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Conserved domains on  [gi|10946612|ref|NP_067286|]
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piwi-like protein 1 [Mus musculus]

Protein Classification

PAZ_piwi_like and Piwi_piwi-like_Euk domain-containing protein( domain architecture ID 12066143)

protein containing domains GAGE, ArgoL1, PAZ_piwi_like, and Piwi_piwi-like_Euk

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 ...
 402-845 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: 671.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 402 NVMKDLAVHTRLTPEQRQREVGRLIDYIHKDDNVQRELRDWGLSFDSNLLSFSGRILQSEKIHQGGKtFDYNPQFADWSK 481
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNV-FVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 482 ETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGIQMKKAIMIEV-DDRTEAYLRALQQKVTSDTQIVVCL 560
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVkDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 561 LSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDMP---LKLAMIVGIDCYHD 637
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYHD 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 638 TTAGRRSIAGFVASINEGMTRWFSRCVFQDRGQEL-VDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNY 716
Cdd:cd04658 240 TITKKKSVVGFVASLNKSITKWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLKKVKEY 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 717 EVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYN 796
Cdd:cd04658 320 EVPQIKKAIKQYSENYSPKLAYIVVNKRINTRFFNQGGNNFSNPPPGTVVDSEITKPEWYDFFLVSQSVRQGTVTPTHYN 399

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 10946612 797 VIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQ 845
Cdd:cd04658 400 VLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 278-416 3.37e-65

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: 214.07  E-value: 3.37e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    278 ETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITD 357
Cdd:smart00949   1 ETVLDFMRQLPSQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGSEITFVEYYKQKYNITIRD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 10946612    358 LKQPVLVSQPKRRRGPGGTlPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPE 416
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGK-GEPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
GAGE pfam05831
GAGE protein; This family consists of several GAGE and XAGE proteins which are found ...
 16-107 1.62e-26

GAGE protein; This family consists of several GAGE and XAGE proteins which are found exclusively in humans. The function of this family is unknown although they have been implicated in human cancers.


:

Pssm-ID: 461753  Cd Length: 107  Bit Score: 104.38  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    16 QETVQHVGAAASQQPGYIPPRPQQSPTEGDLVGRGRQRGmvVGATSKSQELQISAGFQELSLAERGGRRRDFHDLGVNTR 95
Cdd:pfam05831  18 QESSQLVGPVVAQQPSDEQPQQEEPPTESQDITPGQERE--DEGASAIQGPELEADLQELALEKTGGERGDGPDVKGKTL 95

                          90
                  ....*....|..
gi 10946612    96 QNLDHVKESKTG 107
Cdd:pfam05831  96 PNLEPVKMPEAG 107
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
 229-276 1.55e-03

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: 37.12  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 10946612   229 IGRNYY--NPSDPIDIPNHRLVIWPGFTTSILQYENNIMLCTDVSHKVLR 276
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 ...
 402-845 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: 671.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 402 NVMKDLAVHTRLTPEQRQREVGRLIDYIHKDDNVQRELRDWGLSFDSNLLSFSGRILQSEKIHQGGKtFDYNPQFADWSK 481
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNV-FVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 482 ETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGIQMKKAIMIEV-DDRTEAYLRALQQKVTSDTQIVVCL 560
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVkDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 561 LSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDMP---LKLAMIVGIDCYHD 637
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYHD 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 638 TTAGRRSIAGFVASINEGMTRWFSRCVFQDRGQEL-VDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNY 716
Cdd:cd04658 240 TITKKKSVVGFVASLNKSITKWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLKKVKEY 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 717 EVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYN 796
Cdd:cd04658 320 EVPQIKKAIKQYSENYSPKLAYIVVNKRINTRFFNQGGNNFSNPPPGTVVDSEITKPEWYDFFLVSQSVRQGTVTPTHYN 399

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 10946612 797 VIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQ 845
Cdd:cd04658 400 VLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
 556-848 6.70e-129

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: 388.24  E-value: 6.70e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   556 IVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTvMAIATKIALQMNCKMGGE-LWRVDMPLKLAMIVGIDC 634
Cdd:pfam02171   1 LILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRTL-KQTLTNVLLKINVKLGGInYWIVEIKPKVDVIIGFDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   635 YHDT--TAGRRSIAGFVASINEGMTRWFSRCVFQDRGQELVDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKT 712
Cdd:pfam02171  80 SHGTagTDDNPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSEGQFPQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   713 LVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSG-GRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVS 791
Cdd:pfam02171 160 VLNYEVNQIKEACKSLGPGYNPKLTVIVVQKRHHTRFFANDKpDGDQNPPPGTVVDDVITLPEYYDFYLCSHAGLQGTVK 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946612   792 PTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIH 848
Cdd:pfam02171 240 PTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
 556-848 5.83e-124

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: 375.52  E-value: 5.83e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    556 IVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTL---GKQQTVMAIATKIALQMNCKMGGELWRVD---MPLKLAMI 629
Cdd:smart00950   2 IVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTLdkvSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTLI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    630 VGIDCYHDTTAGRRSIAGFVASINeGMTRWFSRCVFQD-RGQELVDGLKVCLQAALRAWSG-CNEYMPSRVIVYRDGVGD 707
Cdd:smart00950  82 IGIDVSHPSAGKGGSVAPSVAAFV-ASGNYLSGNFYQAfVREQGSRQLKEILREALKKYYKsNRKRLPDRIVVYRDGVSE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    708 GQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRS 787
Cdd:smart00950 161 GQFKQVLEYEVKAIKKACKELGPDYKPKLTVIVVQKRHHTRFFPEDGNGRVNVPPGTVVDSVITSPEWYDFYLVSHAGLQ 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10946612    788 GSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIH 848
Cdd:smart00950 241 GTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLLH 301
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 278-416 3.37e-65

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: 214.07  E-value: 3.37e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    278 ETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITD 357
Cdd:smart00949   1 ETVLDFMRQLPSQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGSEITFVEYYKQKYNITIRD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 10946612    358 LKQPVLVSQPKRRRGPGGTlPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPE 416
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGK-GEPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
 277-394 2.78e-64

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: 210.96  E-value: 2.78e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 277 SETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEIT 356
Cdd:cd02845   1 STTVLDRMHKLYRQETDERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEYYKKQYNIEIT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 10946612 357 DLKQPVLVSQPKRRRGPGGTlPGPAMLIPELCYLTGLT 394
Cdd:cd02845  81 DLNQPLLVSRPKRRDPRGGE-KEPIYLIPELCFLTGLT 117
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 281-414 2.03e-45

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: 158.90  E-value: 2.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   281 LDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNN-KTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLK 359
Cdd:pfam02170   1 LDFLKRLQQQKDRRDFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKEITVVDYFKKKYNIDLKYPD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10946612   360 QPVLVSQPKRRRgpggtlpgpAMLIPELCYltgLTDKMRNDFNVMKDLAVHTRLT 414
Cdd:pfam02170  81 QPLLLVGKKRPK---------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
PLN03202 PLN03202
protein argonaute; Provisional
 252-850 1.04e-42

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 167.97  E-value: 1.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  252 GFTTSILQYENNIMLCTDVSHK-VLRSETVLDFMfnLYQQTEEHKFQ---EQVSKELIGLIVLTKYNNKTYRVddIDWDQ 327
Cdd:PLN03202 241 GFHSSFRTTQGGLSLNIDVSTTmIVQPGPVVDFL--IANQNVRDPFQidwSKAKRMLKNLRVKVSPSNQEYKI--TGLSE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  328 NP--KSTF--KKADGS-------EVSFLEYYRKQYNQEIT---DLkqPVL-VSQPKRrrgpggtlpgPAMLIPELCYLTG 392
Cdd:PLN03202 317 KPckEQTFslKQRNGNgnevetvEITVYDYFVKHRGIELRysgDL--PCInVGKPKR----------PTYFPIELCSLVS 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  393 LTdkmrndfNVMKDLAVHTRLT--------PEQRQREVGR-LIDYIHKDDNVqreLRDWGLSFDSNLLSFSGRILQSEKI 463
Cdd:PLN03202 385 LQ-------RYTKALSTLQRSSlveksrqkPQERMKVLTDaLKSSNYDADPM---LRSCGISISSQFTQVEGRVLPAPKL 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  464 hQGGKTFDYNPQFADWSKETRgaPLISVKPLDNWLLIytrrNYEA---ANSLIQNLFKVTPAMGIQMKKAI-MIEVDD-- 537
Cdd:PLN03202 455 -KVGNGEDFFPRNGRWNFNNK--KLVEPTKIERWAVV----NFSArcdIRHLVRDLIKCGEMKGINIEPPFdVFEENPqf 527

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  538 -------RTEAYLRALQQKVTSDTQIVVCLLSsNRK--DKYDAIKKYLCTDCPTPSQCVVARTLGKQQTvmaiaTKIALQ 608
Cdd:PLN03202 528 rrapppvRVEKMFEQIQSKLPGPPQFLLCILP-ERKnsDIYGPWKKKNLSEFGIVTQCIAPTRVNDQYL-----TNVLLK 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  609 MNCKMGG--ELWRVD----MPL--KL-AMIVGIDCYHDT--TAGRRSIAGFVASINEGMTRWFSRCV-FQDRGQELVDGL 676
Cdd:PLN03202 602 INAKLGGlnSLLAIEhspsIPLvsKVpTIILGMDVSHGSpgQSDVPSIAAVVSSRQWPLISRYRASVrTQSPKVEMIDSL 681

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  677 ----------KVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVN 746
Cdd:PLN03202 682 fkpvgdkdddGIIRELLLDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQIIEACKFLDESWSPKFTVIVAQKNHH 761

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  747 ARFFaQSGGRlQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGV 826
Cdd:PLN03202 762 TKFF-QAGSP-DNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGFSADDLQELVHSLSYVYQRSTTA 839

                        650       660
                 ....*....|....*....|....
gi 10946612  827 IRVPAPCQYAHKLAFLVGQSIHRE 850
Cdd:PLN03202 840 ISVVAPVCYAHLAAAQMGQFMKFE 863
GAGE pfam05831
GAGE protein; This family consists of several GAGE and XAGE proteins which are found ...
 16-107 1.62e-26

GAGE protein; This family consists of several GAGE and XAGE proteins which are found exclusively in humans. The function of this family is unknown although they have been implicated in human cancers.


Pssm-ID: 461753  Cd Length: 107  Bit Score: 104.38  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    16 QETVQHVGAAASQQPGYIPPRPQQSPTEGDLVGRGRQRGmvVGATSKSQELQISAGFQELSLAERGGRRRDFHDLGVNTR 95
Cdd:pfam05831  18 QESSQLVGPVVAQQPSDEQPQQEEPPTESQDITPGQERE--DEGASAIQGPELEADLQELALEKTGGERGDGPDVKGKTL 95

                          90
                  ....*....|..
gi 10946612    96 QNLDHVKESKTG 107
Cdd:pfam05831  96 PNLEPVKMPEAG 107
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
 229-276 1.55e-03

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: 37.12  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 10946612   229 IGRNYY--NPSDPIDIPNHRLVIWPGFTTSILQYENNIMLCTDVSHKVLR 276
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 ...
 402-845 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: 671.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 402 NVMKDLAVHTRLTPEQRQREVGRLIDYIHKDDNVQRELRDWGLSFDSNLLSFSGRILQSEKIHQGGKtFDYNPQFADWSK 481
Cdd:cd04658   1 NLMKELAEHTKLNPKERYDTIRQFIQRIQKNPSVQELLKKWGIELDSNPLKIQGRVLPPEQIIMGNV-FVYANSNADWKR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 482 ETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGIQMKKAIMIEV-DDRTEAYLRALQQKVTSDTQIVVCL 560
Cdd:cd04658  80 EIRNQPLYDAVNLNNWVLIYPSRDQREAESFLQTLKQVAGPMGIQISPPKIIKVkDDRIETYIRALKDAFRSDPQLVVII 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 561 LSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDMP---LKLAMIVGIDCYHD 637
Cdd:cd04658 160 LPGNKKDLYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASKIALQINAKLGGIPWTVEIPpfiLKNTMIVGIDVYHD 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 638 TTAGRRSIAGFVASINEGMTRWFSRCVFQDRGQEL-VDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNY 716
Cdd:cd04658 240 TITKKKSVVGFVASLNKSITKWFSKYISQVRGQEEiIDSLGKSMKKALKAYKKENKKLPSRIIIYRDGVGDGQLKKVKEY 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 717 EVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYN 796
Cdd:cd04658 320 EVPQIKKAIKQYSENYSPKLAYIVVNKRINTRFFNQGGNNFSNPPPGTVVDSEITKPEWYDFFLVSQSVRQGTVTPTHYN 399

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 10946612 797 VIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQ 845
Cdd:cd04658 400 VLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
 556-848 6.70e-129

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: 388.24  E-value: 6.70e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   556 IVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTvMAIATKIALQMNCKMGGE-LWRVDMPLKLAMIVGIDC 634
Cdd:pfam02171   1 LILVILPEKNKDLYHSIKKYLETDLGIPSQCILSKTILKRTL-KQTLTNVLLKINVKLGGInYWIVEIKPKVDVIIGFDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   635 YHDT--TAGRRSIAGFVASINEGMTRWFSRCVFQDRGQELVDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKT 712
Cdd:pfam02171  80 SHGTagTDDNPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSEGQFPQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   713 LVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSG-GRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVS 791
Cdd:pfam02171 160 VLNYEVNQIKEACKSLGPGYNPKLTVIVVQKRHHTRFFANDKpDGDQNPPPGTVVDDVITLPEYYDFYLCSHAGLQGTVK 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 10946612   792 PTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIH 848
Cdd:pfam02171 240 PTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
 556-848 5.83e-124

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: 375.52  E-value: 5.83e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    556 IVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTL---GKQQTVMAIATKIALQMNCKMGGELWRVD---MPLKLAMI 629
Cdd:smart00950   2 IVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTLdkvSKRRKLKQYLTNVALKINAKLGGINWVLDvppIPLKPTLI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    630 VGIDCYHDTTAGRRSIAGFVASINeGMTRWFSRCVFQD-RGQELVDGLKVCLQAALRAWSG-CNEYMPSRVIVYRDGVGD 707
Cdd:smart00950  82 IGIDVSHPSAGKGGSVAPSVAAFV-ASGNYLSGNFYQAfVREQGSRQLKEILREALKKYYKsNRKRLPDRIVVYRDGVSE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    708 GQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRS 787
Cdd:smart00950 161 GQFKQVLEYEVKAIKKACKELGPDYKPKLTVIVVQKRHHTRFFPEDGNGRVNVPPGTVVDSVITSPEWYDFYLVSHAGLQ 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10946612    788 GSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIH 848
Cdd:smart00950 241 GTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLLH 301
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
 439-841 2.92e-78

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: 259.85  E-value: 2.92e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 439 LRDWGLSFDSNLLSFSGRILQSEKIHQGGKTFDYNPQFADWskETRGAPLISVKPLDNWLLIY---TRRNYEAANSL--- 512
Cdd:cd04657   3 LKEFGISVSKEMITVPGRVLPPPKLKYGDSSKTVPPRNGSW--NLRGKKFLEGGPIRSWAVLNfagPRRSREERADLrnf 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 513 IQNLFKVTPAMGIQMKkAIMIEVDDRTEAYLRALQQKVTSDTQIVVCLLSSNRKDKYDAIKKylCTDCPT--PSQCVVAR 590
Cdd:cd04657  81 VDQLVKTVIGAGINIT-TAIASVEGRVEELFAKLKQAKGEGPQLVLVILPKKDSDIYGRIKR--LADTELgiHTQCVLAK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 591 TLGKQQTvMAIATKIALQMNCKMGGELWRVD------MPLKLAMIVGIDCYH---DTTAGRRSIAGFVASINEGMTRWFS 661
Cdd:cd04657 158 KVTKKGN-PQYFANVALKINLKLGGINHSLEpdirplLTKEPTMVLGADVTHpspGDPAGAPSIAAVVASVDWHLAQYPA 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 662 RCVFQDRGQELVDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVV 741
Cdd:cd04657 237 SVRLQSHRQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGVSEGQFAQVLNEELPAIRKACAKLYPGYKPKITFIVV 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 742 KKRVNARFFAQSG----GRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLC 817
Cdd:cd04657 317 QKRHHTRFFPTDEddadGKNGNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFTADELQTLTYNLC 396

                       410       420       430
                ....*....|....*....|....*....|
gi 10946612 818 HVYynwpgvIR------VPAPCQYAHKLAF 841
Cdd:cd04657 397 YTY------ARctrsvsIPPPAYYAHLAAA 420
Piwi-like cd02826
Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing ...
 451-842 1.74e-74

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: 248.84  E-value: 1.74e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 451 LSFSGRILQSEKIhqGGKTFDYNPQFADWSKETRGaplisvkplDNWLLIYTRrnYEAANSLIQNL--FKVTPAMGIQMK 528
Cdd:cd02826   3 LILKGRVLPKPQI--LFKNKFLRNIGPFEKPAKIT---------NPVAVIAFR--NEEVDDLVKRLadACRQLGMKIKEI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 529 --KAIMIEVDDRTEAYLRALQQKVTSDTQIVVCLLSSNRKDKYDAIKKYLCTDcPTPSQCVVARTLGKQQTVMAIATKIA 606
Cdd:cd02826  70 piVSWIEDLNNSFKDLKSVFKNAIKAGVQLVIFILKEKKPPLHDEIKRLEAKS-DIPSQVIQLKTAKKMRRLKQTLDNLL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 607 LQMNCKMGGELWRVDMPLKL---AMIVGIDCYH---DTTAGRRSIAGFVASINEGM---TRWFSRCVFQDRGQELVDGLK 677
Cdd:cd02826 149 RKVNSKLGGINYILDSPVKLfksDIFIGFDVSHpdrRTVNGGPSAVGFAANLSNHTflgGFLYVQPSREVKLQDLGEVIK 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 678 VCLQAALRAwsgCNEYMPSRVIVYRDGVGDGQLKtLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFA-QSGGR 756
Cdd:cd02826 229 KCLDGFKKS---TGEGLPEKIVIYRDGVSEGEFK-RVKEEVEEIIKEACEIEESYRPKLVIIVVQKRHNTRFFPnEKNGG 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 757 LQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYA 836
Cdd:cd02826 305 VQNPEPGTVVDHTITSPGLSEFYLASHVARQGTVKPTKYTVVFNDKNWSLNELEILTYILCLTHQNVYSPISLPAPLYYA 384


                ....*.
gi 10946612 837 HKLAFL 842
Cdd:cd02826 385 HKLAKR 390
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
 278-416 3.37e-65

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: 214.07  E-value: 3.37e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    278 ETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITD 357
Cdd:smart00949   1 ETVLDFMRQLPSQGNRSNFQDRCAKDLKGLIVLTRYNNKTYRIDDIDWNLAPKSTFEKSDGSEITFVEYYKQKYNITIRD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 10946612    358 LKQPVLVSQPKRRRGPGGTlPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPE 416
Cdd:smart00949  81 PNQPLLVSRPKRRRNQNGK-GEPVLLPPELCFITGLTDRMRKDFMLMKSIADRTRLSPL 138
PAZ_piwi_like cd02845
PAZ domain, Piwi_like subfamily. In multi-cellular organisms, the Piwi protein appears to be ...
 277-394 2.78e-64

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: 210.96  E-value: 2.78e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 277 SETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEIT 356
Cdd:cd02845   1 STTVLDRMHKLYRQETDERFREECEKELIGSIVLTRYNNKTYRIDDIDFDKTPLSTFKKSDGTEITFVEYYKKQYNIEIT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 10946612 357 DLKQPVLVSQPKRRRGPGGTlPGPAMLIPELCYLTGLT 394
Cdd:cd02845  81 DLNQPLLVSRPKRRDPRGGE-KEPIYLIPELCFLTGLT 117
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
 281-414 2.03e-45

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: 158.90  E-value: 2.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612   281 LDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNN-KTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLK 359
Cdd:pfam02170   1 LDFLKRLQQQKDRRDFRKEAKKALKGLKVYTTYNNpRTYRIDGITFDPTPESTFPLKDGKEITVVDYFKKKYNIDLKYPD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 10946612   360 QPVLVSQPKRRRgpggtlpgpAMLIPELCYltgLTDKMRNDFNVMKDLAVHTRLT 414
Cdd:pfam02170  81 QPLLLVGKKRPK---------VYLPPELCN---LVDGQRYTKKLMPSIAQRTRLL 123
PLN03202 PLN03202
protein argonaute; Provisional
 252-850 1.04e-42

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 167.97  E-value: 1.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  252 GFTTSILQYENNIMLCTDVSHK-VLRSETVLDFMfnLYQQTEEHKFQ---EQVSKELIGLIVLTKYNNKTYRVddIDWDQ 327
Cdd:PLN03202 241 GFHSSFRTTQGGLSLNIDVSTTmIVQPGPVVDFL--IANQNVRDPFQidwSKAKRMLKNLRVKVSPSNQEYKI--TGLSE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  328 NP--KSTF--KKADGS-------EVSFLEYYRKQYNQEIT---DLkqPVL-VSQPKRrrgpggtlpgPAMLIPELCYLTG 392
Cdd:PLN03202 317 KPckEQTFslKQRNGNgnevetvEITVYDYFVKHRGIELRysgDL--PCInVGKPKR----------PTYFPIELCSLVS 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  393 LTdkmrndfNVMKDLAVHTRLT--------PEQRQREVGR-LIDYIHKDDNVqreLRDWGLSFDSNLLSFSGRILQSEKI 463
Cdd:PLN03202 385 LQ-------RYTKALSTLQRSSlveksrqkPQERMKVLTDaLKSSNYDADPM---LRSCGISISSQFTQVEGRVLPAPKL 454

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  464 hQGGKTFDYNPQFADWSKETRgaPLISVKPLDNWLLIytrrNYEA---ANSLIQNLFKVTPAMGIQMKKAI-MIEVDD-- 537
Cdd:PLN03202 455 -KVGNGEDFFPRNGRWNFNNK--KLVEPTKIERWAVV----NFSArcdIRHLVRDLIKCGEMKGINIEPPFdVFEENPqf 527

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  538 -------RTEAYLRALQQKVTSDTQIVVCLLSsNRK--DKYDAIKKYLCTDCPTPSQCVVARTLGKQQTvmaiaTKIALQ 608
Cdd:PLN03202 528 rrapppvRVEKMFEQIQSKLPGPPQFLLCILP-ERKnsDIYGPWKKKNLSEFGIVTQCIAPTRVNDQYL-----TNVLLK 601

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  609 MNCKMGG--ELWRVD----MPL--KL-AMIVGIDCYHDT--TAGRRSIAGFVASINEGMTRWFSRCV-FQDRGQELVDGL 676
Cdd:PLN03202 602 INAKLGGlnSLLAIEhspsIPLvsKVpTIILGMDVSHGSpgQSDVPSIAAVVSSRQWPLISRYRASVrTQSPKVEMIDSL 681

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  677 ----------KVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVN 746
Cdd:PLN03202 682 fkpvgdkdddGIIRELLLDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQIIEACKFLDESWSPKFTVIVAQKNHH 761

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612  747 ARFFaQSGGRlQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGV 826
Cdd:PLN03202 762 TKFF-QAGSP-DNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGFSADDLQELVHSLSYVYQRSTTA 839

                        650       660
                 ....*....|....*....|....
gi 10946612  827 IRVPAPCQYAHKLAFLVGQSIHRE 850
Cdd:PLN03202 840 ISVVAPVCYAHLAAAQMGQFMKFE 863
GAGE pfam05831
GAGE protein; This family consists of several GAGE and XAGE proteins which are found ...
 16-107 1.62e-26

GAGE protein; This family consists of several GAGE and XAGE proteins which are found exclusively in humans. The function of this family is unknown although they have been implicated in human cancers.


Pssm-ID: 461753  Cd Length: 107  Bit Score: 104.38  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612    16 QETVQHVGAAASQQPGYIPPRPQQSPTEGDLVGRGRQRGmvVGATSKSQELQISAGFQELSLAERGGRRRDFHDLGVNTR 95
Cdd:pfam05831  18 QESSQLVGPVVAQQPSDEQPQQEEPPTESQDITPGQERE--DEGASAIQGPELEADLQELALEKTGGERGDGPDVKGKTL 95

                          90
                  ....*....|..
gi 10946612    96 QNLDHVKESKTG 107
Cdd:pfam05831  96 PNLEPVKMPEAG 107
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
 279-391 1.03e-16

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: 76.73  E-value: 1.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 279 TVLDFMFNLYQQTEEHK-----FQEQVSKELIGLIVLTKYN--NKTYRVDDIDWDQNPkSTFKKADGSEVSFLEYYRKQY 351
Cdd:cd02825   3 PVIETMCKFPKDREIDTplldsPREEFTKELKGLKVEDTHNplNRVYRPDGETRLKAP-SQLKHSDGKEITFADYFKERY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 10946612 352 NQEITDLKQPVLVSQPKRRrgpggtLPGPAMLIPELCYLT 391
Cdd:cd02825  82 NLTLTDLNQPLLIVKFSSK------KSYSILLPPELCVIT 115
Piwi_piwi-like_ProArk cd04659
Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA ...
 533-844 1.44e-09

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: 60.86  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 533 IEVDDRTEAYLRALQQKVTSDTQ----IVVCLLSSNRK-----DKYDAIKKYLcTDCPTPSQCVVARTLGKQQTVMAIAT 603
Cdd:cd04659  87 LNRSAQAEAIIEAVDLALSESSQgvdvVIVVLPEDLKElpeefDLYDRLKAKL-LRLGIPTQFVREDTLKNRQDLAYVAW 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 604 KIALQMNCKMGGELWRVD-MPLKLAMIVGIDCYHDTTAGRR--SIAGFVASINEGMTRWFSR--CVFQDRGQELV-DGLK 677
Cdd:cd04659 166 NLALALYAKLGGIPWKLDaDSDPADLYIGIGFARSRDGEVRvtGCAQVFDSDGLGLILRGAPieEPTEDRSPADLkDLLK 245

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 678 VCLQAALRAWsgcNEYMPSRVIVYRDGvgdgqlkTLVNYEVPQFLDCLKSVGRgynpRLTVIVVKKRVNARFFAQSG-GR 756
Cdd:cd04659 246 RVLEGYRESH---RGRDPKRLVLHKDG-------RFTDEEIEGLKEALEELGI----KVDLVEVIKSGPHRLFRFGTyPN 311

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 757 LQNPLPGTVIDVEVTRPewydFFIVSQAVRSGSVSPTHYN-----VIYDSSGLKPDHIQRLTYKLCHVYYNWP-GVIRVP 830
Cdd:cd04659 312 GFPPRRGTYVKLSDDEG----LLWTHGSVPKYNTYPGMGTprpllLRRHSGNTDLEQLASQILGLTKLNWNSFqFYSRLP 387

                       330
                ....*....|....
gi 10946612 831 APCQYAHKLAFLVG 844
Cdd:cd04659 388 VTIHYADRVAKLLK 401
PAZ_CAF_like cd02844
PAZ domain, CAF_like subfamily. CAF (for carpel factory) is a plant homolog of Dicer. CAF has ...
 300-388 2.88e-06

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: 47.42  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 300 VSKELIGLIVLTKYNNKTYrVDDIDWDQNPKSTFKKADGSEV-SFLEYYRKQYNQEITDLKQPVLVSQP----------- 367
Cdd:cd02844  27 CACDLKGSVVTAPHNGRFY-VISGILDLNANSSFPGKEGLGYaTYAEYFKEKYGIVLNHPNQPLLKGKQifnlhnllhnr 105

                        90       100
                ....*....|....*....|....
gi 10946612 368 KRRRGPGGTLPGP---AMLIPELC 388
Cdd:cd02844 106 FEEKGESEEKEKDryfVELPPELC 129
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
 300-388 3.98e-04

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: 40.76  E-value: 3.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 300 VSKELIGLIVLTKY---NNKTYRVDDIDWDQNPKSTFKKADGS-EVSFLEYYRKQYNQEITDLKQPVLVSQPKRRrgpgg 375
Cdd:cd02846  28 LKKALKGLKVEVTHrgnTNRKYKIKGLSAEPASQQTFELKDGEkEISVADYFKEKYNIRLKYPNLPCLQVGRKGK----- 102

                        90
                ....*....|...
gi 10946612 376 tlpgPAMLIPELC 388
Cdd:cd02846 103 ----PNYLPMELC 111
PAZ_dicer_like cd02843
PAZ domain, dicer_like subfamily. Dicer is an RNAse involved in cleaving dsRNA in the RNA ...
 308-363 5.78e-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: 40.51  E-value: 5.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946612 308 IVLTKYNN----KTYRVDDIDWDQNPKSTFKKADGSevSFLEYYRKQYNQEITDLKQPVL 363
Cdd:cd02843  45 VVMPWYRNfdqpQYFYVAEICTDLRPLSKFPGPEYE--TFEEYYKKKYKLDIQNLNQPLL 102
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
 229-276 1.55e-03

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: 37.12  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 10946612   229 IGRNYY--NPSDPIDIPNHRLVIWPGFTTSILQYENNIMLCTDVSHKVLR 276
Cdd:pfam08699   2 VGRSFFspPGENRVDLGGGGLEAWRGFFQSVRPTQGGLLLNVDVSHTAFY 51
 
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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