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Conserved domains on  [gi|763825657|gb|AJQ32057|]
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Sgf29p [Saccharomyces cerevisiae YJM1381]

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. ...
 127-250 4.02e-52

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: 165.83  E-value: 4.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763825657  127 VGSEVAYKPRRG--SADGEWIQCEVLKVVADGTRFEVRDPEPDElGNSGKVYKCNWKELLLIPPGFPT----KNYPPGTK 200
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDE-GKGQKRYKLSRKQIIPLPKWKANpstdPLFPKGTK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 763825657  201 VLARYPETTTFYPAIVIGT--KRDGTCRLRFDGEEEVDKETEVTRRLVLPSP 250
Cdd:pfam07039  80 VLALYPDTTTFYRAEVVSPpkKKDGTYRLKFEDDEDADPLREVPRRYVVPFP 131
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 127-250 4.02e-52

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: 165.83  E-value: 4.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763825657  127 VGSEVAYKPRRG--SADGEWIQCEVLKVVADGTRFEVRDPEPDElGNSGKVYKCNWKELLLIPPGFPT----KNYPPGTK 200
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDE-GKGQKRYKLSRKQIIPLPKWKANpstdPLFPKGTK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 763825657  201 VLARYPETTTFYPAIVIGT--KRDGTCRLRFDGEEEVDKETEVTRRLVLPSP 250
Cdd:pfam07039  80 VLALYPDTTTFYRAEVVSPpkKKDGTYRLKFEDDEDADPLREVPRRYVVPFP 131
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 195-248 1.13e-18

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: 77.27  E-value: 1.13e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 763825657 195 YPPGTKVLARYPETTTFYPAIVIG--TKRDGTCRLRFDGEEEVD---KETEVTRRLVLP 248
Cdd:cd20394    1 FPKGTRVLALYPQTTCFYPATVVSppTRPSDDYSLLFEDDEYADgysPPREVPQRYVVA 59
 
Name Accession Description Interval E-value
DUF1325 pfam07039
SGF29 tudor-like domain; This domain is found in the yeast protein SAGA-associated factor 29. ...
 127-250 4.02e-52

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: 165.83  E-value: 4.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763825657  127 VGSEVAYKPRRG--SADGEWIQCEVLKVVADGTRFEVRDPEPDElGNSGKVYKCNWKELLLIPPGFPT----KNYPPGTK 200
Cdd:pfam07039   1 KGDEVAAKVKAKntDEEEEWILAEVVKYDGDTNRYEVQDIDPDE-GKGQKRYKLSRKQIIPLPKWKANpstdPLFPKGTK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 763825657  201 VLARYPETTTFYPAIVIGT--KRDGTCRLRFDGEEEVDKETEVTRRLVLPSP 250
Cdd:pfam07039  80 VLALYPDTTTFYRAEVVSPpkKKDGTYRLKFEDDEDADPLREVPRRYVVPFP 131
Tudor_SGF29_rpt2 cd20394
second Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 195-248 1.13e-18

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: 77.27  E-value: 1.13e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 763825657 195 YPPGTKVLARYPETTTFYPAIVIG--TKRDGTCRLRFDGEEEVD---KETEVTRRLVLP 248
Cdd:cd20394    1 FPKGTRVLALYPQTTCFYPATVVSppTRPSDDYSLLFEDDEYADgysPPREVPQRYVVA 59
Tudor_SGF29_rpt1 cd20393
first Tudor domain found in SAGA-associated factor 29 (SGF29) and similar proteins; SGF29, ...
 123-187 1.41e-15

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: 69.21  E-value: 1.41e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763825657 123 APILVGSEVAYK-PRRGSADGEWIQCEVLKVVADGTRFEVRDPEPDelGNSGKVYKCNWKELLLIP 187
Cdd:cd20393    1 YPLKPGDQVAARvKKEGEEEEEWILAEVVSYDPETNRYEVEDIDPE--GEGKKRYKLPRRRVIPLP 64
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 198-241 4.62e-06

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: 42.57  E-value: 4.62e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 763825657 198 GTKVLARYPETTTFYPAIVIGTKRDGTCRLRF-DGEEEVDKETEV 241
Cdd:cd04508    1 GDRVEAKWSDDGQWYPATVVAVNDDGKYTVLFdDGNEEEVSEDDI 45
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 197-230 7.50e-05

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. 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: 410454  Cd Length: 52  Bit Score: 39.56  E-value: 7.50e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 763825657 197 PGTKVLARYPETTTFYPAIVIGTKRDGTCRLRFD 230
Cdd:cd20383    1 VGTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFD 34
Tudor_ZGPAT cd20384
Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and ...
 197-235 2.56e-03

Tudor domain found in zinc finger CCCH-type with G patch domain-containing protein (ZGPAT) and similar proteins; ZGPAT, also called ZIP, G patch domain-containing protein 6 (GPATC6), GPATCH6, zinc finger CCCH domain-containing protein 9 (ZC3HDC9), ZC3H9, or zinc finger and G patch domain-containing protein, is a transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. It represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. It contains one Tudor domain. 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: 410455  Cd Length: 55  Bit Score: 35.28  E-value: 2.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 763825657 197 PGTKVLARYpETTTFYPAIVIGTKRDGTCRLRFDGEEEV 235
Cdd:cd20384    7 EGSRCLAKY-DDGLWYPATVTDIDEDGKYTVKFDSYGEV 44
 
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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