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Conserved domains on  [gi|2462505527|ref|XP_054190805|]
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protein argonaute-4 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03202 super family cl33661
protein argonaute; Provisional
 15-416 4.46e-60

protein argonaute; Provisional


The actual alignment was detected with superfamily member PLN03202:

Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 209.58  E-value: 4.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  15 PPRRPGLGTVGKPIRLLANHFQVQIPKIDV--YHYDVDIKPE-KRP---RRVNREVVDTMVRHFKMQiFGDRQPGYDGKR 88
Cdd:PLN03202   33 PMARRGFGSKGQKIQLLTNHFKVSVNNPDGhfFHYSVSLTYEdGRPvdgKGIGRKVIDKVQETYSSD-LAGKDFAYDGEK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  89 NMYTAHPLPigRDRVDMEVTL-------------------PGEG---------KDQTFKVSVQWVSVVSLQLLLEALAGH 140
Cdd:PLN03202  112 SLFTVGALP--QNKLEFTVVLedvssnrnngngspvgngsPNGGdrkrsrrpyQSKTFKVEISFAAKIPMQAIANALRGQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 141 LNEVPDDSVQALDVITR-HLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQP 219
Cdd:PLN03202  190 ESENSQDALRVLDIILRqHAAKQGCLLVRQSFFHNDPKNFVDLGGGVLGCRGFHSSFRTTQGGLSLNIDVSTTMIVQPGP 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 220 IIEFMcevldIQNINEQTKPLTDSQRVKftKEIRGLKVEVTHCGQmkrKYRVCNVTRRPASHQTFPLQLENG-----QAM 294
Cdd:PLN03202  270 VVDFL-----IANQNVRDPFQIDWSKAK--RMLKNLRVKVSPSNQ---EYKITGLSEKPCKEQTFSLKQRNGngnevETV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 295 ECTVAQYFKQKYSLQLKYP-HLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLV 373
Cdd:PLN03202  340 EITVYDYFVKHRGIELRYSgDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2462505527 374 KSNSMvgGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRE 416
Cdd:PLN03202  420 KSSNY--DADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGE 460
 
Name Accession Description Interval E-value
PLN03202 PLN03202
protein argonaute; Provisional
 15-416 4.46e-60

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 209.58  E-value: 4.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  15 PPRRPGLGTVGKPIRLLANHFQVQIPKIDV--YHYDVDIKPE-KRP---RRVNREVVDTMVRHFKMQiFGDRQPGYDGKR 88
Cdd:PLN03202   33 PMARRGFGSKGQKIQLLTNHFKVSVNNPDGhfFHYSVSLTYEdGRPvdgKGIGRKVIDKVQETYSSD-LAGKDFAYDGEK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  89 NMYTAHPLPigRDRVDMEVTL-------------------PGEG---------KDQTFKVSVQWVSVVSLQLLLEALAGH 140
Cdd:PLN03202  112 SLFTVGALP--QNKLEFTVVLedvssnrnngngspvgngsPNGGdrkrsrrpyQSKTFKVEISFAAKIPMQAIANALRGQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 141 LNEVPDDSVQALDVITR-HLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQP 219
Cdd:PLN03202  190 ESENSQDALRVLDIILRqHAAKQGCLLVRQSFFHNDPKNFVDLGGGVLGCRGFHSSFRTTQGGLSLNIDVSTTMIVQPGP 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 220 IIEFMcevldIQNINEQTKPLTDSQRVKftKEIRGLKVEVTHCGQmkrKYRVCNVTRRPASHQTFPLQLENG-----QAM 294
Cdd:PLN03202  270 VVDFL-----IANQNVRDPFQIDWSKAK--RMLKNLRVKVSPSNQ---EYKITGLSEKPCKEQTFSLKQRNGngnevETV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 295 ECTVAQYFKQKYSLQLKYP-HLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLV 373
Cdd:PLN03202  340 EITVYDYFVKHRGIELRYSgDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2462505527 374 KSNSMvgGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRE 416
Cdd:PLN03202  420 KSSNY--DADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGE 460
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
 217-337 1.74e-45

PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the Piwi and Dicer families. PAZ functions as a nucleic acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes.


Pssm-ID: 239212 [Multi-domain]  Cd Length: 114  Bit Score: 152.86  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 217 AQPIIEFMCEVLDIQNINeqtkPLTDSQRVKFTKEIRGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLqleNGQAMEC 296
Cdd:cd02846     1 AQPVIEFLKEFLGFDTPL----GLSDNDRRKLKKALKGLKVEVTHRGNTNRKYKIKGLSAEPASQQTFEL---KDGEKEI 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462505527 297 TVAQYFKQKYSLQLKYPHLPCLQVGQEQKHTYLPLEVCNIV 337
Cdd:cd02846    74 SVADYFKEKYNIRLKYPNLPCLQVGRKGKPNYLPMELCNIV 114
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 228-355 1.97e-42

PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain is found in two families of proteins that are involved in post-transcriptional gene silencing. These are the Piwi family and the Dicer family, that includes the Carpel factory protein. The function of the domains is unknown but has been suggested to mediate complex formation between proteins of the Piwi and Dicer families by hetero-dimerization. The three-dimensional structure of this domain has been solved. The PAZ domain is composed of two subdomains. One subdomain is similar to the OB fold, albeit with a different topology. The OB-fold is well known as a single-stranded nucleic acid binding fold. The second subdomain is composed of a beta-hairpin followed by an alpha-helix. The PAZ domains shows low-affinity nucleic acid binding and appears to interact with the 3' ends of single-stranded regions of RNA in the cleft between the two subdomains. PAZ can bind the characteriztic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.


Pssm-ID: 460472  Cd Length: 123  Bit Score: 145.41  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 228 LDIQNINEQTKPLTDSQRvKFTKEIRGLKVEVTHcgQMKRKYRVCNVTRRPASHQTFPLqlENGQamECTVAQYFKQKYS 307
Cdd:pfam02170   1 LDFLKRLQQQKDRRDFRK-EAKKALKGLKVYTTY--NNPRTYRIDGITFDPTPESTFPL--KDGK--EITVVDYFKKKYN 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462505527 308 LQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKL--TDNQTSTMI 355
Cdd:pfam02170  74 IDLKYPDQPLLLVGKKRPKVYLPPELCNLVDGQRYTKKLmpSIAQRTRLL 123
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 225-359 5.66e-10

This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in two families of proteins that are involved in post-transcriptional gene silencing. These are the Piwi family and the Dicer family, that includes the Carpel factory protein. The function of the domains is unknown but has been suggested to mediate complex formation between proteins of the Piwi and Dicer families by hetero-dimerisation. The three-dimensional structure of this domain has been solved. The PAZ domain is composed of two subdomains. One subdomain is similar to the OB fold, albeit with a different topology. The OB-fold is well known as a single-stranded nucleic acid binding fold. The second subdomain is composed of a beta-hairpin followed by an alpha-helix. The PAZ domains shows low-affinity nucleic acid binding and appears to interact with the 3' ends of single-stranded regions of RNA in the cleft between the two subdomains. PAZ can bind the characteristic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.


Pssm-ID: 198017  Cd Length: 138  Bit Score: 57.30  E-value: 5.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  225 CEVLDIQNINEQTKPLTDSQRvKFTKEIRGLKVEVTHcgqMKRKYRVCNVTRRPASHQTFPLQleNGQamECTVAQYFKQ 304
Cdd:smart00949   1 ETVLDFMRQLPSQGNRSNFQD-RCAKDLKGLIVLTRY---NNKTYRIDDIDWNLAPKSTFEKS--DGS--EITFVEYYKQ 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505527  305 KYSLQLKYPHLPCL--------QVGQEQKHTYLPLEVCNIVA-GQRCIKKLTD-NQTSTMIKATA 359
Cdd:smart00949  73 KYNITIRDPNQPLLvsrpkrrrNQNGKGEPVLLPPELCFITGlTDRMRKDFMLmKSIADRTRLSP 137
 
Name Accession Description Interval E-value
PLN03202 PLN03202
protein argonaute; Provisional
 15-416 4.46e-60

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 209.58  E-value: 4.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  15 PPRRPGLGTVGKPIRLLANHFQVQIPKIDV--YHYDVDIKPE-KRP---RRVNREVVDTMVRHFKMQiFGDRQPGYDGKR 88
Cdd:PLN03202   33 PMARRGFGSKGQKIQLLTNHFKVSVNNPDGhfFHYSVSLTYEdGRPvdgKGIGRKVIDKVQETYSSD-LAGKDFAYDGEK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  89 NMYTAHPLPigRDRVDMEVTL-------------------PGEG---------KDQTFKVSVQWVSVVSLQLLLEALAGH 140
Cdd:PLN03202  112 SLFTVGALP--QNKLEFTVVLedvssnrnngngspvgngsPNGGdrkrsrrpyQSKTFKVEISFAAKIPMQAIANALRGQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 141 LNEVPDDSVQALDVITR-HLPSMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYRAQP 219
Cdd:PLN03202  190 ESENSQDALRVLDIILRqHAAKQGCLLVRQSFFHNDPKNFVDLGGGVLGCRGFHSSFRTTQGGLSLNIDVSTTMIVQPGP 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 220 IIEFMcevldIQNINEQTKPLTDSQRVKftKEIRGLKVEVTHCGQmkrKYRVCNVTRRPASHQTFPLQLENG-----QAM 294
Cdd:PLN03202  270 VVDFL-----IANQNVRDPFQIDWSKAK--RMLKNLRVKVSPSNQ---EYKITGLSEKPCKEQTFSLKQRNGngnevETV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 295 ECTVAQYFKQKYSLQLKYP-HLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLV 373
Cdd:PLN03202  340 EITVYDYFVKHRGIELRYSgDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2462505527 374 KSNSMvgGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQYGGRE 416
Cdd:PLN03202  420 KSSNY--DADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGE 460
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
 217-337 1.74e-45

PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex (RISC), and is an endonuclease that plays a key role in the RNA interference pathway. The PAZ domain has been named after the proteins Piwi,Argonaut, and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the Piwi and Dicer families. PAZ functions as a nucleic acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes.


Pssm-ID: 239212 [Multi-domain]  Cd Length: 114  Bit Score: 152.86  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 217 AQPIIEFMCEVLDIQNINeqtkPLTDSQRVKFTKEIRGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLqleNGQAMEC 296
Cdd:cd02846     1 AQPVIEFLKEFLGFDTPL----GLSDNDRRKLKKALKGLKVEVTHRGNTNRKYKIKGLSAEPASQQTFEL---KDGEKEI 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462505527 297 TVAQYFKQKYSLQLKYPHLPCLQVGQEQKHTYLPLEVCNIV 337
Cdd:cd02846    74 SVADYFKEKYNIRLKYPNLPCLQVGRKGKPNYLPMELCNIV 114
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 228-355 1.97e-42

PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain is found in two families of proteins that are involved in post-transcriptional gene silencing. These are the Piwi family and the Dicer family, that includes the Carpel factory protein. The function of the domains is unknown but has been suggested to mediate complex formation between proteins of the Piwi and Dicer families by hetero-dimerization. The three-dimensional structure of this domain has been solved. The PAZ domain is composed of two subdomains. One subdomain is similar to the OB fold, albeit with a different topology. The OB-fold is well known as a single-stranded nucleic acid binding fold. The second subdomain is composed of a beta-hairpin followed by an alpha-helix. The PAZ domains shows low-affinity nucleic acid binding and appears to interact with the 3' ends of single-stranded regions of RNA in the cleft between the two subdomains. PAZ can bind the characteriztic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.


Pssm-ID: 460472  Cd Length: 123  Bit Score: 145.41  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 228 LDIQNINEQTKPLTDSQRvKFTKEIRGLKVEVTHcgQMKRKYRVCNVTRRPASHQTFPLqlENGQamECTVAQYFKQKYS 307
Cdd:pfam02170   1 LDFLKRLQQQKDRRDFRK-EAKKALKGLKVYTTY--NNPRTYRIDGITFDPTPESTFPL--KDGK--EITVVDYFKKKYN 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462505527 308 LQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKL--TDNQTSTMI 355
Cdd:pfam02170  74 IDLKYPDQPLLLVGKKRPKVYLPPELCNLVDGQRYTKKLmpSIAQRTRLL 123
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
 217-337 1.02e-35

PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two families of proteins that are essential components of RNA-mediated gene-silencing pathways, including RNA interference, the piwi and Dicer families. PAZ functions as a nucleic-acid binding domain, with a strong preference for single-stranded nucleic acids (RNA or DNA) or RNA duplexes with single-stranded 3' overhangs. It has been suggested that the PAZ domain provides a unique mode for the recognition of the two 3'-terminal nucleotides in single-stranded nucleic acids and buries the 3' OH group, and that it might recognize characteristic 3' overhangs in siRNAs within RISC (RNA-induced silencing) and other complexes. This parent model also contains structures of an archaeal PAZ domain.


Pssm-ID: 239207  Cd Length: 115  Bit Score: 127.19  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527 217 AQPIIEFMCEVLDIQNINEqtkPLTDSQRVKFTKEIRGLKVEVTHCgQMKRKYRVCNVTRRPASHQtfplqLENGQAMEC 296
Cdd:cd02825     1 ADPVIETMCKFPKDREIDT---PLLDSPREEFTKELKGLKVEDTHN-PLNRVYRPDGETRLKAPSQ-----LKHSDGKEI 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462505527 297 TVAQYFKQKYSLQLKYPHLPCLQVGQE---QKHTYLPLEVCNIV 337
Cdd:cd02825    72 TFADYFKERYNLTLTDLNQPLLIVKFSskkSYSILLPPELCVIT 115
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
 166-216 3.33e-22

Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally co-occurs with pfam02179 and pfam02171. It is a linker region between the N-terminal and the PAZ domains. It contains an alpha-helix packed against a three-stranded antiparallel beta-sheet with two long beta-strands (beta8 and beta9) of the sheet spanning one face of the adjacent N and PAZ domains. L1 together with linker 2, L2, PAZ and ArgoN forms a compact global fold.


Pssm-ID: 462567  Cd Length: 52  Bit Score: 88.73  E-value: 3.33e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462505527 166 PVGRSFFSPPEGYYHPL-GGGREVWFGFHQSVRPAMWNMMLNIDVSATAFYR 216
Cdd:pfam08699   1 GVGRSFFSPPGENRVDLgGGGLEAWRGFFQSVRPTQGGLLLNVDVSHTAFYK 52
ArgoL2 pfam16488
Argonaute linker 2 domain; ArgoL2 is the second linker domain in eukaryotic argonaute proteins. ...
 364-412 3.10e-13

Argonaute linker 2 domain; ArgoL2 is the second linker domain in eukaryotic argonaute proteins. It starts with two alpha-helices aligned orthogonally to each other followed by a beta-strand involved in linking the two lobes, the PAZ lobe and the Piwi lobe of argonaute to each other. Linker 2 together with the N, PAZ and L1 domains form a compact global fold. Numerous residues from Piwi, L1 and L2 linkers direct the path of the phosphate backbone of nucleotides 7-9, thus allowing DNA-slicing.


Pssm-ID: 465136 [Multi-domain]  Cd Length: 47  Bit Score: 63.58  E-value: 3.10e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462505527 364 DRQEEISRLVKSNSMvgGPDPYLKEFGIVVHNEMTELTGRVLPAPMLQY 412
Cdd:pfam16488   1 ERAESIVEGLKVLGY--DQDPYLREFGISVDPQMITVPGRVLPPPKLKY 47
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 225-359 5.66e-10

This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in two families of proteins that are involved in post-transcriptional gene silencing. These are the Piwi family and the Dicer family, that includes the Carpel factory protein. The function of the domains is unknown but has been suggested to mediate complex formation between proteins of the Piwi and Dicer families by hetero-dimerisation. The three-dimensional structure of this domain has been solved. The PAZ domain is composed of two subdomains. One subdomain is similar to the OB fold, albeit with a different topology. The OB-fold is well known as a single-stranded nucleic acid binding fold. The second subdomain is composed of a beta-hairpin followed by an alpha-helix. The PAZ domains shows low-affinity nucleic acid binding and appears to interact with the 3' ends of single-stranded regions of RNA in the cleft between the two subdomains. PAZ can bind the characteristic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.


Pssm-ID: 198017  Cd Length: 138  Bit Score: 57.30  E-value: 5.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  225 CEVLDIQNINEQTKPLTDSQRvKFTKEIRGLKVEVTHcgqMKRKYRVCNVTRRPASHQTFPLQleNGQamECTVAQYFKQ 304
Cdd:smart00949   1 ETVLDFMRQLPSQGNRSNFQD-RCAKDLKGLIVLTRY---NNKTYRIDDIDWNLAPKSTFEKS--DGS--EITFVEYYKQ 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505527  305 KYSLQLKYPHLPCL--------QVGQEQKHTYLPLEVCNIVA-GQRCIKKLTD-NQTSTMIKATA 359
Cdd:smart00949  73 KYNITIRDPNQPLLvsrpkrrrNQNGKGEPVLLPPELCFITGlTDRMRKDFMLmKSIADRTRLSP 137
ArgoN pfam16486
N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in ...
 26-155 3.28e-09

N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in eukaryotes. ArgoN is composed of an antiparallel four-stranded beta sheet core that has two alpha helices positioned along one face of the sheet and an extended beta strand towards its N-terminus. The core fold of the N domain most closely resembles the catalytic domain of replication-initiator protein Rep. The N domain is linked to the PAZ domain via linker 1 region, and together these three regions are designated the PAZ-containing lobe of argonaute.


Pssm-ID: 465134  Cd Length: 93  Bit Score: 53.83  E-value: 3.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505527  26 KPIRLLANHFQVQipkidvyhydvdikpekrprrvnrevvdtmvrhfkmqifgdrqpgyDGKRNMYTAHPLPIGRDRVDM 105
Cdd:pfam16486   1 RPITLRANYFPVT----------------------------------------------DGRKNLYSAKKLPFGEEEFVV 34

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505527 106 EVTLPGEG--------KDQTFKVSVQWVSVVSLQLLLEALAGHLNEVPDDSVQALDVI 155
Cdd:pfam16486  35 LDEEPGRGarkrpgvrRPRTFKVTIKFTKTINLQDLLEYLRGKQDNTPLEAIQALDIV 92
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
 384-418 9.35e-09

Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of the RNA-induced silencing complex (RISC) and related complexes. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing.


Pssm-ID: 240015 [Multi-domain]  Cd Length: 426  Bit Score: 56.85  E-value: 9.35e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462505527 384 PYLKEFGIVVHNEMTELTGRVLPAPMLQYGGREFH 418
Cdd:cd04657     1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGDSSKT 35
 
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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