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Conserved domains on  [gi|1815499587|gb|QIE08218|]
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PCP-tevS-cNOT7 [Vector 2p_pSin-PCP-tevS-cNOT7-MS2]

Protein Classification

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 ...
140-419 1.08e-118

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: 348.06  E-value: 1.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 140 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 217
Cdd:COG5228     6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 218 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 297
Cdd:COG5228    86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 298 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 377
Cdd:COG5228   166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1815499587 378 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 419
Cdd:COG5228   246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
Phage_coat pfam09063
Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. ...
5-125 6.03e-74

Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. They adopt a secondary structure consisting of a six stranded beta sheet and an alpha helix.


:

Pssm-ID: 401125  Cd Length: 127  Bit Score: 227.37  E-value: 6.03e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587   5 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDSG------LPKVRY 78
Cdd:pfam09063   1 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCGtsvcgeLPKVRY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1815499587  79 TQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR 125
Cdd:pfam09063  81 TQVWSHDVTIVANSTEASRKSLYDLTKSLVAQAQSEDLVVNLVPLGR 127
 
Name Accession Description Interval E-value
POP2 COG5228
mRNA deadenylase subunit [RNA processing and modification];
140-419 1.08e-118

mRNA deadenylase subunit [RNA processing and modification];


Pssm-ID: 227553  Cd Length: 299  Bit Score: 348.06  E-value: 1.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 140 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 217
Cdd:COG5228     6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 218 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 297
Cdd:COG5228    86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 298 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 377
Cdd:COG5228   166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1815499587 378 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 419
Cdd:COG5228   246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
Phage_coat pfam09063
Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. ...
5-125 6.03e-74

Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. They adopt a secondary structure consisting of a six stranded beta sheet and an alpha helix.


Pssm-ID: 401125  Cd Length: 127  Bit Score: 227.37  E-value: 6.03e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587   5 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDSG------LPKVRY 78
Cdd:pfam09063   1 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCGtsvcgeLPKVRY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1815499587  79 TQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR 125
Cdd:pfam09063  81 TQVWSHDVTIVANSTEASRKSLYDLTKSLVAQAQSEDLVVNLVPLGR 127
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
158-378 1.46e-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: 62.43  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 158 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 228
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 229 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 303
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 304 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 360
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
                         250       260
                  ....*....|....*....|..
gi 1815499587 361 ----IGPQHQAGSDSLLTGMAF 378
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 375
 
Name Accession Description Interval E-value
POP2 COG5228
mRNA deadenylase subunit [RNA processing and modification];
140-419 1.08e-118

mRNA deadenylase subunit [RNA processing and modification];


Pssm-ID: 227553  Cd Length: 299  Bit Score: 348.06  E-value: 1.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 140 AMPAATVD--HSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQL 217
Cdd:COG5228     6 SMPPIFLDgpNYLFIRDVWKSNLYSEMAVIRQLISRYNHVSMDTEFPGVVARPIGTFKSSVDYHYQTLRANVDFLKIIQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 218 GLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFH 297
Cdd:COG5228    86 GLSLSDENGNKPNGPSTWQFNFEFDLKKDMYATESIELLRKSGIDFKKHENLGIDVFEFSELLMDSGLVMDESVTWITFH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 298 SGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMA 377
Cdd:COG5228   166 SAYDFGYLIKILTNDPLPNNKEDFYWWLHQYFPNFYDIKLVYKSVLNNSKGLQEIKNDLQLQRSGQQHQAGSDALLTADE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1815499587 378 FFKMREMFFEDHIDDAKYCgHLYGLG-SGSSYVQNGTGNAYEE 419
Cdd:COG5228   246 FFLPRFSIFTTSIGQSLLM-LLSGCQlSKLSLHKFPNGTDFAK 287
Phage_coat pfam09063
Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. ...
5-125 6.03e-74

Phage PP7 coat protein; Members of this family form the capsid of P. aeruginosa phage PP7. They adopt a secondary structure consisting of a six stranded beta sheet and an alpha helix.


Pssm-ID: 401125  Cd Length: 127  Bit Score: 227.37  E-value: 6.03e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587   5 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDSG------LPKVRY 78
Cdd:pfam09063   1 SKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCGtsvcgeLPKVRY 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1815499587  79 TQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR 125
Cdd:pfam09063  81 TQVWSHDVTIVANSTEASRKSLYDLTKSLVAQAQSEDLVVNLVPLGR 127
CAF1 pfam04857
CAF1 family ribonuclease; The major pathways of mRNA turnover in eukaryotes initiate with ...
158-378 1.46e-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: 62.43  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 158 CNLDEEMKKIRQVIRKYNYVAM--------DTEFPGVVARPIGEFRSNA-DYQYQLLRCNVDLLKIIQLGLTFMNEQGEY 228
Cdd:pfam04857 127 LSRAEEEKLRERLEERQQASPSdiplldveDKEFVERVRSKIKEWLDSGeDKGEKLNIDNPVSRLLLQQLLKHQLVRVLL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 229 PPGTSTWQFNFKFNLTEDMYAQDSIELlttsgIQFKKHEEEGIETQ----YFAELLMTSGvvlcegvKWLSFHSG-YDFG 303
Cdd:pfam04857 207 VELLSRGKQKVVQVVKKSSEDEELLEK-----EEKKDEEEERLESAvgfrLVFDALSKSR-------KPIVGHNGlLDLL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815499587 304 YLIKILtNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGG-----LQEVAEQLELER------------------ 360
Cdd:pfam04857 275 FLYQQF-YGPLPETLEEFKALIHELFPGIYDTKYLATTDAEFKVRlpsssLEELFEKLCKENfsspsvetppfesdyhde 353
                         250       260
                  ....*....|....*....|..
gi 1815499587 361 ----IGPQHQAGSDSLLTGMAF 378
Cdd:pfam04857 354 sskyGGKAHEAGYDAYMTGYVF 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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