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Conserved domains on  [gi|530387871|ref|XP_005273608|]
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piwi-like protein 2 isoform X2 [Homo sapiens]

Protein Classification

argonaute/piwi family protein( domain architecture ID 11179628)

argonaute/piwi family protein contains argonaute linker 1 (ArgoL1), PAZ (Piwi Argonaut and Zwille), and Piwi domains; similar to Homo sapiens Piwi-like protein 2, an endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity

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 ...
512-802 5.58e-118

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: 363.89  E-value: 5.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 512 RAMKDLAQQINLSPKQHHSALECLLQRIAKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQELNWVKE 591
Cdd:cd04658    1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNVFVYANSNADWKRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 592 VTRDPSILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDDRIETYVRTIQSTLGaeGKIQMVVC 671
Cdd:cd04658   81 IRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFR--SDPQLVVI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 672 IIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVDIP---LKQLMVIGMDVYH 748
Cdd:cd04658  159 ILPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYH 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530387871 749 DPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQE-IVDSLKLCLVGSLKKFYEE 802
Cdd:cd04658  239 DTITKKKSVVGFVASLNKSITKWFSKYISQVRGQEeIIDSLGKSMKKALKAYKKE 293
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
387-504 2.65e-58

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: 194.02  E-value: 2.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 387 NDCVLDVMHAIYQQNK-EHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVK 465
Cdd:cd02845    1 STTVLDRMHKLYRQETdERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEYYKKQYNIEIT 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530387871 466 EEDQPLLIHRPSERQDNHGMllKGEILLLPELSFMTGIP 504
Cdd:cd02845   81 DLNQPLLVSRPKRRDPRGGE--KEPIYLIPELCFLTGLT 117
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
339-386 2.24e-08

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: 50.98  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530387871  339 VGRNFYDPTSA--MVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIR 386
Cdd:pfam08699   2 VGRSFFSPPGEnrVDLGGGGLEAWRGFFQSVRPTQGGLLLNVDVSHTAFY 51
 
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 ...
512-802 5.58e-118

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: 363.89  E-value: 5.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 512 RAMKDLAQQINLSPKQHHSALECLLQRIAKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQELNWVKE 591
Cdd:cd04658    1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNVFVYANSNADWKRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 592 VTRDPSILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDDRIETYVRTIQSTLGaeGKIQMVVC 671
Cdd:cd04658   81 IRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFR--SDPQLVVI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 672 IIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVDIP---LKQLMVIGMDVYH 748
Cdd:cd04658  159 ILPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYH 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530387871 749 DPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQE-IVDSLKLCLVGSLKKFYEE 802
Cdd:cd04658  239 DTITKKKSVVGFVASLNKSITKWFSKYISQVRGQEeIIDSLGKSMKKALKAYKKE 293
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
387-504 2.65e-58

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: 194.02  E-value: 2.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 387 NDCVLDVMHAIYQQNK-EHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVK 465
Cdd:cd02845    1 STTVLDRMHKLYRQETdERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEYYKKQYNIEIT 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530387871 466 EEDQPLLIHRPSERQDNHGMllKGEILLLPELSFMTGIP 504
Cdd:cd02845   81 DLNQPLLVSRPKRRDPRGGE--KEPIYLIPELCFLTGLT 117
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
388-526 3.26e-57

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: 191.73  E-value: 3.26e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   388 DCVLDVMHAIY-QQNKEHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKE 466
Cdd:smart00949   1 ETVLDFMRQLPsQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGSEITFVEYYKQKYNITIRD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   467 EDQPLLIHRPSERQDNHGMLlkGEILLLPELSFMTGIPEKMKKDFRAMKDLAQQINLSPK 526
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGKG--EPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
391-524 4.24e-41

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: 146.57  E-value: 4.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871  391 LDVMHAIYQQNKEH-FQDECTKLLVGNIVITRYNN-RTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKEED 468
Cdd:pfam02170   1 LDFLKRLQQQKDRRdFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKEITVVDYFKKKYNIDLKYPD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530387871  469 QPLLIHRPSERQdnhgmllkgeILLLPELSFmtgIPEKMKKDFRAMKDLAQQINLS 524
Cdd:pfam02170  81 QPLLLVGKKRPK----------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
668-801 1.59e-36

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: 139.78  E-value: 1.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   668 MVVCIIMGP-RDDLYGAIKKLCCVQSPVPSQVVNVRTI---GQPTRLRSVAQKILLQINCKLGGELWGVD---IPLKQLM 740
Cdd:smart00950   1 LIVVILPGEkKTDLYHEIKKYLETKLGVPTQCVQAKTLdkvSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTL 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530387871   741 VIGMDVYHDPSRGMRSVVGFVASINlTLTKWYSRVVFQ-MPHQEIVDSLKLCLVGSLKKFYE 801
Cdd:smart00950  81 IIGIDVSHPSAGKGGSVAPSVAAFV-ASGNYLSGNFYQaFVREQGSRQLKEILREALKKYYK 141
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
669-802 7.39e-30

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: 120.14  E-value: 7.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871  669 VVCIIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTrLRSVAQKILLQINCKLGGE-LWGVDIPLKQLMVIGMDVY 747
Cdd:pfam02171   2 ILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRT-LKQTLTNVLLKINVKLGGInYWIVEIKPKVDVIIGFDIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530387871  748 HDPSRGM--RSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKFYEE 802
Cdd:pfam02171  81 HGTAGTDdnPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKS 137
PLN03202 PLN03202
protein argonaute; Provisional
362-788 6.14e-12

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 69.36  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 362 GYAASIRRTDGGLFLLADVSHK-VIRNDCVLDVMhaIYQQNKEH-FQDECTK---LLVGNIVITRYNNRTYRIDDVDWNK 436
Cdd:PLN03202 241 GFHSSFRTTQGGLSLNIDVSTTmIVQPGPVVDFL--IANQNVRDpFQIDWSKakrMLKNLRVKVSPSNQEYKITGLSEKP 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 437 TPKDSFTMS---------DGKEITFLEYYSKNYGITVK-EEDQPLL-IHRPserqdNHGMLLKGEILLLPELSFMTGIPE 505
Cdd:PLN03202 319 CKEQTFSLKqrngngnevETVEITVYDYFVKHRGIELRySGDLPCInVGKP-----KRPTYFPIELCSLVSLQRYTKALS 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 506 KMKkdfRAmkDLAQQINLSPKQHHSALECLLQRiaKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQE 585
Cdd:PLN03202 394 TLQ---RS--SLVEKSRQKPQERMKVLTDALKS--SNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRN 466
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 586 LNWV---KEVTRDPSILTipmhfWAL--FypkRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDD---------RIET 651
Cdd:PLN03202 467 GRWNfnnKKLVEPTKIER-----WAVvnF---SARCDIRHLVRDLIKCGEMKGINIEPPFDVFEENPqfrrapppvRVEK 538
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 652 YVRTIQSTLGaeGKIQMVVCIIMGPRD-DLYGAIKKLCCVQSPVPSQVVnvrtigQPTRLRS-VAQKILLQINCKLGG-- 727
Cdd:PLN03202 539 MFEQIQSKLP--GPPQFLLCILPERKNsDIYGPWKKKNLSEFGIVTQCI------APTRVNDqYLTNVLLKINAKLGGln 610
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530387871 728 ELWGVD----IPLKQ---LMVIGMDVYHDpSRG---MRSVVGFVASINLTL-TKWYSRVVFQMPHQEIVDSL 788
Cdd:PLN03202 611 SLLAIEhspsIPLVSkvpTIILGMDVSHG-SPGqsdVPSIAAVVSSRQWPLiSRYRASVRTQSPKVEMIDSL 681
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
339-386 2.24e-08

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: 50.98  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530387871  339 VGRNFYDPTSA--MVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIR 386
Cdd:pfam08699   2 VGRSFFSPPGEnrVDLGGGGLEAWRGFFQSVRPTQGGLLLNVDVSHTAFY 51
 
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 ...
512-802 5.58e-118

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: 363.89  E-value: 5.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 512 RAMKDLAQQINLSPKQHHSALECLLQRIAKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQELNWVKE 591
Cdd:cd04658    1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNVFVYANSNADWKRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 592 VTRDPSILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDDRIETYVRTIQSTLGaeGKIQMVVC 671
Cdd:cd04658   81 IRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVKDDRIETYIRALKDAFR--SDPQLVVI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 672 IIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVDIP---LKQLMVIGMDVYH 748
Cdd:cd04658  159 ILPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYH 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530387871 749 DPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQE-IVDSLKLCLVGSLKKFYEE 802
Cdd:cd04658  239 DTITKKKSVVGFVASLNKSITKWFSKYISQVRGQEeIIDSLGKSMKKALKAYKKE 293
Piwi-like cd02826
Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing ...
559-801 7.27e-59

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: 205.31  E-value: 7.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 559 DVHKIEGRVLPMERINLKNTsFITSQELNWVKEVtrdpsiLTIPMHFWALFYP------KRAMDQARELVNMLEKiagpi 632
Cdd:cd02826    1 TPLILKGRVLPKPQILFKNK-FLRNIGPFEKPAK------ITNPVAVIAFRNEevddlvKRLADACRQLGMKIKE----- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 633 gmrMSPPAWVELKDDRIETYVRTIQSTLGAEgkIQMVVCIIMGPRDDLYGAIKKLCCVqSPVPSQVVNVRTIGQPTRLRS 712
Cdd:cd02826   69 ---IPIVSWIEDLNNSFKDLKSVFKNAIKAG--VQLVIFILKEKKPPLHDEIKRLEAK-SDIPSQVIQLKTAKKMRRLKQ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 713 VAQKILLQINCKLGGELWGVDIP---LKQLMVIGMDVYHDPSR---GMRSVVGFVASIN---LTLTKWYSRVVFQMPHQE 783
Cdd:cd02826  143 TLDNLLRKVNSKLGGINYILDSPvklFKSDIFIGFDVSHPDRRtvnGGPSAVGFAANLSnhtFLGGFLYVQPSREVKLQD 222
                        250
                 ....*....|....*...
gi 530387871 784 IVDSLKLCLVGSLKKFYE 801
Cdd:cd02826  223 LGEVIKKCLDGFKKSTGE 240
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
387-504 2.65e-58

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: 194.02  E-value: 2.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 387 NDCVLDVMHAIYQQNK-EHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVK 465
Cdd:cd02845    1 STTVLDRMHKLYRQETdERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEYYKKQYNIEIT 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530387871 466 EEDQPLLIHRPSERQDNHGMllKGEILLLPELSFMTGIP 504
Cdd:cd02845   81 DLNQPLLVSRPKRRDPRGGE--KEPIYLIPELCFLTGLT 117
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
388-526 3.26e-57

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: 191.73  E-value: 3.26e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   388 DCVLDVMHAIY-QQNKEHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKE 466
Cdd:smart00949   1 ETVLDFMRQLPsQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGSEITFVEYYKQKYNITIRD 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   467 EDQPLLIHRPSERQDNHGMLlkGEILLLPELSFMTGIPEKMKKDFRAMKDLAQQINLSPK 526
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGKG--EPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
391-524 4.24e-41

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: 146.57  E-value: 4.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871  391 LDVMHAIYQQNKEH-FQDECTKLLVGNIVITRYNN-RTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKEED 468
Cdd:pfam02170   1 LDFLKRLQQQKDRRdFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKEITVVDYFKKKYNIDLKYPD 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530387871  469 QPLLIHRPSERQdnhgmllkgeILLLPELSFmtgIPEKMKKDFRAMKDLAQQINLS 524
Cdd:pfam02170  81 QPLLLVGKKRPK----------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
668-801 1.59e-36

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: 139.78  E-value: 1.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871   668 MVVCIIMGP-RDDLYGAIKKLCCVQSPVPSQVVNVRTI---GQPTRLRSVAQKILLQINCKLGGELWGVD---IPLKQLM 740
Cdd:smart00950   1 LIVVILPGEkKTDLYHEIKKYLETKLGVPTQCVQAKTLdkvSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTL 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530387871   741 VIGMDVYHDPSRGMRSVVGFVASINlTLTKWYSRVVFQ-MPHQEIVDSLKLCLVGSLKKFYE 801
Cdd:smart00950  81 IIGIDVSHPSAGKGGSVAPSVAAFV-ASGNYLSGNFYQaFVREQGSRQLKEILREALKKYYK 141
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
387-501 1.99e-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: 130.27  E-value: 1.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 387 NDCVLDVMHAIYQQNK------EHFQDECTKLLVGNIVITRYN--NRTYRIDDVDWNKTPKDsFTMSDGKEITFLEYYSK 458
Cdd:cd02825    1 ADPVIETMCKFPKDREidtpllDSPREEFTKELKGLKVEDTHNplNRVYRPDGETRLKAPSQ-LKHSDGKEITFADYFKE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530387871 459 NYGITVKEEDQPLLIHRPSERqdnhgmlLKGEILLLPELSFMT 501
Cdd:cd02825   80 RYNLTLTDLNQPLLIVKFSSK-------KSYSILLPPELCVIT 115
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
669-802 7.39e-30

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: 120.14  E-value: 7.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871  669 VVCIIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTrLRSVAQKILLQINCKLGGE-LWGVDIPLKQLMVIGMDVY 747
Cdd:pfam02171   2 ILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRT-LKQTLTNVLLKINVKLGGInYWIVEIKPKVDVIIGFDIS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530387871  748 HDPSRGM--RSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKFYEE 802
Cdd:pfam02171  81 HGTAGTDdnPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKS 137
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
551-801 1.61e-20

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: 94.99  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 551 RWGLRLQKDVHKIEGRVLPMERINLKNTSFIT-----SQELNWVKEVTRDP----SILTIPMhfwalfyPKRAMDQAREL 621
Cdd:cd04657    5 EFGISVSKEMITVPGRVLPPPKLKYGDSSKTVpprngSWNLRGKKFLEGGPirswAVLNFAG-------PRRSREERADL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 622 VNM---LEKIAGPIGMRMSPPAwvELKDDRIETYVRTIQSTLGaeGKIQMVVCIIMGPRDDLYGAIKKLCCVQSPVPSQV 698
Cdd:cd04657   78 RNFvdqLVKTVIGAGINITTAI--ASVEGRVEELFAKLKQAKG--EGPQLVLVILPKKDSDIYGRIKRLADTELGIHTQC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 699 VNVRTIGQPTRLRSVAQkILLQINCKLGGELWGVD------IPLKQLMVIGMDVYH---DPSRGMRSVVGFVASINLTLT 769
Cdd:cd04657  154 VLAKKVTKKGNPQYFAN-VALKINLKLGGINHSLEpdirplLTKEPTMVLGADVTHpspGDPAGAPSIAAVVASVDWHLA 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 530387871 770 KWYSRVVFQMPHQEIVDSLKLCLVGSLKKFYE 801
Cdd:cd04657  233 QYPASVRLQSHRQEIIDDLESMVRELLRAFKK 264
PLN03202 PLN03202
protein argonaute; Provisional
362-788 6.14e-12

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 69.36  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 362 GYAASIRRTDGGLFLLADVSHK-VIRNDCVLDVMhaIYQQNKEH-FQDECTK---LLVGNIVITRYNNRTYRIDDVDWNK 436
Cdd:PLN03202 241 GFHSSFRTTQGGLSLNIDVSTTmIVQPGPVVDFL--IANQNVRDpFQIDWSKakrMLKNLRVKVSPSNQEYKITGLSEKP 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 437 TPKDSFTMS---------DGKEITFLEYYSKNYGITVK-EEDQPLL-IHRPserqdNHGMLLKGEILLLPELSFMTGIPE 505
Cdd:PLN03202 319 CKEQTFSLKqrngngnevETVEITVYDYFVKHRGIELRySGDLPCInVGKP-----KRPTYFPIELCSLVSLQRYTKALS 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 506 KMKkdfRAmkDLAQQINLSPKQHHSALECLLQRiaKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQE 585
Cdd:PLN03202 394 TLQ---RS--SLVEKSRQKPQERMKVLTDALKS--SNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRN 466
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 586 LNWV---KEVTRDPSILTipmhfWAL--FypkRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDD---------RIET 651
Cdd:PLN03202 467 GRWNfnnKKLVEPTKIER-----WAVvnF---SARCDIRHLVRDLIKCGEMKGINIEPPFDVFEENPqfrrapppvRVEK 538
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 652 YVRTIQSTLGaeGKIQMVVCIIMGPRD-DLYGAIKKLCCVQSPVPSQVVnvrtigQPTRLRS-VAQKILLQINCKLGG-- 727
Cdd:PLN03202 539 MFEQIQSKLP--GPPQFLLCILPERKNsDIYGPWKKKNLSEFGIVTQCI------APTRVNDqYLTNVLLKINAKLGGln 610
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530387871 728 ELWGVD----IPLKQ---LMVIGMDVYHDpSRG---MRSVVGFVASINLTL-TKWYSRVVFQMPHQEIVDSL 788
Cdd:PLN03202 611 SLLAIEhspsIPLVSkvpTIILGMDVSHG-SPGqsdVPSIAAVVSSRQWPLiSRYRASVRTQSPKVEMIDSL 681
PAZ_CAF_like cd02844
PAZ domain, CAF_like subfamily. CAF (for carpel factory) is a plant homolog of Dicer. CAF has ...
393-513 5.24e-10

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: 58.20  E-value: 5.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 393 VMHAIYQQNKE----HFQDE--CTKLLVGNIVITRYNNRTYRIDDVdWNKTPKDSFTMSDGKEI-TFLEYYSKNYGITVK 465
Cdd:cd02844    5 LMHRDYSTNEAsdllHLADGsfCACDLKGSVVTAPHNGRFYVISGI-LDLNANSSFPGKEGLGYaTYAEYFKEKYGIVLN 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530387871 466 EEDQPLLIHRPSERQDNhgmllkgeiLLLPELSFMTGIPEKMKKDFRA 513
Cdd:cd02844   84 HPNQPLLKGKQIFNLHN---------LLHNRFEEKGESEEKEKDRYFV 122
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
339-386 2.24e-08

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: 50.98  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530387871  339 VGRNFYDPTSA--MVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIR 386
Cdd:pfam08699   2 VGRSFFSPPGEnrVDLGGGGLEAWRGFFQSVRPTQGGLLLNVDVSHTAFY 51
Piwi_piwi-like_ProArk cd04659
Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA ...
677-760 8.22e-06

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: 48.92  E-value: 8.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387871 677 RDDLYGAIKKLCcVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVD-IPLKQLMVIGMDVYHDPsRGMR 755
Cdd:cd04659  128 EFDLYDRLKAKL-LRLGIPTQFVREDTLKNRQDLAYVAWNLALALYAKLGGIPWKLDaDSDPADLYIGIGFARSR-DGEV 205

                 ....*
gi 530387871 756 SVVGF 760
Cdd:cd04659  206 RVTGC 210
PAZ_dicer_like cd02843
PAZ domain, dicer_like subfamily. Dicer is an RNAse involved in cleaving dsRNA in the RNA ...
401-472 2.45e-04

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: 41.66  E-value: 2.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530387871 401 NKEHFQDEctkllvgnIVITRYNNRT----YRIDDVDWNKTPKDSFtmSDGKEITFLEYYSKNYGITVKEEDQPLL 472
Cdd:cd02843   37 DAEDYQDA--------VVMPWYRNFDqpqyFYVAEICTDLRPLSKF--PGPEYETFEEYYKKKYKLDIQNLNQPLL 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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