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Conserved domains on  [gi|22026966|ref|NP_652027|]
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NAT1, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
W2_eIF4G1_like cd11559
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
744-890 4.73e-52

C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.


:

Pssm-ID: 211397  Cd Length: 134  Bit Score: 178.25  E-value: 4.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 744 YPLLKVQAEMLKQLQSDPNPNNFYKWIKANVDNKYYKDPGFIQALMTVVVKYVTkettladnldpkehPEKSVTQKEQQL 823
Cdd:cd11559   1 LPLLRVQAELLKLLQEDPNPDELYKWIKENVSPELYASPGFVRALMTAVLKYAI--------------EEKSLPEKEKAL 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22026966 824 LENYSQMLQTFLGQNE-LQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDK 890
Cdd:cd11559  67 LEKYAPLLQKYLDDDEqLQLQALYALQALVHTLEFPKGLLLRFFDALYDEDVIEEEAFLKWKEDVDPA 134
MIF4G pfam02854
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
1-173 5.71e-29

MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.


:

Pssm-ID: 397130  Cd Length: 203  Bit Score: 115.15  E-value: 5.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966     1 MYAQLCKRLSEEapsfdkepsNSSTFLRLLIAVCRDKFNNRLKRDENDnrpppeneadeeerrHLAKQRMLGNVKFIGEL 80
Cdd:pfam02854  54 AYARLCSGLNLR---------NPTDFGIHLLNRLQEEFEKRFELEENE---------------QGNRRRRLGLVRFLGEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    81 NKLDMLSKNVLHQCIMELFDKKKKRTAgtQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLER---RSKSSEYPP 157
Cdd:pfam02854 110 YKFGLLTEKILFECLKELLSSLTKEDL--KRDLFNLECLLTLLTTIGKLLENEKLPKLMDQFLDEIQKyvlSKDDPKLSS 187
                         170
                  ....*....|....*.
gi 22026966   158 RIRFMLKDVIELRQNN 173
Cdd:pfam02854 188 RLRFMLQDLIELRKNK 203
MA3 smart00544
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
558-671 7.98e-19

Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and/or regions similar to MIF4G domains Ponting (TIBS) "Novel eIF4G domain homologues" in press


:

Pssm-ID: 214714  Cd Length: 113  Bit Score: 82.68  E-value: 7.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    558 VSEVKEDAAIPVTTPDRFTKLVDGFLELKLPEKaLKDVCINLLMEVLDRvNDVFLERAVRLLQTLRKQSNIKPNIVVEIF 637
Cdd:smart00544   1 LKKKIFLIIEEYLSSGDTDEAVHCLLELKLPEQ-HHEVVKVLLTCALEE-KRTYREMYSVLLSRLCQANVISTKQFEKGF 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 22026966    638 KQVVNKMNEREALNPRIVSLVASLLAKTICEPAL 671
Cdd:smart00544  79 WRLLEDIEDLELDIPNAWRNLAEFVARLISDGIL 112
RAM super family cl21165
mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in ...
247-290 1.82e-04

mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 102 and 154 amino acids in length. There is a single completely conserved residue D that may be functionally important. RAM is a family of eukaryotic proteins that are an obligate component of the mammalian cap methyltransferase, RNMT (RNA guanine-7 methyltransferase). RAM consists of an N-terminal RNMT-activating domain and a C-terminal RNA-binding domain. Either RAM or RNMT independently have rather weak binding affinity for RNA, but together their RNA affinity is significantly increased. RAM is necessary for efficient cap methylation, maintaining mRNA expression levels, for mRNA translation and for cell viability.


The actual alignment was detected with superfamily member pfam15320:

Pssm-ID: 464643 [Multi-domain]  Cd Length: 83  Bit Score: 40.81  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 22026966   247 PIVSPFATSNR----DRDRDNRQYNNRG--DRNRDRDQGGSGGANYGNRY 290
Cdd:pfam15320  29 PIVEPWNNNGRgggnQRGRDNRFNDRRGggDRGRDRRRGWGGDRRRNQRW 78
 
Name Accession Description Interval E-value
W2_eIF4G1_like cd11559
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
744-890 4.73e-52

C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.


Pssm-ID: 211397  Cd Length: 134  Bit Score: 178.25  E-value: 4.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 744 YPLLKVQAEMLKQLQSDPNPNNFYKWIKANVDNKYYKDPGFIQALMTVVVKYVTkettladnldpkehPEKSVTQKEQQL 823
Cdd:cd11559   1 LPLLRVQAELLKLLQEDPNPDELYKWIKENVSPELYASPGFVRALMTAVLKYAI--------------EEKSLPEKEKAL 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22026966 824 LENYSQMLQTFLGQNE-LQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDK 890
Cdd:cd11559  67 LEKYAPLLQKYLDDDEqLQLQALYALQALVHTLEFPKGLLLRFFDALYDEDVIEEEAFLKWKEDVDPA 134
MIF4G pfam02854
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
1-173 5.71e-29

MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.


Pssm-ID: 397130  Cd Length: 203  Bit Score: 115.15  E-value: 5.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966     1 MYAQLCKRLSEEapsfdkepsNSSTFLRLLIAVCRDKFNNRLKRDENDnrpppeneadeeerrHLAKQRMLGNVKFIGEL 80
Cdd:pfam02854  54 AYARLCSGLNLR---------NPTDFGIHLLNRLQEEFEKRFELEENE---------------QGNRRRRLGLVRFLGEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    81 NKLDMLSKNVLHQCIMELFDKKKKRTAgtQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLER---RSKSSEYPP 157
Cdd:pfam02854 110 YKFGLLTEKILFECLKELLSSLTKEDL--KRDLFNLECLLTLLTTIGKLLENEKLPKLMDQFLDEIQKyvlSKDDPKLSS 187
                         170
                  ....*....|....*.
gi 22026966   158 RIRFMLKDVIELRQNN 173
Cdd:pfam02854 188 RLRFMLQDLIELRKNK 203
MIF4G smart00543
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
1-173 1.36e-25

Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA. Ponting (TiBS) "Novel eIF4G domain homologues (in press)


Pssm-ID: 214713  Cd Length: 200  Bit Score: 105.14  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966      1 MYAQLCKRLSEEAPsfdkepsnssTFLRLLIAVCRDKFNNRLkrdendnrpppeneadeEERRHLAKQRMLGNVKFIGEL 80
Cdd:smart00543  54 AYARLCALLNAKNP----------DFGSLLLERLQEEFEKGL-----------------ESEEESDKQRRLGLVRFLGEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966     81 NKLDMLSKNVLHQCIMELFDKKKKRTAgtQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLER---RSKSSEYPP 157
Cdd:smart00543 107 YNFQVLTSKIILELLKELLNDLTKLDP--PRSDFSVECLLSLLPTCGKDLEREKSPKLLDEILERLQDyllKKDKTELSS 184
                          170
                   ....*....|....*.
gi 22026966    158 RIRFMLKDVIELRQNN 173
Cdd:smart00543 185 RLRFMLELLIELRKNK 200
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
841-916 1.75e-24

eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of several translation initiation factors.


Pssm-ID: 460415  Cd Length: 76  Bit Score: 97.60  E-value: 1.75e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026966   841 QLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDKYPGKGSALFQVNAWLTWLQEAESEDD 916
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDVSSAEKGMKKVRKQAKPFVEWLEEAEEESD 76
MA3 smart00544
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
558-671 7.98e-19

Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and/or regions similar to MIF4G domains Ponting (TIBS) "Novel eIF4G domain homologues" in press


Pssm-ID: 214714  Cd Length: 113  Bit Score: 82.68  E-value: 7.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    558 VSEVKEDAAIPVTTPDRFTKLVDGFLELKLPEKaLKDVCINLLMEVLDRvNDVFLERAVRLLQTLRKQSNIKPNIVVEIF 637
Cdd:smart00544   1 LKKKIFLIIEEYLSSGDTDEAVHCLLELKLPEQ-HHEVVKVLLTCALEE-KRTYREMYSVLLSRLCQANVISTKQFEKGF 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 22026966    638 KQVVNKMNEREALNPRIVSLVASLLAKTICEPAL 671
Cdd:smart00544  79 WRLLEDIEDLELDIPNAWRNLAEFVARLISDGIL 112
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
830-911 1.17e-17

Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;


Pssm-ID: 214705  Cd Length: 83  Bit Score: 78.48  E-value: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    830 MLQTFLGQNELQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDKyPGKGSALFQVNAWLTWLQ 909
Cdd:smart00515   3 LLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSA-EGKKKVRKNAKPFVTWLQ 81

                   ..
gi 22026966    910 EA 911
Cdd:smart00515  82 EA 83
RAM pfam15320
mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in ...
247-290 1.82e-04

mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 102 and 154 amino acids in length. There is a single completely conserved residue D that may be functionally important. RAM is a family of eukaryotic proteins that are an obligate component of the mammalian cap methyltransferase, RNMT (RNA guanine-7 methyltransferase). RAM consists of an N-terminal RNMT-activating domain and a C-terminal RNA-binding domain. Either RAM or RNMT independently have rather weak binding affinity for RNA, but together their RNA affinity is significantly increased. RAM is necessary for efficient cap methylation, maintaining mRNA expression levels, for mRNA translation and for cell viability.


Pssm-ID: 464643 [Multi-domain]  Cd Length: 83  Bit Score: 40.81  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 22026966   247 PIVSPFATSNR----DRDRDNRQYNNRG--DRNRDRDQGGSGGANYGNRY 290
Cdd:pfam15320  29 PIVEPWNNNGRgggnQRGRDNRFNDRRGggDRGRDRRRGWGGDRRRNQRW 78
 
Name Accession Description Interval E-value
W2_eIF4G1_like cd11559
C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar ...
744-890 4.73e-52

C-terminal W2 domain of eukaryotic translation initiation factor 4 gamma 1 and similar proteins; eIF4G1 is a component of the multi-subunit eukaryotic translation initiation factor 4F, which facilitates recruitment of the mRNA to the ribosome, a rate-limiting step during translation initiation. This C-terminal domain, whose structure resembles that of a set of concatenated HEAT repeats, has been associated with binding to/recruiting the kinase Mnk1, which phosphorylates eIF4E.


Pssm-ID: 211397  Cd Length: 134  Bit Score: 178.25  E-value: 4.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 744 YPLLKVQAEMLKQLQSDPNPNNFYKWIKANVDNKYYKDPGFIQALMTVVVKYVTkettladnldpkehPEKSVTQKEQQL 823
Cdd:cd11559   1 LPLLRVQAELLKLLQEDPNPDELYKWIKENVSPELYASPGFVRALMTAVLKYAI--------------EEKSLPEKEKAL 66
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22026966 824 LENYSQMLQTFLGQNE-LQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDK 890
Cdd:cd11559  67 LEKYAPLLQKYLDDDEqLQLQALYALQALVHTLEFPKGLLLRFFDALYDEDVIEEEAFLKWKEDVDPA 134
MIF4G pfam02854
MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). ...
1-173 5.71e-29

MIF4G domain; MIF4G is named after Middle domain of eukaryotic initiation factor 4G (eIF4G). Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA.


Pssm-ID: 397130  Cd Length: 203  Bit Score: 115.15  E-value: 5.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966     1 MYAQLCKRLSEEapsfdkepsNSSTFLRLLIAVCRDKFNNRLKRDENDnrpppeneadeeerrHLAKQRMLGNVKFIGEL 80
Cdd:pfam02854  54 AYARLCSGLNLR---------NPTDFGIHLLNRLQEEFEKRFELEENE---------------QGNRRRRLGLVRFLGEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    81 NKLDMLSKNVLHQCIMELFDKKKKRTAgtQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLER---RSKSSEYPP 157
Cdd:pfam02854 110 YKFGLLTEKILFECLKELLSSLTKEDL--KRDLFNLECLLTLLTTIGKLLENEKLPKLMDQFLDEIQKyvlSKDDPKLSS 187
                         170
                  ....*....|....*.
gi 22026966   158 RIRFMLKDVIELRQNN 173
Cdd:pfam02854 188 RLRFMLQDLIELRKNK 203
MIF4G smart00543
Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The ...
1-173 1.36e-25

Middle domain of eukaryotic initiation factor 4G (eIF4G); Also occurs in NMD2p and CBP80. The domain is rich in alpha-helices and may contain multiple alpha-helical repeats. In eIF4G, this domain binds eIF4A, eIF3, RNA and DNA. Ponting (TiBS) "Novel eIF4G domain homologues (in press)


Pssm-ID: 214713  Cd Length: 200  Bit Score: 105.14  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966      1 MYAQLCKRLSEEAPsfdkepsnssTFLRLLIAVCRDKFNNRLkrdendnrpppeneadeEERRHLAKQRMLGNVKFIGEL 80
Cdd:smart00543  54 AYARLCALLNAKNP----------DFGSLLLERLQEEFEKGL-----------------ESEEESDKQRRLGLVRFLGEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966     81 NKLDMLSKNVLHQCIMELFDKKKKRTAgtQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLER---RSKSSEYPP 157
Cdd:smart00543 107 YNFQVLTSKIILELLKELLNDLTKLDP--PRSDFSVECLLSLLPTCGKDLEREKSPKLLDEILERLQDyllKKDKTELSS 184
                          170
                   ....*....|....*.
gi 22026966    158 RIRFMLKDVIELRQNN 173
Cdd:smart00543 185 RLRFMLELLIELRKNK 200
W2 pfam02020
eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of ...
841-916 1.75e-24

eIF4-gamma/eIF5/eIF2-epsilon; This domain of unknown function is found at the C-terminus of several translation initiation factors.


Pssm-ID: 460415  Cd Length: 76  Bit Score: 97.60  E-value: 1.75e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22026966   841 QLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDKYPGKGSALFQVNAWLTWLQEAESEDD 916
Cdd:pfam02020   1 QVDLLLALQEFCAKLEELLKLLLKILKALYDLDIVEEEAILKWWEDVSSAEKGMKKVRKQAKPFVEWLEEAEEESD 76
MA3 smart00544
Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and ...
558-671 7.98e-19

Domain in DAP-5, eIF4G, MA-3 and other proteins; Highly alpha-helical. May contain repeats and/or regions similar to MIF4G domains Ponting (TIBS) "Novel eIF4G domain homologues" in press


Pssm-ID: 214714  Cd Length: 113  Bit Score: 82.68  E-value: 7.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    558 VSEVKEDAAIPVTTPDRFTKLVDGFLELKLPEKaLKDVCINLLMEVLDRvNDVFLERAVRLLQTLRKQSNIKPNIVVEIF 637
Cdd:smart00544   1 LKKKIFLIIEEYLSSGDTDEAVHCLLELKLPEQ-HHEVVKVLLTCALEE-KRTYREMYSVLLSRLCQANVISTKQFEKGF 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 22026966    638 KQVVNKMNEREALNPRIVSLVASLLAKTICEPAL 671
Cdd:smart00544  79 WRLLEDIEDLELDIPNAWRNLAEFVARLISDGIL 112
eIF5C smart00515
Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;
830-911 1.17e-17

Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5;


Pssm-ID: 214705  Cd Length: 83  Bit Score: 78.48  E-value: 1.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966    830 MLQTFLGQNELQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDKyPGKGSALFQVNAWLTWLQ 909
Cdd:smart00515   3 LLKFLAKDEEEQLELLYAIEEFCVELEKLGKLLPKILKSLYDADILEEEAILKWYEKAVSA-EGKKKVRKNAKPFVTWLQ 81

                   ..
gi 22026966    910 EA 911
Cdd:smart00515  82 EA 83
W2_eIF2B_epsilon cd11558
C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a ...
788-916 3.86e-10

C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon; eIF2B is a heteropentameric complex which functions as a guanine nucleotide exchange factor in the recycling of eIF-2 during the initiation of translation in eukaryotes. The epsilon and gamma subunits are sequence similar and both are essential in yeast. Epsilon appears to be the catalytically active subunit, with gamma enhancing its activity. The C-terminal domain of the eIF2B epsilon subunit contains bipartite motifs rich in acidic and aromatic residues, which are responsible for the interaction with eIF2. The structure of the domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211396  Cd Length: 169  Bit Score: 59.58  E-value: 3.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 788 LMTVVVKYVTKETTLADNLDPKEHPEKSVTqkeqqLLENYSQMLQTFLGQNELQLMALYALQTFC-YNENFPK--GMLCr 864
Cdd:cd11558  45 VRRAVVKALLELILEVSSTSTAELLEALKK-----LLSKWGPLLENYVKSQDDQVELLLALEEFClESEEGGPlfAKLL- 118
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22026966 865 wfKYLYESEIIEEEAFVLWKEEISDKYPGKGSALF-QVNAWLTWLQEAESEDD 916
Cdd:cd11558 119 --HALYDLDILEEEAILEWWEEPDAGADEEMKKVReLVKKFIEWLEEAEEESD 169
W2_eIF5 cd11561
C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase ...
766-916 3.78e-09

C-terminal W2 domain of eukaryotic translation initiation factor 5; eIF5 functions as a GTPase acceleration protein (GAP), as well as a GDP dissociation inhibitor (GDI) during translational initiation in eukaryotes. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211399  Cd Length: 157  Bit Score: 56.47  E-value: 3.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 766 FYKWIKANVDNKYYKDpgfiqalmtvvVKYVTKETTLADNLDPK------EHPEKSVTQKEqqlLENYSQMLQTFLGQNE 839
Cdd:cd11561  11 LGEFLKKNKDESGLSE-----------LKEILKEAERLDVVKDKavlvlaEVLFDENIVKE---IKKRKALLLKLVTDEK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 840 LQLMALYALQTFCYNEN---FPKgmLCRWFKYLYESEIIEEEAFVLWKEEISDKY-PGKGSALFQVNA--WLTWLQEAES 913
Cdd:cd11561  77 AQKALLGGIERFCGKHSpelLKK--VPLILKALYDNDILEEEVILKWYEKVSKKYvSKEKSKKVRKAAepFVEWLEEAEE 154

                ...
gi 22026966 914 EDD 916
Cdd:cd11561 155 EEE 157
W2_eIF5C_like cd11560
C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; ...
721-914 9.01e-09

C-terminal W2 domain of the eukaryotic translation initiation factor 5C and similar proteins; eIF5C appears to be essential for the initiation of protein translation; its actual function, and specifically that of the C-terminal W2 domain, are not well understood. The Drosophila ortholog, kra (krasavietz) or exba (extra bases), may be involved in translational inhibition in neural development. The structure of this C-terminal domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211398 [Multi-domain]  Cd Length: 194  Bit Score: 56.07  E-value: 9.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 721 LPEADRNKERLAGILEDRKLSFLYPLLKVQA------EMLKQLQSDPNPNNFYKWIKANVDNKYYKDPGFIQALMTVVVk 794
Cdd:cd11560   3 FPPNKRTEEHFAEHFKEEGLDELVEFYRKQAsqeikkELQQELKEMIAEEEPVKEIIAAVKEQMKKSSLPEHEVVGLLW- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 795 yvtkeTTLADNLDPKEHPEKSVTQKEQQLlENYSQMLQTFLGQNELQLMALYALQTFCY-NENFPKgMLCRWFKYLYESE 873
Cdd:cd11560  82 -----TALMDAVEWSKKEDQIAEQALRHL-KKYAPLLAAFCTTARAELALLNKIQEYCYeNMKFMK-VFQKIVKLLYKAD 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22026966 874 IIEEEAFVLW-KEEISDKypGKGSALFQVNAWLTWLQEAESE 914
Cdd:cd11560 155 VLSEDAILKWyKKGHSPK--GKQVFLKQMEPFVEWLQEAEEE 194
W2 cd11473
C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of ...
748-883 2.33e-08

C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon; This domain is found at the C-terminus of several translation initiation factors, including the epsilon chain of eIF2b, where it has been found to catalyze the conversion of eIF2.GDP to its active eIF2.GTP form. The structure of the domain resembles that of a set of concatenated HEAT repeats.


Pssm-ID: 211395  Cd Length: 135  Bit Score: 53.63  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22026966 748 KVQAEMLKQLQSDPNPN-NFYKWIKANVDNKYYKDPGFIQALMTVVVKYVtkettladnldpKEHPEKSVTQKEQQL--L 824
Cdd:cd11473   5 KLRDSLLKELEEDKSSDvESVKAAKSKLDLDPISLEEVVKVLLTAVVNAV------------ESADSISLTQKEQLVlvL 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22026966 825 ENYSQMLQTFLG-QNELQLMALYALQTFCY---NENFPKgMLCRWFKYLYESEIIEEEAFVLW 883
Cdd:cd11473  73 KKYGPVLRELLKlIKKDQLYLLLKIEKLCLqlkLSELIS-LLEKILDLLYDADVLSEEAILSW 134
RAM pfam15320
mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in ...
247-290 1.82e-04

mRNA cap methylation, RNMT-activating mini protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 102 and 154 amino acids in length. There is a single completely conserved residue D that may be functionally important. RAM is a family of eukaryotic proteins that are an obligate component of the mammalian cap methyltransferase, RNMT (RNA guanine-7 methyltransferase). RAM consists of an N-terminal RNMT-activating domain and a C-terminal RNA-binding domain. Either RAM or RNMT independently have rather weak binding affinity for RNA, but together their RNA affinity is significantly increased. RAM is necessary for efficient cap methylation, maintaining mRNA expression levels, for mRNA translation and for cell viability.


Pssm-ID: 464643 [Multi-domain]  Cd Length: 83  Bit Score: 40.81  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 22026966   247 PIVSPFATSNR----DRDRDNRQYNNRG--DRNRDRDQGGSGGANYGNRY 290
Cdd:pfam15320  29 PIVEPWNNNGRgggnQRGRDNRFNDRRGggDRGRDRRRGWGGDRRRNQRW 78
 
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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