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Conserved domains on  [gi|1032278285|gb|OAO92613|]
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hypothetical protein AXX17_AT5G54750 [Arabidopsis thaliana]

Protein Classification

N-acetyltransferase( domain architecture ID 10140595)

N-acetyltransferase catalyzes the transfer of the acetyl group from acetyl coenzyme A donor to a substrate; contains Tudor-like Agenet domains, Jas domain(s) which in plant transcriptional repressors bind Groucho/Tup1-type co-repressor TOPLESS (TPL) and TPL-related proteins (TPRs), and plant homeodomain (PHD) finger(s) which bind zinc and may be involved in protein-protein interaction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 85-214 2.31e-76

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240072  Cd Length: 130  Bit Score: 238.11  E-value: 2.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  85 FCRNGTTIGVQSFVFVLSKGEDRYVAYLEDMYEDKRGLKKVKVRWFHYTKEVKGAVALKNPNPKEVFITPHSQVISAECV 164
Cdd:cd04721     1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDSVNPREIFLSPNLQVISVECI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032278285 165 DGPATVLTREHYEECVASFPNSLLARVHMCYRQLRNSKVKPFDLSKLRGY 214
Cdd:cd04721    81 DGLATVLTREHYEKFQSVPKNSSELQAYFCYRQIDNNKVKPFDITQLRGY 130
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
 309-381 1.48e-12

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


:

Pssm-ID: 461700  Cd Length: 61  Bit Score: 62.72  E-value: 1.48e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032278285 309 KIEFLCQDSGIRGCWFRCTVLDV-SRKQVKLQYDDIEDEDGYGNLEEWVPAFKsampdklgirlsnrptIRPAP 381
Cdd:pfam05641   3 KVEVLSDEEGFRGAWFRAKVIKVlKGDKYLVEYDDLLDEDGGGPLEEWVPASD----------------IRPCP 60
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 390-447 5.40e-11

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


:

Pssm-ID: 214798  Cd Length: 59  Bit Score: 58.10  E-value: 5.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  390 DLTIGEAVDAWWNDGWWEGVVIAtgKPDTEDLKIYIPG--ENLCLTVLRKDIRISRDWVG 447
Cdd:smart00743   2 DFKEGDRVEVFSEDSWWEAVVTK--VLGDGKYLVEYKGesEPLELTVDWSDLRPHPPWVD 59
 
Name Accession Description Interval E-value
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 85-214 2.31e-76

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240072  Cd Length: 130  Bit Score: 238.11  E-value: 2.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  85 FCRNGTTIGVQSFVFVLSKGEDRYVAYLEDMYEDKRGLKKVKVRWFHYTKEVKGAVALKNPNPKEVFITPHSQVISAECV 164
Cdd:cd04721     1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDSVNPREIFLSPNLQVISVECI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032278285 165 DGPATVLTREHYEECVASFPNSLLARVHMCYRQLRNSKVKPFDLSKLRGY 214
Cdd:cd04721    81 DGLATVLTREHYEKFQSVPKNSSELQAYFCYRQIDNNKVKPFDITQLRGY 130
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
 309-381 1.48e-12

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


Pssm-ID: 461700  Cd Length: 61  Bit Score: 62.72  E-value: 1.48e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032278285 309 KIEFLCQDSGIRGCWFRCTVLDV-SRKQVKLQYDDIEDEDGYGNLEEWVPAFKsampdklgirlsnrptIRPAP 381
Cdd:pfam05641   3 KVEVLSDEEGFRGAWFRAKVIKVlKGDKYLVEYDDLLDEDGGGPLEEWVPASD----------------IRPCP 60
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 390-447 5.40e-11

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 58.10  E-value: 5.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  390 DLTIGEAVDAWWNDGWWEGVVIAtgKPDTEDLKIYIPG--ENLCLTVLRKDIRISRDWVG 447
Cdd:smart00743   2 DFKEGDRVEVFSEDSWWEAVVTK--VLGDGKYLVEYKGesEPLELTVDWSDLRPHPPWVD 59
BAH smart00439
Bromo adjacent homology domain;
91-180 5.35e-09

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 54.22  E-value: 5.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285   91 TIGVQSFVFVL--SKGEDRYVAYLEDMYEDKRG--LKKVKVRWFHYTKEVKGAVAlKNPNPKEVFITPHSQVISAECVDG 166
Cdd:smart00439   1 TISVGDFVLVEpdDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKA-ALFDKNEVFLSDEYDTVPLSDIIG 79

                           90
                   ....*....|....
gi 1032278285  167 PATVLTREHYEECV 180
Cdd:smart00439  80 KCNVLYKSDYPGLR 93
Tudor_Agenet_AtDUF_rpt1_3 cd20405
first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 ...
 305-381 6.99e-08

first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the first and third Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410476  Cd Length: 65  Bit Score: 49.56  E-value: 6.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032278285 305 KTDAKIEFLCQDSGIRGCWFRCTVLDVS--RKQVKLQYDDIEDEDGYGNLEEWVPAfksampdklgirlsnrPTIRPAP 381
Cdd:cd20405     2 SKGTEVEVSSEEEGFRGSWYRAIVVKEPegEKKFLVKYDELLLDDGSEPLEETVDL----------------RRVRPVP 64
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 91-179 1.57e-07

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 50.00  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  91 TIGVQSFVFVLSKGEDR--YVAYLEDMYED-KRGLKKVKVRWFhYTKEVKGAVALKNPNPKEVFITPHSQVISAECVDGP 167
Cdd:pfam01426   2 TYSVGDFVLVEPDDADEpyYVARIEELFEDtKNGKKMVRVQWF-YRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                          90
                  ....*....|..
gi 1032278285 168 ATVLTREHYEEC 179
Cdd:pfam01426  81 CSVLHKSDLESL 92
Tudor_Agenet_AtDUF_rpt2_4 cd20406
second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 ...
 393-412 1.78e-03

second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the second and fourth Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410477  Cd Length: 47  Bit Score: 36.42  E-value: 1.78e-03
                          10        20
                  ....*....|....*....|
gi 1032278285 393 IGEAVDAWWNDGWWEGVVIA 412
Cdd:cd20406     1 LGDKVDAFYNGGWWPGVVTK 20
 
Name Accession Description Interval E-value
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 85-214 2.31e-76

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240072  Cd Length: 130  Bit Score: 238.11  E-value: 2.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  85 FCRNGTTIGVQSFVFVLSKGEDRYVAYLEDMYEDKRGLKKVKVRWFHYTKEVKGAVALKNPNPKEVFITPHSQVISAECV 164
Cdd:cd04721     1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDSVNPREIFLSPNLQVISVECI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032278285 165 DGPATVLTREHYEECVASFPNSLLARVHMCYRQLRNSKVKPFDLSKLRGY 214
Cdd:cd04721    81 DGLATVLTREHYEKFQSVPKNSSELQAYFCYRQIDNNKVKPFDITQLRGY 130
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 89-196 1.14e-12

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 64.73  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  89 GTTIGVQSFVFVLSKG--EDRYVAYLEDMYEDKRGLKKVKVRWFHYTKEVKGAvalKNPN--PKEVFITPHSQVISAECV 164
Cdd:cd04714     1 KEIIRVGDCVLFKSPGrpSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGG---RKPNhgEKELFASDHQDENSVQTI 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1032278285 165 DGPATVLTREHYEECVASfpNSLLARVHMCYR 196
Cdd:cd04714    78 EHKCYVLTFAEYERLARV--KKKPQDGVDFYY 107
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
 309-381 1.48e-12

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


Pssm-ID: 461700  Cd Length: 61  Bit Score: 62.72  E-value: 1.48e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032278285 309 KIEFLCQDSGIRGCWFRCTVLDV-SRKQVKLQYDDIEDEDGYGNLEEWVPAFKsampdklgirlsnrptIRPAP 381
Cdd:pfam05641   3 KVEVLSDEEGFRGAWFRAKVIKVlKGDKYLVEYDDLLDEDGGGPLEEWVPASD----------------IRPCP 60
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 390-447 5.40e-11

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 58.10  E-value: 5.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  390 DLTIGEAVDAWWNDGWWEGVVIAtgKPDTEDLKIYIPG--ENLCLTVLRKDIRISRDWVG 447
Cdd:smart00743   2 DFKEGDRVEVFSEDSWWEAVVTK--VLGDGKYLVEYKGesEPLELTVDWSDLRPHPPWVD 59
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 77-170 3.86e-10

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240064  Cd Length: 146  Bit Score: 58.25  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  77 KQLKHYPSFCRNGTTIGVQSFV-FVLSKGEDRYVAYLEDMYEDKRGLKKVKVRWFHYTKEV--KGAVALKNPNPKEVFIT 153
Cdd:cd04713     6 KKKCHYTSFEKDGNKYRLEDCVlLVPEDDQKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIekKKGGNWKAEDPRELFYS 85

                          90
                  ....*....|....*..
gi 1032278285 154 PHSQVISAECVDGPATV 170
Cdd:cd04713    86 FHRDEVPAESVLHPCKV 102
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 89-178 8.30e-10

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 56.63  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  89 GTTIGVQSFVFVLS----KGEDRYVAYLEDMYEDKRGLKKVKVRWF-HYTKEVKGAVALKNPNpkEVFITPHSQVISAEC 163
Cdd:cd04370     1 GITYEVGDSVYVEPddsiKSDPPYIARIEELWEDTNGSKQVKVRWFyRPEETPKGLSPFALRR--ELFLSDHLDEIPVES 78

                          90
                  ....*....|....*
gi 1032278285 164 VDGPATVLTREHYEE 178
Cdd:cd04370    79 IIGKCKVLFVSEFEG 93
BAH smart00439
Bromo adjacent homology domain;
91-180 5.35e-09

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 54.22  E-value: 5.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285   91 TIGVQSFVFVL--SKGEDRYVAYLEDMYEDKRG--LKKVKVRWFHYTKEVKGAVAlKNPNPKEVFITPHSQVISAECVDG 166
Cdd:smart00439   1 TISVGDFVLVEpdDADEPYYIGRIEEIFETKKNseSKMVRVRWFYRPEETVLEKA-ALFDKNEVFLSDEYDTVPLSDIIG 79

                           90
                   ....*....|....
gi 1032278285  167 PATVLTREHYEECV 180
Cdd:smart00439  80 KCNVLYKSDYPGLR 93
Tudor_Agenet_AtDUF_rpt1_3 cd20405
first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 ...
 305-381 6.99e-08

first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the first and third Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410476  Cd Length: 65  Bit Score: 49.56  E-value: 6.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032278285 305 KTDAKIEFLCQDSGIRGCWFRCTVLDVS--RKQVKLQYDDIEDEDGYGNLEEWVPAfksampdklgirlsnrPTIRPAP 381
Cdd:cd20405     2 SKGTEVEVSSEEEGFRGSWYRAIVVKEPegEKKFLVKYDELLLDDGSEPLEETVDL----------------RRVRPVP 64
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 91-179 1.57e-07

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 50.00  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  91 TIGVQSFVFVLSKGEDR--YVAYLEDMYED-KRGLKKVKVRWFhYTKEVKGAVALKNPNPKEVFITPHSQVISAECVDGP 167
Cdd:pfam01426   2 TYSVGDFVLVEPDDADEpyYVARIEELFEDtKNGKKMVRVQWF-YRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                          90
                  ....*....|..
gi 1032278285 168 ATVLTREHYEEC 179
Cdd:pfam01426  81 CSVLHKSDLESL 92
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 99-204 6.85e-04

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240070  Cd Length: 128  Bit Score: 40.05  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032278285  99 FVLSKGEDR---YVAYLEDMYED---KRGLKKVKVRWFHYTKEV---KGAVALKNPNPKEVFITPHSQV---ISAECVDG 166
Cdd:cd04719     9 FVLIEGEDAdgpDVARILHLYEDgneDDDPKRAIVQWFSRPSEVpknKRKLLGREPHSQEVFFYSRSSCdndIDAETIIG 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1032278285 167 PATVLTREHYEEcvasFPNSLLA-RVHMCYRQLRNSKVK 204
Cdd:cd04719    89 KVRVEPVEPKTD----LPETKKKtGGPLFVKRYWDTKTF 123
Tudor_Agenet_AtDUF_rpt2_4 cd20406
second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 ...
 393-412 1.78e-03

second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the second and fourth Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410477  Cd Length: 47  Bit Score: 36.42  E-value: 1.78e-03
                          10        20
                  ....*....|....*....|
gi 1032278285 393 IGEAVDAWWNDGWWEGVVIA 412
Cdd:cd20406     1 LGDKVDAFYNGGWWPGVVTK 20
 
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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