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Conserved domains on  [gi|2123789139|ref|NP_001383775|]
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tRNA-specific adenosine deaminase 1 isoform 2 [Rattus norvegicus]

Protein Classification

adenosine deaminase family protein( domain architecture ID 5878)

adenosine deaminase family protein such as tRNA-specific adenosine deaminase 1 (TAD1), which is similar to yeast tRNA-specific adenosine deaminase that deaminates adenosine-37 to inosine in tRNA-Ala

EC:  3.5.4.-
Gene Ontology:  GO:0004000|GO:0046872

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
A_deamin super family cl02661
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
2-441 8.62e-105

Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate adenosine to form inosine. In long double-stranded RNA, this process is non-specific; it occurs site-specifically in RNA transcripts. The former is important in defence against viruses, whereas the latter may affect splicing or untranslated regions. They are primarily nuclear proteins, but a longer isoform of ADAR1 is found predominantly in the cytoplasm. ADARs are derived from the Tad1-like tRNA deaminases that are present across eukaryotes. These in turn belong to the nucleotide/nucleic acid deaminase superfamily and are characterized by a distinct insert between the two conserved cysteines that are involved in binding zinc.


The actual alignment was detected with superfamily member smart00552:

Pssm-ID: 470647  Cd Length: 374  Bit Score: 316.24  E-value: 8.62e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139    2 WTADEIAQLCYAHYIKLPKQGKPEPnREWTLLAAVVKIQTPANQacdtpdkqiqvtKEVVSMGTGTKCIGQSKMRESGDI 81
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGL-REWTILAGVVMTNGMDNE------------KQVVSLGTGTKCISGEKLSPNGLV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139   82 LNDSHAEVIARRSFQRYILHQLHVAAVLKEDSIFLPGTQRGLWRLRPDLSFVFFSSHTPCGDASIIPKLEFEEQPccpvi 161
Cdd:smart00552  68 LNDCHAEILARRGFLRFLYSELQLFNSSSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKND----- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  162 rnwannspgegsetlegsrnkrscegpdspvakkkrlgtpagslsdcVAHHgaqesgPAKPDASSSgltkeeldavngta 241
Cdd:smart00552 143 -----------------------------------------------DSKH------PVRKNIKRS-------------- 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  242 sgsfkvvdiYRTGAKCVPGETGDlrkpgAAYHQVGLLRVKPGRGDRTCSMSCSDKMARWNVLGCQGALLMHFLEkPIYLS 321
Cdd:smart00552 156 ---------KLRTKIEIGEGTVP-----VRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLS 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  322 AVVIGQCPYSQEAMRRALTGRCQETLVLPRGFEVQELKIQ-QSSLLFeqsrcavHRKRGDSPGRlvpcgaAISWSAVPQ- 399
Cdd:smart00552 221 SIVLGKSLYSAEHLERALYGRLDPLDGLPTPFRVNRPLISlVSVADF-------QRQTAKSPNF------SVNWSQGDEs 287
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2123789139  400 QPLDVTANGFPQGTTKkeigsprARSRISKVELFRSFQKLLS 441
Cdd:smart00552 288 LEILNGLTGKTQKSLG-------SPSRLCKKALFRLFQKLCS 322
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
2-441 8.62e-105

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);


Pssm-ID: 214718  Cd Length: 374  Bit Score: 316.24  E-value: 8.62e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139    2 WTADEIAQLCYAHYIKLPKQGKPEPnREWTLLAAVVKIQTPANQacdtpdkqiqvtKEVVSMGTGTKCIGQSKMRESGDI 81
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGL-REWTILAGVVMTNGMDNE------------KQVVSLGTGTKCISGEKLSPNGLV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139   82 LNDSHAEVIARRSFQRYILHQLHVAAVLKEDSIFLPGTQRGLWRLRPDLSFVFFSSHTPCGDASIIPKLEFEEQPccpvi 161
Cdd:smart00552  68 LNDCHAEILARRGFLRFLYSELQLFNSSSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKND----- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  162 rnwannspgegsetlegsrnkrscegpdspvakkkrlgtpagslsdcVAHHgaqesgPAKPDASSSgltkeeldavngta 241
Cdd:smart00552 143 -----------------------------------------------DSKH------PVRKNIKRS-------------- 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  242 sgsfkvvdiYRTGAKCVPGETGDlrkpgAAYHQVGLLRVKPGRGDRTCSMSCSDKMARWNVLGCQGALLMHFLEkPIYLS 321
Cdd:smart00552 156 ---------KLRTKIEIGEGTVP-----VRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLS 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  322 AVVIGQCPYSQEAMRRALTGRCQETLVLPRGFEVQELKIQ-QSSLLFeqsrcavHRKRGDSPGRlvpcgaAISWSAVPQ- 399
Cdd:smart00552 221 SIVLGKSLYSAEHLERALYGRLDPLDGLPTPFRVNRPLISlVSVADF-------QRQTAKSPNF------SVNWSQGDEs 287
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2123789139  400 QPLDVTANGFPQGTTKkeigsprARSRISKVELFRSFQKLLS 441
Cdd:smart00552 288 LEILNGLTGKTQKSLG-------SPSRLCKKALFRLFQKLCS 322
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
62-451 1.31e-99

Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate adenosine to form inosine. In long double-stranded RNA, this process is non-specific; it occurs site-specifically in RNA transcripts. The former is important in defence against viruses, whereas the latter may affect splicing or untranslated regions. They are primarily nuclear proteins, but a longer isoform of ADAR1 is found predominantly in the cytoplasm. ADARs are derived from the Tad1-like tRNA deaminases that are present across eukaryotes. These in turn belong to the nucleotide/nucleic acid deaminase superfamily and are characterized by a distinct insert between the two conserved cysteines that are involved in binding zinc.


Pssm-ID: 460458  Cd Length: 278  Bit Score: 299.48  E-value: 1.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  62 SMGTGTKCIGQSKMRESGDILNDSHAEVIARRSFQRYILHQLHVAAVLKED-SIFLPGTQRGLWRLRPDLSFVFFSSHTP 140
Cdd:pfam02137   1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNPSkSIFEPNPDSGKLRLKPGISFHLYISQTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 141 CGDASIIPKLEFE--EQPCCPVIRNwannspgegsetlegsrnkrscegpdspvakkkrlgtpAGSLSdcvahhgaqesg 218
Cdd:pfam02137  81 CGDARIFSPLELEpeSSPAHPVRRF--------------------------------------RGQLR------------ 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 219 pakpdasssglTKEEldavngtasgsfkvvdiyrTGAKCVPGE-TGDLRKPGaayhqvgllrVKPGRgdRTCSMSCSDKM 297
Cdd:pfam02137 111 -----------LKVE-------------------TGAKTIPVEsSEDQTWDG----------VKPGR--RTLSMSCSDKL 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 298 ARWNVLGCQGALLMHFLEkPIYLSAVVIGQCPYSQEAMRRALTGRCQETL-VLPRGFEVQELKIQQSsllfeqsrcavhr 376
Cdd:pfam02137 149 ARWNVLGVQGALLSHFIE-PIYLSSITVGGSLYDTEHLERAIYQRLDGVLdSLPPPYRVNKPLIGQV------------- 214
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123789139 377 krgdspgrlvpcgaaiswsavpqqpldvtangfpqgttkkeigspraRSRISKVELFRSFQKLLSCIAEDERPDS 451
Cdd:pfam02137 215 -----------------------------------------------ASRLCKAALFSRFLKLLSELSREDLLAP 242
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
2-441 8.62e-105

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);


Pssm-ID: 214718  Cd Length: 374  Bit Score: 316.24  E-value: 8.62e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139    2 WTADEIAQLCYAHYIKLPKQGKPEPnREWTLLAAVVKIQTPANQacdtpdkqiqvtKEVVSMGTGTKCIGQSKMRESGDI 81
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGL-REWTILAGVVMTNGMDNE------------KQVVSLGTGTKCISGEKLSPNGLV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139   82 LNDSHAEVIARRSFQRYILHQLHVAAVLKEDSIFLPGTQRGLWRLRPDLSFVFFSSHTPCGDASIIPKLEFEEQPccpvi 161
Cdd:smart00552  68 LNDCHAEILARRGFLRFLYSELQLFNSSSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKND----- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  162 rnwannspgegsetlegsrnkrscegpdspvakkkrlgtpagslsdcVAHHgaqesgPAKPDASSSgltkeeldavngta 241
Cdd:smart00552 143 -----------------------------------------------DSKH------PVRKNIKRS-------------- 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  242 sgsfkvvdiYRTGAKCVPGETGDlrkpgAAYHQVGLLRVKPGRGDRTCSMSCSDKMARWNVLGCQGALLMHFLEkPIYLS 321
Cdd:smart00552 156 ---------KLRTKIEIGEGTVP-----VRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLS 220
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  322 AVVIGQCPYSQEAMRRALTGRCQETLVLPRGFEVQELKIQ-QSSLLFeqsrcavHRKRGDSPGRlvpcgaAISWSAVPQ- 399
Cdd:smart00552 221 SIVLGKSLYSAEHLERALYGRLDPLDGLPTPFRVNRPLISlVSVADF-------QRQTAKSPNF------SVNWSQGDEs 287
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2123789139  400 QPLDVTANGFPQGTTKkeigsprARSRISKVELFRSFQKLLS 441
Cdd:smart00552 288 LEILNGLTGKTQKSLG-------SPSRLCKKALFRLFQKLCS 322
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
62-451 1.31e-99

Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate adenosine to form inosine. In long double-stranded RNA, this process is non-specific; it occurs site-specifically in RNA transcripts. The former is important in defence against viruses, whereas the latter may affect splicing or untranslated regions. They are primarily nuclear proteins, but a longer isoform of ADAR1 is found predominantly in the cytoplasm. ADARs are derived from the Tad1-like tRNA deaminases that are present across eukaryotes. These in turn belong to the nucleotide/nucleic acid deaminase superfamily and are characterized by a distinct insert between the two conserved cysteines that are involved in binding zinc.


Pssm-ID: 460458  Cd Length: 278  Bit Score: 299.48  E-value: 1.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139  62 SMGTGTKCIGQSKMRESGDILNDSHAEVIARRSFQRYILHQLHVAAVLKED-SIFLPGTQRGLWRLRPDLSFVFFSSHTP 140
Cdd:pfam02137   1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLLLALSGNPSkSIFEPNPDSGKLRLKPGISFHLYISQTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 141 CGDASIIPKLEFE--EQPCCPVIRNwannspgegsetlegsrnkrscegpdspvakkkrlgtpAGSLSdcvahhgaqesg 218
Cdd:pfam02137  81 CGDARIFSPLELEpeSSPAHPVRRF--------------------------------------RGQLR------------ 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 219 pakpdasssglTKEEldavngtasgsfkvvdiyrTGAKCVPGE-TGDLRKPGaayhqvgllrVKPGRgdRTCSMSCSDKM 297
Cdd:pfam02137 111 -----------LKVE-------------------TGAKTIPVEsSEDQTWDG----------VKPGR--RTLSMSCSDKL 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123789139 298 ARWNVLGCQGALLMHFLEkPIYLSAVVIGQCPYSQEAMRRALTGRCQETL-VLPRGFEVQELKIQQSsllfeqsrcavhr 376
Cdd:pfam02137 149 ARWNVLGVQGALLSHFIE-PIYLSSITVGGSLYDTEHLERAIYQRLDGVLdSLPPPYRVNKPLIGQV------------- 214
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123789139 377 krgdspgrlvpcgaaiswsavpqqpldvtangfpqgttkkeigspraRSRISKVELFRSFQKLLSCIAEDERPDS 451
Cdd:pfam02137 215 -----------------------------------------------ASRLCKAALFSRFLKLLSELSREDLLAP 242
 
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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