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MULTISPECIES: GNAT family N-acetyltransferase [pseudomallei group]

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];
14-158 1.69e-34

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 118.26  E-value: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  14 LRGERAGDAAALARVIVAAFADEPqggqfERRIVDALRVDGRLSVSLVAVRDGRLVGHVAFSPVAIgAGGEGWHGLAPLA 93
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR-----EAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDI-DGEGPALLLGPLA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490298409  94 VWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFGFGPAGDIVFPQAPPDALMALPF 158
Cdd:COG3153   75 VDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPsllPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
14-158 1.69e-34

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 118.26  E-value: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  14 LRGERAGDAAALARVIVAAFADEPqggqfERRIVDALRVDGRLSVSLVAVRDGRLVGHVAFSPVAIgAGGEGWHGLAPLA 93
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR-----EAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDI-DGEGPALLLGPLA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490298409  94 VWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFGFGPAGDIVFPQAPPDALMALPF 158
Cdd:COG3153   75 VDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPsllPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-137 1.00e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.15  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409   60 LVAVRDGRLVGHVAFSPVaigaGGEGWHGLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFG 136
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPL----DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNraaAFYEKLG 81


                  .
gi 490298409  137 F 137
Cdd:pfam13508  82 F 82
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-125 4.73e-07

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: 44.96  E-value: 4.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490298409  59 SLVAVRDGRLVGHVAFSPVAigaGGEGWHGLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVV 125
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDG---SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 43-123 3.64e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.45  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  43 ERRIVDALRVDGRLSvsLVAVRDGRLVGHVAfspvaigAGGEGWHG-LAPLAVWPGCQRQGIGAALVRAGLDALRragAR 121
Cdd:PRK03624  33 EMDIERKLNHDPSLF--LVAEVGGEVVGTVM-------GGYDGHRGwAYYLAVHPDFRGRGIGRALVARLEKKLI---AR 100


                 ..
gi 490298409 122 GC 123
Cdd:PRK03624 101 GC 102
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
14-158 1.69e-34

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 118.26  E-value: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  14 LRGERAGDAAALARVIVAAFADEPqggqfERRIVDALRVDGRLSVSLVAVRDGRLVGHVAFSPVAIgAGGEGWHGLAPLA 93
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGR-----EAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDI-DGEGPALLLGPLA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490298409  94 VWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFGFGPAGDIVFPQAPPDALMALPF 158
Cdd:COG3153   75 VDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPsllPFYERFGFRPAGELGLTLGPDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 12-148 9.99e-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: 53.84  E-value: 9.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  12 VTLRGERAGDAAALARVIvAAFADEPQGGQFerrivdalrvdgrlsvsLVAVRDGRLVGHVAFSPVaigagGEGWHGLAP 91
Cdd:COG1246    1 MTIRPATPDDVPAILELI-RPYALEEEIGEF-----------------WVAEEDGEIVGCAALHPL-----DEDLAELRS 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  92 LAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVL---GEPAYYARFGFGPAGDIVFPQA 148
Cdd:COG1246   58 LAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLttsAAIHFYEKLGFEEIDKEDLPYA 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 60-137 1.00e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.15  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409   60 LVAVRDGRLVGHVAFSPVaigaGGEGWHGLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFG 136
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPL----DDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNraaAFYEKLG 81


                  .
gi 490298409  137 F 137
Cdd:pfam13508  82 F 82
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-137 1.63e-08

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: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409   25 LARVIVAAFADEPQGGQFERRIVDALRVDGRLSVSLVAVRDGRLVGHVAFSPVAigaGGEGWHGLAPLAVWPGCQRQGIG 104
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 490298409  105 AALVRAGLDALRRAGARGCVVLGEP------AYYARFGF 137
Cdd:pfam00583  78 TALLQALLEWARERGCERIFLEVAAdnlaaiALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-141 1.66e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  12 VTLRGERAGDAAALARVI-------VAAFADEPQGGQFERRIVDALRVDGRLSvsLVAVRDGRLVGHVAFSPVAIGAGGe 84
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYneaiaegTATFETEPPSEEEREAWFAAILAPGRPV--LVAEEDGEVVGFASLGPFRPRPAY- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490298409  85 GWHGLAPLAVWPGCQRQGIGAALVRAGLDALRRAGAR---GCVVLGEPA---YYARFGFGPAG 141
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARARGYRrlvAVVLADNEAsiaLYEKLGFEEVG 141
Eis COG4552
Predicted acetyltransferase [General function prediction only];
13-171 3.43e-08

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 51.82  E-value: 3.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  13 TLRGERAGDAAALARVIVAAFADEPQGGQFE--RRIVDALRVdgrlsvsLVAVRDGRLVGHVAFSPVAIGAGGEGW--HG 88
Cdd:COG4552    2 EIRPLTEDDLDAFARLLAYAFGPEPDDEELEayRPLLEPGRV-------LGVFDDGELVGTLALYPFTLNVGGARVpmAG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  89 LAPLAVWPGCQRQGIGAALVRAGLDALRRAGARgCVVLG--EPAYYARFGFGPAGDIVFPQAPPDalmALPFgehAPRPA 166
Cdd:COG4552   75 ITGVAVAPEHRRRGVARALLREALAELRERGQP-LSALYpfEPGFYRRFGYELAGDRRRYTIPPE---SLPL---RPDAP 147


                 ....*
gi 490298409 167 GELRY 171
Cdd:COG4552  148 GRVRR 152
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 32-139 2.88e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 47.18  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409   32 AFADEPQGG--QFERRIVDALRVdgrlsvsLVAVRDGRLVGHVAFSPVAIGAGGEGWH--GLAPLAVWPGCQRQGIGAAL 107
Cdd:pfam13527  19 AFQDEDSPElrEYFRPLLEEGRV-------LGAFDDGELVSTLALYPFELNVPGKTLPaaGITGVATYPEYRGRGVMSRL 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 490298409  108 VRAGLDALRRAGARgcVVLG---EPAYYARFGFGP 139
Cdd:pfam13527  92 LRRSLEEMRERGVP--LSFLypsSYPIYRRFGYEI 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-125 4.73e-07

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: 44.96  E-value: 4.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490298409  59 SLVAVRDGRLVGHVAFSPVAigaGGEGWHGLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVV 125
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDG---SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 92-158 6.87e-06

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 42.72  E-value: 6.87e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490298409  92 LAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP------AYYARFGFGPAGDIVFPQAPPDALMALPF 158
Cdd:COG0456   19 LAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREdneaaiALYEKLGFEEVGERPNYYGDDALVMEKEL 91
PRK03624 PRK03624
putative acetyltransferase; Provisional
 43-123 3.64e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.45  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  43 ERRIVDALRVDGRLSvsLVAVRDGRLVGHVAfspvaigAGGEGWHG-LAPLAVWPGCQRQGIGAALVRAGLDALRragAR 121
Cdd:PRK03624  33 EMDIERKLNHDPSLF--LVAEVGGEVVGTVM-------GGYDGHRGwAYYLAVHPDFRGRGIGRALVARLEKKLI---AR 100


                 ..
gi 490298409 122 GC 123
Cdd:PRK03624 101 GC 102
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 60-137 5.72e-05

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: 40.72  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409   60 LVAVRDGRLVGHVAFSpvaigaggEGWHgLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVL------GEPaYYA 133
Cdd:pfam13673  34 FVAFEGGQIVGVIALR--------DRGH-ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTvnaspyAVP-FYE 103


                  ....
gi 490298409  134 RFGF 137
Cdd:pfam13673 104 KLGF 107
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
60-143 1.16e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.17  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  60 LVAVRDGRLVGHVAFSPvaigAGGEGWHgLAPLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVLGEP---AYYARFG 136
Cdd:COG2153   37 LLAYDDGELVATARLLP----PGDGEAK-IGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAhavGFYEKLG 111


                 ....*..
gi 490298409 137 FGPAGDI 143
Cdd:COG2153  112 FVPVGEE 118
PRK07757 PRK07757
N-acetyltransferase;
61-137 1.44e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.18  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  61 VAVRDGRLVGHVAFSPVaigaggegWHGLA---PLAVWPGCQRQGIGAALVRAGLDALRRAGARGCVVLG-EPAYYARFG 136
Cdd:PRK07757  45 VAEEEGEIVGCCALHIL--------WEDLAeirSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALTyQPEFFEKLG 116


                 .
gi 490298409 137 F 137
Cdd:PRK07757 117 F 117
PRK01346 PRK01346
enhanced intracellular survival protein Eis;
12-140 4.14e-04

enhanced intracellular survival protein Eis;


Pssm-ID: 234945 [Multi-domain]  Cd Length: 411  Bit Score: 39.91  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  12 VTLRGERAGDAAALARVIVAAFADEPQGGQFERRivDALRVDGRlsvSLVAVRDGRLVGHVAFSPVAI---GAGGEGWHG 88
Cdd:PRK01346   7 ITIRTATEEDWPAWFRAAATGFGDSPSDEELEAW--RALVEPDR---TLGAFDGDEVVGTAGAFDLRLtvpGGAVLPAAG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490298409  89 LAPLAVWPGCQRQGIGAALVRAGLDALRRAG-ARGCVVLGEPAYYARFGFGPA 140
Cdd:PRK01346  82 VTAVTVAPTHRRRGLLTALMREQLRRIRERGePVAALTASEGGIYGRFGYGPA 134
PRK07922 PRK07922
amino-acid N-acetyltransferase;
44-137 8.59e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 35.28  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490298409  44 RRIVDALRVDGRL----SVSL--------VAVR-DGRLVG----HVAfspvaigaggegWHGLA---PLAVWPGCQRQGI 103
Cdd:PRK07922  20 KRLVDPYAQGRILleknLVTLyeavqefwVAEHlDGEVVGcgalHVM------------WEDLAeirTVAVDPAARGRGV 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490298409 104 GAALVRAGLDALRRAGARGCVVLG-EPAYYARFGF 137
Cdd:PRK07922  88 GHAIVERLLDVARELGLSRVFVLTfEVEFFARHGF 122
 
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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