NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002239292|ref|XP_015623881|]
View 

uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
155-245 6.54e-12

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 6.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 155 GFVHYRFVLEEDVpvVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKLRYVISSTSPS 234
Cdd:COG0456     1 GFALLGLVDGGDE--AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
                          90
                  ....*....|..
gi 1002239292 235 -RVDPLIGLEKN 245
Cdd:COG0456    79 yYGDDALVMEKE 90
TraY super family cl27023
TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved ...
32-58 3.36e-03

TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved in bacterial conjugation where it is required for efficient nick formation in the F plasmid. These proteins have a ribbon-helix-helix fold and are likely to be DNA-binding proteins.


The actual alignment was detected with superfamily member PRK13740:

Pssm-ID: 452705  Cd Length: 70  Bit Score: 35.53  E-value: 3.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 1002239292  32 GRKKAVEELIRkavaVKDHLAQFPDFH 58
Cdd:PRK13740   34 GRSKTNEVQIR----LRDHLKRFPDFY 56
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
155-245 6.54e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 6.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 155 GFVHYRFVLEEDVpvVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKLRYVISSTSPS 234
Cdd:COG0456     1 GFALLGLVDGGDE--AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
                          90
                  ....*....|..
gi 1002239292 235 -RVDPLIGLEKN 245
Cdd:COG0456    79 yYGDDALVMEKE 90
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
147-224 8.84e-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: 55.22  E-value: 8.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002239292 147 ACNEDRLIGFVHYRFVLEEDvPVVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKL 224
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKL 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
147-209 5.60e-06

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: 43.03  E-value: 5.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002239292 147 ACNEDRLIGFVHYRFVLEEDvPVVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLT 209
Cdd:cd04301     4 AEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
151-246 2.31e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 43.09  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 151 DRLIGFVHYRFVLEEdvpvVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKLRYVIss 230
Cdd:TIGR01575  40 GKVVGYAGVQIVLDE----AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNE-- 113
                          90
                  ....*....|....*.
gi 1002239292 231 tspsrvdplIGLEKNY 246
Cdd:TIGR01575 114 ---------IAIRRNY 120
PRK13740 PRK13740
conjugal transfer relaxosome protein TraY;
32-58 3.36e-03

conjugal transfer relaxosome protein TraY;


Pssm-ID: 184292  Cd Length: 70  Bit Score: 35.53  E-value: 3.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 1002239292  32 GRKKAVEELIRkavaVKDHLAQFPDFH 58
Cdd:PRK13740   34 GRSKTNEVQIR----LRDHLKRFPDFY 56
PRK03624 PRK03624
putative acetyltransferase; Provisional
172-226 6.58e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.06  E-value: 6.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002239292 172 VYELQMVPSAQGKGLGKFLMELIE--LIA--CKSqmgaVMLTVQKANNLAMAFYKKLRY 226
Cdd:PRK03624   71 AYYLAVHPDFRGRGIGRALVARLEkkLIArgCPK----INLQVREDNDAVLGFYEALGY 125
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
155-245 6.54e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.44  E-value: 6.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 155 GFVHYRFVLEEDVpvVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKLRYVISSTSPS 234
Cdd:COG0456     1 GFALLGLVDGGDE--AEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
                          90
                  ....*....|..
gi 1002239292 235 -RVDPLIGLEKN 245
Cdd:COG0456    79 yYGDDALVMEKE 90
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
147-224 8.84e-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: 55.22  E-value: 8.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002239292 147 ACNEDRLIGFVHYRFVLEEDvPVVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKL 224
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDEP-PVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKL 114
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
132-238 7.71e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.13  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 132 QNIMKQDSGLEFTHEACNeDRLIGFVHYRFVleeDVPVVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQ 211
Cdd:COG0454    25 KAMEGSLAGAEFIAVDDK-GEPIGFAGLRRL---DDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTL 100
                          90       100
                  ....*....|....*....|....*..
gi 1002239292 212 KANNLAMAFYKKLRYVISSTSPSRVDP 238
Cdd:COG0454   101 DGNPAAIRFYERLGFKEIERYVAYVGG 127
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
147-238 2.65e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.62  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 147 ACNEDRLIGFVHY-RFVLEEDVPVVYVYELqMV-PSAQGKGLGKFLMELIELIACKSQMGAVMLTvqkANNLAMAFYKKL 224
Cdd:COG3153    44 AEDDGEIVGHVALsPVDIDGEGPALLLGPL-AVdPEYRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERF 119
                          90
                  ....*....|....
gi 1002239292 225 RYVISSTSPSRVDP 238
Cdd:COG3153   120 GFRPAGELGLTLGP 133
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
147-233 1.02e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 50.38  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 147 ACNEDRLIGFVH---------YRFVLEEDVpvvYVyelqmVPSAQGKGLGKFLMEliELIA-CKSQ-MGAVMLTVQKANN 215
Cdd:COG1247    57 AEEDGEVVGFASlgpfrprpaYRGTAEESI---YV-----DPDARGRGIGRALLE--ALIErARARgYRRLVAVVLADNE 126
                          90
                  ....*....|....*...
gi 1002239292 216 LAMAFYKKLRYVISSTSP 233
Cdd:COG1247   127 ASIALYEKLGFEEVGTLP 144
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
147-224 1.03e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.60  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 147 ACNEDRLIGFVHYRFVLEEDvpvvYVYELQMV--PSAQGKGLGKFLMELIELIACKSQMGAVMLTVqkaNNLAMAFYKKL 224
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEG----ALAELRLAvhPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKL 80
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
147-209 5.60e-06

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: 43.03  E-value: 5.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002239292 147 ACNEDRLIGFVHYRFVLEEDvPVVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLT 209
Cdd:cd04301     4 AEDDGEIVGFASLSPDGSGG-DTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
151-246 2.31e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 43.09  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 151 DRLIGFVHYRFVLEEdvpvVYVYELQMVPSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKANNLAMAFYKKLRYVIss 230
Cdd:TIGR01575  40 GKVVGYAGVQIVLDE----AHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNE-- 113
                          90
                  ....*....|....*.
gi 1002239292 231 tspsrvdplIGLEKNY 246
Cdd:TIGR01575 114 ---------IAIRRNY 120
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
150-224 2.90e-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: 39.98  E-value: 2.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002239292 150 EDRLIGFVHYRFVLEEdvpvvyVYELQMV---PSAQGKGLGKFLMELIELIACKSQMGAVMLTvqkANNLAMAFYKKL 224
Cdd:COG1246    36 DGEIVGCAALHPLDED------LAELRSLavhPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKL 104
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
147-230 2.83e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.09  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239292 147 ACNEDRLIGFVhyRFVLEEDvpvvYVYELQMV---PSAQGKGLGKFLMELIELIACKSQMGAVMLTVQKAnnlAMAFYKK 223
Cdd:COG2153    39 AYDDGELVATA--RLLPPGD----GEAKIGRVavlPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEK 109

                  ....*..
gi 1002239292 224 LRYVISS 230
Cdd:COG2153   110 LGFVPVG 116
PRK13740 PRK13740
conjugal transfer relaxosome protein TraY;
32-58 3.36e-03

conjugal transfer relaxosome protein TraY;


Pssm-ID: 184292  Cd Length: 70  Bit Score: 35.53  E-value: 3.36e-03
                          10        20
                  ....*....|....*....|....*..
gi 1002239292  32 GRKKAVEELIRkavaVKDHLAQFPDFH 58
Cdd:PRK13740   34 GRSKTNEVQIR----LRDHLKRFPDFY 56
PRK03624 PRK03624
putative acetyltransferase; Provisional
172-226 6.58e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.06  E-value: 6.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002239292 172 VYELQMVPSAQGKGLGKFLMELIE--LIA--CKSqmgaVMLTVQKANNLAMAFYKKLRY 226
Cdd:PRK03624   71 AYYLAVHPDFRGRGIGRALVARLEkkLIArgCPK----INLQVREDNDAVLGFYEALGY 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH