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Conserved domains on  [gi|490239306|ref|WP_004137582|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

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

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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];
1-148 9.93e-22

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.82  E-value: 9.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   1 MFKIRIAGPEDAALLNEMANASYRHHFAHLWHNADELEhylqqeySMAALAPSLADPQCCWLIAEAA-RPVGFAKYacGQ 79
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEE-------EREAWFAAILAPGRPVLVAEEDgEVVGFASL--GP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  80 NIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:COG1247   72 FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-148 9.93e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.82  E-value: 9.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   1 MFKIRIAGPEDAALLNEMANASYRHHFAHLWHNADELEhylqqeySMAALAPSLADPQCCWLIAEAA-RPVGFAKYacGQ 79
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEE-------EREAWFAAILAPGRPVLVAEEDgEVVGFASL--GP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  80 NIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:COG1247   72 FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 56-145 5.14e-11

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: 56.76  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   56 DPQCCWLIAEAARPVGFAKYacgqNIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTS 135
Cdd:pfam00583  31 ASEGFFVAEEDGELVGFASL----SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 490239306  136 ARRFYERQGM 145
Cdd:pfam00583 107 AIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 34-149 1.16e-09

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: 53.49  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   34 ADELEHYLQQEYSM----AALAPSLADPQCCWLIAEAARPVgfAKYACGQNIHPEGPsgtlLHKLYLLPDATGHRYGEQI 109
Cdd:TIGR01575   2 LKAVLEIEAAAFAFpwteAQFAEELANYHLCYLLARIGGKV--VGYAGVQIVLDEAH----ILNIAVKPEYQGQGIGRAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490239306  110 FRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHVK 149
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-128 7.38e-06

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: 41.88  E-value: 7.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  60 CWLIAEAARPVGFAKYAcgqnIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLE 128
Cdd:cd04301    1 FLVAEDDGEIVGFASLS----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 98-148 3.21e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.76  E-value: 3.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490239306  98 PDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:PRK09491  73 PDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEV 123
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-148 9.93e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 85.82  E-value: 9.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   1 MFKIRIAGPEDAALLNEMANASYRHHFAHLWHNADELEhylqqeySMAALAPSLADPQCCWLIAEAA-RPVGFAKYacGQ 79
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEE-------EREAWFAAILAPGRPVLVAEEDgEVVGFASL--GP 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  80 NIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:COG1247   72 FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 2-154 2.39e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 63.53  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   2 FKIRIAGPEDAallnemanasyrhhfaHLWHNADELEHYLQQEYSmaalapslADPQCCWLIAEAA-RPVGFAkyacgqN 80
Cdd:COG0454    1 MSIRKATPEDI----------------NFILLIEALDAELKAMEG--------SLAGAEFIAVDDKgEPIGFA------G 50

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490239306  81 IHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHVKDVAFH 154
Cdd:COG0454   51 LRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 91-148 3.41e-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: 3.41e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490239306  91 LHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEV 73
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 56-145 5.14e-11

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: 56.76  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   56 DPQCCWLIAEAARPVGFAKYacgqNIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTS 135
Cdd:pfam00583  31 ASEGFFVAEEDGELVGFASL----SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLA 106

                          90
                  ....*....|
gi 490239306  136 ARRFYERQGM 145
Cdd:pfam00583 107 AIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 56-149 5.97e-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: 54.23  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306  56 DPQCCWLIAEAARPVGFAkyacgqNIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEvlaVNTS 135
Cdd:COG1246   26 EIGEFWVAEEDGEIVGCA------ALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSA 96

                         90
                 ....*....|....
gi 490239306 136 ARRFYERQGMQHVK 149
Cdd:COG1246   97 AIHFYEKLGFEEID 110
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 34-149 1.16e-09

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: 53.49  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   34 ADELEHYLQQEYSM----AALAPSLADPQCCWLIAEAARPVgfAKYACGQNIHPEGPsgtlLHKLYLLPDATGHRYGEQI 109
Cdd:TIGR01575   2 LKAVLEIEAAAFAFpwteAQFAEELANYHLCYLLARIGGKV--VGYAGVQIVLDEAH----ILNIAVKPEYQGQGIGRAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490239306  110 FRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHVK 149
Cdd:TIGR01575  76 LRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-154 1.25e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.55  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   4 IRIAGPEDAALLNEMANASYRHHFAHlwhnadelehylqqeYSMAALAPSLADPQCcwLIAEAA-RPVGfakYACGQNIH 82
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREA---------------ELVDRLREDPAAGLS--LVAEDDgEIVG---HVALSPVD 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490239306  83 PEGPSGTL-LHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLwleVLAVNTSARRFYERQGMQHVKDVAFH 154
Cdd:COG3153   61 IDGEGPALlLGPLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAGELGLT 130
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
68-153 4.67e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 50.68  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306  68 RPVGFAKyacgqnIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQH 147
Cdd:COG3393    1 ELVAMAG------VRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRP 74


                 ....*.
gi 490239306 148 VKDVAF 153
Cdd:COG3393   75 VGEYAT 80
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-148 4.65e-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: 50.00  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   1 MFKIRIAGPEDAALLNEMAN-ASYRHHFAHLWHNADELEHYLQQeysmaALAPSLADPQCCWLIAEAA--RPVGFAKYac 77
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNdPEVARYLPGPPYSLEEARAWLER-----LLADWADGGALPFAIEDKEdgELIGVVGL-- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239306  78 gQNIHPEGPSGTLlhKLYLLPDATGHRYGEQIFRAVETRAKEK-GERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:COG1670   80 -YDIDRANRSAEI--GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-144 9.80e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 44.75  E-value: 9.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239306   56 DPQCCWLIAEAARPVGFAKYACGQNIHpegpsGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGerwLWLEVLAVNTS 135
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEG-----ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGG---IKLLELETTNR 72


                  ....*....
gi 490239306  136 ARRFYERQG 144
Cdd:pfam13508  73 AAAFYEKLG 81
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 60-128 7.38e-06

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: 41.88  E-value: 7.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  60 CWLIAEAARPVGFAKYAcgqnIHPEGPSGTLLHKLYLLPDATGHRYGEQIFRAVETRAKEKGERWLWLE 128
Cdd:cd04301    1 FLVAEDDGEIVGFASLS----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 98-148 3.21e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 38.76  E-value: 3.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490239306  98 PDATGHRYGEQIFRAVETRAKEKGERWLWLEVLAVNTSARRFYERQGMQHV 148
Cdd:PRK09491  73 PDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEV 123
PRK10562 PRK10562
putative acetyltransferase; Provisional
 94-162 1.32e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 37.35  E-value: 1.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239306  94 LYLLPDATGHRYGEQIFRAVETRAkekgeRWLWLEVLAVNTSARRFYERQGMqHVKDVAFHSATQESTL 162
Cdd:PRK10562  74 LFVAPKAVRRGIGKALMQHVQQRY-----PHLSLEVYQKNQRAVNFYHAQGF-RIVDSAWQEETQHPTW 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.
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