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Conserved domains on  [gi|1720354853|ref|XP_030109152|]
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nonsense-mediated mRNA decay factor SMG7 isoform X5 [Mus musculus]

Protein Classification

EST1 family protein( domain architecture ID 12105293)

EST1 family protein similar to Saccharomyces cerevisiae telomere elongation protein EST1 that associates with telomerase and is directly involved in telomere replication

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
 179-438 1.98e-58

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


:

Pssm-ID: 431239  Cd Length: 279  Bit Score: 202.64  E-value: 1.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  179 AESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKAL------------ESRD 246
Cdd:pfam10373    1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRskleqgelklspESLQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  247 ELKTKWGVSDFIKAFIKFHGHVYLSKSL----EKLSPLREKLEEQFK-RLLFQKAFNSQQLVHVTVINLFQLHHLRDFSN 321
Cdd:pfam10373   81 EGTPGDLLERLISLFLYLHGKLYTPTDFsefpELEDEVLKKLEILLKeSLLSRYLKSRSLLLKMLLINIFAFENAKDKSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  322 ETEqhsysqDEQLCWTQLLALFMSFLGILCKCPLQNDSQES---NNAYPLPAVKVSMDWLRLRPRVFQ-----EAVVDER 393
Cdd:pfam10373  161 PEE------TKQFLLRLALRFFFTLFGLLLEEVNTLEALKSftpVATRYLPALRVYLCWLKSNPSVLEfedkdEKLVDSL 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354853  394 QYIWPWLIS--LLNSFHPREDDLSNTnaTPLPEEFELQGFLALRPSF 438
Cdd:pfam10373  235 SDLWNELLSstLLNSSFDVEKRPKRD--YLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
 63-175 4.47e-16

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


:

Pssm-ID: 463062  Cd Length: 98  Bit Score: 74.65  E-value: 4.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853   63 KVEQDLWNHA-------FKNQITTLQGQAKNRANPN-RSEVQANLSLFLEAASGFYTQLLQELCTvfnvdlpcrvkssql 134
Cdd:pfam10374    1 KVLDLLWRKThypiikwFRKWRKRLDGNSKKKKYPVeFRKLNSKLRKFLKSAQKFYYGLIQRLVS--------------- 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720354853  135 giisnKQTHSStivkpQSSSCSYICQHCLVHLGDIARYRNQ 175
Cdd:pfam10374   66 -----REASSS-----LTALALLSCHRCLIYLGDLHRYREL 96
 
Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
 179-438 1.98e-58

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


Pssm-ID: 431239  Cd Length: 279  Bit Score: 202.64  E-value: 1.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  179 AESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKAL------------ESRD 246
Cdd:pfam10373    1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRskleqgelklspESLQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  247 ELKTKWGVSDFIKAFIKFHGHVYLSKSL----EKLSPLREKLEEQFK-RLLFQKAFNSQQLVHVTVINLFQLHHLRDFSN 321
Cdd:pfam10373   81 EGTPGDLLERLISLFLYLHGKLYTPTDFsefpELEDEVLKKLEILLKeSLLSRYLKSRSLLLKMLLINIFAFENAKDKSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  322 ETEqhsysqDEQLCWTQLLALFMSFLGILCKCPLQNDSQES---NNAYPLPAVKVSMDWLRLRPRVFQ-----EAVVDER 393
Cdd:pfam10373  161 PEE------TKQFLLRLALRFFFTLFGLLLEEVNTLEALKSftpVATRYLPALRVYLCWLKSNPSVLEfedkdEKLVDSL 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354853  394 QYIWPWLIS--LLNSFHPREDDLSNTnaTPLPEEFELQGFLALRPSF 438
Cdd:pfam10373  235 SDLWNELLSstLLNSSFDVEKRPKRD--YLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
 63-175 4.47e-16

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


Pssm-ID: 463062  Cd Length: 98  Bit Score: 74.65  E-value: 4.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853   63 KVEQDLWNHA-------FKNQITTLQGQAKNRANPN-RSEVQANLSLFLEAASGFYTQLLQELCTvfnvdlpcrvkssql 134
Cdd:pfam10374    1 KVLDLLWRKThypiikwFRKWRKRLDGNSKKKKYPVeFRKLNSKLRKFLKSAQKFYYGLIQRLVS--------------- 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720354853  135 giisnKQTHSStivkpQSSSCSYICQHCLVHLGDIARYRNQ 175
Cdd:pfam10374   66 -----REASSS-----LTALALLSCHRCLIYLGDLHRYREL 96
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
163-302 1.35e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKAL 242
Cdd:COG0457     79 LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLG 158

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  243 ESRDELKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQL 302
Cdd:COG0457    159 RYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAA 218
 
Name Accession Description Interval E-value
EST1_DNA_bind pfam10373
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ...
 179-438 1.98e-58

Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1.


Pssm-ID: 431239  Cd Length: 279  Bit Score: 202.64  E-value: 1.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  179 AESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKAL------------ESRD 246
Cdd:pfam10373    1 ALRYYLLAILLLPSNGEPYNQLGVIALYVGNHLDAVYYFLRSLLSRNPFPTAKNNLELLFDKIRskleqgelklspESLQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  247 ELKTKWGVSDFIKAFIKFHGHVYLSKSL----EKLSPLREKLEEQFK-RLLFQKAFNSQQLVHVTVINLFQLHHLRDFSN 321
Cdd:pfam10373   81 EGTPGDLLERLISLFLYLHGKLYTPTDFsefpELEDEVLKKLEILLKeSLLSRYLKSRSLLLKMLLINIFAFENAKDKSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  322 ETEqhsysqDEQLCWTQLLALFMSFLGILCKCPLQNDSQES---NNAYPLPAVKVSMDWLRLRPRVFQ-----EAVVDER 393
Cdd:pfam10373  161 PEE------TKQFLLRLALRFFFTLFGLLLEEVNTLEALKSftpVATRYLPALRVYLCWLKSNPSVLEfedkdEKLVDSL 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720354853  394 QYIWPWLIS--LLNSFHPREDDLSNTnaTPLPEEFELQGFLALRPSF 438
Cdd:pfam10373  235 SDLWNELLSstLLNSSFDVEKRPKRD--YLLEEDVELKGFSPLGYRL 279
EST1 pfam10374
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ...
 63-175 4.47e-16

Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat.


Pssm-ID: 463062  Cd Length: 98  Bit Score: 74.65  E-value: 4.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853   63 KVEQDLWNHA-------FKNQITTLQGQAKNRANPN-RSEVQANLSLFLEAASGFYTQLLQELCTvfnvdlpcrvkssql 134
Cdd:pfam10374    1 KVLDLLWRKThypiikwFRKWRKRLDGNSKKKKYPVeFRKLNSKLRKFLKSAQKFYYGLIQRLVS--------------- 65

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720354853  135 giisnKQTHSStivkpQSSSCSYICQHCLVHLGDIARYRNQ 175
Cdd:pfam10374   66 -----REASSS-----LTALALLSCHRCLIYLGDLHRYREL 96
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
163-302 1.35e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKAL 242
Cdd:COG0457     79 LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLG 158

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720354853  243 ESRDELKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQL 302
Cdd:COG0457    159 RYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAA 218
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 163-241 2.44e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 42.30  E-value: 2.44e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVkFPFPAASTNLQKALSKA 241
Cdd:COG4235     54 LLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL-LPADAPARLLEASIAEA 131
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 163-241 6.17e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.33  E-value: 6.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKA 241
Cdd:COG4783     41 FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRAL 119
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 169-241 1.15e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.71  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720354853  169 IARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKA 241
Cdd:COG5010     63 LYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
162-240 1.29e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 1.29e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720354853  162 CLVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSK 240
Cdd:COG0457     10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
169-210 2.37e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.23  E-value: 2.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720354853  169 IARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDH 210
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRY 42
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 163-210 5.20e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 5.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDH 210
Cdd:COG5010     91 YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQD 138
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
163-240 6.75e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.60  E-value: 6.75e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720354853  163 LVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSK 240
Cdd:COG0457     45 LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLE 122
 
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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