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Conserved domains on  [gi|442632519|ref|NP_001261882|]
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argonaute 2, isoform E [Drosophila melanogaster]

Protein Classification

argonaute/piwi family protein( domain architecture ID 11243136)

argonaute/piwi family protein may play a central role in RNA silencing processes, as an essential component of the RNA-induced silencing complex (RISC) that is responsible for the gene silencing phenomenon known as RNA interference (RNAi); contains argonaute linker 1 (ArgoL1), PAZ (Piwi Argonaut and Zwille), ArgoN (N-terminal domain of argonaute) and Piwi domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
334-756 0e+00

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: 525.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 334 PTISRFGIRIANDFIVVSTRVLSPPQVEYH-SKRFTMVKNGSWRMDGMKFLEPKPkAHKCAVLYCDPRSGRKMNYTQLND 412
Cdd:cd04657    1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGdSSKTVPPRNGSWNLRGKKFLEGGP-IRSWAVLNFAGPRRSREERADLRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 413 FGNLIISQGKAVNISLDSDVTYrpftdDERSLDTIFADLKRS---QHDLAIVIIPQFRIS-YDTIKQKAELQHGILTQCI 488
Cdd:cd04657   80 FVDQLVKTVIGAGINITTAIAS-----VEGRVEELFAKLKQAkgeGPQLVLVILPKKDSDiYGRIKRLADTELGIHTQCV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 489 KQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPR-LPMMKNTMYIGADVTHPSP-DQREIPSVVGVAASHDPYGASY 566
Cdd:cd04657  155 LAKKVTKKGNPQYFANVALKINLKLGGINHSLEPDIRpLLTKEPTMVLGADVTHPSPgDPAGAPSIAAVVASVDWHLAQY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 567 NMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACDKVGC--KPKICCV 644
Cdd:cd04657  235 PASVRLQSHRQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGVSEGQFAQVLNEELPAIRKACAKLYPgyKPKITFI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 645 IVVKRHHTRFFPSGDVTTSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYN 724
Cdd:cd04657  315 VVQKRHHTRFFPTDEDDADGKNGNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFTADELQTLTYN 394
                        410       420       430
                 ....*....|....*....|....*....|..
gi 442632519 725 LCHMFPRCNRSVSYPAPAYLAHLVAARGRVYL 756
Cdd:cd04657  395 LCYTYARCTRSVSIPPPAYYAHLAAARARCYL 426
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
175-289 2.79e-32

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: 121.03  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 175 MPMIEYLERFSLKAKINnTTNLDYSRRFLEPFLRGINVVYTPPQsfqsAPRVYRVNGLSRAPASSETFEHDGKKVTIASY 254
Cdd:cd02825    2 DPVIETMCKFPKDREID-TPLLDSPREEFTKELKGLKVEDTHNP----LNRVYRPDGETRLKAPSQLKHSDGKEITFADY 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442632519 255 FHSRNYP-LKFPQLHCLNVGSS---IKSILLPIELCSIE 289
Cdd:cd02825   77 FKERYNLtLTDLNQPLLIVKFSskkSYSILLPPELCVIT 115
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
124-171 3.02e-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: 50.60  E-value: 3.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442632519  124 VGRSFFKMSDPNNRHELDDGYEALVGLYQAFMLGD-RPFLNVDISHKSF 171
Cdd:pfam08699   2 VGRSFFSPPGENRVDLGGGGLEAWRGFFQSVRPTQgGLLLNVDVSHTAF 50
ArgoN pfam16486
N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in ...
41-113 1.35e-06

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


:

Pssm-ID: 465134  Cd Length: 93  Bit Score: 47.28  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   41 DGKASCYSVDKLPLNSQNPEVTVTDRNG---------RTLRYTIEIKETGdsTIDLKSLTTYMNDRIFDKPMRAMQCVEV 111
Cdd:pfam16486  14 DGRKNLYSAKKLPFGEEEFVVLDEEPGRgarkrpgvrRPRTFKVTIKFTK--TINLQDLLEYLRGKQDNTPLEAIQALDI 91

                  ..
gi 442632519  112 VL 113
Cdd:pfam16486  92 VL 93
 
Name Accession Description Interval E-value
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
334-756 0e+00

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: 525.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 334 PTISRFGIRIANDFIVVSTRVLSPPQVEYH-SKRFTMVKNGSWRMDGMKFLEPKPkAHKCAVLYCDPRSGRKMNYTQLND 412
Cdd:cd04657    1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGdSSKTVPPRNGSWNLRGKKFLEGGP-IRSWAVLNFAGPRRSREERADLRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 413 FGNLIISQGKAVNISLDSDVTYrpftdDERSLDTIFADLKRS---QHDLAIVIIPQFRIS-YDTIKQKAELQHGILTQCI 488
Cdd:cd04657   80 FVDQLVKTVIGAGINITTAIAS-----VEGRVEELFAKLKQAkgeGPQLVLVILPKKDSDiYGRIKRLADTELGIHTQCV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 489 KQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPR-LPMMKNTMYIGADVTHPSP-DQREIPSVVGVAASHDPYGASY 566
Cdd:cd04657  155 LAKKVTKKGNPQYFANVALKINLKLGGINHSLEPDIRpLLTKEPTMVLGADVTHPSPgDPAGAPSIAAVVASVDWHLAQY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 567 NMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACDKVGC--KPKICCV 644
Cdd:cd04657  235 PASVRLQSHRQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGVSEGQFAQVLNEELPAIRKACAKLYPgyKPKITFI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 645 IVVKRHHTRFFPSGDVTTSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYN 724
Cdd:cd04657  315 VVQKRHHTRFFPTDEDDADGKNGNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFTADELQTLTYN 394
                        410       420       430
                 ....*....|....*....|....*....|..
gi 442632519 725 LCHMFPRCNRSVSYPAPAYLAHLVAARGRVYL 756
Cdd:cd04657  395 LCYTYARCTRSVSIPPPAYYAHLAAARARCYL 426
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
458-756 1.67e-103

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: 320.44  E-value: 1.67e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   458 LAIVIIPQFRIS--YDTIKQKAELQHGILTQCIKQFTVE----RKCNNQTIGNILLKINSKLNGINHKIKDDPrlPMMKN 531
Cdd:smart00950   1 LIVVILPGEKKTdlYHEIKKYLETKLGVPTQCVQAKTLDkvskRRKLKQYLTNVALKINAKLGGINWVLDVPP--IPLKP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   532 TMYIGADVTHPSPD--QREIPSVVGVAASHDPYGASYnmqYRLQRGAlEEIEDMFSITLEHLR-VYKEYRNAYPDHIIYY 608
Cdd:smart00950  79 TLIIGIDVSHPSAGkgGSVAPSVAAFVASGNYLSGNF---YQAFVRE-QGSRQLKEILREALKkYYKSNRKRLPDRIVVY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   609 RDGVSDGQFPKIKNEELRCIKQACDKVG--CKPKICCVIVVKRHHTRFFPSGdvttSNKFNNVDPGTVVDRTIVHPNEMQ 686
Cdd:smart00950 155 RDGVSEGQFKQVLEYEVKAIKKACKELGpdYKPKLTVIVVQKRHHTRFFPED----GNGRVNVPPGTVVDSVITSPEWYD 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   687 FFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGRVYL 756
Cdd:smart00950 231 FYLVSHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLL 300
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
460-753 2.72e-80

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: 259.58  E-value: 2.72e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  460 IVIIPQFRIS-YDTIKQKAELQHGILTQCIKQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPRlpmmKNTMYIGAD 538
Cdd:pfam02171   3 LVILPEKNKDlYHSIKKYLETDLGIPSQCILSKTILKRTLKQTLTNVLLKINVKLGGINYWIVEIKP----KVDVIIGFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  539 VTHPSPDQREIPSVVGVAASHDPYGASYNMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFP 618
Cdd:pfam02171  79 ISHGTAGTDDNPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSEGQFP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  619 KIKNEELRCIKQACDKVGCK--PKICCVIVVKRHHTRFFPSGDvttSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQ 696
Cdd:pfam02171 159 QVLNYEVNQIKEACKSLGPGynPKLTVIVVQKRHHTRFFANDK---PDGDQNPPPGTVVDDVITLPEYYDFYLCSHAGLQ 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632519  697 GTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGR 753
Cdd:pfam02171 236 GTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVR 292
PLN03202 PLN03202
protein argonaute; Provisional
6-750 1.85e-77

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 268.51  E-value: 1.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   6 YHYDVKIMPE--RP-------KKFYRQAFEQFRVDqLGGAVLAYDGKASCYSVDKLPLNsqNPEVTV------TDRNG-- 68
Cdd:PLN03202  65 FHYSVSLTYEdgRPvdgkgigRKVIDKVQETYSSD-LAGKDFAYDGEKSLFTVGALPQN--KLEFTVvledvsSNRNNgn 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  69 ---------------------RTLRYTIEIKETgdSTIDLKSLTTYMNDRIFDKPMRAMQCVEVVLaspCHNKAIR---- 123
Cdd:PLN03202 142 gspvgngspnggdrkrsrrpyQSKTFKVEISFA--AKIPMQAIANALRGQESENSQDALRVLDIIL---RQHAAKQgcll 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 124 VGRSFFKmSDPNNRHELDDGYEALVGLYQAFmlgdRP-----FLNVDISHKSFPISMPMIEYLerfSLKAKINNTTNLDY 198
Cdd:PLN03202 217 VRQSFFH-NDPKNFVDLGGGVLGCRGFHSSF----RTtqgglSLNIDVSTTMIVQPGPVVDFL---IANQNVRDPFQIDW 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 199 S--RRFLEPfLRginvVYTPPQSFQsaprvYRVNGLSRAPASSETF----------EHDGKKVTIASYF-HSRNYPLKFP 265
Cdd:PLN03202 289 SkaKRMLKN-LR----VKVSPSNQE-----YKITGLSEKPCKEQTFslkqrngngnEVETVEITVYDYFvKHRGIELRYS 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 266 -QLHCLNVGSSIKSILLPIELCSIEEGQALNRKDGATQVANMIKYAATSTNVRKRKIMNLLQYFQHNLDPTISRFGIRIA 344
Cdd:PLN03202 359 gDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDALKSSNYDADPMLRSCGISIS 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 345 NDFIVVSTRVLSPPQVEYHSKRFTMVKNGSWRMDGMKFLEPKpKAHKCAVL----YCDPRsgrkmnyTQLNDfgnlIISQ 420
Cdd:PLN03202 439 SQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPT-KIERWAVVnfsaRCDIR-------HLVRD----LIKC 506
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 421 GKAVNISLDS-------DVTYR---PFTDDERSLDTIFADLKRSQHDLaIVIIPQFRIS--YDTIKQKAELQHGILTQCI 488
Cdd:PLN03202 507 GEMKGINIEPpfdvfeeNPQFRrapPPVRVEKMFEQIQSKLPGPPQFL-LCILPERKNSdiYGPWKKKNLSEFGIVTQCI 585
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 489 KQFTVerkcNNQTIGNILLKINSKLNGINH--KIKDDPRLPMMKN--TMYIGADVTHPSPDQREIPSVVGVAAS-HDPYG 563
Cdd:PLN03202 586 APTRV----NDQYLTNVLLKINAKLGGLNSllAIEHSPSIPLVSKvpTIILGMDVSHGSPGQSDVPSIAAVVSSrQWPLI 661
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 564 ASYNMQYRLQRGALEEIEDMFS---------ITLEHL-RVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACD 633
Cdd:PLN03202 662 SRYRASVRTQSPKVEMIDSLFKpvgdkdddgIIRELLlDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQIIEACK 741
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 634 KVGCK--PKICCVIVVKRHHTRFFPSGDVttsnkfNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTG 711
Cdd:PLN03202 742 FLDESwsPKFTVIVAQKNHHTKFFQAGSP------DNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEI 815
                        810       820       830
                 ....*....|....*....|....*....|....*....
gi 442632519 712 NLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAA 750
Cdd:PLN03202 816 GFSADDLQELVHSLSYVYQRSTTAISVVAPVCYAHLAAA 854
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
175-289 2.79e-32

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: 121.03  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 175 MPMIEYLERFSLKAKINnTTNLDYSRRFLEPFLRGINVVYTPPQsfqsAPRVYRVNGLSRAPASSETFEHDGKKVTIASY 254
Cdd:cd02825    2 DPVIETMCKFPKDREID-TPLLDSPREEFTKELKGLKVEDTHNP----LNRVYRPDGETRLKAPSQLKHSDGKEITFADY 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442632519 255 FHSRNYP-LKFPQLHCLNVGSS---IKSILLPIELCSIE 289
Cdd:cd02825   77 FKERYNLtLTDLNQPLLIVKFSskkSYSILLPPELCVIT 115
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
178-307 1.47e-20

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: 88.02  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  178 IEYLERFSLKAKINNttnldySRRFLEPFLRGINVVYTPpqsfqSAPRVYRVNGLSRAPASSETFE-HDGKKVTIASYFH 256
Cdd:pfam02170   1 LDFLKRLQQQKDRRD------FRKEAKKALKGLKVYTTY-----NNPRTYRIDGITFDPTPESTFPlKDGKEITVVDYFK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442632519  257 SR-NYPLKFPQLHCLNVGSSIKSILLPIELCSIEEGQALNRKDGAT--QVANMI 307
Cdd:pfam02170  70 KKyNIDLKYPDQPLLLVGKKRPKVYLPPELCNLVDGQRYTKKLMPSiaQRTRLL 123
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
124-171 3.02e-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: 50.60  E-value: 3.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442632519  124 VGRSFFKMSDPNNRHELDDGYEALVGLYQAFMLGD-RPFLNVDISHKSF 171
Cdd:pfam08699   2 VGRSFFSPPGENRVDLGGGGLEAWRGFFQSVRPTQgGLLLNVDVSHTAF 50
ArgoN pfam16486
N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in ...
41-113 1.35e-06

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


Pssm-ID: 465134  Cd Length: 93  Bit Score: 47.28  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   41 DGKASCYSVDKLPLNSQNPEVTVTDRNG---------RTLRYTIEIKETGdsTIDLKSLTTYMNDRIFDKPMRAMQCVEV 111
Cdd:pfam16486  14 DGRKNLYSAKKLPFGEEEFVVLDEEPGRgarkrpgvrRPRTFKVTIKFTK--TINLQDLLEYLRGKQDNTPLEAIQALDI 91

                  ..
gi 442632519  112 VL 113
Cdd:pfam16486  92 VL 93
 
Name Accession Description Interval E-value
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
334-756 0e+00

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: 525.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 334 PTISRFGIRIANDFIVVSTRVLSPPQVEYH-SKRFTMVKNGSWRMDGMKFLEPKPkAHKCAVLYCDPRSGRKMNYTQLND 412
Cdd:cd04657    1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGdSSKTVPPRNGSWNLRGKKFLEGGP-IRSWAVLNFAGPRRSREERADLRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 413 FGNLIISQGKAVNISLDSDVTYrpftdDERSLDTIFADLKRS---QHDLAIVIIPQFRIS-YDTIKQKAELQHGILTQCI 488
Cdd:cd04657   80 FVDQLVKTVIGAGINITTAIAS-----VEGRVEELFAKLKQAkgeGPQLVLVILPKKDSDiYGRIKRLADTELGIHTQCV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 489 KQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPR-LPMMKNTMYIGADVTHPSP-DQREIPSVVGVAASHDPYGASY 566
Cdd:cd04657  155 LAKKVTKKGNPQYFANVALKINLKLGGINHSLEPDIRpLLTKEPTMVLGADVTHPSPgDPAGAPSIAAVVASVDWHLAQY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 567 NMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACDKVGC--KPKICCV 644
Cdd:cd04657  235 PASVRLQSHRQEIIDDLESMVRELLRAFKKATGKLPERIIYYRDGVSEGQFAQVLNEELPAIRKACAKLYPgyKPKITFI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 645 IVVKRHHTRFFPSGDVTTSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYN 724
Cdd:cd04657  315 VVQKRHHTRFFPTDEDDADGKNGNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARPTHYHVLWDEIGFTADELQTLTYN 394
                        410       420       430
                 ....*....|....*....|....*....|..
gi 442632519 725 LCHMFPRCNRSVSYPAPAYLAHLVAARGRVYL 756
Cdd:cd04657  395 LCYTYARCTRSVSIPPPAYYAHLAAARARCYL 426
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
458-756 1.67e-103

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: 320.44  E-value: 1.67e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   458 LAIVIIPQFRIS--YDTIKQKAELQHGILTQCIKQFTVE----RKCNNQTIGNILLKINSKLNGINHKIKDDPrlPMMKN 531
Cdd:smart00950   1 LIVVILPGEKKTdlYHEIKKYLETKLGVPTQCVQAKTLDkvskRRKLKQYLTNVALKINAKLGGINWVLDVPP--IPLKP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   532 TMYIGADVTHPSPD--QREIPSVVGVAASHDPYGASYnmqYRLQRGAlEEIEDMFSITLEHLR-VYKEYRNAYPDHIIYY 608
Cdd:smart00950  79 TLIIGIDVSHPSAGkgGSVAPSVAAFVASGNYLSGNF---YQAFVRE-QGSRQLKEILREALKkYYKSNRKRLPDRIVVY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   609 RDGVSDGQFPKIKNEELRCIKQACDKVG--CKPKICCVIVVKRHHTRFFPSGdvttSNKFNNVDPGTVVDRTIVHPNEMQ 686
Cdd:smart00950 155 RDGVSEGQFKQVLEYEVKAIKKACKELGpdYKPKLTVIVVQKRHHTRFFPED----GNGRVNVPPGTVVDSVITSPEWYD 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   687 FFMVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGRVYL 756
Cdd:smart00950 231 FYLVSHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQLL 300
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
460-753 2.72e-80

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: 259.58  E-value: 2.72e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  460 IVIIPQFRIS-YDTIKQKAELQHGILTQCIKQFTVERKCNNQTIGNILLKINSKLNGINHKIKDDPRlpmmKNTMYIGAD 538
Cdd:pfam02171   3 LVILPEKNKDlYHSIKKYLETDLGIPSQCILSKTILKRTLKQTLTNVLLKINVKLGGINYWIVEIKP----KVDVIIGFD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  539 VTHPSPDQREIPSVVGVAASHDPYGASYNMQYRLQRGALEEIEDMFSITLEHLRVYKEYRNAYPDHIIYYRDGVSDGQFP 618
Cdd:pfam02171  79 ISHGTAGTDDNPSVAAVVASFDKGNSRYFGTVRTQASGQELLEPLKDIIKELLRSFQKSSRKKPERIIVYRDGVSEGQFP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  619 KIKNEELRCIKQACDKVGCK--PKICCVIVVKRHHTRFFPSGDvttSNKFNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQ 696
Cdd:pfam02171 159 QVLNYEVNQIKEACKSLGPGynPKLTVIVVQKRHHTRFFANDK---PDGDQNPPPGTVVDDVITLPEYYDFYLCSHAGLQ 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442632519  697 GTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGR 753
Cdd:pfam02171 236 GTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVR 292
Piwi_piwi-like_Euk cd04658
Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found ...
305-746 3.75e-79

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: 261.82  E-value: 3.75e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 305 NMIKYAATSTNV----RKRKIMNLLQYFQHNLDPT--ISRFGIRIANDFIVVSTRVLSPPQVEYHSKRFTMVKNGSWRMD 378
Cdd:cd04658    1 NLMKELAEHTKLnpkeRYDTIRQFIQRIQKNPSVQelLKKWGIELDSNPLKIQGRVLPPEQIIMGNVFVYANSNADWKRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 379 GMKFLEPKPKAHKCAVLYCDPRsgrkmNYTQLNDFGNLIISQGKAVNISLDsdvtyRPFTD--DERSLDTIFADLK---R 453
Cdd:cd04658   81 IRNQPLYDAVNLNNWVLIYPSR-----DQREAESFLQTLKQVAGPMGIQIS-----PPKIIkvKDDRIETYIRALKdafR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 454 SQHDLAIVIIPQFRIS-YDTIKQKAELQHGILTQCIKQFTVERKCNNQTIGN-ILLKINSKLNGINHKIKDDPRlpMMKN 531
Cdd:cd04658  151 SDPQLVVIILPGNKKDlYDAIKKFCCVECPVPSQVITSRTLKKKKNLRSIASkIALQINAKLGGIPWTVEIPPF--ILKN 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 532 TMYIGADVTHPSPDQREipSVVGVAASHDPYGASYNMQYRLQRGALEEIEDMFSITLEH-LRVYKEYRNAYPDHIIYYRD 610
Cdd:cd04658  229 TMIVGIDVYHDTITKKK--SVVGFVASLNKSITKWFSKYISQVRGQEEIIDSLGKSMKKaLKAYKKENKKLPSRIIIYRD 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 611 GVSDGQFPKIKNEELRCIKQACDKVGC--KPKICCVIVVKRHHTRFFPSGDvttsNKFNNVDPGTVVDRTIVHPNEMQFF 688
Cdd:cd04658  307 GVGDGQLKKVKEYEVPQIKKAIKQYSEnySPKLAYIVVNKRINTRFFNQGG----NNFSNPPPGTVVDSEITKPEWYDFF 382
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442632519 689 MVSHQAIQGTAKPTRYNVIENTGNLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAH 746
Cdd:cd04658  383 LVSQSVRQGTVTPTHYNVLYDTTGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAH 440
PLN03202 PLN03202
protein argonaute; Provisional
6-750 1.85e-77

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 268.51  E-value: 1.85e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   6 YHYDVKIMPE--RP-------KKFYRQAFEQFRVDqLGGAVLAYDGKASCYSVDKLPLNsqNPEVTV------TDRNG-- 68
Cdd:PLN03202  65 FHYSVSLTYEdgRPvdgkgigRKVIDKVQETYSSD-LAGKDFAYDGEKSLFTVGALPQN--KLEFTVvledvsSNRNNgn 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  69 ---------------------RTLRYTIEIKETgdSTIDLKSLTTYMNDRIFDKPMRAMQCVEVVLaspCHNKAIR---- 123
Cdd:PLN03202 142 gspvgngspnggdrkrsrrpyQSKTFKVEISFA--AKIPMQAIANALRGQESENSQDALRVLDIIL---RQHAAKQgcll 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 124 VGRSFFKmSDPNNRHELDDGYEALVGLYQAFmlgdRP-----FLNVDISHKSFPISMPMIEYLerfSLKAKINNTTNLDY 198
Cdd:PLN03202 217 VRQSFFH-NDPKNFVDLGGGVLGCRGFHSSF----RTtqgglSLNIDVSTTMIVQPGPVVDFL---IANQNVRDPFQIDW 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 199 S--RRFLEPfLRginvVYTPPQSFQsaprvYRVNGLSRAPASSETF----------EHDGKKVTIASYF-HSRNYPLKFP 265
Cdd:PLN03202 289 SkaKRMLKN-LR----VKVSPSNQE-----YKITGLSEKPCKEQTFslkqrngngnEVETVEITVYDYFvKHRGIELRYS 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 266 -QLHCLNVGSSIKSILLPIELCSIEEGQALNRKDGATQVANMIKYAATSTNVRKRKIMNLLQYFQHNLDPTISRFGIRIA 344
Cdd:PLN03202 359 gDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDALKSSNYDADPMLRSCGISIS 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 345 NDFIVVSTRVLSPPQVEYHSKRFTMVKNGSWRMDGMKFLEPKpKAHKCAVL----YCDPRsgrkmnyTQLNDfgnlIISQ 420
Cdd:PLN03202 439 SQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPT-KIERWAVVnfsaRCDIR-------HLVRD----LIKC 506
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 421 GKAVNISLDS-------DVTYR---PFTDDERSLDTIFADLKRSQHDLaIVIIPQFRIS--YDTIKQKAELQHGILTQCI 488
Cdd:PLN03202 507 GEMKGINIEPpfdvfeeNPQFRrapPPVRVEKMFEQIQSKLPGPPQFL-LCILPERKNSdiYGPWKKKNLSEFGIVTQCI 585
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 489 KQFTVerkcNNQTIGNILLKINSKLNGINH--KIKDDPRLPMMKN--TMYIGADVTHPSPDQREIPSVVGVAAS-HDPYG 563
Cdd:PLN03202 586 APTRV----NDQYLTNVLLKINAKLGGLNSllAIEHSPSIPLVSKvpTIILGMDVSHGSPGQSDVPSIAAVVSSrQWPLI 661
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 564 ASYNMQYRLQRGALEEIEDMFS---------ITLEHL-RVYKEYRNAYPDHIIYYRDGVSDGQFPKIKNEELRCIKQACD 633
Cdd:PLN03202 662 SRYRASVRTQSPKVEMIDSLFKpvgdkdddgIIRELLlDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQIIEACK 741
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 634 KVGCK--PKICCVIVVKRHHTRFFPSGDVttsnkfNNVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTG 711
Cdd:PLN03202 742 FLDESwsPKFTVIVAQKNHHTKFFQAGSP------DNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEI 815
                        810       820       830
                 ....*....|....*....|....*....|....*....
gi 442632519 712 NLDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAA 750
Cdd:PLN03202 816 GFSADDLQELVHSLSYVYQRSTTAISVVAPVCYAHLAAA 854
Piwi-like cd02826
Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing ...
405-753 3.19e-67

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: 228.04  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 405 MNYTQLNDFGNLIISQ----GKAVNISLDSDVTYRPFTDDErSLDTIFADLKRSQHDLAIVIIPQFRIS-YDTIKqKAEL 479
Cdd:cd02826   43 FRNEEVDDLVKRLADAcrqlGMKIKEIPIVSWIEDLNNSFK-DLKSVFKNAIKAGVQLVIFILKEKKPPlHDEIK-RLEA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 480 QHGILTQCIKQFTVERKCNN-QTIGNILLKINSKLNGINHKIKDDPRLpmMKNTMYIGADVTHPSPDQREI-PSVVGVAA 557
Cdd:cd02826  121 KSDIPSQVIQLKTAKKMRRLkQTLDNLLRKVNSKLGGINYILDSPVKL--FKSDIFIGFDVSHPDRRTVNGgPSAVGFAA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 558 SH-DPYGASYNMQYRLQR-GALEEIEDMFSitlEHLRVYKEYRNAY-PDHIIYYRDGVSDGQFPKIKNEELRCIKQACD- 633
Cdd:cd02826  199 NLsNHTFLGGFLYVQPSReVKLQDLGEVIK---KCLDGFKKSTGEGlPEKIVIYRDGVSEGEFKRVKEEVEEIIKEACEi 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 634 KVGCKPKICCVIVVKRHHTRFFPSGDvttsNKFN-NVDPGTVVDRTIVHPNEMQFFMVSHQAIQGTAKPTRYNVIENTGN 712
Cdd:cd02826  276 EESYRPKLVIIVVQKRHNTRFFPNEK----NGGVqNPEPGTVVDHTITSPGLSEFYLASHVARQGTVKPTKYTVVFNDKN 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 442632519 713 LDIDLLQQLTYNLCHMFPRCNRSVSYPAPAYLAHLVAARGR 753
Cdd:cd02826  352 WSLNELEILTYILCLTHQNVYSPISLPAPLYYAHKLAKRGR 392
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
175-289 2.79e-32

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: 121.03  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 175 MPMIEYLERFSLKAKINnTTNLDYSRRFLEPFLRGINVVYTPPQsfqsAPRVYRVNGLSRAPASSETFEHDGKKVTIASY 254
Cdd:cd02825    2 DPVIETMCKFPKDREID-TPLLDSPREEFTKELKGLKVEDTHNP----LNRVYRPDGETRLKAPSQLKHSDGKEITFADY 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442632519 255 FHSRNYP-LKFPQLHCLNVGSS---IKSILLPIELCSIE 289
Cdd:cd02825   77 FKERYNLtLTDLNQPLLIVKFSskkSYSILLPPELCVIT 115
ArgoMid pfam16487
Mid domain of argonaute; The ArgoMid domain is found to be part of the Piwi-lobe of the ...
369-454 1.13e-29

Mid domain of argonaute; The ArgoMid domain is found to be part of the Piwi-lobe of the argonaute proteins. It is composed of a parallel four-stranded beta-sheet core surrounded by four alpha-helices and two additional short alpha-helices. It most closely resembles the amino terminal tryptic core of the E.coli lactose repressor. There is an extensive interface between the Mid and the Piwi domains. The conserved C-terminal half or the Mid has extensive interactions with Piwi, with a deep basic pocket on the surface of the `Mid adjacent to the interface with Piwi. The Mid carries a binding pocket for the 5' phosphate overhang of the guide strand of DNA. The N, Mid, and Piwi domains form a base upon which the PAZ domain sits, resembling a duck. The 5' phosphate and the U1 base are held in place by a conserved network of interactions from protein residues of the Mid and Piwi domains in order to place the guide uniquely in the proper position observed in all Argonaute-RNA complexes.


Pssm-ID: 465135 [Multi-domain]  Cd Length: 83  Bit Score: 112.33  E-value: 1.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  369 MVKNGSWRMDGMKFLEPkPKAHKCAVLYCDPrsGRKMNYTQLNDFGNLIISQGKAVNISLDSDVTYRPFTDDERSLDTIF 448
Cdd:pfam16487   1 TPNNGSWDMRGKQFLEG-IKIHKWAILCFAS--QRRVPENKLRDFTRQLVRQSNDVGMPIEEKPCICKYADGVRQVETLF 77

                  ....*.
gi 442632519  449 ADLKRS 454
Cdd:pfam16487  78 RDLKKK 83
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
174-288 1.96e-23

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: 95.85  E-value: 1.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 174 SMPMIEYLERFSLKAKINNTTNLDysRRFLEPFLRGINVVYTPpqsFQSAPRVYRVNGLSRAPASSETFEHDG--KKVTI 251
Cdd:cd02846    1 AQPVIEFLKEFLGFDTPLGLSDND--RRKLKKALKGLKVEVTH---RGNTNRKYKIKGLSAEPASQQTFELKDgeKEISV 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442632519 252 ASYFHSR-NYPLKFPQLHCLNVGSSIKSILLPIELCSI 288
Cdd:cd02846   76 ADYFKEKyNIRLKYPNLPCLQVGRKGKPNYLPMELCNI 113
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
178-307 1.47e-20

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: 88.02  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519  178 IEYLERFSLKAKINNttnldySRRFLEPFLRGINVVYTPpqsfqSAPRVYRVNGLSRAPASSETFE-HDGKKVTIASYFH 256
Cdd:pfam02170   1 LDFLKRLQQQKDRRD------FRKEAKKALKGLKVYTTY-----NNPRTYRIDGITFDPTPESTFPlKDGKEITVVDYFK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442632519  257 SR-NYPLKFPQLHCLNVGSSIKSILLPIELCSIEEGQALNRKDGAT--QVANMI 307
Cdd:pfam02170  70 KKyNIDLKYPDQPLLLVGKKRPKVYLPPELCNLVDGQRYTKKLMPSiaQRTRLL 123
Piwi_piwi-like_ProArk cd04659
Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA ...
412-749 2.41e-14

Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA silencing refers to a group of related gene-silencing mechanisms mediated by short RNA molecules, including siRNAs, miRNAs, and heterochromatin-related guide RNAs. The central component of the RNA-induced silencing complex (RISC) and related complexes is Argonaute. The PIWI domain is the C-terminal portion of Argonaute and consists of two subdomains, one of which provides the 5' anchoring of the guide RNA and the other, the catalytic site for slicing. This domain is also found in closely related proteins, including the Piwi subfamily, where it is believed to perform a crucial role in germline cells, via a similar mechanism.


Pssm-ID: 240017 [Multi-domain]  Cd Length: 404  Bit Score: 75.88  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 412 DFGNLIISQGKAVNISLDSDVTYRPFTDDERSLDTIFADLKRSQH----DLAIVIIPQFRIS-------YDTIKQKAeLQ 480
Cdd:cd04659   63 KFPGFGGGNKNALGKNKISVFRLDLNRSAQAEAIIEAVDLALSESsqgvDVVIVVLPEDLKElpeefdlYDRLKAKL-LR 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 481 HGILTQCIKQFTV-ERKCNNQTIGNILLKINSKLNGINHKIKDDPRlpmmKNTMYIGADVtHPSPDQREIpsVVGVAASH 559
Cdd:cd04659  142 LGIPTQFVREDTLkNRQDLAYVAWNLALALYAKLGGIPWKLDADSD----PADLYIGIGF-ARSRDGEVR--VTGCAQVF 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 560 DPYGAS-----YNMQYRLQRGALEEIEDMFSITLEHLRvyKEYRNAYPDHIIYYRDGvsdgqfpKIKNEELRCIKQACDK 634
Cdd:cd04659  215 DSDGLGlilrgAPIEEPTEDRSPADLKDLLKRVLEGYR--ESHRGRDPKRLVLHKDG-------RFTDEEIEGLKEALEE 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519 635 VGckPKICCVIVVKRHHTRFFPSGdvtTSNKFNNVDPGTVV---DRTIVHPNEMQFFMVSHQAIQGTAKPTRynVIENTG 711
Cdd:cd04659  286 LG--IKVDLVEVIKSGPHRLFRFG---TYPNGFPPRRGTYVklsDDEGLLWTHGSVPKYNTYPGMGTPRPLL--LRRHSG 358
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 442632519 712 NLDIDLLQQLTYNLCHMFPR-CNRSVSYPAPAYLAHLVA 749
Cdd:cd04659  359 NTDLEQLASQILGLTKLNWNsFQFYSRLPVTIHYADRVA 397
ArgoL2 pfam16488
Argonaute linker 2 domain; ArgoL2 is the second linker domain in eukaryotic argonaute proteins. ...
316-362 5.21e-14

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


Pssm-ID: 465136 [Multi-domain]  Cd Length: 47  Bit Score: 66.67  E-value: 5.21e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 442632519  316 VRKRKIMNLLQYFQHNLDPTISRFGIRIANDFIVVSTRVLSPPQVEY 362
Cdd:pfam16488   1 ERAESIVEGLKVLGYDQDPYLREFGISVDPQMITVPGRVLPPPKLKY 47
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
124-171 3.02e-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: 50.60  E-value: 3.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442632519  124 VGRSFFKMSDPNNRHELDDGYEALVGLYQAFMLGD-RPFLNVDISHKSF 171
Cdd:pfam08699   2 VGRSFFSPPGENRVDLGGGGLEAWRGFFQSVRPTQgGLLLNVDVSHTAF 50
ArgoN pfam16486
N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in ...
41-113 1.35e-06

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


Pssm-ID: 465134  Cd Length: 93  Bit Score: 47.28  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632519   41 DGKASCYSVDKLPLNSQNPEVTVTDRNG---------RTLRYTIEIKETGdsTIDLKSLTTYMNDRIFDKPMRAMQCVEV 111
Cdd:pfam16486  14 DGRKNLYSAKKLPFGEEEFVVLDEEPGRgarkrpgvrRPRTFKVTIKFTK--TINLQDLLEYLRGKQDNTPLEAIQALDI 91

                  ..
gi 442632519  112 VL 113
Cdd:pfam16486  92 VL 93
 
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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