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Conserved domains on  [gi|46048439|ref|NP_036323|]
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N-alpha-acetyltransferase 80 isoform 1 [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
90-211 8.63e-16

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 72.81  E-value: 8.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439  90 RPELLDACADLINDQWPRSRTSRLHSLGQSSDAFPLCLMLlsphptlEAAPVVVGHARLSRV--LNQPQSLLVETVVVAR 167
Cdd:COG3153   5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVA-------EDDGEIVGHVALSPVdiDGEGPALLLGPLAVDP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 46048439 168 ALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQVH-FYTHLGYQ 211
Cdd:COG3153  78 EYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLpFYERFGFR 122
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
90-211 8.63e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 72.81  E-value: 8.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439  90 RPELLDACADLINDQWPRSRTSRLHSLGQSSDAFPLCLMLlsphptlEAAPVVVGHARLSRV--LNQPQSLLVETVVVAR 167
Cdd:COG3153   5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVA-------EDDGEIVGHVALSPVdiDGEGPALLLGPLAVDP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 46048439 168 ALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQVH-FYTHLGYQ 211
Cdd:COG3153  78 EYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLpFYERFGFR 122
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 141-210 8.83e-13

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: 63.69  E-value: 8.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048439   141 VVVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGY 210
Cdd:pfam00583  43 ELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADnlaaIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 142-197 7.28e-10

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: 54.20  E-value: 7.28e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048439 142 VVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLT 197
Cdd:cd04301  10 IVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 165-228 8.37e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 47.62  E-value: 8.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46048439  165 VARALRGRGFGRRLMEGLEVFARARGFRKLHL---TTHDQV-HFYTHLGYQlgepVQGLVFTSRRLPA 228
Cdd:PRK03624  76 VHPDFRGRGIGRALVARLEKKLIARGCPKINLqvrEDNDAVlGFYEALGYE----EQDRISLGKRLIE 139
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
90-211 8.63e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 72.81  E-value: 8.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439  90 RPELLDACADLINDQWPRSRTSRLHSLGQSSDAFPLCLMLlsphptlEAAPVVVGHARLSRV--LNQPQSLLVETVVVAR 167
Cdd:COG3153   5 TPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVA-------EDDGEIVGHVALSPVdiDGEGPALLLGPLAVDP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 46048439 168 ALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQVH-FYTHLGYQ 211
Cdd:COG3153  78 EYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLpFYERFGFR 122
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 142-215 2.05e-13

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: 66.17  E-value: 2.05e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46048439 142 VVGHARLsrVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHL-TTHDQVHFYTHLGYQLGEP 215
Cdd:COG1246  39 IVGCAAL--HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLlTTSAAIHFYEKLGFEEIDK 111
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 141-210 8.83e-13

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: 63.69  E-value: 8.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048439   141 VVVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGY 210
Cdd:pfam00583  43 ELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADnlaaIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 142-211 4.45e-12

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 62.38  E-value: 4.45e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048439 142 VVGHARLSRvLNQPqSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGYQ 211
Cdd:COG0454  45 PIGFAGLRR-LDDK-VLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGnpaaIRFYERLGFK 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
90-211 5.02e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 63.09  E-value: 5.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439  90 RPELLDACADLINDqWPRSRTSRLHSLGQSSDAFP--LCLMLLSPHPTL--EAAPVVVGHARLSRVLNQP--QSLLVETV 163
Cdd:COG1247   8 TPEDAPAIAAIYNE-AIAEGTATFETEPPSEEEREawFAAILAPGRPVLvaEEDGEVVGFASLGPFRPRPayRGTAEESI 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 46048439 164 VVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGYQ 211
Cdd:COG1247  87 YVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneasIALYEKLGFE 138
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 144-211 3.61e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.51  E-value: 3.61e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46048439 144 GHARLSRVLnQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGYQ 211
Cdd:COG0456   1 GFALLGLVD-GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDneaaIALYEKLGFE 71
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 142-211 1.85e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.31  E-value: 1.85e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46048439   142 VVGHARLSRVLNQPQSLLVEtVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ-VHFYTHLGYQ 211
Cdd:pfam13508  14 IVGFAALLPLDDEGALAELR-LAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRaAAFYEKLGFE 83
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
142-215 2.12e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 57.50  E-value: 2.12e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46048439 142 VVGHARLsrVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLttHDQVH---FYTHLGYQ-LGEP 215
Cdd:COG2153  45 LVATARL--LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVL--SAQAHavgFYEKLGFVpVGEE 118
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 142-197 7.28e-10

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: 54.20  E-value: 7.28e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048439 142 VVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLT 197
Cdd:cd04301  10 IVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
142-211 4.03e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.91  E-value: 4.03e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048439 142 VVGHARLSRVLnqPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQ----VHFYTHLGYQ 211
Cdd:COG3393   2 LVAMAGVRAES--PGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADnpaaRRLYERLGFR 73
PRK03624 PRK03624
putative acetyltransferase; Provisional
 165-228 8.37e-07

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 47.62  E-value: 8.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46048439  165 VARALRGRGFGRRLMEGLEVFARARGFRKLHL---TTHDQV-HFYTHLGYQlgepVQGLVFTSRRLPA 228
Cdd:PRK03624  76 VHPDFRGRGIGRALVARLEKKLIARGCPKINLqvrEDNDAVlGFYEALGYE----EQDRISLGKRLIE 139
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 143-226 1.44e-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: 46.50  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439   143 VGHARLSRvlNQPQSLLVetvvVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHDQVH---FYTHLGYQLGEPVQ-- 217
Cdd:pfam13673  43 VGVIALRD--RGHISLLF----VDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPYavpFYEKLGFRATGPEQef 116

                          90
                  ....*....|
gi 46048439   218 -GLVFTSRRL 226
Cdd:pfam13673 117 nGIRFVPMEK 126
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
155-194 3.46e-04

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 40.69  E-value: 3.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 46048439 155 PQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRKL 194
Cdd:COG3818  82 DNFLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRV 121
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 160-210 6.85e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 39.30  E-value: 6.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46048439  160 VETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHL-TTHDQVHFYTHLGY 210
Cdd:PLN02706  88 IEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILdCSEENKAFYEKCGY 139
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
163-192 2.32e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 36.67  E-value: 2.32e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 46048439 163 VVVARALRGRGFGRRLMEGLEVFARARGFR 192
Cdd:COG2388  38 TEVPPALRGQGIASALVEAALDDARERGLK 67
PTZ00330 PTZ00330
acetyltransferase; Provisional
 160-214 2.74e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 37.51  E-value: 2.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048439  160 VETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHL-TTHDQVHFYTHLGYQLGE 214
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILdCTEDMVAFYKKLGFRACE 140
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 164-192 3.47e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 35.57  E-value: 3.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 46048439   164 VVARALRGRGFGRRLMEGLEVFARARGFR 192
Cdd:pfam14542  30 EVPPALRGQGIASKLVKAALDDAREEGLK 58
PRK07922 PRK07922
amino-acid N-acetyltransferase;
160-221 4.44e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 37.21  E-value: 4.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048439  160 VETVVVARALRGRGFGRRLMEGLEVFARARGFRKLHLTTHdQVHFYTHLGYQL--GEPVQGLVF 221
Cdd:PRK07922  73 IRTVAVDPAARGRGVGHAIVERLLDVARELGLSRVFVLTF-EVEFFARHGFVEidGTPVTPEVY 135
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 82-212 7.45e-03

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: 36.52  E-value: 7.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439  82 LTLEPVhrRPELLDACADLIND-----QWPRSRTS---------RLHSLGQSSDAFPLCLmllsphpTLEAAPVVVGHAR 147
Cdd:COG1670   8 LRLRPL--RPEDAEALAELLNDpevarYLPGPPYSleearawleRLLADWADGGALPFAI-------EDKEDGELIGVVG 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048439 148 LSRVLNQPQSLLVeTVVVARALRGRGFGRRLMEGLEVFA-RARGFRKLHLTTHDQ----VHFYTHLGYQL 212
Cdd:COG1670  79 LYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDntasIRVLEKLGFRL 147
 
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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