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Conserved domains on  [gi|1767515693|gb|KAB7649150|]
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N-acetyltransferase [Bacillus sp. B2-WWTP-C-10-Post-4]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pentapeptide_4 pfam13599
Pentapeptide repeats (9 copies);
175-251 6.20e-23

Pentapeptide repeats (9 copies);


:

Pssm-ID: 433339 [Multi-domain]  Cd Length: 78  Bit Score: 90.03  E-value: 6.20e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767515693 175 DMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSGSKFNLVTLGGVQF 251
Cdd:pfam13599   2 DFTRCSFEGCKLSGTEFYHATLKDCNFTECNLVNVNFDDCNLRDVDFLEAQLKNAQFSGCNLKNSNFSDVKLKGADF 78
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 74-146 5.17e-11

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


:

Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 5.17e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767515693  74 DKEIIGGIIVTISGKSYGRID-RIFVNPVYQGKGIGSHVMKLIE--KEYPNIKIWDLETSSRQInnhHFYKKMGYQ 146
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAA---AFYEKLGFE 83
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-160 3.60e-07

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693   7 MISIEKATILDAEKLTEIMKRTFDAEAkqwlygqddvIDYNIQPPgysSVEMMEYSIEELDS-----FKVVMDKEIIG-- 79
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGT----------ATFETEPP---SEEEREAWFAAILApgrpvLVAEEDGEVVGfa 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  80 --GIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPNIKIWDLETSSRQINN--HHFYKKMGYQMIFESEDEY 155
Cdd:COG1247    68 slGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEasIALYEKLGFEEVGTLPEVG 147


                  ....*
gi 1767515693 156 CYVKR 160
Cdd:COG1247   148 FKFGR 152
 
Name Accession Description Interval E-value
Pentapeptide_4 pfam13599
Pentapeptide repeats (9 copies);
175-251 6.20e-23

Pentapeptide repeats (9 copies);


Pssm-ID: 433339 [Multi-domain]  Cd Length: 78  Bit Score: 90.03  E-value: 6.20e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767515693 175 DMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSGSKFNLVTLGGVQF 251
Cdd:pfam13599   2 DFTRCSFEGCKLSGTEFYHATLKDCNFTECNLVNVNFDDCNLRDVDFLEAQLKNAQFSGCNLKNSNFSDVKLKGADF 78
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
163-308 3.06e-14

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 69.58  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 163 TSSNKESVVTNKDMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADL---NLSGS 239
Cdd:COG1357    23 SGANLSGALSGANLSGANLSGANLTGANLSGADLSGADLSGANLSGADLSGANLTGADLSGANLANLSGANLsgaNLSGA 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767515693 240 KFNLVTLGGVQFKNTSLGDEKepiL----FDKCDLEGSTISNSNLKNIEIENCDIVGMKLNGILIE--NLLNLYN 308
Cdd:COG1357   103 NLRGANLSGANLSGADLSGAD---LsganLSGADLSGANLSGANLSGADLSGADLSGANLSGANLSgaNLANLEG 174
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 74-146 5.17e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 5.17e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767515693  74 DKEIIGGIIVTISGKSYGRID-RIFVNPVYQGKGIGSHVMKLIE--KEYPNIKIWDLETSSRQInnhHFYKKMGYQ 146
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAA---AFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 56-148 5.28e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 59.30  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  56 VEMMEYSIEELDS------FKVVMDKEIIGGII-VTISGKSYGRIDRIFVNPVYQGKGIGSHVMK-LIE--KEYpNIKIW 125
Cdd:COG0454    17 IEALDAELKAMEGslagaeFIAVDDKGEPIGFAgLRRLDDKVLELKRLYVLPEYRGKGIGKALLEaLLEwaRER-GCTAL 95

                          90       100
                  ....*....|....*....|...
gi 1767515693 126 DLETSSRQINNHHFYKKMGYQMI 148
Cdd:COG0454    96 ELDTLDGNPAAIRFYERLGFKEI 118
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-160 3.60e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693   7 MISIEKATILDAEKLTEIMKRTFDAEAkqwlygqddvIDYNIQPPgysSVEMMEYSIEELDS-----FKVVMDKEIIG-- 79
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGT----------ATFETEPP---SEEEREAWFAAILApgrpvLVAEEDGEVVGfa 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  80 --GIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPNIKIWDLETSSRQINN--HHFYKKMGYQMIFESEDEY 155
Cdd:COG1247    68 slGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEasIALYEKLGFEEVGTLPEVG 147


                  ....*
gi 1767515693 156 CYVKR 160
Cdd:COG1247   148 FKFGR 152
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 74-118 3.75e-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: 46.50  E-value: 3.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1767515693  74 DKEIIGGIIVTISGKS--YGRIDRIFVNPVYQGKGIGSHVMKLIEKE 118
Cdd:cd04301     7 DGEIVGFASLSPDGSGgdTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
PRK15377 PRK15377
type III secretion system effector HECT-type E3 ubiquitin transferase;
160-275 1.79e-04

type III secretion system effector HECT-type E3 ubiquitin transferase;


Pssm-ID: 185275 [Multi-domain]  Cd Length: 782  Bit Score: 43.13  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 160 RIKTSSNKESVVTNKDMKNSQYENCNLANTEYYQVNLKNSSFV-GSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSG 238
Cdd:PRK15377  181 RLRQEAGEELTYADRDFSNADFRNINFSKINPSGFMLRDGDIIkGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSN 260

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1767515693 239 SKFNLVTLGGVQFKNTSLgdEKEPILFDKCDLEGSTI 275
Cdd:PRK15377  261 TKFSNSDMNEASLKYSIT--TQQQPSFIETTLKNTII 295
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 74-148 6.32e-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: 39.23  E-value: 6.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767515693  74 DKEIIGGIIVTISGKSyGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPNI---KIWdLETSSRQINNHHFYKKMGYQMI 148
Cdd:TIGR01575  39 GGKVVGYAGVQIVLDE-AHILNIAVKPEYQGQGIGRALLRELIDEAKGRgvnEIF-LEVRVSNIAAQALYKKLGFNEI 114
 
Name Accession Description Interval E-value
Pentapeptide_4 pfam13599
Pentapeptide repeats (9 copies);
175-251 6.20e-23

Pentapeptide repeats (9 copies);


Pssm-ID: 433339 [Multi-domain]  Cd Length: 78  Bit Score: 90.03  E-value: 6.20e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767515693 175 DMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSGSKFNLVTLGGVQF 251
Cdd:pfam13599   2 DFTRCSFEGCKLSGTEFYHATLKDCNFTECNLVNVNFDDCNLRDVDFLEAQLKNAQFSGCNLKNSNFSDVKLKGADF 78
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
163-308 3.06e-14

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 69.58  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 163 TSSNKESVVTNKDMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADL---NLSGS 239
Cdd:COG1357    23 SGANLSGALSGANLSGANLSGANLTGANLSGADLSGADLSGANLSGADLSGANLTGADLSGANLANLSGANLsgaNLSGA 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767515693 240 KFNLVTLGGVQFKNTSLGDEKepiL----FDKCDLEGSTISNSNLKNIEIENCDIVGMKLNGILIE--NLLNLYN 308
Cdd:COG1357   103 NLRGANLSGANLSGADLSGAD---LsganLSGADLSGANLSGANLSGADLSGADLSGANLSGANLSgaNLANLEG 174
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
175-297 1.56e-12

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 64.96  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 175 DMKNSQYENCNLANTEYYQVNLKN----SSFVGSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSGSKFNLVTLGGVQ 250
Cdd:COG1357     1 DLSGADLSGADLSGADLSGADLSGanlsGALSGANLSGANLSGANLTGANLSGADLSGADLSGANLSGADLSGANLTGAD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1767515693 251 FKNTSLgdekepILFDKCDLEGSTISNSNLKNIEIENCDIVGMKLNG 297
Cdd:COG1357    81 LSGANL------ANLSGANLSGANLSGANLRGANLSGANLSGADLSG 121
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 74-146 5.17e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.85  E-value: 5.17e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767515693  74 DKEIIGGIIVTISGKSYGRID-RIFVNPVYQGKGIGSHVMKLIE--KEYPNIKIWDLETSSRQInnhHFYKKMGYQ 146
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAElRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAA---AFYEKLGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 56-148 5.28e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 59.30  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  56 VEMMEYSIEELDS------FKVVMDKEIIGGII-VTISGKSYGRIDRIFVNPVYQGKGIGSHVMK-LIE--KEYpNIKIW 125
Cdd:COG0454    17 IEALDAELKAMEGslagaeFIAVDDKGEPIGFAgLRRLDDKVLELKRLYVLPEYRGKGIGKALLEaLLEwaRER-GCTAL 95

                          90       100
                  ....*....|....*....|...
gi 1767515693 126 DLETSSRQINNHHFYKKMGYQMI 148
Cdd:COG0454    96 ELDTLDGNPAAIRFYERLGFKEI 118
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 46-145 1.12e-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: 57.91  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  46 YNIQPPGYSSVEMMEYSIEELDSFK--------VVMDKEIIGGIIVTI--SGKSYGRIDRIFVNPVYQGKGIGSHVMKLI 115
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDEdasegffvAEEDGELVGFASLSIidDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1767515693 116 EKEYP--NIKIWDLETSSRQINNHHFYKKMGY 145
Cdd:pfam00583  85 LEWARerGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 64-162 1.19e-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: 58.46  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  64 EELDSFKVVM-DKEIIGGIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKE-----YPniKIWdLETSSRQinnH 137
Cdd:COG1246    25 EEIGEFWVAEeDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEarelgLK--RLF-LLTTSAA---I 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1767515693 138 HFYKKMGYQMIFESE---------DEYCYVKRIK 162
Cdd:COG1246    99 HFYEKLGFEEIDKEDlpyakvwqrDSVVMEKDLE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 81-162 6.04e-09

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 52.35  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  81 IIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYP--NIKIWDLETSSRQINNHHFYKKMGYQMI-----FESED 153
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARerGARRLRLEVREDNEAAIALYEKLGFEEVgerpnYYGDD 83


                  ....*....
gi 1767515693 154 EYCYVKRIK 162
Cdd:COG0456    84 ALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-148 1.63e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 49.70  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  10 IEKATILDAEKLTEIMKRTFDAEAKQwlygqddvidyniqppgySSVEMMEYSIEELDSFKVVMDKEIIGGIIVT----I 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREA------------------ELVDRLREDPAAGLSLVAEDDGEIVGHVALSpvdiD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767515693  86 SGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYP--NIKIWDLETSSrqiNNHHFYKKMGYQMI 148
Cdd:COG3153    63 GEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARerGARAVVLLGDP---SLLPFYERFGFRPA 124
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
7-160 3.60e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.22  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693   7 MISIEKATILDAEKLTEIMKRTFDAEAkqwlygqddvIDYNIQPPgysSVEMMEYSIEELDS-----FKVVMDKEIIG-- 79
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAIAEGT----------ATFETEPP---SEEEREAWFAAILApgrpvLVAEEDGEVVGfa 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  80 --GIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPNIKIWDLETSSRQINN--HHFYKKMGYQMIFESEDEY 155
Cdd:COG1247    68 slGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEasIALYEKLGFEEVGTLPEVG 147


                  ....*
gi 1767515693 156 CYVKR 160
Cdd:COG1247   148 FKFGR 152
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 74-118 3.75e-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: 46.50  E-value: 3.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1767515693  74 DKEIIGGIIVTISGKS--YGRIDRIFVNPVYQGKGIGSHVMKLIEKE 118
Cdd:cd04301     7 DGEIVGFASLSPDGSGgdTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
76-150 4.25e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.21  E-value: 4.25e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767515693  76 EIIGGIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEY--PNIKIWDLETSSRQINNHHFYKKMGYQMIFE 150
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREAlaRGARTPFLYVDADNPAARRLYERLGFRPVGE 77
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
175-252 9.21e-07

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 48.40  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 175 DMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFRWS--SYADL---NLSGSKF---NLVTL 246
Cdd:COG1357    93 NLSGANLSGANLRGANLSGANLSGADLSGADLSGANLSGADLSGANLSGANLSGAdlSGADLsgaNLSGANLsgaNLANL 172


                  ....*.
gi 1767515693 247 GGVQFK 252
Cdd:COG1357   173 EGADLK 178
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 69-148 1.64e-06

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: 46.50  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693  69 FKVVMDKEIIGgiivTISGKSYGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPN--IKIWDLETSSrQINNHHFYKKMGYQ 146
Cdd:pfam13673  34 FVAFEGGQIVG----VIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKdgIKLSELTVNA-SPYAVPFYEKLGFR 108


                  ..
gi 1767515693 147 MI 148
Cdd:pfam13673 109 AT 110
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
74-146 9.92e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.40  E-value: 9.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767515693  74 DKEIIGGIIVTISGKSYGRIDRIFVNPVYQGKGIGSHVMK-LIE--KEYPNIKIWDletsSRQINNHHFYKKMGYQ 146
Cdd:COG2153    42 DGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEaAIEeaRERGARRIVL----SAQAHAVGFYEKLGFV 113
PRK15377 PRK15377
type III secretion system effector HECT-type E3 ubiquitin transferase;
160-275 1.79e-04

type III secretion system effector HECT-type E3 ubiquitin transferase;


Pssm-ID: 185275 [Multi-domain]  Cd Length: 782  Bit Score: 43.13  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 160 RIKTSSNKESVVTNKDMKNSQYENCNLANTEYYQVNLKNSSFV-GSNIMNTNMSNCNVSQSKFRNINFRWSSYADLNLSG 238
Cdd:PRK15377  181 RLRQEAGEELTYADRDFSNADFRNINFSKINPSGFMLRDGDIIkGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSN 260

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1767515693 239 SKFNLVTLGGVQFKNTSLgdEKEPILFDKCDLEGSTI 275
Cdd:PRK15377  261 TKFSNSDMNEASLKYSIT--TQQQPSFIETTLKNTII 295
Pentapeptide pfam00805
Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The ...
 184-227 4.34e-04

Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The repeats were first identified in hglK. The function of these repeats is unknown. The structure of this repeat has been predicted to be a beta-helix. The repeat can be approximately described as A(D/N)LXX, where X can be any amino acid.


Pssm-ID: 459943 [Multi-domain]  Cd Length: 40  Bit Score: 37.32  E-value: 4.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767515693 184 CNLANteyyqVNLKNSSFVGSNIMNTNMSNCNVSQSKFRNINFR 227
Cdd:pfam00805   1 ANLSG-----ANLSGANLSGANLSGANLTGANLSGADLSGANLS 39
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 74-148 6.32e-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: 39.23  E-value: 6.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767515693  74 DKEIIGGIIVTISGKSyGRIDRIFVNPVYQGKGIGSHVMKLIEKEYPNI---KIWdLETSSRQINNHHFYKKMGYQMI 148
Cdd:TIGR01575  39 GGKVVGYAGVQIVLDE-AHILNIAVKPEYQGQGIGRALLRELIDEAKGRgvnEIF-LEVRVSNIAAQALYKKLGFNEI 114
Pentapeptide pfam00805
Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The ...
 209-248 3.39e-03

Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The repeats were first identified in hglK. The function of these repeats is unknown. The structure of this repeat has been predicted to be a beta-helix. The repeat can be approximately described as A(D/N)LXX, where X can be any amino acid.


Pssm-ID: 459943 [Multi-domain]  Cd Length: 40  Bit Score: 34.62  E-value: 3.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1767515693 209 TNMSNCNVSQSKFRNINFRWSSYADLNLSGSKFNLVTLGG 248
Cdd:pfam00805   1 ANLSGANLSGANLSGANLSGANLTGANLSGADLSGANLSG 40
Pentapeptide_4 pfam13599
Pentapeptide repeats (9 copies);
204-290 4.00e-03

Pentapeptide repeats (9 copies);


Pssm-ID: 433339 [Multi-domain]  Cd Length: 78  Bit Score: 35.71  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 204 SNIMNTNMSNCNVSQSKFRNINFRwssyaDLNLSGSKFNlvtlgGVQFKNTSLGDekepILFDKCDLEGSTISNSNLKNI 283
Cdd:pfam13599   1 ADFTRCSFEGCKLSGTEFYHATLK-----DCNFTECNLV-----NVNFDDCNLRD----VDFLEAQLKNAQFSGCNLKNS 66


                  ....*..
gi 1767515693 284 EIENCDI 290
Cdd:pfam13599  67 NFSDVKL 73
Pentapeptide_4 pfam13599
Pentapeptide repeats (9 copies);
167-226 5.63e-03

Pentapeptide repeats (9 copies);


Pssm-ID: 433339 [Multi-domain]  Cd Length: 78  Bit Score: 35.33  E-value: 5.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767515693 167 KESVVTNKDMKNSQYENCNLANTEYYQVNLKNSSFVGSNIMNTNMSNCnvsqsKFRNINF 226
Cdd:pfam13599  24 KDCNFTECNLVNVNFDDCNLRDVDFLEAQLKNAQFSGCNLKNSNFSDV-----KLKGADF 78
Pentapeptide pfam00805
Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The ...
 199-242 6.44e-03

Pentapeptide repeats (8 copies); These repeats are found in many cyanobacterial proteins. The repeats were first identified in hglK. The function of these repeats is unknown. The structure of this repeat has been predicted to be a beta-helix. The repeat can be approximately described as A(D/N)LXX, where X can be any amino acid.


Pssm-ID: 459943 [Multi-domain]  Cd Length: 40  Bit Score: 33.85  E-value: 6.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767515693 199 SSFVGSNIMNTNMSNCNVSQSKFRNINFRWSsyadlNLSGSKFN 242
Cdd:pfam00805   1 ANLSGANLSGANLSGANLSGANLTGANLSGA-----DLSGANLS 39
 
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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