NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|544826501|ref|WP_021242491|]
View 

GNAT family N-acetyltransferase [Enterobacter roggenkampii]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-156 4.56e-20

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 81.19  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQAIRHGCTTsYDAEVIarwTPDLMPERYRQMVIE-YPFYVVEDEkGDVAATGYLD------ 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTAT-FETEPP---SEEEREAWFAAILAPgRPVLVAEED-GEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  74 -LDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRL---TLDATPNAQSFYLKLGFVTLRENYHHSRMAGADLRC 149
Cdd:COG1247   77 aYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLvavVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDL 156


                 ....*..
gi 544826501 150 FEMAITL 156
Cdd:COG1247  157 VLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-156 4.56e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 81.19  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQAIRHGCTTsYDAEVIarwTPDLMPERYRQMVIE-YPFYVVEDEkGDVAATGYLD------ 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTAT-FETEPP---SEEEREAWFAAILAPgRPVLVAEED-GEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  74 -LDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRL---TLDATPNAQSFYLKLGFVTLRENYHHSRMAGADLRC 149
Cdd:COG1247   77 aYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLvavVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDL 156


                 ....*..
gi 544826501 150 FEMAITL 156
Cdd:COG1247  157 VLMQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-131 9.11e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 62.86  E-value: 9.11e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544826501   56 FYVVEDEK---GDVAATGYLDLDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGFV 131
Cdd:pfam13508   5 FFVAEDDGkivGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 57-131 3.86e-10

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 54.71  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  57 YVVEDEK-GDVAATGYLDLDT----HC-----LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYL 126
Cdd:PLN02706  56 CVIEDAAsGRIIATGSVFVERkfirNCgkvghIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYE 135


                 ....*
gi 544826501 127 KLGFV 131
Cdd:PLN02706 136 KCGYV 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-116 9.40e-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: 43.80  E-value: 9.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544826501  56 FYVVEDEkGDVAATGYLDLDTHC-----LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLD 116
Cdd:cd04301    1 FLVAEDD-GEIVGFASLSPDGSGgdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-156 4.56e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 81.19  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQAIRHGCTTsYDAEVIarwTPDLMPERYRQMVIE-YPFYVVEDEkGDVAATGYLD------ 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTAT-FETEPP---SEEEREAWFAAILAPgRPVLVAEED-GEVVGFASLGpfrprp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  74 -LDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRL---TLDATPNAQSFYLKLGFVTLRENYHHSRMAGADLRC 149
Cdd:COG1247   77 aYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLvavVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDL 156


                 ....*..
gi 544826501 150 FEMAITL 156
Cdd:COG1247  157 VLMQKRL 163
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-135 9.58e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 74.32  E-value: 9.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQAirhgcttsydaeviarwtpdlmpERYRQMVIEYP--FYVVEDEKGDVAATG---YLDLD 75
Cdd:COG0454    1 MSIRKATPEDINFILLIEALD-----------------------AELKAMEGSLAgaEFIAVDDKGEPIGFAglrRLDDK 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544826501  76 THCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLD---ATPNAQSFYLKLGFVTLRE 135
Cdd:COG0454   58 VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDtldGNPAAIRFYERLGFKEIER 120
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-154 6.04e-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: 72.33  E-value: 6.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAEtlwnirnqairhgcttsydaEVIARWTPDLMPERYRQmvieypFYVVEDEkGDVAATGYLDL--DTHC 78
Cdd:COG1246    1 MTIRPATPDDVP--------------------AILELIRPYALEEEIGE------FWVAEED-GEIVGCAALHPldEDLA 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544826501  79 -LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGFVTL-RENYHHSRMAGADLRCFEMAI 154
Cdd:COG1246   54 eLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIdKEDLPYAKVWQRDSVVMEKDL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-131 9.11e-14

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 62.86  E-value: 9.11e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544826501   56 FYVVEDEK---GDVAATGYLDLDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGFV 131
Cdd:pfam13508   5 FFVAEDDGkivGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-135 1.52e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 63.57  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   3 LRKATPQEAETLWNIRNQAIRHGcttsYDAEVIARWTPDLMPERyrqmvieypFYVVEDEkGDVAATG-------YLDLD 75
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPG----REAELVDRLREDPAAGL---------SLVAEDD-GEIVGHValspvdiDGEGP 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  76 THCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGFVTLRE 135
Cdd:COG3153   67 ALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGE 126
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 26-133 1.88e-13

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 63.06  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   26 CTTSYDAEVIARWTPDLMPERYRQMVI--EYPFYVVEDEkGDVAatGYLDLDTHC-LEAIFTLPAASGKGMATRIIEALK 102
Cdd:pfam13673   1 EAPDYSEEGIETFYEFISPEALRERIDqgEYFFFVAFEG-GQIV--GVIALRDRGhISLLFVDPDYQGQGIGKALLEAVE 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 544826501  103 HEARSRGI--TRLTLDATPNAQSFYLKLGFVTL 133
Cdd:pfam13673  78 DYAEKDGIklSELTVNASPYAVPFYEKLGFRAT 110
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 79-139 5.33e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 5.33e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544826501  79 LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPN---AQSFYLKLGFVTLRENYHH 139
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaAIALYEKLGFEEVGERPNY 79
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
56-132 1.85e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.19  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  56 FYVVEDekGDVAATG---YLDLDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGFVT 132
Cdd:COG2153   37 LLAYDD--GELVATArllPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVP 114
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 57-131 3.86e-10

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 54.71  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  57 YVVEDEK-GDVAATGYLDLDT----HC-----LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYL 126
Cdd:PLN02706  56 CVIEDAAsGRIIATGSVFVERkfirNCgkvghIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKAFYE 135


                 ....*
gi 544826501 127 KLGFV 131
Cdd:PLN02706 136 KCGYV 140
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
79-135 4.41e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.99  E-value: 4.41e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  79 LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTL---DATPNAQSFYLKLGFVTLRE 135
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLyvdADNPAARRLYERLGFRPVGE 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 30-130 1.73e-09

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: 52.52  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   30 YDAEVIARWTPDLMPERYRQMVIEYPFYVVEDEKGDVAATGYL-----DLDTHCLEAIFTLPAASGKGMATRIIEALKHE 104
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLsiiddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEW 87

                          90       100
                  ....*....|....*....|....*....
gi 544826501  105 ARSRGITRLTLDATPN---AQSFYLKLGF 130
Cdd:pfam00583  88 ARERGCERIFLEVAADnlaAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-155 1.48e-08

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: 51.15  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQA--IRHGCTTSYDAEVIARWTPDLMPERYRQMVieYPFYVVEDEKGDVAATGYL---DLD 75
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPevARYLPGPPYSLEEARAWLERLLADWADGGA--LPFAIEDKEDGELIGVVGLydiDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501  76 THCLE-AIFTLPAASGKGMATRIIEALKHEA-RSRGITRLTLDATPN---AQSFYLKLGFVTLRENYHHSRMAGADLRCF 150
Cdd:COG1670   86 NRSAEiGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDntaSIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                 ....*
gi 544826501 151 EMAIT 155
Cdd:COG1670  166 LYSLL 170
PRK07757 PRK07757
N-acetyltransferase;
1-130 1.65e-07

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 47.88  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   1 MTLRKATPQEAETLWNIRNQAIRHGcttsydaeviarwtpdLMPERYRQMVIEY--PFYVVEDEkGDVAATGYLDLDTHC 78
Cdd:PRK07757   2 MEIRKARLSDVKAIHALINVYAKKG----------------LMLPRSLDELYENirDFYVAEEE-GEIVGCCALHILWED 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 544826501  79 LEAIFTL---PAASGKGMATRIIEALKHEARSRGITR---LTLDatpnaQSFYLKLGF 130
Cdd:PRK07757  65 LAEIRSLavsEDYRGQGIGRMLVEACLEEARELGVKRvfaLTYQ-----PEFFEKLGF 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-116 9.40e-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: 43.80  E-value: 9.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544826501  56 FYVVEDEkGDVAATGYLDLDTHC-----LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLD 116
Cdd:cd04301    1 FLVAEDD-GEIVGFASLSPDGSGgdtayIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 67-137 1.17e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 41.55  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544826501   67 AATGYLDLDTHCLEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPN--AQSFYLKLGFVTLRENY 137
Cdd:pfam08445  12 LAAWCLRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNtpSRRLYEKLGFRKIDETY 84
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-130 4.84e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 38.06  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544826501   2 TLRKATPQEAETLWNIRNQAI--RHGCTTSYDAEVIARWTPDLMPERyrqmvieyPFYVVEDEKGDvaATGYLDLDTHCL 79
Cdd:PRK10514   3 SIRRSRHEEGERLVAIWRRSVdaTHDFLSAEDRAEIEELVRSFLPEA--------PLWVAVDERDQ--PVGFMLLSGGHM 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544826501  80 EAIFTLPAASGKGMATRIIEalkhEARSRgITRLTLDATP-NAQS--FYLKLGF 130
Cdd:PRK10514  73 EALFVDPDVRGCGVGRMLVE----HALSL-HPELTTDVNEqNEQAvgFYKKMGF 121
PTZ00330 PTZ00330
acetyltransferase; Provisional
 79-130 1.59e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 36.74  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544826501  79 LEAIFTLPAASGKGMATRIIEALKHEARSRGITRLTLDATPNAQSFYLKLGF 130
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGF 136
 
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