGLVERIVCLAHNLGRPIATCGEARHKLRL 295
Cdd:COG3246   238 VL-AKSNAELVERAVRIAEELGREVATPAEAREILGL 273
BKACE pfam05853
beta-keto acid cleavage enzyme; BKACE, beta-keto acid cleavage enzyme plays, a role in lysine ...
 24-295 5.57e-93

beta-keto acid cleavage enzyme; BKACE, beta-keto acid cleavage enzyme plays, a role in lysine degradation. In certain instances it catalyzes the conversion of 3-keto-5-aminohexanoate and acetyl-CoA into acetoacetate and 3-aminobutyryl-CoA. The family is found to have at least 14 slightly different potential new enzymatic activities, all of which can therefore be designated as beta-keto acid cleavage enzymes.


Pssm-ID: 461759  Cd Length: 274  Bit Score: 282.45  E-value: 5.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923  24 VIINACLSGNVPTKETSPHLPVSVDEIVNDAIAVLDSGASILHIHARAP-DGTPAWQPEIYGRIFEGIRCHQPEAILVAS 102
Cdd:pfam05853   1 VIITVAPTGAITTKSDNPALPVTPEEIAEEAIAAAEAGAAIVHLHVRDPeDGRPSQDPELYREIVAAIREARPDVIINLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 103 TSGRQHADLGKRSAVLTLdgkAKPDMASLTLGSMNFPAQSSV--NSPETMQSLCLRMRERGITPELEAFDLGMLNYAFYL 180
Cdd:pfam05853  81 TGGGGGMTVEERLAPVEA---LRPEMASLNMGSMNFGLGDLVfeNTPADIEELARRMRERGVKPEIECFDVGHLRNAARL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 181 QRKGFLPQTCYVNLLMGSLGTVPGRMLDLA---NLVREIPRDWIWAGAGIGRYQLAVNNAALLMGGHVRVGLEDNPcYDY 257
Cdd:pfam05853 158 LDRGLLKGPLHFQFVLGVPGGMPATPENLLflkATADRLPGGATWSVAGIGRAQLPLATAAIALGGHVRVGLEDNL-YLG 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278273923 258 VECEAATNKGLVERIVCLAHNLGRPIATCGEARHKLRL 295
Cdd:pfam05853 237 KGELAPSNAELVERAVRIAEELGREVATPAEAREILGL 274
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 306-454 2.73e-17

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: 78.11  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 306 VIIRKISVEDVGLAMDLLSKWNMAPvqasaaitrperdhlEMDNTFVACIQDKVVGVASWLPIDPLRAETASLAVAPEFI 385
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYALEE---------------EIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYR 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278273923 386 GCGIGYKLQEARLAEMRSQGIRHVRTETdRPDVIRWYvSKFGYRITGTNPKKHAFSLAERDYWTVLELE 454
Cdd:COG1246    66 GRGIGRRLLEALLAEARELGLKRLFLLT-TSAAIHFY-EKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
PRK07757 PRK07757
N-acetyltransferase;
305-431 1.06e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 54.04  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 305 QVIIRKISVEDVGLAMDLLSKWnmapvqASAAITRPeRDHLEMDNT----FVACIQDKVVGVAS----WLPIdplrAETA 376
Cdd:PRK07757    1 MMEIRKARLSDVKAIHALINVY------AKKGLMLP-RSLDELYENirdfYVAEEEGEIVGCCAlhilWEDL----AEIR 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278273923 377 SLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETDRPDvirwYVSKFGYRIT 431
Cdd:PRK07757   70 SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQPE----FFEKLGFREV 120
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 320-428 1.17e-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: 52.91  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 320 MDLLSKWNMAPVQASAAITRPERDHLEMDNTFVACIQDKVVGVASWLPID--PLRAETASLAVAPEFIGCGIGYKLQEAR 397
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDdePPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1278273923 398 LAEMRSQGIRHVRTETDRPDV--IRWYVsKFGY 428
Cdd:pfam00583  85 LEWARERGCERIFLEVAADNLaaIALYE-KLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 351-412 1.04e-07

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: 48.81  E-value: 1.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278273923 351 FVACIQDKVVGVASWLPIDPL--RAETASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTE 412
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGgdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
COG3246 COG3246
Uncharacterized conserved protein, DUF849 family [Function unknown];
21-295 5.69e-104

Uncharacterized conserved protein, DUF849 family [Function unknown];


Pssm-ID: 442477  Cd Length: 276  Bit Score: 310.52  E-value: 5.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923  21 TEPVIINACLSGNVPTKETSPHLPVSVDEIVNDAIAVLDSGASILHIHARAPDGTPAWQPEIYGRIFEGIRCHQPEAILV 100
Cdd:COG3246     1 MRKVIITCAITGAIHTKSMNPALPVTPEEIAEDAIAAAEAGAAIVHLHVRDPDGRPSQDPELFREIVERIREACPDVIIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 101 ASTSGRQHADLGKRSAVLTldgKAKPDMASLTLGSMNF--PAQSSVNSPETMQSLCLRMRERGITPELEAFDLGMLNYAF 178
Cdd:COG3246    81 LTTGGGGGMTVEERLAHLA---ELKPEMASLDMGSMNFglGDRVFENTPADIEELAREMQERGVKPEIECFDTGHLYNAA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 179 YLQRKGFLPQTCYVNLLMGSLGTVPGRMLDLANLVREIPRDWIWAGAGIGRYQLAVNNAALLMGGHVRVGLEDNPCYDYV 258
Cdd:COG3246   158 RLIDRGLLKGPLHFQFVLGVPGGMPADPENLLAMVDRLPDGATWSVAGIGRHQLPLAAMAIALGGHVRVGLEDNLYLDKG 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278273923 259 ECeAATNKGLVERIVCLAHNLGRPIATCGEARHKLRL 295
Cdd:COG3246   238 VL-AKSNAELVERAVRIAEELGREVATPAEAREILGL 273
BKACE pfam05853
beta-keto acid cleavage enzyme; BKACE, beta-keto acid cleavage enzyme plays, a role in lysine ...
 24-295 5.57e-93

beta-keto acid cleavage enzyme; BKACE, beta-keto acid cleavage enzyme plays, a role in lysine degradation. In certain instances it catalyzes the conversion of 3-keto-5-aminohexanoate and acetyl-CoA into acetoacetate and 3-aminobutyryl-CoA. The family is found to have at least 14 slightly different potential new enzymatic activities, all of which can therefore be designated as beta-keto acid cleavage enzymes.


Pssm-ID: 461759  Cd Length: 274  Bit Score: 282.45  E-value: 5.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923  24 VIINACLSGNVPTKETSPHLPVSVDEIVNDAIAVLDSGASILHIHARAP-DGTPAWQPEIYGRIFEGIRCHQPEAILVAS 102
Cdd:pfam05853   1 VIITVAPTGAITTKSDNPALPVTPEEIAEEAIAAAEAGAAIVHLHVRDPeDGRPSQDPELYREIVAAIREARPDVIINLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 103 TSGRQHADLGKRSAVLTLdgkAKPDMASLTLGSMNFPAQSSV--NSPETMQSLCLRMRERGITPELEAFDLGMLNYAFYL 180
Cdd:pfam05853  81 TGGGGGMTVEERLAPVEA---LRPEMASLNMGSMNFGLGDLVfeNTPADIEELARRMRERGVKPEIECFDVGHLRNAARL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 181 QRKGFLPQTCYVNLLMGSLGTVPGRMLDLA---NLVREIPRDWIWAGAGIGRYQLAVNNAALLMGGHVRVGLEDNPcYDY 257
Cdd:pfam05853 158 LDRGLLKGPLHFQFVLGVPGGMPATPENLLflkATADRLPGGATWSVAGIGRAQLPLATAAIALGGHVRVGLEDNL-YLG 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278273923 258 VECEAATNKGLVERIVCLAHNLGRPIATCGEARHKLRL 295
Cdd:pfam05853 237 KGELAPSNAELVERAVRIAEELGREVATPAEAREILGL 274
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 306-454 2.73e-17

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: 78.11  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 306 VIIRKISVEDVGLAMDLLSKWNMAPvqasaaitrperdhlEMDNTFVACIQDKVVGVASWLPIDPLRAETASLAVAPEFI 385
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYALEE---------------EIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYR 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278273923 386 GCGIGYKLQEARLAEMRSQGIRHVRTETdRPDVIRWYvSKFGYRITGTNPKKHAFSLAERDYWTVLELE 454
Cdd:COG1246    66 GRGIGRRLLEALLAEARELGLKRLFLLT-TSAAIHFY-EKLGFEEIDKEDLPYAKVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
342-453 2.58e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 342 RDHLEMDNTFVACIQDKVVGVAS----WLPIDPLRAETASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETDrPD 417
Cdd:COG3153    33 REDPAAGLSLVAEDDGEIVGHVAlspvDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD-PS 111

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1278273923 418 VIRWYvSKFGYRITGTnpkkHAFSLAERDYWTVLEL 453
Cdd:COG3153   112 LLPFY-ERFGFRPAGE----LGLTLGPDEVFLAKEL 142
PRK07757 PRK07757
N-acetyltransferase;
305-431 1.06e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 54.04  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 305 QVIIRKISVEDVGLAMDLLSKWnmapvqASAAITRPeRDHLEMDNT----FVACIQDKVVGVAS----WLPIdplrAETA 376
Cdd:PRK07757    1 MMEIRKARLSDVKAIHALINVY------AKKGLMLP-RSLDELYENirdfYVAEEEGEIVGCCAlhilWEDL----AEIR 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278273923 377 SLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETDRPDvirwYVSKFGYRIT 431
Cdd:PRK07757   70 SLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTYQPE----FFEKLGFREV 120
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 320-428 1.17e-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: 52.91  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 320 MDLLSKWNMAPVQASAAITRPERDHLEMDNTFVACIQDKVVGVASWLPID--PLRAETASLAVAPEFIGCGIGYKLQEAR 397
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDdePPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1278273923 398 LAEMRSQGIRHVRTETDRPDV--IRWYVsKFGY 428
Cdd:pfam00583  85 LEWARERGCERIFLEVAADNLaaIALYE-KLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 351-430 6.76e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 351 FVACIQDKVVGVASWLPIDPLRAET-ASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETDRPDvIRWYvSKFGYR 429
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAeLRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRA-AAFY-EKLGFE 83


                  .
gi 1278273923 430 I 430
Cdd:pfam13508  84 E 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
340-432 1.03e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 50.57  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 340 PERDHLEMDNT-FVACIQDKVVGVASWLPIDPlraETASL---AVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETdR 415
Cdd:COG2153    25 LELDGKDEDARhLLAYDDGELVATARLLPPGD---GEAKIgrvAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA-Q 100

                          90
                  ....*....|....*..
gi 1278273923 416 PDVIRWYvSKFGYRITG 432
Cdd:COG2153   101 AHAVGFY-EKLGFVPVG 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 351-412 1.04e-07

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: 48.81  E-value: 1.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278273923 351 FVACIQDKVVGVASWLPIDPL--RAETASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTE 412
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGgdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
350-436 1.21e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 350 TFVACIQDKVVGVASWLPI--DPLRAETA--SLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVRTETDRPDV--IRWYv 423
Cdd:COG1247    54 VLVAEEDGEVVGFASLGPFrpRPAYRGTAeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEasIALY- 132

                          90
                  ....*....|...
gi 1278273923 424 SKFGYRITGTNPK 436
Cdd:COG1247   133 EKLGFEEVGTLPE 145
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 362-435 1.55e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 48.88  E-value: 1.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278273923 362 VASWLPIDPLRAETASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHVR--TETDRPDVIRWYvSKFGYRITGTNP 435
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRleVREDNEAAIALY-EKLGFEEVGERP 77
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 306-433 1.08e-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: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278273923 306 VIIRKISVEDVGLamdllskwnMAPVQASAAITRpERDHLEMDNTFVA-CIQDKVVGVASWLPIDPLRAETASLAVAPEF 384
Cdd:COG0454     1 MSIRKATPEDINF---------ILLIEALDAELK-AMEGSLAGAEFIAvDDKGEPIGFAGLRRLDDKVLELKRLYVLPEY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1278273923 385 IGCGIGYKLQEARLAEMRSQGIRHVRTET--DRPDVIRWYVsKFGYRITGT 433
Cdd:COG0454    71 RGKGIGKALLEALLEWARERGCTALELDTldGNPAAIRFYE-RLGFKEIER 120
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
378-433 3.88e-04

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 41.45  E-value: 3.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278273923 378 LAVAPEFIGCGIGYKLQEARLAEMRSQGIR--HVRTETDRPDVIRWYVsKFGYRITGT 433
Cdd:PRK10975  132 LAVFPGAQGRGIGARLMQAALNWCQARGLTrlRVATQMGNLAALRLYI-RSGANIEST 188
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
358-433 2.85e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 36.81  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278273923 358 KVVGVASWLPIDPLRAETASLAVAPEFIGCGIGYKLQEARLAEMRSQGIRHV--RTETDRPDVIRWYvSKFGYRITGT 433
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPflYVDADNPAARRLY-ERLGFRPVGE 77
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH