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Conserved domains on  [gi|1440323446|emb|STW45821|]
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N-acetyltransferase GCN5 [Klebsiella variicola]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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

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List of domain hits

 Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 57-139 6.20e-11

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: 56.15  E-value: 6.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  57 GRIVGDGAINFD------IVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFESVRPESEGM 130
Cdd:COG1246    37 GEIVGCAALHPLdedlaeLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPY 116


                  ....*....
gi 1440323446 131 ARVWRTRSR 139
Cdd:COG1246   117 AKVWQRDSV 125
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 57-139 6.20e-11

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: 56.15  E-value: 6.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  57 GRIVGDGAINFD------IVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFESVRPESEGM 130
Cdd:COG1246    37 GEIVGCAALHPLdedlaeLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPY 116


                  ....*....
gi 1440323446 131 ARVWRTRSR 139
Cdd:COG1246   117 AKVWQRDSV 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-121 2.48e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 2.48e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440323446  57 GRIVG-------DGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFE 121
Cdd:pfam13508  12 GKIVGfaallplDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 55-123 8.18e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.31  E-value: 8.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323446  55 AMGRIVGDGAINFDIvdvAVDPAHQGKGLGRLVMEKLIAWLDANAFdgayVTLVADVPE-------LYAKFGFESV 123
Cdd:PRK09491   55 AITQVVLDEATLFNI---AVDPDYQRQGLGRALLEHLIDELEKRGV----ATLWLEVRAsnaaaiaLYESLGFNEV 123
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 13-123 5.74e-06

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.70  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  13 SAEAFCHlrvaagmsPRPLEGARAGL--PHSCYGVhilwqetPIAMGRIVGDGAINFD-----IVDVAVDPAHQGKGLGR 85
Cdd:TIGR01575   9 EAAAFAF--------PWTEAQFAEELanYHLCYLL-------ARIGGKVVGYAGVQIVldeahILNIAVKPEYQGQGIGR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1440323446  86 LVMEKLIAWLDANafDGAYVTL---VADVP--ELYAKFGFESV 123
Cdd:TIGR01575  74 ALLRELIDEAKGR--GVNEIFLevrVSNIAaqALYKKLGFNEI 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-106 1.28e-05

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: 40.34  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1440323446  55 AMGRIVGDGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVT 106
Cdd:cd04301    14 ASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 57-139 6.20e-11

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: 56.15  E-value: 6.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  57 GRIVGDGAINFD------IVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFESVRPESEGM 130
Cdd:COG1246    37 GEIVGCAALHPLdedlaeLRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPY 116


                  ....*....
gi 1440323446 131 ARVWRTRSR 139
Cdd:COG1246   117 AKVWQRDSV 125
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-121 2.48e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 2.48e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440323446  57 GRIVG-------DGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFE 121
Cdd:pfam13508  12 GKIVGfaallplDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
69-130 4.99e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.94  E-value: 4.99e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1440323446  69 IVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPELYAKFGFESVRPESEGM 130
Cdd:COG3153    70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTL 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-124 1.49e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 51.58  E-value: 1.49e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1440323446  69 IVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVP---ELYAKFGFESVR 124
Cdd:COG0456    16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEaaiALYEKLGFEEVG 74
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-128 2.37e-09

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: 51.89  E-value: 2.37e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323446  57 GRIVGDGAI--NFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVP--ELYAKFGFESVRPESE 128
Cdd:pfam13673  40 GQIVGVIALrdRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPYavPFYEKLGFRATGPEQE 115
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 34-124 2.59e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.98  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  34 ARAGLPHSCYGVHILWQETPIAMG--RIVGDGAINFDivDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADV 111
Cdd:COG0454    26 AMEGSLAGAEFIAVDDKGEPIGFAglRRLDDKVLELK--RLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGN 103

                          90
                  ....*....|....*.
gi 1440323446 112 PE---LYAKFGFESVR 124
Cdd:COG0454   104 PAairFYERLGFKEIE 119
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-126 3.78e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 51.34  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  45 VHILW--QETPIAMGRIVGDGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANafDGAYVTLVADVP--ELYAKFGF 120
Cdd:COG2153    35 RHLLAydDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARER--GARRIVLSAQAHavGFYEKLGF 112


                  ....*.
gi 1440323446 121 ESVRPE 126
Cdd:COG2153   113 VPVGEE 118
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 55-120 9.36e-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: 50.21  E-value: 9.36e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440323446  55 AMGRIVGDGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVP---ELYAKFGF 120
Cdd:pfam00583  48 ASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLaaiALYEKLGF 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
53-124 1.20e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.14  E-value: 1.20e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440323446  53 PIAMGRIVGDGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVTLVADVPE---LYAKFGFESVR 124
Cdd:COG3393     2 LVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAarrLYERLGFRPVG 76
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
70-135 3.00e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.61  E-value: 3.00e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440323446  70 VDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDgayvTLVADVPE-------LYAKFGFESV--RPESEGMARVWR 135
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEALIERARARGYR----RLVAVVLAdneasiaLYEKLGFEEVgtLPEVGFKFGRWL 154
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 55-123 8.18e-07

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.31  E-value: 8.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323446  55 AMGRIVGDGAINFDIvdvAVDPAHQGKGLGRLVMEKLIAWLDANAFdgayVTLVADVPE-------LYAKFGFESV 123
Cdd:PRK09491   55 AITQVVLDEATLFNI---AVDPDYQRQGLGRALLEHLIDELEKRGV----ATLWLEVRAsnaaaiaLYESLGFNEV 123
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 13-123 5.74e-06

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.70  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  13 SAEAFCHlrvaagmsPRPLEGARAGL--PHSCYGVhilwqetPIAMGRIVGDGAINFD-----IVDVAVDPAHQGKGLGR 85
Cdd:TIGR01575   9 EAAAFAF--------PWTEAQFAEELanYHLCYLL-------ARIGGKVVGYAGVQIVldeahILNIAVKPEYQGQGIGR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1440323446  86 LVMEKLIAWLDANafDGAYVTL---VADVP--ELYAKFGFESV 123
Cdd:TIGR01575  74 ALLRELIDEAKGR--GVNEIFLevrVSNIAaqALYKKLGFNEI 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-106 1.28e-05

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: 40.34  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1440323446  55 AMGRIVGDGAINFDIVDVAVDPAHQGKGLGRLVMEKLIAWLDANAFDGAYVT 106
Cdd:cd04301    14 ASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
57-127 4.80e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.87  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323446  57 GRIVGDGAINF------DIVDVAVDPAHQGKGLGRLVMEKLIAwlDANAFDgayvtlVADV------PELYAKFGFESVR 124
Cdd:PRK07757   50 GEIVGCCALHIlwedlaEIRSLAVSEDYRGQGIGRMLVEACLE--EARELG------VKRVfaltyqPEFFEKLGFREVD 121


                  ...
gi 1440323446 125 PES 127
Cdd:PRK07757  122 KEA 124
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 57-120 7.72e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 37.38  E-value: 7.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440323446  57 GRIVGDGAINFD------------IVDVAVDPAHQGKGLGRLVMEKLIawlDANAFDGAYVTLVADVPEL---YAKFGF 120
Cdd:PLN02706   64 GRIIATGSVFVErkfirncgkvghIEDVVVDSAARGKGLGKKIIEALT---EHARSAGCYKVILDCSEENkafYEKCGY 139
PRK07922 PRK07922
amino-acid N-acetyltransferase;
57-93 1.58e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 36.82  E-value: 1.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1440323446  57 GRIVGDGAINF------DIVDVAVDPAHQGKGLGRLVMEKLIA 93
Cdd:PRK07922   55 GEVVGCGALHVmwedlaEIRTVAVDPAARGRGVGHAIVERLLD 97
Eis COG4552
Predicted acetyltransferase [General function prediction only];
69-121 9.88e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 34.87  E-value: 9.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440323446  69 IVDVAVDPAHQGKGLGRLVMEKLIAwlDANAFDGAYVTLVADVPELYAKFGFE 121
Cdd:COG4552    75 ITGVAVAPEHRRRGVARALLREALA--ELRERGQPLSALYPFEPGFYRRFGYE 125
 
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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