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Conserved domains on  [gi|17136494|ref|NP_476734|]
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aubergine, isoform A [Drosophila melanogaster]

Protein Classification

PAZ_piwi_like and Piwi_piwi-like_Euk domain-containing protein( domain architecture ID 10120291)

PAZ_piwi_like and Piwi_piwi-like_Euk domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Piwi_piwi-like_Euk cd04658
Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found ...
 400-849 0e+00

Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found in Piwi and closely related proteins, where it is believed to perform a crucial role in germline cells, via RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The mechanism in Piwi is believed to be similar to that in Argonaute, the central component of the RNA-induced silencing complex (RISC). 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: 240016 [Multi-domain]  Cd Length: 448  Bit Score: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 400 RTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNqKIFVCDARADWTN 479
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGN-VFVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 480 EFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVV 559
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 560 MRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIaprqQKPTGLMSIATKVVIQMNAKLMGAPWQVVIP---LHGLMTVGFD 636
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTL----KKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGID 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 637 VCHSPKNKNKSYGAFVATMDQKESfRYFSTVNEHIKGQEL-SEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLY 715
Cdd:cd04658 236 VYHDTITKKKSVVGFVASLNKSIT-KWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLK 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 716 QVVNSEVNTLKDRLdeiyKSAGKQEGCRMTFIIVSKRINSRYFTGHR----NPVPGTVVDDVITLPERYDFFLVSQAVRI 791
Cdd:cd04658 315 KVKEYEVPQIKKAI----KQYSENYSPKLAYIVVNKRINTRFFNQGGnnfsNPPPGTVVDSEITKPEWYDFFLVSQSVRQ 390

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136494 792 GTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAE 849
Cdd:cd04658 391 GTVTPTHYNVLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
 272-392 3.06e-49

PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be essential for the maintenance of germline stem cells. In the Drosophila male germline, Piwi was shown to be involved in the silencing of retrotransposons in the male gametes. The Piwi proteins share their domain architecture with other members of the argonaute family. 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: 239211  Cd Length: 117  Bit Score: 169.36  E-value: 3.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 272 ICHKVMRTETLYNILsdaiRDSDDYQSTFKRAVmGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDG-EISYVDYYKKRY 350
Cdd:cd02845   1 STTVLDRMHKLYRQE----TDERFREECEKELI-GSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGtEITFVEYYKKQY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17136494 351 NIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMT 392
Cdd:cd02845  76 NIEITDLNQPLLVSRPKRRDPRGGEKEPIYLIPELCFLTGLT 117
 
Name Accession Description Interval E-value
Piwi_piwi-like_Euk cd04658
Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found ...
 400-849 0e+00

Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found in Piwi and closely related proteins, where it is believed to perform a crucial role in germline cells, via RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The mechanism in Piwi is believed to be similar to that in Argonaute, the central component of the RNA-induced silencing complex (RISC). 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: 240016 [Multi-domain]  Cd Length: 448  Bit Score: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 400 RTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNqKIFVCDARADWTN 479
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGN-VFVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 480 EFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVV 559
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 560 MRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIaprqQKPTGLMSIATKVVIQMNAKLMGAPWQVVIP---LHGLMTVGFD 636
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTL----KKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGID 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 637 VCHSPKNKNKSYGAFVATMDQKESfRYFSTVNEHIKGQEL-SEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLY 715
Cdd:cd04658 236 VYHDTITKKKSVVGFVASLNKSIT-KWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLK 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 716 QVVNSEVNTLKDRLdeiyKSAGKQEGCRMTFIIVSKRINSRYFTGHR----NPVPGTVVDDVITLPERYDFFLVSQAVRI 791
Cdd:cd04658 315 KVKEYEVPQIKKAI----KQYSENYSPKLAYIVVNKRINTRFFNQGGnnfsNPPPGTVVDSEITKPEWYDFFLVSQSVRQ 390

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136494 792 GTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAE 849
Cdd:cd04658 391 GTVTPTHYNVLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
 555-852 2.06e-122

Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this domain is the dsRNA guided hydrolysis of ssRNA. Determination of the crystal structure of Argonaute reveals that PIWI is an RNase H domain, and identifies Argonaute as Slicer, the enzyme that cleaves mRNA in the RNAi RISC complex. In addition, Mg+2 dependence and production of 3'-OH and 5' phosphate products are shared characteriztics of RNaseH and RISC. The PIWI domain core has a tertiary structure belonging to the RNase H family of enzymes. RNase H fold proteins all have a five-stranded mixed beta-sheet surrounded by helices. By analogy to RNase H enzymes which cleave single-stranded RNA guided by the DNA strand in an RNA/DNA hybrid, the PIWI domain can be inferred to cleave single-stranded RNA, for example mRNA, guided by double stranded siRNA.


Pssm-ID: 396649  Cd Length: 296  Bit Score: 371.67  E-value: 2.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   555 IVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIAPRQqkptgLMSIATKVVIQMNAKLMGA-PWQVVIPLHGLMTV 633
Cdd:pfam02171   1 LILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRT-----LKQTLTNVLLKINVKLGGInYWIVEIKPKVDVII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   634 GFDVCHSPKN--KNKSYGAFVATMDqKESFRYFSTVNEHIKGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGD 711
Cdd:pfam02171  76 GFDISHGTAGtdDNPSVAAVVASFD-KGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   712 GQLYQVVNSEVNTLKdrldEIYKSAGKQEGCRMTFIIVSKRINSRYFT-----GHRNPVPGTVVDDVITLPERYDFFLVS 786
Cdd:pfam02171 155 GQFPQVLNYEVNQIK----EACKSLGPGYNPKLTVIVVQKRHHTRFFAndkpdGDQNPPPGTVVDDVITLPEYYDFYLCS 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136494   787 QAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESIN 852
Cdd:pfam02171 231 HAGLQGTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
 555-852 4.99e-105

This domain is found in the protein Piwi and its relatives; The function of this domain is the dsRNA guided hydrolysis of ssRNA. Determination of the crystal structure of Argonaute reveals that PIWI is an RNase H domain, and identifies Argonaute as Slicer, the enzyme that cleaves mRNA in the RNAi RISC complex.. In addition, Mg+2 dependence and production of 3'-OH and 5' phosphate products are shared characteristics of RNaseH and RISC. The PIWI domain core has a tertiary structure belonging to the RNase H family of enzymes. RNase H fold proteins all have a five-stranded mixed beta-sheet surrounded by helices. By analogy to RNase H enzymes which cleave single-stranded RNA guided by the DNA strand in an RNA/DNA hybrid, the PIWI domain can be inferred to cleave single-stranded RNA, for example mRNA, guided by double stranded siRNA.


Pssm-ID: 214930  Cd Length: 301  Bit Score: 326.60  E-value: 4.99e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    555 IVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIaPRQQKPTGLMSIATKVVIQMNAKLMGAPWQVV---IPLHGLM 631
Cdd:smart00950   2 IVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTL-DKVSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    632 TVGFDVCHSPKNKNKSYGAFVATMDqkESFRYFSTVNEHI-KGQELSEQMSVNMACALRSYQEQHRS-LPERILFFRDGV 709
Cdd:smart00950  81 IIGIDVSHPSAGKGGSVAPSVAAFV--ASGNYLSGNFYQAfVREQGSRQLKEILREALKKYYKSNRKrLPDRIVVYRDGV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    710 GDGQLYQVVNSEVNTLKDRLDEIYKSagkqEGCRMTFIIVSKRINSRYFT----GHRNPVPGTVVDDVITLPERYDFFLV 785
Cdd:smart00950 159 SEGQFKQVLEYEVKAIKKACKELGPD----YKPKLTVIVVQKRHHTRFFPedgnGRVNVPPGTVVDSVITSPEWYDFYLV 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136494    786 SQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESIN 852
Cdd:smart00950 235 SHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLLH 301
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
 272-392 3.06e-49

PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be essential for the maintenance of germline stem cells. In the Drosophila male germline, Piwi was shown to be involved in the silencing of retrotransposons in the male gametes. The Piwi proteins share their domain architecture with other members of the argonaute family. 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: 239211  Cd Length: 117  Bit Score: 169.36  E-value: 3.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 272 ICHKVMRTETLYNILsdaiRDSDDYQSTFKRAVmGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDG-EISYVDYYKKRY 350
Cdd:cd02845   1 STTVLDRMHKLYRQE----TDERFREECEKELI-GSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGtEITFVEYYKKQY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17136494 351 NIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMT 392
Cdd:cd02845  76 NIEITDLNQPLLVSRPKRRDPRGGEKEPIYLIPELCFLTGLT 117
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 280-414 3.23e-48

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: 167.46  E-value: 3.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    280 ETLYNILSD--AIRDSDDYQSTFKRAVMGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDG-EISYVDYYKKRYNIIIRD 356
Cdd:smart00949   1 ETVLDFMRQlpSQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGsEITFVEYYKQKYNITIRD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136494    357 LKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMTDAMRADFRTLRAMSEHTRLNPD 414
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGKGEPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 291-412 9.26e-32

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: 119.99  E-value: 9.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   291 RDSDDYQSTFKRAVMGMVILTDYNN-KTYRIDDVDFQSTPLCKFKTNDGE-ISYVDYYKKRYNIIIRDLKQPLVMSRPTD 368
Cdd:pfam02170  11 KDRRDFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKeITVVDYFKKKYNIDLKYPDQPLLLVGKKR 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17136494   369 KNirggndqaIMIIPELARatgMTDAMRADFRTLRAMSEHTRLN 412
Cdd:pfam02170  91 PK--------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
PLN03202 PLN03202
protein argonaute; Provisional
 407-841 7.28e-31

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 130.61  E-value: 7.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  407 EHTRLNPDrriERLRMFNKRLK-SCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGN-QKIFVCDARADWTNEfrtc 484
Cdd:PLN03202 402 EKSRQKPQ---ERMKVLTDALKsSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNgEDFFPRNGRWNFNNK---- 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  485 SMFKNVHINRWYVITPSRNLrETQEFVQMCIRTASSMKMNICNP--IYEEIPDDRNGTYSQAIDNAAA-------NDPQI 555
Cdd:PLN03202 475 KLVEPTKIERWAVVNFSARC-DIRHLVRDLIKCGEMKGINIEPPfdVFEENPQFRRAPPPVRVEKMFEqiqsklpGPPQF 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  556 VMVVM-RSPNEEKYSCIKKRTCVDRPVPSQVvtlkvIAPRQQKPTGLmsiaTKVVIQMNAKLMG---------APwqvVI 625
Cdd:PLN03202 554 LLCILpERKNSDIYGPWKKKNLSEFGIVTQC-----IAPTRVNDQYL----TNVLLKINAKLGGlnsllaiehSP---SI 621

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  626 PLhgLMTV-----GFDVCH-SPKNKN-KSYGAFVATMDQKESFRYFSTVN------EHI----KGQELSEQMSVNMACAL 688
Cdd:PLN03202 622 PL--VSKVptiilGMDVSHgSPGQSDvPSIAAVVSSRQWPLISRYRASVRtqspkvEMIdslfKPVGDKDDDGIIRELLL 699

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  689 RSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVntlkDRLDEIYKSAGKQEGCRMTFIIVSKRINSRYF--TGHRNPVP 766
Cdd:PLN03202 700 DFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIEL----DQIIEACKFLDESWSPKFTVIVAQKNHHTKFFqaGSPDNVPP 775

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136494  767 GTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPA-VChYAH 841
Cdd:PLN03202 776 GTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGFSADDLQELVHSLSYVYQRSTTAISVVApVC-YAH 850
 
Name Accession Description Interval E-value
Piwi_piwi-like_Euk cd04658
Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found ...
 400-849 0e+00

Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found in Piwi and closely related proteins, where it is believed to perform a crucial role in germline cells, via RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The mechanism in Piwi is believed to be similar to that in Argonaute, the central component of the RNA-induced silencing complex (RISC). 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: 240016 [Multi-domain]  Cd Length: 448  Bit Score: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 400 RTLRAMSEHTRLNPDRRIERLRMFNKRLKSCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGNqKIFVCDARADWTN 479
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGN-VFVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 480 EFRTCSMFKNVHINRWYVITPSRNLRETQEFVQMCIRTASSMKMNICNPIYEEIPDDRNGTYSQAIDNAAANDPQIVMVV 559
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 560 MRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIaprqQKPTGLMSIATKVVIQMNAKLMGAPWQVVIP---LHGLMTVGFD 636
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTL----KKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGID 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 637 VCHSPKNKNKSYGAFVATMDQKESfRYFSTVNEHIKGQEL-SEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLY 715
Cdd:cd04658 236 VYHDTITKKKSVVGFVASLNKSIT-KWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLK 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 716 QVVNSEVNTLKDRLdeiyKSAGKQEGCRMTFIIVSKRINSRYFTGHR----NPVPGTVVDDVITLPERYDFFLVSQAVRI 791
Cdd:cd04658 315 KVKEYEVPQIKKAI----KQYSENYSPKLAYIVVNKRINTRFFNQGGnnfsNPPPGTVVDSEITKPEWYDFFLVSQSVRQ 390

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136494 792 GTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAE 849
Cdd:cd04658 391 GTVTPTHYNVLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
 555-852 2.06e-122

Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this domain is the dsRNA guided hydrolysis of ssRNA. Determination of the crystal structure of Argonaute reveals that PIWI is an RNase H domain, and identifies Argonaute as Slicer, the enzyme that cleaves mRNA in the RNAi RISC complex. In addition, Mg+2 dependence and production of 3'-OH and 5' phosphate products are shared characteriztics of RNaseH and RISC. The PIWI domain core has a tertiary structure belonging to the RNase H family of enzymes. RNase H fold proteins all have a five-stranded mixed beta-sheet surrounded by helices. By analogy to RNase H enzymes which cleave single-stranded RNA guided by the DNA strand in an RNA/DNA hybrid, the PIWI domain can be inferred to cleave single-stranded RNA, for example mRNA, guided by double stranded siRNA.


Pssm-ID: 396649  Cd Length: 296  Bit Score: 371.67  E-value: 2.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   555 IVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIAPRQqkptgLMSIATKVVIQMNAKLMGA-PWQVVIPLHGLMTV 633
Cdd:pfam02171   1 LILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRT-----LKQTLTNVLLKINVKLGGInYWIVEIKPKVDVII 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   634 GFDVCHSPKN--KNKSYGAFVATMDqKESFRYFSTVNEHIKGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGD 711
Cdd:pfam02171  76 GFDISHGTAGtdDNPSVAAVVASFD-KGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   712 GQLYQVVNSEVNTLKdrldEIYKSAGKQEGCRMTFIIVSKRINSRYFT-----GHRNPVPGTVVDDVITLPERYDFFLVS 786
Cdd:pfam02171 155 GQFPQVLNYEVNQIK----EACKSLGPGYNPKLTVIVVQKRHHTRFFAndkpdGDQNPPPGTVVDDVITLPEYYDFYLCS 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136494   787 QAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESIN 852
Cdd:pfam02171 231 HAGLQGTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
 555-852 4.99e-105

This domain is found in the protein Piwi and its relatives; The function of this domain is the dsRNA guided hydrolysis of ssRNA. Determination of the crystal structure of Argonaute reveals that PIWI is an RNase H domain, and identifies Argonaute as Slicer, the enzyme that cleaves mRNA in the RNAi RISC complex.. In addition, Mg+2 dependence and production of 3'-OH and 5' phosphate products are shared characteristics of RNaseH and RISC. The PIWI domain core has a tertiary structure belonging to the RNase H family of enzymes. RNase H fold proteins all have a five-stranded mixed beta-sheet surrounded by helices. By analogy to RNase H enzymes which cleave single-stranded RNA guided by the DNA strand in an RNA/DNA hybrid, the PIWI domain can be inferred to cleave single-stranded RNA, for example mRNA, guided by double stranded siRNA.


Pssm-ID: 214930  Cd Length: 301  Bit Score: 326.60  E-value: 4.99e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    555 IVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTLKVIaPRQQKPTGLMSIATKVVIQMNAKLMGAPWQVV---IPLHGLM 631
Cdd:smart00950   2 IVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTL-DKVSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    632 TVGFDVCHSPKNKNKSYGAFVATMDqkESFRYFSTVNEHI-KGQELSEQMSVNMACALRSYQEQHRS-LPERILFFRDGV 709
Cdd:smart00950  81 IIGIDVSHPSAGKGGSVAPSVAAFV--ASGNYLSGNFYQAfVREQGSRQLKEILREALKKYYKSNRKrLPDRIVVYRDGV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    710 GDGQLYQVVNSEVNTLKDRLDEIYKSagkqEGCRMTFIIVSKRINSRYFT----GHRNPVPGTVVDDVITLPERYDFFLV 785
Cdd:smart00950 159 SEGQFKQVLEYEVKAIKKACKELGPD----YKPKLTVIVVQKRHHTRFFPedgnGRVNVPPGTVVDSVITSPEWYDFYLV 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136494    786 SQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAFLVAESIN 852
Cdd:smart00950 235 SHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLLH 301
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
 435-845 4.54e-65

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: 224.41  E-value: 4.54e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 435 ETLKSWNIELDSALVEIPARVLPPEKILFGNQKIFVCDARADWtnEFRTCSMFKNVHINRWYVIT-----PSRNLRET-Q 508
Cdd:cd04657   1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGDSSKTVPPRNGSW--NLRGKKFLEGGPIRSWAVLNfagprRSREERADlR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 509 EFVQMCIRTASSMKMNICNPIyeEIPDDRNGTYSQAIDNAAANDPQIVMVVMRSPNEEKYSCIKKRTCVDRPVPSQVVTL 588
Cdd:cd04657  79 NFVDQLVKTVIGAGINITTAI--ASVEGRVEELFAKLKQAKGEGPQLVLVILPKKDSDIYGRIKRLADTELGIHTQCVLA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 589 KVIAPRQQKPTglmsiATKVVIQMNAKLMGAPWQVVIPLHGL------MTVGFDVCHSP---KNKNKSYGAFVATMDQKE 659
Cdd:cd04657 157 KKVTKKGNPQY-----FANVALKINLKLGGINHSLEPDIRPLltkeptMVLGADVTHPSpgdPAGAPSIAAVVASVDWHL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 660 SfRYFSTV--NEHikGQELSEQMSVNMACALRSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVNTLKdrldEIYKSAG 737
Cdd:cd04657 232 A-QYPASVrlQSH--RQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGVSEGQFAQVLNEELPAIR----KACAKLY 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 738 KQEGCRMTFIIVSKRINSRYF--------TGHRNPVPGTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLN 809
Cdd:cd04657 305 PGYKPKITFIVVQKRHHTRFFptdeddadGKNGNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFT 384

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 17136494 810 ADKLQMLSYKMTHMYYNYSGTIRVPAVCHYAHKLAF 845
Cdd:cd04657 385 ADELQTLTYNLCYTYARCTRSVSIPPPAYYAHLAAA 420
Piwi-like cd02826
Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing ...
 454-846 3.48e-53

Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The central component of the RNA-induced silencing complex (RISC) and related complexes is Argonaute. 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. This domain is also found in closely related proteins, including the Piwi subfamily, where it is believed to perform a crucial role in germline cells, via a similar mechanism.


Pssm-ID: 239208 [Multi-domain]  Cd Length: 393  Bit Score: 190.29  E-value: 3.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 454 RVLPPEKILFGNQKifvcdaradwtneFRTCSMF--KNVHINRWYVITPSrnlretQEFVQMCIRTASSMKMNICNPIYE 531
Cdd:cd02826   8 RVLPKPQILFKNKF-------------LRNIGPFekPAKITNPVAVIAFR------NEEVDDLVKRLADACRQLGMKIKE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 532 EIP-------DDRNGTYSQAIDNAAANDPQIVMVVMRSPNEEKYSCIKKRTCVdRPVPSQVVTLKVIaprqQKPTGLMSI 604
Cdd:cd02826  69 IPIvswiedlNNSFKDLKSVFKNAIKAGVQLVIFILKEKKPPLHDEIKRLEAK-SDIPSQVIQLKTA----KKMRRLKQT 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 605 ATKVVIQMNAKLMGAPWQVVIP---LHGLMTVGFDVCHSPKNKNKSYGA---FVATMDQKE---SFRYFSTVNEHIkgqe 675
Cdd:cd02826 144 LDNLLRKVNSKLGGINYILDSPvklFKSDIFIGFDVSHPDRRTVNGGPSavgFAANLSNHTflgGFLYVQPSREVK---- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 676 LSEQMSVNMACaLRSYQEQHRS-LPERILFFRDGVGDGQlYQVVNSEVntlkDRLDEIYKSAGKQEGCRMTFIIVSKRIN 754
Cdd:cd02826 220 LQDLGEVIKKC-LDGFKKSTGEgLPEKIVIYRDGVSEGE-FKRVKEEV----EEIIKEACEIEESYRPKLVIIVVQKRHN 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 755 SRYF----TGHR-NPVPGTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSG 829
Cdd:cd02826 294 TRFFpnekNGGVqNPEPGTVVDHTITSPGLSEFYLASHVARQGTVKPTKYTVVFNDKNWSLNELEILTYILCLTHQNVYS 373

                       410
                ....*....|....*..
gi 17136494 830 TIRVPAVCHYAHKLAFL 846
Cdd:cd02826 374 PISLPAPLYYAHKLAKR 390
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
 272-392 3.06e-49

PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be essential for the maintenance of germline stem cells. In the Drosophila male germline, Piwi was shown to be involved in the silencing of retrotransposons in the male gametes. The Piwi proteins share their domain architecture with other members of the argonaute family. 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: 239211  Cd Length: 117  Bit Score: 169.36  E-value: 3.06e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 272 ICHKVMRTETLYNILsdaiRDSDDYQSTFKRAVmGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDG-EISYVDYYKKRY 350
Cdd:cd02845   1 STTVLDRMHKLYRQE----TDERFREECEKELI-GSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGtEITFVEYYKKQY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17136494 351 NIIIRDLKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMT 392
Cdd:cd02845  76 NIEITDLNQPLLVSRPKRRDPRGGEKEPIYLIPELCFLTGLT 117
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 280-414 3.23e-48

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: 167.46  E-value: 3.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494    280 ETLYNILSD--AIRDSDDYQSTFKRAVMGMVILTDYNNKTYRIDDVDFQSTPLCKFKTNDG-EISYVDYYKKRYNIIIRD 356
Cdd:smart00949   1 ETVLDFMRQlpSQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGsEITFVEYYKQKYNITIRD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136494    357 LKQPLVMSRPTDKNIRGGNDQAIMIIPELARATGMTDAMRADFRTLRAMSEHTRLNPD 414
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGKGEPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 291-412 9.26e-32

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: 119.99  E-value: 9.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494   291 RDSDDYQSTFKRAVMGMVILTDYNN-KTYRIDDVDFQSTPLCKFKTNDGE-ISYVDYYKKRYNIIIRDLKQPLVMSRPTD 368
Cdd:pfam02170  11 KDRRDFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKeITVVDYFKKKYNIDLKYPDQPLLLVGKKR 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17136494   369 KNirggndqaIMIIPELARatgMTDAMRADFRTLRAMSEHTRLN 412
Cdd:pfam02170  91 PK--------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
PLN03202 PLN03202
protein argonaute; Provisional
 407-841 7.28e-31

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 130.61  E-value: 7.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  407 EHTRLNPDrriERLRMFNKRLK-SCKQSVETLKSWNIELDSALVEIPARVLPPEKILFGN-QKIFVCDARADWTNEfrtc 484
Cdd:PLN03202 402 EKSRQKPQ---ERMKVLTDALKsSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNgEDFFPRNGRWNFNNK---- 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  485 SMFKNVHINRWYVITPSRNLrETQEFVQMCIRTASSMKMNICNP--IYEEIPDDRNGTYSQAIDNAAA-------NDPQI 555
Cdd:PLN03202 475 KLVEPTKIERWAVVNFSARC-DIRHLVRDLIKCGEMKGINIEPPfdVFEENPQFRRAPPPVRVEKMFEqiqsklpGPPQF 553

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  556 VMVVM-RSPNEEKYSCIKKRTCVDRPVPSQVvtlkvIAPRQQKPTGLmsiaTKVVIQMNAKLMG---------APwqvVI 625
Cdd:PLN03202 554 LLCILpERKNSDIYGPWKKKNLSEFGIVTQC-----IAPTRVNDQYL----TNVLLKINAKLGGlnsllaiehSP---SI 621

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  626 PLhgLMTV-----GFDVCH-SPKNKN-KSYGAFVATMDQKESFRYFSTVN------EHI----KGQELSEQMSVNMACAL 688
Cdd:PLN03202 622 PL--VSKVptiilGMDVSHgSPGQSDvPSIAAVVSSRQWPLISRYRASVRtqspkvEMIdslfKPVGDKDDDGIIRELLL 699

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494  689 RSYQEQHRSLPERILFFRDGVGDGQLYQVVNSEVntlkDRLDEIYKSAGKQEGCRMTFIIVSKRINSRYF--TGHRNPVP 766
Cdd:PLN03202 700 DFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIEL----DQIIEACKFLDESWSPKFTVIVAQKNHHTKFFqaGSPDNVPP 775

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136494  767 GTVVDDVITLPERYDFFLVSQAVRIGTVSPTSYNVISDNMGLNADKLQMLSYKMTHMYYNYSGTIRVPA-VChYAH 841
Cdd:PLN03202 776 GTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGFSADDLQELVHSLSYVYQRSTTAISVVApVC-YAH 850
Piwi_piwi-like_ProArk cd04659
Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA ...
 541-849 3.46e-14

Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The central component of the RNA-induced silencing complex (RISC) and related complexes is Argonaute. 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. This domain is also found in closely related proteins, including the Piwi subfamily, where it is believed to perform a crucial role in germline cells, via a similar mechanism.


Pssm-ID: 240017 [Multi-domain]  Cd Length: 404  Bit Score: 75.50  E-value: 3.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 541 YSQAIDNA---AANDPQIVMVVM------RSPNEEKYSCIKKRTcVDRPVPSQVVTLKVIAPRQQKPTglmsIATKVVIQ 611
Cdd:cd04659  96 IIEAVDLAlseSSQGVDVVIVVLpedlkeLPEEFDLYDRLKAKL-LRLGIPTQFVREDTLKNRQDLAY----VAWNLALA 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 612 MNAKLMGAPWQVV-IPLHGLMTVGFDVCHSPKNKNKSYG-AFVATMDQK-ESFRYFSTVNEhiKGQELSEQMSVNMACAL 688
Cdd:cd04659 171 LYAKLGGIPWKLDaDSDPADLYIGIGFARSRDGEVRVTGcAQVFDSDGLgLILRGAPIEEP--TEDRSPADLKDLLKRVL 248

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 689 RSYQEQHR-SLPERILFFRDGvgdgqlyQVVNSEVNTLKDrldeiyksAGKQEGCRMTFIIVSKRINSRYF----TGHRN 763
Cdd:cd04659 249 EGYRESHRgRDPKRLVLHKDG-------RFTDEEIEGLKE--------ALEELGIKVDLVEVIKSGPHRLFrfgtYPNGF 313

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 764 PVP-GTVV----DDVITLPERYDFFLVSQAVRiGTVSPTSYNVISDNMGLNADKLQMlsYKMTHMYYN-YSGTIRVPAVC 837
Cdd:cd04659 314 PPRrGTYVklsdDEGLLWTHGSVPKYNTYPGM-GTPRPLLLRRHSGNTDLEQLASQI--LGLTKLNWNsFQFYSRLPVTI 390

                       330
                ....*....|..
gi 17136494 838 HYAHKLAFLVAE 849
Cdd:cd04659 391 HYADRVAKLLKR 402
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
 271-389 2.88e-09

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: 55.54  E-value: 2.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 271 EICHKVMRTETLYNILSDaiRDSDDYQSTFKravmGMVILTDYN--NKTYRIDDVDFQSTPlCKFKTNDG-EISYVDYYK 347
Cdd:cd02825   6 ETMCKFPKDREIDTPLLD--SPREEFTKELK----GLKVEDTHNplNRVYRPDGETRLKAP-SQLKHSDGkEITFADYFK 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17136494 348 KRYNIIIRDLKQPLVMSRPTDKNIrggndQAIMIIPELARAT 389
Cdd:cd02825  79 ERYNLTLTDLNQPLLIVKFSSKKS-----YSILLPPELCVIT 115
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
 293-371 5.79e-06

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: 46.16  E-value: 5.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136494 293 SDDYQSTFKRAVMGMVILTDY---NNKTYRIDDVDFQSTPLCKFKTNDG--EISYVDYYKKRYNIIIRDLKQPLVMSRPT 367
Cdd:cd02846  21 SDNDRRKLKKALKGLKVEVTHrgnTNRKYKIKGLSAEPASQQTFELKDGekEISVADYFKEKYNIRLKYPNLPCLQVGRK 100


                ....
gi 17136494 368 DKNI 371
Cdd:cd02846 101 GKPN 104
PAZ_CAF_like cd02844
PAZ domain, CAF_like subfamily. CAF (for carpel factory) is a plant homolog of Dicer. CAF has ...
 301-366 8.79e-05

PAZ domain, CAF_like subfamily. CAF (for carpel factory) is a plant homolog of Dicer. CAF has been implicated in flower morphogenesis and in early Arabidopsis development and might function through posttranscriptional regulation of specific mRNA molecules. PAZ domains are 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: 239210  Cd Length: 135  Bit Score: 43.18  E-value: 8.79e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136494 301 KRAVMGMVILTDYNNKTYRIDDV-DFQSTPLCKFKTNDGEISYVDYYKKRYNIIIRDLKQPLVMSRP 366
Cdd:cd02844  28 ACDLKGSVVTAPHNGRFYVISGIlDLNANSSFPGKEGLGYATYAEYFKEKYGIVLNHPNQPLLKGKQ 94
PAZ_dicer_like cd02843
PAZ domain, dicer_like subfamily. Dicer is an RNAse involved in cleaving dsRNA in the RNA ...
 328-362 4.93e-03

PAZ domain, dicer_like subfamily. Dicer is an RNAse involved in cleaving dsRNA in the RNA interference pathway. It generates dsRNAs which are approximately 20 bp long (siRNAs), which in turn target hydrolysis of homologous RNAs. PAZ domains are 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: 239209  Cd Length: 122  Bit Score: 37.81  E-value: 4.93e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17136494 328 TPLCKFKTNDGEiSYVDYYKKRYNIIIRDLKQPLV 362
Cdd:cd02843  69 RPLSKFPGPEYE-TFEEYYKKKYKLDIQNLNQPLL 102
 
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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