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Conserved domains on  [gi|2320504014|ref|WP_263836855|]
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N-acetyltransferase [Vibrio natriegens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-145 1.02e-13

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.75  E-value: 1.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2320504014  72 LIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGEMDT 145
Cdd:COG0456     5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-145 1.02e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.75  E-value: 1.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2320504014  72 LIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGEMDT 145
Cdd:COG0456     5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 42-137 9.92e-10

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: 52.91  E-value: 9.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  42 FERLTSWPDAGFYHAINKDETIGQIEFRkdlIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRY 121
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLS---IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEV 100

                          90
                  ....*....|....*.
gi 2320504014 122 LPANSQGVAFYRKHGW 137
Cdd:pfam00583 101 AADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-119 3.39e-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: 47.66  E-value: 3.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320504014  53 FYHAINKDETIGQIEFRkdlIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQL 119
Cdd:cd04301     1 FLVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 12-142 1.46e-05

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: 42.32  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  12 LDLCIAFRKDAYAVSYgsldgfnieeTAAWFERLTSWPDAGFYHAINKDETIGQIEFRKDLidDEGvkygYINLFYLKPE 91
Cdd:TIGR01575   2 LKAVLEIEAAAFAFPW----------TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVL--DEA----HILNIAVKPE 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2320504014  92 FRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGE 142
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 72-145 1.02e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 62.75  E-value: 1.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2320504014  72 LIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGEMDT 145
Cdd:COG0456     5 LGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
31-144 7.82e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.63  E-value: 7.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  31 DGFNIEETAAWFERLTSWPDAGFYH-AINKDETIGQIEFRKDLIDDEGvKYGYINLFYLKPEFRGQGLGGELQDFIFSQL 109
Cdd:COG3153    18 AAFGPGREAELVDRLREDPAAGLSLvAEDDGEIVGHVALSPVDIDGEG-PALLLGPLAVDPEYRGQGIGRALMRAALEAA 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2320504014 110 KSAKCQYVQLRylpANSQGVAFYRKHGWKDVGEMD 144
Cdd:COG3153    97 RERGARAVVLL---GDPSLLPFYERFGFRPAGELG 128
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
36-149 1.39e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 56.16  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  36 EETAAWFERLTSwPDAGFYHAINKDETIGQIEFRkDLIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQ 115
Cdd:COG1247    38 EEREAWFAAILA-PGRPVLVAEEDGEVVGFASLG-PFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYR 115

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2320504014 116 YVQLRYLPANSQGVAFYRKHGWKDVGEMDTRGQL 149
Cdd:COG1247   116 RLVAVVLADNEASIALYEKLGFEEVGTLPEVGFK 149
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 42-137 9.92e-10

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: 52.91  E-value: 9.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  42 FERLTSWPDAGFYHAINKDETIGQIEFRkdlIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRY 121
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELVGFASLS---IIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEV 100

                          90
                  ....*....|....*.
gi 2320504014 122 LPANSQGVAFYRKHGW 137
Cdd:pfam00583 101 AADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 12-144 1.46e-09

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: 53.85  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  12 LDLCIAFRKDAYAVSYGSLDGFNIEETAAWFERLTS-WPDAGFYH-AI---NKDETIGQIEFRKDLIDDEGVKYGYinlf 86
Cdd:COG1670    18 AEALAELLNDPEVARYLPGPPYSLEEARAWLERLLAdWADGGALPfAIedkEDGELIGVVGLYDIDRANRSAEIGY---- 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2320504014  87 YLKPEFRGQGLGGE----LQDFIFSQLksaKCQYVQLRYLPANSQGVAFYRKHGWKDVGEMD 144
Cdd:COG1670    94 WLAPAYWGKGYATEalraLLDYAFEEL---GLHRVEAEVDPDNTASIRVLEKLGFRLEGTLR 152
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 59-143 9.63e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.82  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  59 KDETIGQIEFRKdlIDDEGvkyGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWK 138
Cdd:COG0454    42 KGEPIGFAGLRR--LDDKV---LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFK 116


                  ....*
gi 2320504014 139 DVGEM 143
Cdd:COG0454   117 EIERY 121
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 53-143 1.06e-08

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: 50.73  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  53 FYHAINKDETIGQIEFRKDliddegvkyGYINLFYLKPEFRGQGLGGELQDFIfsqLKSAKCQYVQLRYLPANSQ--GVA 130
Cdd:pfam13673  33 FFVAFEGGQIVGVIALRDR---------GHISLLFVDPDYQGQGIGKALLEAV---EDYAEKDGIKLSELTVNASpyAVP 100

                          90
                  ....*....|...
gi 2320504014 131 FYRKHGWKDVGEM 143
Cdd:pfam13673 101 FYEKLGFRATGPE 113
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-138 1.98e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.99  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  49 PDAGFYHAINKDETIGQIEFRkdlIDDEGVKYGYINLfYLKPEFRGQGLGGELQDFIfsqLKSAKCQYVQLRYLPANSQG 128
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALL---PLDDEGALAELRL-AVHPEYRGQGIGRALLEAA---EAAAKEGGIKLLELETTNRA 73

                          90
                  ....*....|
gi 2320504014 129 VAFYRKHGWK 138
Cdd:pfam13508  74 AAFYEKLGFE 83
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
80-145 2.37e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 2.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320504014  80 YGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGEMDT 145
Cdd:COG3393    15 VAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-119 3.39e-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: 47.66  E-value: 3.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2320504014  53 FYHAINKDETIGQIEFRkdlIDDEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVQL 119
Cdd:cd04301     1 FLVAEDDGEIVGFASLS---PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 79-144 1.26e-07

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: 47.68  E-value: 1.26e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320504014  79 KYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVqlrYLPANSQGVAFYRKHGWKDVGEMD 144
Cdd:COG1246    51 DLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRL---FLLTTSAAIHFYEKLGFEEIDKED 113
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 12-142 1.46e-05

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: 42.32  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  12 LDLCIAFRKDAYAVSYgsldgfnieeTAAWFERLTSWPDAGFYHAINKDETIGQIEFRKDLidDEGvkygYINLFYLKPE 91
Cdd:TIGR01575   2 LKAVLEIEAAAFAFPW----------TEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVL--DEA----HILNIAVKPE 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2320504014  92 FRGQGLGGELQDFIFSQLKSAKCQYVQLRYLPANSQGVAFYRKHGWKDVGE 142
Cdd:TIGR01575  66 YQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAI 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
75-142 2.34e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 41.71  E-value: 2.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320504014  75 DEGVKYGYINLFYLKPEFRGQGLGGELQDFIFSQLKSAKCQYVqlrYLPANSQGVAFYRKHGWKDVGE 142
Cdd:COG2153    53 PPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRI---VLSAQAHAVGFYEKLGFVPVGE 117
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-138 5.27e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  12 LDLCIAFRKDAYAVSYGSLDGFNIEETAAWFER--LTSWPDAGFYHAI--NKDETIGQIEFRKDLIDDEGVKYGYInlfy 87
Cdd:pfam13302  12 AEALFELLSDPEVMRYGVPWPLTLEEAREWLARiwAADEAERGYGWAIelKDTGFIGSIGLYDIDGEPERAELGYW---- 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2320504014  88 LKPEFRGQGLGGE----LQDFIFSQLksaKCQYVQLRYLPANSQGVAFYRKHGWK 138
Cdd:pfam13302  88 LGPDYWGKGYATEavraLLEYAFEEL---GLPRLVARIDPENTASRRVLEKLGFK 139
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
49-140 3.81e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 34.75  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320504014  49 PDAGFYHAINKDETIGQIEFRkdliDDEGVKYgyINLFYLKPEFRGQGLGGELQDFIFSQLKSAK------CQYVqlryl 122
Cdd:COG2388     7 EEKGRFELEVDGELAGELTYR----LEGGVII--ITHTEVPPALRGQGIASALVEAALDDARERGlkvvplCPFV----- 75

                          90
                  ....*....|....*....
gi 2320504014 123 pansqgVAFYRKHG-WKDV 140
Cdd:COG2388    76 ------AAYFERHPeYADL 88
 
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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