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Conserved domains on  [gi|488869563|ref|WP_002781802|]
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MULTISPECIES: UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase [Campylobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PseH super family cl29702
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 5-146 4.74e-56

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


The actual alignment was detected with superfamily member TIGR03585:

Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 172.54  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563    5 KNFTELNSQEIELIFKWRNHPDINQFMKT-KYIDFEEHLRFLKKLHQDSSKKYFLVFQDEQIIGVIDFVNIT--TKSCEF 81
Cdd:TIGR03585   1 KNFTPLNSEELELVLEWRNHPDVRANMYSdHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTDINlvHKSAFW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488869563   82 GLYAKPNLK-GVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTI------YDEDKDFYHIC 146
Cdd:TIGR03585  81 GIYANPFCKpGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFERegvfrqGGEYYDVLLMY 152
 
Name Accession Description Interval E-value
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 5-146 4.74e-56

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 172.54  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563    5 KNFTELNSQEIELIFKWRNHPDINQFMKT-KYIDFEEHLRFLKKLHQDSSKKYFLVFQDEQIIGVIDFVNIT--TKSCEF 81
Cdd:TIGR03585   1 KNFTPLNSEELELVLEWRNHPDVRANMYSdHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTDINlvHKSAFW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488869563   82 GLYAKPNLK-GVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTI------YDEDKDFYHIC 146
Cdd:TIGR03585  81 GIYANPFCKpGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFERegvfrqGGEYYDVLLMY 152
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 15-145 2.56e-20

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: 81.97  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  15 IELIFKWRNHPDINQFMKTKYIDFEEHLRFLKKLHQDSSKKYFLVF-----QDEQIIGVIDFVNI--TTKSCEFGLYAKP 87
Cdd:COG1670   18 AEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFaiedkEDGELIGVVGLYDIdrANRSAEIGYWLAP 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  88 NL--KGVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTIYDEDKDFYHI 145
Cdd:COG1670   98 AYwgKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 10-134 1.98e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.43  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   10 LNSQEIELIFKWRNHPDINQFMKTKYIDFEEHLRFLKKLHQDSSKK---YFLVF-QDEQIIGVIDFVNIT--TKSCEFGL 83
Cdd:pfam13302   7 LTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAErgyGWAIElKDTGFIGSIGLYDIDgePERAELGY 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488869563   84 YAKPNLKGVGqiLMNE----IIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFT 134
Cdd:pfam13302  87 WLGPDYWGKG--YATEavraLLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
48-151 7.29e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 38.20  E-value: 7.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  48 LHQDSSKKYFLVFQDEQIIGVIDFVNI--TTKSCEFGLYAKPNLKGVG---QILMNEIIKYAfenlKVNTLKAYVFK--- 119
Cdd:PRK10151  61 LHQRGYAKMFMIFKEDELIGVLSFNRIepLNKTAYIGYWLDESHQGQGiisQALQALIHHYA----QSGELRRFVIKcrv 136

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488869563 120 DNRKALKLYQQNHFTiydedkdfYHICLKQSD 151
Cdd:PRK10151 137 DNPASNQVALRNGFT--------LEGCLKQAE 160
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-106 2.09e-03

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: 34.94  E-value: 2.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488869563  56 YFLVFQDEQIIGVIDFV--NITTKSCEFG-LYAKPNL--KGVGQILMNEIIKYAFE 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdGSGGDTAYIGdLAVLPEYrgKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 5-146 4.74e-56

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 172.54  E-value: 4.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563    5 KNFTELNSQEIELIFKWRNHPDINQFMKT-KYIDFEEHLRFLKKLHQDSSKKYFLVFQDEQIIGVIDFVNIT--TKSCEF 81
Cdd:TIGR03585   1 KNFTPLNSEELELVLEWRNHPDVRANMYSdHLIDWEEHLHFIEALKQDPNRRYWIVCQESRPIGVISFTDINlvHKSAFW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488869563   82 GLYAKPNLK-GVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTI------YDEDKDFYHIC 146
Cdd:TIGR03585  81 GIYANPFCKpGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFERegvfrqGGEYYDVLLMY 152
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 15-145 2.56e-20

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: 81.97  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  15 IELIFKWRNHPDINQFMKTKYIDFEEHLRFLKKLHQDSSKKYFLVF-----QDEQIIGVIDFVNI--TTKSCEFGLYAKP 87
Cdd:COG1670   18 AEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFaiedkEDGELIGVVGLYDIdrANRSAEIGYWLAP 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  88 NL--KGVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTIYDEDKDFYHI 145
Cdd:COG1670   98 AYwgKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 10-134 1.98e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.43  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   10 LNSQEIELIFKWRNHPDINQFMKTKYIDFEEHLRFLKKLHQDSSKK---YFLVF-QDEQIIGVIDFVNIT--TKSCEFGL 83
Cdd:pfam13302   7 LTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAErgyGWAIElKDTGFIGSIGLYDIDgePERAELGY 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488869563   84 YAKPNLKGVGqiLMNE----IIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFT 134
Cdd:pfam13302  87 WLGPDYWGKG--YATEavraLLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 35-133 4.06e-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: 54.06  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   35 YIDFEEHLRFLKKLHQDSSKKYFLVFQDEQIIGVIDFVNITTKSC---EFGLYAKPNL--KGVGQILMNEIIKYAFEnLK 109
Cdd:pfam00583  14 EPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPvgeIEGLAVAPEYrgKGIGTALLQALLEWARE-RG 92

                          90       100
                  ....*....|....*....|....
gi 488869563  110 VNTLKAYVFKDNRKALKLYQQNHF 133
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 90-144 4.08e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 45.42  E-value: 4.08e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488869563  90 KGVGQILMNEIIKYAFENlKVNTLKAYVFKDNRKALKLYQQNHFTIYDEDKDFYH 144
Cdd:COG0456   28 RGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG 81
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
10-145 6.68e-06

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 43.51  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   10 LNSQEIELIFKWRNHPDINQFMKTKYID--FEEHLRFLKKLHQDSsKKYFLVFQDEQIIGVIDFVNITTKSCE----FGL 83
Cdd:pfam13420   4 LTQNDLKEIRRWYAEDRVNPAFTQEYAHssIEEFETFLAAYLSPG-EIVFGVAESDRLIGYATLRQFDYVKTHkaelSFY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488869563   84 YAKPNLKGVGQILMNEIIKYAFENLKVNTLKAYVFKDNRKALKLYQQNHFTIYDEDKDFYHI 145
Cdd:pfam13420  83 VVKNNDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKK 144
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 48-144 2.32e-04

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: 38.82  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  48 LHQDSSKKYFLVFQDEQIIGVIDFVNITTKSCEFG-LYAKPNL--KGVGQILMNEIIKYAfENLKVNTLKAYVfkdNRKA 124
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRsLAVHPDYrgRGIGRRLLEALLAEA-RELGLKRLFLLT---TSAA 97

                         90       100
                 ....*....|....*....|
gi 488869563 125 LKLYQQNHFTIYDEDKDFYH 144
Cdd:COG1246   98 IHFYEKLGFEEIDKEDLPYA 117
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
48-151 7.29e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 38.20  E-value: 7.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563  48 LHQDSSKKYFLVFQDEQIIGVIDFVNI--TTKSCEFGLYAKPNLKGVG---QILMNEIIKYAfenlKVNTLKAYVFK--- 119
Cdd:PRK10151  61 LHQRGYAKMFMIFKEDELIGVLSFNRIepLNKTAYIGYWLDESHQGQGiisQALQALIHHYA----QSGELRRFVIKcrv 136

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488869563 120 DNRKALKLYQQNHFTiydedkdfYHICLKQSD 151
Cdd:PRK10151 137 DNPASNQVALRNGFT--------LEGCLKQAE 160
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-135 1.35e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.89  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   56 YFLVFQDEQIIGVIDFVNI--TTKSCEFGLYAKPNL--KGVGQILMNEIIKYAfenlKVNTLKAYVFKDNRKALKLYQQN 131
Cdd:pfam13508   5 FFVAEDDGKIVGFAALLPLddEGALAELRLAVHPEYrgQGIGRALLEAAEAAA----KEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 488869563  132 HFTI 135
Cdd:pfam13508  81 GFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-106 2.09e-03

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: 34.94  E-value: 2.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488869563  56 YFLVFQDEQIIGVIDFV--NITTKSCEFG-LYAKPNL--KGVGQILMNEIIKYAFE 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSpdGSGGDTAYIGdLAVLPEYrgKGIGSALLEAAEEEARE 56
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 55-144 9.76e-03

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: 34.23  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488869563   55 KYFLVFQDEQIIGVIdFVNITTKSCE-FGLYAKPNLK--GVGQILMNEIIKYAFENlKVNTLKAYVFKDNRKALKLYQQN 131
Cdd:TIGR01575  32 CYLLARIGGKVVGYA-GVQIVLDEAHiLNIAVKPEYQgqGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKL 109

                          90
                  ....*....|...
gi 488869563  132 HFTIYDEDKDFYH 144
Cdd:TIGR01575 110 GFNEIAIRRNYYP 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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