NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442627813|ref|NP_001260450|]
View 

adenosine deaminase, tRNA-specific 1, isoform B [Drosophila melanogaster]

Protein Classification

A_deamin domain-containing protein( domain architecture ID 10651130)

A_deamin domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
7-389 1.02e-156

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


:

Pssm-ID: 214718  Cd Length: 374  Bit Score: 446.05  E-value: 1.02e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813     7 PTVKEIAELCLKKFESLPKTGKPTANQWTILAGIVEFNRNTEACQLVSLGCGTKCIGESKLCPNGLILNDSHAEVLARRG 86
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813    87 FLRFLYQEL------KQDRIFHWNSTLSTYDMDEHVEFHFLSTQTPCGDACILEEEQPAAR--AKRQRLDEDSEMVYTGA 158
Cdd:smart00552  81 FLRFLYSELqlfnssSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNddSKHPVRKNIKRSKLRTK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   159 KLISDLSDDPMLQTPGALRTKPGRGERTLSMSCSDKIARWNVIGVQGALLDVLISkPIYFSSLNFCCDDAQLESLERAIF 238
Cdd:smart00552 161 IEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLSSIVLGKSLYSAEHLERALY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   239 KRFDCRTFKHTRFQPQRPQINIDPGIRFefsqRSDWQPSPN-GLIWSQVPEELrPYEISVNGKRQgvtkkkmKTSQAALA 317
Cdd:smart00552 240 GRLDPLDGLPTPFRVNRPLISLVSVADF----QRQTAKSPNfSVNWSQGDESL-EILNGLTGKTQ-------KSLGSPSR 307
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627813   318 ISKYKLFLTFLELVKFNPKlsemfdqqlSDPERIAYASCKDLARDYQFAW----REIKEKYFLQWTKKPHELLDFN 389
Cdd:smart00552 308 LCKKALFRLFQKLCSKLKR---------DDLLHISYAEAKEAASEYQEAKqllfEALNKAGLGSWIKKPPEQDQFK 374
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
7-389 1.02e-156

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 446.05  E-value: 1.02e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813     7 PTVKEIAELCLKKFESLPKTGKPTANQWTILAGIVEFNRNTEACQLVSLGCGTKCIGESKLCPNGLILNDSHAEVLARRG 86
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813    87 FLRFLYQEL------KQDRIFHWNSTLSTYDMDEHVEFHFLSTQTPCGDACILEEEQPAAR--AKRQRLDEDSEMVYTGA 158
Cdd:smart00552  81 FLRFLYSELqlfnssSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNddSKHPVRKNIKRSKLRTK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   159 KLISDLSDDPMLQTPGALRTKPGRGERTLSMSCSDKIARWNVIGVQGALLDVLISkPIYFSSLNFCCDDAQLESLERAIF 238
Cdd:smart00552 161 IEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLSSIVLGKSLYSAEHLERALY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   239 KRFDCRTFKHTRFQPQRPQINIDPGIRFefsqRSDWQPSPN-GLIWSQVPEELrPYEISVNGKRQgvtkkkmKTSQAALA 317
Cdd:smart00552 240 GRLDPLDGLPTPFRVNRPLISLVSVADF----QRQTAKSPNfSVNWSQGDESL-EILNGLTGKTQ-------KSLGSPSR 307
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627813   318 ISKYKLFLTFLELVKFNPKlsemfdqqlSDPERIAYASCKDLARDYQFAW----REIKEKYFLQWTKKPHELLDFN 389
Cdd:smart00552 308 LCKKALFRLFQKLCSKLKR---------DDLLHISYAEAKEAASEYQEAKqllfEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
54-382 2.72e-92

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: 278.68  E-value: 2.72e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   54 SLGCGTKCIGESKLCPNGLILNDSHAEVLARRGFLRFLYQEL-------KQDRIFHWNSTLSTYDMDEHVEFHFLSTQTP 126
Cdd:pfam02137   1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLllalsgnPSKSIFEPNPDSGKLRLKPGISFHLYISQTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  127 CGDACIL------EEEQPAARAKRQRLDEDSEmVYTGAKLISDLSDDPmLQTPGalrTKPGRgeRTLSMSCSDKIARWNV 200
Cdd:pfam02137  81 CGDARIFsplelePESSPAHPVRRFRGQLRLK-VETGAKTIPVESSED-QTWDG---VKPGR--RTLSMSCSDKLARWNV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  201 IGVQGALLDVLIsKPIYFSSLNF--CCDDAqlESLERAIFKRFDCRTFKHTR-FQPQRPQInidpgirfefsqrsdwqps 277
Cdd:pfam02137 154 LGVQGALLSHFI-EPIYLSSITVggSLYDT--EHLERAIYQRLDGVLDSLPPpYRVNKPLI------------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  278 pngliwsqvpeelrpyeisvngkrqgvtkkkmktSQAALAISKYKLFLTFLELVKFNPKLSEmfdqqlsdPERIAYASCK 357
Cdd:pfam02137 212 ----------------------------------GQVASRLCKAALFSRFLKLLSELSREDL--------LAPLTYHEAK 249
                         330       340
                  ....*....|....*....|....*....
gi 442627813  358 DLARDYQFA---WRE-IKEKYFLQWTKKP 382
Cdd:pfam02137 250 AAAKDYQEAkqqLKSlLRQQGLGSWIRKP 278
 
Name Accession Description Interval E-value
ADEAMc smart00552
tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase);
7-389 1.02e-156

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


Pssm-ID: 214718  Cd Length: 374  Bit Score: 446.05  E-value: 1.02e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813     7 PTVKEIAELCLKKFESLPKTGKPTANQWTILAGIVEFNRNTEACQLVSLGCGTKCIGESKLCPNGLILNDSHAEVLARRG 86
Cdd:smart00552   1 DTGDEISQLVLEKFGSLPKIGKPGLREWTILAGVVMTNGMDNEKQVVSLGTGTKCISGEKLSPNGLVLNDCHAEILARRG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813    87 FLRFLYQEL------KQDRIFHWNSTLSTYDMDEHVEFHFLSTQTPCGDACILEEEQPAAR--AKRQRLDEDSEMVYTGA 158
Cdd:smart00552  81 FLRFLYSELqlfnssSEDSIFEKNKEGGKYKLKSNVLFHLYISTLPCGDASIFSPLEPLKNddSKHPVRKNIKRSKLRTK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   159 KLISDLSDDPMLQTPGALRTKPGRGERTLSMSCSDKIARWNVIGVQGALLDVLISkPIYFSSLNFCCDDAQLESLERAIF 238
Cdd:smart00552 161 IEIGEGTVPVRSSDIVQTWDGIGDGERLLSMSCSDKIARWNVLGVQGALLSHFIE-PIYLSSIVLGKSLYSAEHLERALY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   239 KRFDCRTFKHTRFQPQRPQINIDPGIRFefsqRSDWQPSPN-GLIWSQVPEELrPYEISVNGKRQgvtkkkmKTSQAALA 317
Cdd:smart00552 240 GRLDPLDGLPTPFRVNRPLISLVSVADF----QRQTAKSPNfSVNWSQGDESL-EILNGLTGKTQ-------KSLGSPSR 307
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627813   318 ISKYKLFLTFLELVKFNPKlsemfdqqlSDPERIAYASCKDLARDYQFAW----REIKEKYFLQWTKKPHELLDFN 389
Cdd:smart00552 308 LCKKALFRLFQKLCSKLKR---------DDLLHISYAEAKEAASEYQEAKqllfEALNKAGLGSWIKKPPEQDQFK 374
A_deamin pfam02137
Adenosine-deaminase (editase) domain; Adenosine deaminases acting on RNA (ADARs) can deaminate ...
54-382 2.72e-92

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: 278.68  E-value: 2.72e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813   54 SLGCGTKCIGESKLCPNGLILNDSHAEVLARRGFLRFLYQEL-------KQDRIFHWNSTLSTYDMDEHVEFHFLSTQTP 126
Cdd:pfam02137   1 ALGTGTKCIGGSKLSPSGRVLNDSHAEVIARRSLLRYLYSQLllalsgnPSKSIFEPNPDSGKLRLKPGISFHLYISQTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  127 CGDACIL------EEEQPAARAKRQRLDEDSEmVYTGAKLISDLSDDPmLQTPGalrTKPGRgeRTLSMSCSDKIARWNV 200
Cdd:pfam02137  81 CGDARIFsplelePESSPAHPVRRFRGQLRLK-VETGAKTIPVESSED-QTWDG---VKPGR--RTLSMSCSDKLARWNV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  201 IGVQGALLDVLIsKPIYFSSLNF--CCDDAqlESLERAIFKRFDCRTFKHTR-FQPQRPQInidpgirfefsqrsdwqps 277
Cdd:pfam02137 154 LGVQGALLSHFI-EPIYLSSITVggSLYDT--EHLERAIYQRLDGVLDSLPPpYRVNKPLI------------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627813  278 pngliwsqvpeelrpyeisvngkrqgvtkkkmktSQAALAISKYKLFLTFLELVKFNPKLSEmfdqqlsdPERIAYASCK 357
Cdd:pfam02137 212 ----------------------------------GQVASRLCKAALFSRFLKLLSELSREDL--------LAPLTYHEAK 249
                         330       340
                  ....*....|....*....|....*....
gi 442627813  358 DLARDYQFA---WRE-IKEKYFLQWTKKP 382
Cdd:pfam02137 250 AAAKDYQEAkqqLKSlLRQQGLGSWIRKP 278
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH