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Conserved domains on  [gi|295322082|pdb|3MEW|A]
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Chain A, SAGA-associated factor 29 homolog

Protein Classification

SAGA-associated factor 29 family protein( domain architecture ID 10537134)

SAGA-associated factor 29 family protein is a DUF1325 domain-containing protein; similar to Homo sapiens SAGA-associated factor 29, a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 30-159 1.00e-60

SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. This domain is related to members of the Tudor domain superfamily such as pfam05641. The SAGA complex is involved in RNA polymerase II-dependent transcriptional regulation. The membership of the tudor domain superfamily suggests this domain may bind to RNA.


:

Pssm-ID: 462071 [Multi-domain]  Cd Length: 131  Bit Score: 183.93  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MEW_A         30 PGDKVAARVKAV--DGDEQWILAEVVSYSHATNKYEVDDIDEE---GKERHTLSRRRVIPLPQWKANPETDPEalFQKEQ 104
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDegkGQKRYKLSRKQIIPLPKWKANPSTDPL--FPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3MEW_A        105 LVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADgysPPLNVAQRYVVAC 159
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDEDAD---PLREVPRRYVVPF 130
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 30-159 1.00e-60

SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. This domain is related to members of the Tudor domain superfamily such as pfam05641. The SAGA complex is involved in RNA polymerase II-dependent transcriptional regulation. The membership of the tudor domain superfamily suggests this domain may bind to RNA.


Pssm-ID: 462071 [Multi-domain]  Cd Length: 131  Bit Score: 183.93  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MEW_A         30 PGDKVAARVKAV--DGDEQWILAEVVSYSHATNKYEVDDIDEE---GKERHTLSRRRVIPLPQWKANPETDPEalFQKEQ 104
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDegkGQKRYKLSRKQIIPLPKWKANPSTDPL--FPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3MEW_A        105 LVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADgysPPLNVAQRYVVAC 159
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDEDAD---PLREVPRRYVVPF 130
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 100-159 3.76e-33

second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, also called coiled-coil domain-containing protein 101, or SAGA complex-associated factor 29, is a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes, like the TFTC-HAT, ATAC or STAGA complexes. It specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). SGF29 contains two Tudor domains. The model corresponds to the second one. 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: 410465  Cd Length: 60  Bit Score: 111.55  E-value: 3.76e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
3MEW_A      100 FQKEQLVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVAC 159
Cdd:cd20394   1 FPKGTRVLALYPQTTCFYPATVVSPPTRPSDDYSLLFEDDEYADGYSPPREVPQRYVVAL 60
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 30-159 1.00e-60

SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. This domain is related to members of the Tudor domain superfamily such as pfam05641. The SAGA complex is involved in RNA polymerase II-dependent transcriptional regulation. The membership of the tudor domain superfamily suggests this domain may bind to RNA.


Pssm-ID: 462071 [Multi-domain]  Cd Length: 131  Bit Score: 183.93  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MEW_A         30 PGDKVAARVKAV--DGDEQWILAEVVSYSHATNKYEVDDIDEE---GKERHTLSRRRVIPLPQWKANPETDPEalFQKEQ 104
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDegkGQKRYKLSRKQIIPLPKWKANPSTDPL--FPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
3MEW_A        105 LVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADgysPPLNVAQRYVVAC 159
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDEDAD---PLREVPRRYVVPF 130
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 100-159 3.76e-33

second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, also called coiled-coil domain-containing protein 101, or SAGA complex-associated factor 29, is a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes, like the TFTC-HAT, ATAC or STAGA complexes. It specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). SGF29 contains two Tudor domains. The model corresponds to the second one. 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: 410465  Cd Length: 60  Bit Score: 111.55  E-value: 3.76e-33
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
3MEW_A      100 FQKEQLVLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVAC 159
Cdd:cd20394   1 FPKGTRVLALYPQTTCFYPATVVSPPTRPSDDYSLLFEDDEYADGYSPPREVPQRYVVAL 60
Tudor_SGF29_rpt1 cd20393
first Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 26-89 4.94e-27

first Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, also called coiled-coil domain-containing protein 101, or SAGA complex-associated factor 29, is a chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes, like the TFTC-HAT, ATAC or STAGA complexes. It specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for the trimethylated form (H3K4me3). SGF29 contains two Tudor domains. The model corresponds to the first one. 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: 410464  Cd Length: 67  Bit Score: 96.18  E-value: 4.94e-27
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3MEW_A       26 YVARPGDKVAARVKAV-DGDEQWILAEVVSYSHATNKYEVDDIDEEG--KERHTLSRRRVIPLPQWK 89
Cdd:cd20393   1 YPLKPGDQVAARVKKEgEEEEEWILAEVVSYDPETNRYEVEDIDPEGegKKRYKLPRRRVIPLPTWA 67
 
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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