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Conserved domains on  [gi|851903916|ref|WP_048212793|]
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MULTISPECIES: GNAT family N-acetyltransferase [Citrobacter]

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];
5-144 5.97e-18

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.51  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   5 LRATTLADTAALPAIERSAsqrflqipelaWIADDQIISVAQHQAFAATGLSWLAQADEHPVGFLVAETLDSS-----LF 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDgegpaLL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  80 IAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFrdvPWNAPLYARLGFELLADETLPA 144
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTL 131
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-144 5.97e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.51  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   5 LRATTLADTAALPAIERSAsqrflqipelaWIADDQIISVAQHQAFAATGLSWLAQADEHPVGFLVAETLDSS-----LF 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDgegpaLL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  80 IAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFrdvPWNAPLYARLGFELLADETLPA 144
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTL 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-135 1.98e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.48  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   57 WLAQADEHPVGFLVAETLDSSLFIAELSL--HQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDvpwNAPLYARLGF 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLavHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYEKLGF 82


                  .
gi 851903916  135 E 135
Cdd:pfam13508  83 E 83
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-117 2.22e-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: 53.82  E-value: 2.22e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  56 SWLAQADEHPVGFLVAETLDSS---LFIAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLT 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGgdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK07757 PRK07757
N-acetyltransferase;
57-145 1.23e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 42.87  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916  57 WLAQADEHPVGF----LVAETLdsslfiAE---LSLHQAWQGKGIGRRLLNYVAEQARAKG-YTSLTLTtfrdvpWNAPL 128
Cdd:PRK07757  44 YVAEEEGEIVGCcalhILWEDL------AEirsLAVSEDYRGQGIGRMLVEACLEEARELGvKRVFALT------YQPEF 111

                         90
                 ....*....|....*..
gi 851903916 129 YARLGFELLADETLPAK 145
Cdd:PRK07757 112 FEKLGFREVDKEALPQK 128
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-144 5.97e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 75.51  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   5 LRATTLADTAALPAIERSAsqrflqipelaWIADDQIISVAQHQAFAATGLSWLAQADEHPVGFLVAETLDSS-----LF 79
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA-----------FGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDgegpaLL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  80 IAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFrdvPWNAPLYARLGFELLADETLPA 144
Cdd:COG3153   70 LGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGD---PSLLPFYERFGFRPAGELGLTL 131
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 57-152 2.40e-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: 73.87  E-value: 2.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916  57 WLAQADEHPVGFLVAETLDSSL-FIAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDVpwnAPLYARLGFE 135
Cdd:COG1246   31 WVAEEDGEIVGCAALHPLDEDLaELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAA---IHFYEKLGFE 107

                         90
                 ....*....|....*..
gi 851903916 136 LLADETLPAKLRQKREE 152
Cdd:COG1246  108 EIDKEDLPYAKVWQRDS 124
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 3-141 7.13e-17

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 72.78  E-value: 7.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   3 ITLRATTLADTAALPAIERSAsqrflqiPELAwiadDQIISVAQHQAFAATglswlaqADEHPVGFLVAETLDS-SLFIA 81
Cdd:COG0454    1 MSIRKATPEDINFILLIEALD-------AELK----AMEGSLAGAEFIAVD-------DKGEPIGFAGLRRLDDkVLELK 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916  82 ELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDVPWNAPLYARLGFELLADET 141
Cdd:COG0454   63 RLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYV 122
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
2-138 6.35e-16

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.79  E-value: 6.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   2 NITLRATTLADTAALPAIERSAsqrflqIPELAWIADDQIISVAQHQAFAATGLS-----WLAQADEHPVGFLVAE---T 73
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEA------IAEGTATFETEPPSEEEREAWFAAILApgrpvLVAEEDGEVVGFASLGpfrP 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916  74 LDSSLFIAELSL--HQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFrdvPWNAP---LYARLGFELLA 138
Cdd:COG1247   75 RPAYRGTAEESIyvDPDARGRGIGRALLEALIERARARGYRRLVAVVL---ADNEAsiaLYEKLGFEEVG 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-135 1.98e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.48  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   57 WLAQADEHPVGFLVAETLDSSLFIAELSL--HQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDvpwNAPLYARLGF 134
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELRLavHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYEKLGF 82


                  .
gi 851903916  135 E 135
Cdd:pfam13508  83 E 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-134 9.24e-14

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: 64.08  E-value: 9.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   25 QRFLQIPELAWIADDQIISVAQHQAFA--ATGLSWLAQADEHPVGFLVAETLDSS---LFIAELSLHQAWQGKGIGRRLL 99
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDedASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 851903916  100 NYVAEQARAKGYTSLTLTTFRDVPWNAPLYARLGF 134
Cdd:pfam00583  82 QALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 67-135 3.39e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.98  E-value: 3.39e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851903916  67 GFLVAETLDSS--LFIAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDVPWNAPLYARLGFE 135
Cdd:COG0456    1 GFALLGLVDGGdeAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFE 71
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-117 2.22e-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: 53.82  E-value: 2.22e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  56 SWLAQADEHPVGFLVAETLDSS---LFIAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLT 117
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGgdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
86-139 2.12e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.14  E-value: 2.12e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851903916  86 HQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDVPWNAPLYARLGFELLAD 139
Cdd:COG3393   24 HPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGE 77
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-141 1.17e-07

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: 48.04  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   57 WLAQADEHPVGflVAETLDSSlFIAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTfrdvpwNA-----PLYAR 131
Cdd:pfam13673  34 FVAFEGGQIVG--VIALRDRG-HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTV------NAspyavPFYEK 104

                          90
                  ....*....|
gi 851903916  132 LGFELLADET 141
Cdd:pfam13673 105 LGFRATGPEQ 114
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
86-142 9.63e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.86  E-value: 9.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851903916  86 HQAWQGKGIGRRLLNYVAEQARAKGYTSLTLttfrdvpwNA-----PLYARLGFELLADETL 142
Cdd:COG2153   67 LPEYRGQGLGRALMEAAIEEARERGARRIVL--------SAqahavGFYEKLGFVPVGEEFL 120
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-136 1.02e-05

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: 43.45  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916   1 MNITLRATTLADTAALPAIERSASQ-RFLQIPELAWIADDQIISVAQHQAFAATGLSWLA--QADEHPVGFLVAETLDSS 77
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVaRYLPGPPYSLEEARAWLERLLADWADGGALPFAIedKEDGELIGVVGLYDIDRA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851903916  78 LFIAEL--SLHQAWQGKGIGRRLLNYVAEQARAK-GYTSLTLTTFrdvPWNAP---LYARLGFEL 136
Cdd:COG1670   86 NRSAEIgyWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVD---PDNTAsirVLEKLGFRL 147
PRK07757 PRK07757
N-acetyltransferase;
57-145 1.23e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 42.87  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851903916  57 WLAQADEHPVGF----LVAETLdsslfiAE---LSLHQAWQGKGIGRRLLNYVAEQARAKG-YTSLTLTtfrdvpWNAPL 128
Cdd:PRK07757  44 YVAEEEGEIVGCcalhILWEDL------AEirsLAVSEDYRGQGIGRMLVEACLEEARELGvKRVFALT------YQPEF 111

                         90
                 ....*....|....*..
gi 851903916 129 YARLGFELLADETLPAK 145
Cdd:PRK07757 112 FEKLGFREVDKEALPQK 128
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 80-149 1.82e-05

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 43.60  E-value: 1.82e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851903916  80 IAELSLHQAWQGKGIGRRLLNYVAEQARAKGYTSL-TLTTfRDVPWnaplYARLGFELLADETLPAKLRQK 149
Cdd:PRK05279 362 MACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRLfVLTT-RTAHW----FLERGFVPVDVDDLPEAKRQL 427
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 86-111 9.65e-04

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 38.66  E-value: 9.65e-04
                         10        20
                 ....*....|....*....|....*.
gi 851903916  86 HQAWQGKGIGRRLLNYVAEQARAKGY 111
Cdd:COG1444  494 HPALQRRGLGSRLLAEIREEAKEEGL 519
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 62-134 1.15e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.22  E-value: 1.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851903916  62 DEHPVGFLVAET-LD-SSLF-IAelsLHQAWQGKGIGRRLLNYVAEQARAKGYTSLTLTTFRDvpwNAP---LYARLGF 134
Cdd:PRK09491  48 NGQMAAFAITQVvLDeATLFnIA---VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRAS---NAAaiaLYESLGF 120
 
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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