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MULTISPECIES: GNAT family N-acetyltransferase [unclassified Blautia]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11465536)

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
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
167-245 5.32e-16

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


:

Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 71.09  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 167 LVGLAACSADCDDMWQI-GVDVLPEYRRQGIASALTSRLTKEIINRG-KVPFYCTAWSNVRSVRNAVKSGFIPAWVEMTA 244
Cdd:COG3393     2 LVAMAGVRAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALARGaRTPFLYVDADNPAARRLYERLGFRPVGEYATV 81

                  .
gi 1474260043 245 K 245
Cdd:COG3393    82 L 82
Eis super family cl34773
Predicted acetyltransferase [General function prediction only];
125-200 2.94e-04

Predicted acetyltransferase [General function prediction only];


The actual alignment was detected with superfamily member COG4552:

Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.42  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 125 YETRVLTQEDFADLYR-------PEWSNALCEDRKNL----DVLGVgaYDGSTLVGLAAcSADCD--------DMWQI-G 184
Cdd:COG4552     1 MEIRPLTEDDLDAFARllayafgPEPDDEELEAYRPLlepgRVLGV--FDDGELVGTLA-LYPFTlnvggarvPMAGItG 77
                          90
                  ....*....|....*.
gi 1474260043 185 VDVLPEYRRQGIASAL 200
Cdd:COG4552    78 VAVAPEHRRRGVARAL 93
 
Name Accession Description Interval E-value
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
167-245 5.32e-16

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 71.09  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 167 LVGLAACSADCDDMWQI-GVDVLPEYRRQGIASALTSRLTKEIINRG-KVPFYCTAWSNVRSVRNAVKSGFIPAWVEMTA 244
Cdd:COG3393     2 LVAMAGVRAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALARGaRTPFLYVDADNPAARRLYERLGFRPVGEYATV 81

                  .
gi 1474260043 245 K 245
Cdd:COG3393    82 L 82
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
121-236 2.53e-09

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 56.13  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 121 LSCAYETRVLTQEDFADLYRPEWSNALCEDRKNLDV-----LGVGAYDGSTLVglAACS--ADCDDMWQIGVDVLPEYRR 193
Cdd:pfam12746 113 LPQGYTLKKIDEELYEACLEEEWSRDFVSQFSSYEDflkngLGFVILKDGEIV--SGASsySVYEGGIEIEIDTHPDYRG 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1474260043 194 QGIASALTSRLTKEIINRGKVPfyctAWS--NVRSVRNAVKSGFI 236
Cdd:pfam12746 191 KGLATICAAALILECLKRGLYP----SWDahNEASVALAEKLGYE 231
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
159-212 4.05e-05

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: 40.72  E-value: 4.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260043 159 VGAYDGSTLVGLAACSAD--CDDMWQIG-VDVLPEYRRQGIASALTSRLTKEIINRG 212
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDgsGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERG 58
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
159-214 1.57e-04

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: 40.39  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1474260043 159 VGAYDGSTLVGLAACSADCD--DMWQIGVDvlPEYRRQGIASALTSRLTKEIINRGKV 214
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDeaHILNIAVK--PEYQGQGIGRALLRELIDEAKGRGVN 89
Eis COG4552
Predicted acetyltransferase [General function prediction only];
125-200 2.94e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.42  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 125 YETRVLTQEDFADLYR-------PEWSNALCEDRKNL----DVLGVgaYDGSTLVGLAAcSADCD--------DMWQI-G 184
Cdd:COG4552     1 MEIRPLTEDDLDAFARllayafgPEPDDEELEAYRPLlepgRVLGV--FDDGELVGTLA-LYPFTlnvggarvPMAGItG 77
                          90
                  ....*....|....*.
gi 1474260043 185 VDVLPEYRRQGIASAL 200
Cdd:COG4552    78 VAVAPEHRRRGVARAL 93
 
Name Accession Description Interval E-value
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
167-245 5.32e-16

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 71.09  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 167 LVGLAACSADCDDMWQI-GVDVLPEYRRQGIASALTSRLTKEIINRG-KVPFYCTAWSNVRSVRNAVKSGFIPAWVEMTA 244
Cdd:COG3393     2 LVAMAGVRAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALARGaRTPFLYVDADNPAARRLYERLGFRPVGEYATV 81

                  .
gi 1474260043 245 K 245
Cdd:COG3393    82 L 82
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
121-236 2.53e-09

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 56.13  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 121 LSCAYETRVLTQEDFADLYRPEWSNALCEDRKNLDV-----LGVGAYDGSTLVglAACS--ADCDDMWQIGVDVLPEYRR 193
Cdd:pfam12746 113 LPQGYTLKKIDEELYEACLEEEWSRDFVSQFSSYEDflkngLGFVILKDGEIV--SGASsySVYEGGIEIEIDTHPDYRG 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1474260043 194 QGIASALTSRLTKEIINRGKVPfyctAWS--NVRSVRNAVKSGFI 236
Cdd:pfam12746 191 KGLATICAAALILECLKRGLYP----SWDahNEASVALAEKLGYE 231
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
125-235 1.20e-06

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: 46.36  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 125 YETRVLTQEDFADLYRPEWSNALCEDRKNLDVLGVGAYDGSTLVGLAACSADcDDMWQ----IGVDVLPEYRRQGIASAL 200
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSII-DDEPPvgeiEGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1474260043 201 TSRLTKEIINRGKVPFYCTAW-SNVRSVRNAVKSGF 235
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAaDNLAAIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
132-220 1.25e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 46.72  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 132 QEDFADLYR-------PEWSNALCEDRKNLDVLG--VGAYDGSTLVGLAACSADCDDMWQIG-VDVLPEYRRQGIASALT 201
Cdd:COG2153     1 AEELYDALAlrrevfvVEQGVPPYLELDGKDEDArhLLAYDDGELVATARLLPPGDGEAKIGrVAVLPEYRGQGLGRALM 80
                          90
                  ....*....|....*....
gi 1474260043 202 SRLTKEIINRGKVPFYCTA 220
Cdd:COG2153    81 EAAIEEARERGARRIVLSA 99
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
184-241 3.58e-06

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 44.24  E-value: 3.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1474260043 184 GVDVLPEYRRQGIASALTSRLTKEIINRGKVPFYCTAWSNVRSVRNAVKSGFIPAWVE 241
Cdd:pfam08445  26 ALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTPSRRLYEKLGFRKIDET 83
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
130-238 1.28e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.92  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 130 LTQEDFADLYRPEWSNALCEDRknLDVLGVGAYDGSTLVGLAACS----ADCDDMWQIG-VDVLPEYRRQGIASALTSRL 204
Cdd:COG3153    15 LLRAAFGPGREAELVDRLREDP--AAGLSLVAEDDGEIVGHVALSpvdiDGEGPALLLGpLAVDPEYRGQGIGRALMRAA 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1474260043 205 TKEIINRGKVpfYCTAWSNVRSVRNAVKSGFIPA 238
Cdd:COG3153    93 LEAARERGAR--AVVLLGDPSLLPFYERFGFRPA 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
159-212 4.05e-05

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: 40.72  E-value: 4.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1474260043 159 VGAYDGSTLVGLAACSAD--CDDMWQIG-VDVLPEYRRQGIASALTSRLTKEIINRG 212
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDgsGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERG 58
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
161-220 6.01e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.52  E-value: 6.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1474260043 161 AYDGSTLVGLAACSADCDDMWQIGVD--VLPEYRRQGIASALTSRLTKEIINRGKVPFYCTA 220
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRlaVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET 69
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
159-214 1.57e-04

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: 40.39  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1474260043 159 VGAYDGSTLVGLAACSADCD--DMWQIGVDvlPEYRRQGIASALTSRLTKEIINRGKV 214
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIVLDeaHILNIAVK--PEYQGQGIGRALLRELIDEAKGRGVN 89
Eis COG4552
Predicted acetyltransferase [General function prediction only];
125-200 2.94e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.42  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 125 YETRVLTQEDFADLYR-------PEWSNALCEDRKNL----DVLGVgaYDGSTLVGLAAcSADCD--------DMWQI-G 184
Cdd:COG4552     1 MEIRPLTEDDLDAFARllayafgPEPDDEELEAYRPLlepgRVLGV--FDDGELVGTLA-LYPFTlnvggarvPMAGItG 77
                          90
                  ....*....|....*.
gi 1474260043 185 VDVLPEYRRQGIASAL 200
Cdd:COG4552    78 VAVAPEHRRRGVARAL 93
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
180-228 1.50e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 36.94  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1474260043 180 MWQIGVDvlPEYRRQGIASALTSRLTKEIINRGKVPFYCTAW-SNVRSVR 228
Cdd:COG0456    16 IEDLAVD--PEYRGRGIGRALLEAALERARERGARRLRLEVReDNEAAIA 63
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
128-247 2.20e-03

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: 37.28  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 128 RVLTQEDFADLYRPEWSNALCEDRKNLDVlgvgAYDGSTLVGLAACSADCDDMWQIG-VDVLPEYRRQGIASALTSRLTK 206
Cdd:COG1246     4 RPATPDDVPAILELIRPYALEEEIGEFWV----AEEDGEIVGCAALHPLDEDLAELRsLAVHPDYRGRGIGRRLLEALLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1474260043 207 EIINRGKVPFYCtaWSNVRSVRNAVKSGFIPawVEMTAKPA 247
Cdd:COG1246    80 EARELGLKRLFL--LTTSAAIHFYEKLGFEE--IDKEDLPY 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
159-243 5.86e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 36.18  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 159 VGAYDGSTLVGLAAcsadcddMWQIGVD--------VLPEYRRQGIASALTSRLTKEIINRGKVPFY-CTAWSNVRSVRN 229
Cdd:COG0454    37 IAVDDKGEPIGFAG-------LRRLDDKvlelkrlyVLPEYRGKGIGKALLEALLEWARERGCTALElDTLDGNPAAIRF 109
                          90
                  ....*....|....*.
gi 1474260043 230 AVKSGF--IPAWVEMT 243
Cdd:COG0454   110 YERLGFkeIERYVAYV 125
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
128-237 7.99e-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: 36.13  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1474260043 128 RVLTQEDFADLYR----PEWS-----------------NALCEDRKNLDVLGVGAYDGST--LVGLAACSaDCDDMWQ-- 182
Cdd:COG1670    11 RPLRPEDAEALAEllndPEVArylpgppysleearawlERLLADWADGGALPFAIEDKEDgeLIGVVGLY-DIDRANRsa 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1474260043 183 -IGVDVLPEYRRQGIASALTSRLTKEIINRGKVP--FYCTAWSNVRSVRNAVKSGFIP 237
Cdd:COG1670    90 eIGYWLAPAYWGKGYATEALRALLDYAFEELGLHrvEAEVDPDNTASIRVLEKLGFRL 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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