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Conserved domains on  [gi|665402492|ref|NP_001286673|]
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SAGA-associated factor 29kDa, isoform B [Drosophila melanogaster]

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. ...
 143-273 9.91e-55

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: 173.53  E-value: 9.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492  143 VGDNVAAL--AKGIDEEENWILAEVVQFLHRQNKYDVIDIDEEQKD---RHVLSKRKVIPLPLMRANPETDghALFPKDT 217
Cdd:pfam07039   1 KGDEVAAKvkAKNTDEEEEWILAEVVKYDGDTNRYEVQDIDPDEGKgqkRYKLSRKQIIPLPKWKANPSTD--PLFPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665402492  218 VVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSytngYAEPLP-VAQRYVIAYR 273
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDE----DADPLReVPRRYVVPFP 131
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-87 5.35e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492   2 PLTAESAAQQIQDRLKDIQQNIHNVDEERRRAENSIASLVRSLHATNQKVKPL---LKASLTEAAQEEATIRAALAKIHE 78
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarrIRALEQELAALEAELAELEKEIAE 94


                 ....*....
gi 665402492  79 IRSIRNERR 87
Cdd:COG4942   95 LRAELEAQK 103
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 143-273 9.91e-55

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: 173.53  E-value: 9.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492  143 VGDNVAAL--AKGIDEEENWILAEVVQFLHRQNKYDVIDIDEEQKD---RHVLSKRKVIPLPLMRANPETDghALFPKDT 217
Cdd:pfam07039   1 KGDEVAAKvkAKNTDEEEEWILAEVVKYDGDTNRYEVQDIDPDEGKgqkRYKLSRKQIIPLPKWKANPSTD--PLFPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665402492  218 VVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSytngYAEPLP-VAQRYVIAYR 273
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDE----DADPLReVPRRYVVPFP 131
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 213-272 1.67e-29

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: 106.16  E-value: 1.67e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492 213 FPKDTVVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSYTNGYAEPLPVAQRYVIAY 272
Cdd:cd20394    1 FPKGTRVLALYPQTTCFYPATVVSPPTRPSDDYSLLFEDDEYADGYSPPREVPQRYVVAL 60
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-87 5.35e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492   2 PLTAESAAQQIQDRLKDIQQNIHNVDEERRRAENSIASLVRSLHATNQKVKPL---LKASLTEAAQEEATIRAALAKIHE 78
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarrIRALEQELAALEAELAELEKEIAE 94


                 ....*....
gi 665402492  79 IRSIRNERR 87
Cdd:COG4942   95 LRAELEAQK 103
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 143-273 9.91e-55

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: 173.53  E-value: 9.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492  143 VGDNVAAL--AKGIDEEENWILAEVVQFLHRQNKYDVIDIDEEQKD---RHVLSKRKVIPLPLMRANPETDghALFPKDT 217
Cdd:pfam07039   1 KGDEVAAKvkAKNTDEEEEWILAEVVKYDGDTNRYEVQDIDPDEGKgqkRYKLSRKQIIPLPKWKANPSTD--PLFPKGT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 665402492  218 VVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSytngYAEPLP-VAQRYVIAYR 273
Cdd:pfam07039  79 KVLALYPDTTTFYRAEVVSPPKKKDGTYRLKFEDDE----DADPLReVPRRYVVPFP 131
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 213-272 1.67e-29

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: 106.16  E-value: 1.67e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492 213 FPKDTVVMALYPQTTCFYKAIVHRLPQTATEDYEVLFEDSSYTNGYAEPLPVAQRYVIAY 272
Cdd:cd20394    1 FPKGTRVLALYPQTTCFYPATVVSPPTRPSDDYSLLFEDDEYADGYSPPREVPQRYVVAL 60
Tudor_SGF29_rpt1 cd20393
first Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 139-202 2.65e-21

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: 85.00  E-value: 2.65e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665402492 139 YVAKVGDNVAAL-AKGIDEEENWILAEVVQFLHRQNKYDVIDIDEE--QKDRHVLSKRKVIPLPLMR 202
Cdd:cd20393    1 YPLKPGDQVAARvKKEGEEEEEWILAEVVSYDPETNRYEVEDIDPEgeGKKRYKLPRRRVIPLPTWA 67
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 217-251 2.46e-03

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 35.25  E-value: 2.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 665402492 217 TVVMALYPQTTCFYKAIVHRLPQTATedYEVLFED 251
Cdd:cd04508    2 DRVEAKWSDDGQWYPATVVAVNDDGK--YTVLFDD 34
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-87 5.35e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.82  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402492   2 PLTAESAAQQIQDRLKDIQQNIHNVDEERRRAENSIASLVRSLHATNQKVKPL---LKASLTEAAQEEATIRAALAKIHE 78
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarrIRALEQELAALEAELAELEKEIAE 94


                 ....*....
gi 665402492  79 IRSIRNERR 87
Cdd:COG4942   95 LRAELEAQK 103
 
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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