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Conserved domains on  [gi|15595675|ref|NP_249169|]
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N-acetyltransferase [Pseudomonas aeruginosa PAO1]

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 2.09e-33

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 115.48  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   2 TLEIRPAVPADAEQILAFIIELADYERARHEVVTDVEGIRRSLFAEGSPTR--ALMCLSEGRPIGYAvYFYSYSTWLGRN 79
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGrpVLVAEEDGEVVGFA-SLGPFRPRPAYR 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595675  80 GIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQDEWVR-YRLDGEAL 153
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 2.09e-33

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 115.48  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   2 TLEIRPAVPADAEQILAFIIELADYERARHEVVTDVEGIRRSLFAEGSPTR--ALMCLSEGRPIGYAvYFYSYSTWLGRN 79
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGrpVLVAEEDGEVVGFA-SLGPFRPRPAYR 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595675  80 GIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQDEWVR-YRLDGEAL 153
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
25-136 5.74e-15

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: 66.77  E-value: 5.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    25 DYERARHEVVTDVEGIRRSLFAEGSPTRALMCLSEGRPIGYAVYFYSYSTWlgrNGIYLEDLYVTPEYRGVGAGRRLLRE 104
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQA 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 15595675   105 LAREAVANDCGRLEWSVLDWNQPAIDFYRSIG 136
Cdd:pfam00583  84 LLEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
54-118 5.16e-08

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: 47.27  E-value: 5.16e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595675  54 LMCLSEGRPIGYAVYfysYSTWLGRNGIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLE 118
Cdd:cd04301   2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PTZ00330 PTZ00330
acetyltransferase; Provisional
3-136 4.37e-05

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 41.37  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    3 LEIRPAVPADAEQILAFIIELADYERARHEVVTDVEGIRRSlfaEGSPTRALMCLSEGRPIGYAVYFYSYS-TWLGRNGI 81
Cdd:PTZ00330   7 LELRDLEEGDLGSVLELLSHLTSAPALSQEELEQIAARRRL---AGVVTRVFVHSPTQRIVGTASLFVEPKfTRGGKCVG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15595675   82 YLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLewsVLDWNQPAIDFYRSIG 136
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKV---ILDCTEDMVAFYKKLG 135
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-153 2.09e-33

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 115.48  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   2 TLEIRPAVPADAEQILAFIIELADYERARHEVVTDVEGIRRSLFAEGSPTR--ALMCLSEGRPIGYAvYFYSYSTWLGRN 79
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGrpVLVAEEDGEVVGFA-SLGPFRPRPAYR 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595675  80 GIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQDEWVR-YRLDGEAL 153
Cdd:COG1247  80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvGFKFGRWL 154
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
3-154 2.29e-20

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 81.25  E-value: 2.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   3 LEIRPAVPADAEQILAfIIELADYERARHEVVTDVEGIRRSLfaegsptralmclsEGRPIGYAVYFYsystwLGRNGIY 82
Cdd:COG0454   1 MSIRKATPEDINFILL-IEALDAELKAMEGSLAGAEFIAVDD--------------KGEPIGFAGLRR-----LDDKVLE 60
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595675  83 LEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQDEWVRYRLDGEALR 154
Cdd:COG0454  61 LKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
64-151 1.30e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.45  E-value: 1.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675  64 GYAVYFYSYstwlGRNGIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQDEW 143
Cdd:COG0456   1 GFALLGLVD----GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76

                ....*...
gi 15595675 144 VRYRLDGE 151
Cdd:COG0456  77 PNYYGDDA 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
25-136 5.74e-15

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: 66.77  E-value: 5.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    25 DYERARHEVVTDVEGIRRSLFAEGSPTRALMCLSEGRPIGYAVYFYSYSTWlgrNGIYLEDLYVTPEYRGVGAGRRLLRE 104
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP---PVGEIEGLAVAPEYRGKGIGTALLQA 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 15595675   105 LAREAVANDCGRLEWSVLDWNQPAIDFYRSIG 136
Cdd:pfam00583  84 LLEWARERGCERIFLEVAADNLAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-153 1.95e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 63.57  E-value: 1.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   5 IRPAVPADAEQILAfIIELADYERARHEVVtdvegirRSLFAEGSPTRALMCLSEGRPIGYAVYFYSYSTWlGRNGIYLE 84
Cdd:COG3153   1 IRPATPEDAEAIAA-LLRAAFGPGREAELV-------DRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDG-EGPALLLG 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595675  85 DLYVTPEYRGVGAGRRLLRELAREAVANDCGRLewsVLDWNQPAIDFYRSIGALPQDEWVRYRLDGEAL 153
Cdd:COG3153  72 PLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
3-136 1.12e-10

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: 55.77  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   3 LEIRPAVPADAEQILAFIIELADYERARHEVVtdvegirrslfaegsptralmCLSEGRPIGYAVyFYSYSTWLGrngiY 82
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEEEIGEFWV---------------------AEEDGEIVGCAA-LHPLDEDLA----E 54
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15595675  83 LEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEwsvLDWNQPAIDFYRSIG 136
Cdd:COG1246  55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF---LLTTSAAIHFYEKLG 105
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
59-136 2.34e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.60  E-value: 2.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595675    59 EGRPIGYAVYFYSYstwlGRNGIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEwsvLDWNQPAIDFYRSIG 136
Cdd:pfam13508  11 DGKIVGFAALLPLD----DEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLE---LETTNRAAAFYEKLG 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
54-118 5.16e-08

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: 47.27  E-value: 5.16e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595675  54 LMCLSEGRPIGYAVYfysYSTWLGRNGIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLE 118
Cdd:cd04301   2 LVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
56-136 1.43e-06

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: 44.95  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    56 CLSEGRPIGYAvyfysySTwlgRNGIYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVldwNQ--PAIDFYR 133
Cdd:pfam13673  36 AFEGGQIVGVI------AL---RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV---NAspYAVPFYE 103

                  ...
gi 15595675   134 SIG 136
Cdd:pfam13673 104 KLG 106
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
51-136 3.04e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.02  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675  51 TRALMCLSEGRPIGYA-VYFYSYSTW-LGRngiyledLYVTPEYRGVGAGRRLLRELAREAVANDCGRLewsVLDWNQPA 128
Cdd:COG2153  34 ARHLLAYDDGELVATArLLPPGDGEAkIGR-------VAVLPEYRGQGLGRALMEAAIEEARERGARRI---VLSAQAHA 103

                ....*...
gi 15595675 129 IDFYRSIG 136
Cdd:COG2153 104 VGFYEKLG 111
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-136 4.33e-06

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: 44.22  E-value: 4.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675   1 MTLEIRPAVPADAEQILAFI--IELADYERARHEVVTDVEGIRRSLFAEGSPTRALMCL----SEGRPIGYaVYFYSYST 74
Cdd:COG1670   6 ERLRLRPLRPEDAEALAELLndPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAiedkEDGELIGV-VGLYDIDR 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595675  75 WLGRNGIyleDLYVTPEYRGVGAGRRLLRELAREAVAN-DCGRLEWSVLDWNQPAIDFYRSIG 136
Cdd:COG1670  85 ANRSAEI---GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLG 144
PTZ00330 PTZ00330
acetyltransferase; Provisional
3-136 4.37e-05

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 41.37  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    3 LEIRPAVPADAEQILAFIIELADYERARHEVVTDVEGIRRSlfaEGSPTRALMCLSEGRPIGYAVYFYSYS-TWLGRNGI 81
Cdd:PTZ00330   7 LELRDLEEGDLGSVLELLSHLTSAPALSQEELEQIAARRRL---AGVVTRVFVHSPTQRIVGTASLFVEPKfTRGGKCVG 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15595675   82 YLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLewsVLDWNQPAIDFYRSIG 136
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKV---ILDCTEDMVAFYKKLG 135
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
4-111 6.52e-04

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 37.97  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    4 EIRPAVPADAEQILAFIIELADYERARHEVvtdVEGIRRSLfaEGSPTRALMCLSEGRPIG----YAVYFYSYSTWLGRn 79
Cdd:PRK10146   5 ELRPATQYDTDAVYALICELKQAEFDHQAF---RVGFNANL--RDPNMRYHLALLDGEVVGmiglHLQFHLHHVNWIGE- 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15595675   80 giyLEDLYVTPEYRGVGAGRRLL---RELAREAVA 111
Cdd:PRK10146  79 ---IQELVVMPQARGLNVGSKLLawaEEEARQAGA 110
PRK03624 PRK03624
putative acetyltransferase; Provisional
1-141 1.62e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.83  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595675    1 MTLEIRPAVPADAEQILAfIIELADYERARHEVVTDVEGIRR---SLFaegsptraLMCLSEGRPIGYAVYFYSystwlG 77
Cdd:PRK03624   1 DAMEIRVFRQADFEAVIA-LWERCDLTRPWNDPEMDIERKLNhdpSLF--------LVAEVGGEVVGTVMGGYD-----G 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595675   78 RNGiYLEDLYVTPEYRGVGAGRRLLRELAREAVANDCGRLEWSVLDWNQPAIDFYRSIGALPQD 141
Cdd:PRK03624  67 HRG-WAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQD 129
 
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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