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Conserved domains on  [gi|1046863624|ref|XP_017455617|]
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CCR4-NOT transcription complex subunit 7 isoform X1 [Rattus norvegicus]

Protein Classification

CAF1 family ribonuclease( domain architecture ID 581404)

CAF1 family ribonuclease such as Xenopus laevis CCR4-NOT transcription complex subunit 7 and Arabidopsis thaliana probable CCR4-associated factor 1 homolog

CATH:  3.30.420.10
EC:  3.1.13.-
SCOP:  4001124

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAF1 super family cl23804
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
1-292 7.48e-115

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


The actual alignment was detected with superfamily member COG5228:

Pssm-ID: 474062  Cd Length: 299  Bit Score: 333.04  E-value: 7.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624   1 MPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLG 78
Cdd:COG5228     7 MPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  79 LTFMNEQGEYPPGTSTWQFNFKFNLTsgtalgpgnpyfwEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGV 158
Cdd:COG5228    87 LSLSDENGNKPNGPSTWQFNFEFDLK-------------KDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 159 VLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQH 238
Cdd:COG5228   154 VMDESVTWITFHSAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQH 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046863624 239 QAGSDSLLTGMAFFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 292
Cdd:COG5228   234 QAGSDALLTADEFFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
 
Name Accession Description Interval E-value
POP2 COG5228
mRNA deadenylase subunit [RNA processing and modification];
1-292 7.48e-115

mRNA deadenylase subunit [RNA processing and modification];


Pssm-ID: 227553  Cd Length: 299  Bit Score: 333.04  E-value: 7.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624   1 MPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLG 78
Cdd:COG5228     7 MPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  79 LTFMNEQGEYPPGTSTWQFNFKFNLTsgtalgpgnpyfwEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGV 158
Cdd:COG5228    87 LSLSDENGNKPNGPSTWQFNFEFDLK-------------KDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 159 VLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQH 238
Cdd:COG5228   154 VMDESVTWITFHSAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQH 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046863624 239 QAGSDSLLTGMAFFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 292
Cdd:COG5228   234 QAGSDALLTADEFFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
15-251 8.97e-10

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


Pssm-ID: 461457  Cd Length: 375  Bit Score: 58.96  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  15 VWACNLDEEMKKIRQVIRKYNYVAMDTEFPGV--VARPIGEFRSNADYqYQLLRCNVDLLKIIQLGLTFM---NEQGEY- 88
Cdd:pfam04857   1 VTRSNFKELLPEILKAIKEADFVAIDLEFTGLgsPWRKSSLFDTPEER-YLKLRDAAERFSILQFGLCCFredEEKSKYt 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  89 -----------PPG---------TSTWQF----NFKFN--LTSG------------------------------------ 106
Cdd:pfam04857  80 akpynfylfprTELdpdrdfscqASSLQFlakhGFDFNklFYEGipylsraeeeklrerleerqqaspsdiplldvedke 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 107 --------------------TALGPGNPYFWEDMYAQ-------------DSIELLTTSGIQFKKHEEEGIETQYFAELL 153
Cdd:pfam04857 160 fvervrskikewldsgedkgEKLNIDNPVSRLLLQQLlkhqlvrvllvelLSRGKQKVVQVVKKSSEDEELLEKEEKKDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 154 MTSGVVLCEGV-----------KWLSFHSG-YDFGYLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG 221
Cdd:pfam04857 240 EEERLESAVGFrlvfdalsksrKPIVGHNGlLDLLFLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVR 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046863624 222 -----LQEVAEQLELER----------------------IGPQHQAGSDSLLTGMAF 251
Cdd:pfam04857 319 lpsssLEELFEKLCKENfsspsvetppfesdyhdesskyGGKAHEAGYDAYMTGYVF 375
 
Name Accession Description Interval E-value
POP2 COG5228
mRNA deadenylase subunit [RNA processing and modification];
1-292 7.48e-115

mRNA deadenylase subunit [RNA processing and modification];


Pssm-ID: 227553  Cd Length: 299  Bit Score: 333.04  E-value: 7.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624   1 MPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLG 78
Cdd:COG5228     7 MPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  79 LTFMNEQGEYPPGTSTWQFNFKFNLTsgtalgpgnpyfwEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGV 158
Cdd:COG5228    87 LSLSDENGNKPNGPSTWQFNFEFDLK-------------KDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 159 VLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQH 238
Cdd:COG5228   154 VMDESVTWITFHSAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQH 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046863624 239 QAGSDSLLTGMAFFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 292
Cdd:COG5228   234 QAGSDALLTADEFFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
15-251 8.97e-10

CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localizes to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain pfam01424. This family of proteins is related to other exonucleases pfam00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 has been resolved at 2.3 Angstrom resolution.


Pssm-ID: 461457  Cd Length: 375  Bit Score: 58.96  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  15 VWACNLDEEMKKIRQVIRKYNYVAMDTEFPGV--VARPIGEFRSNADYqYQLLRCNVDLLKIIQLGLTFM---NEQGEY- 88
Cdd:pfam04857   1 VTRSNFKELLPEILKAIKEADFVAIDLEFTGLgsPWRKSSLFDTPEER-YLKLRDAAERFSILQFGLCCFredEEKSKYt 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624  89 -----------PPG---------TSTWQF----NFKFN--LTSG------------------------------------ 106
Cdd:pfam04857  80 akpynfylfprTELdpdrdfscqASSLQFlakhGFDFNklFYEGipylsraeeeklrerleerqqaspsdiplldvedke 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 107 --------------------TALGPGNPYFWEDMYAQ-------------DSIELLTTSGIQFKKHEEEGIETQYFAELL 153
Cdd:pfam04857 160 fvervrskikewldsgedkgEKLNIDNPVSRLLLQQLlkhqlvrvllvelLSRGKQKVVQVVKKSSEDEELLEKEEKKDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046863624 154 MTSGVVLCEGV-----------KWLSFHSG-YDFGYLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG 221
Cdd:pfam04857 240 EEERLESAVGFrlvfdalsksrKPIVGHNGlLDLLFLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVR 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046863624 222 -----LQEVAEQLELER----------------------IGPQHQAGSDSLLTGMAF 251
Cdd:pfam04857 319 lpsssLEELFEKLCKENfsspsvetppfesdyhdesskyGGKAHEAGYDAYMTGYVF 375
 
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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