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Conserved domains on  [gi|42569579|ref|NP_180853|]
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Argonaute family protein [Arabidopsis thaliana]

Protein Classification

PAZ domain-containing protein( domain architecture ID 11477566)

PAZ (Piwi Argonaut and Zwille) domain-containing protein similar to PAZ domain region of argonaute proteins which play central roles in RNA silencing processes, as essential components of the RNA-induced silencing complex (RISC) that is responsible for the gene silencing phenomenon known as RNA interference (RNAi)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03202 PLN03202
protein argonaute; Provisional
15-878 0e+00

protein argonaute; Provisional


:

Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 1661.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   15 EPEQPSHRDYDITTRRGVGTTGNPIELCTNHFNVSVRQPDVVFYQYTVSITTENGDAVDGTGISRKLMDQLFKTYSSDLD 94
Cdd:PLN03202  22 PTKKPSKPKRLPMARRGFGSKGQKIQLLTNHFKVSVNNPDGHFFHYSVSLTYEDGRPVDGKGIGRKVIDKVQETYSSDLA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   95 GKRLAYDGEKTLYTVGPLPQNEFDFLVIVEGSFSKRDCGVSDGGS----SSGTCKRSKRSFLPRSYKVQIHYAAEIPLKT 170
Cdd:PLN03202 102 GKDFAYDGEKSLFTVGALPQNKLEFTVVLEDVSSNRNNGNGSPVGngspNGGDRKRSRRPYQSKTFKVEISFAAKIPMQA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  171 VLGTQRGayTPDKSAQDALRVLDIVLRQQAAERGCLLVRQAFFHSDGHPM-KVGGGVIGIRGLHSSFRPTHGGLSLNIDV 249
Cdd:PLN03202 182 IANALRG--QESENSQDALRVLDIILRQHAAKQGCLLVRQSFFHNDPKNFvDLGGGVLGCRGFHSSFRTTQGGLSLNIDV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  250 STTMILEPGPVIEFLKANQSVETPRQIDWIKAAKMLKHMRVKATHRNMEFKIIGLSSKPCNQQLFSMKIKDGER-EVPIR 328
Cdd:PLN03202 260 STTMIVQPGPVVDFLIANQNVRDPFQIDWSKAKRMLKNLRVKVSPSNQEYKITGLSEKPCKEQTFSLKQRNGNGnEVETV 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  329 EITVYDYF-KQTYTEPISSAYFPCLDVGKPDRPNYLPLEFCNLVSLQRYTKPLSGRQRVLLVESSRQKPLERIKTLNDAM 407
Cdd:PLN03202 340 EITVYDYFvKHRGIELRYSGDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  408 HTYCYDKDPFLAGCGISIEKEMTQVEGRVLKPPMLKFGKNEDFQPCNGRWNFNNKMLLEPRAIKSWAIVNFSFPCDSSHI 487
Cdd:PLN03202 420 KSSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPTKIERWAVVNFSARCDIRHL 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  488 SRELISCGMRKGIEIDRPFALVEEDPQYKKAGPVERVEKMIATMKLKFPDPPHFILCILPERKTSDIYGPWKKICLTEEG 567
Cdd:PLN03202 500 VRDLIKCGEMKGINIEPPFDVFEENPQFRRAPPPVRVEKMFEQIQSKLPGPPQFLLCILPERKNSDIYGPWKKKNLSEFG 579
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  568 IHTQCICPIKISDQYLTNVLLKINSKLGGINSLLGIEYSYNIPLINKIPTLILGMDVSHGPPGRADVPSVAAVVGSKCWP 647
Cdd:PLN03202 580 IVTQCIAPTRVNDQYLTNVLLKINAKLGGLNSLLAIEHSPSIPLVSKVPTIILGMDVSHGSPGQSDVPSIAAVVSSRQWP 659
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  648 LISRYRAAVRTQSPRLEMIDSLFQPIENTEkgDNGIMNELFVEFYRTSRARKPKQIIIFRDGVSESQFEQVLKIEVDQII 727
Cdd:PLN03202 660 LISRYRASVRTQSPKVEMIDSLFKPVGDKD--DDGIIRELLLDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQII 737
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  728 KAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPENVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGF 807
Cdd:PLN03202 738 EACKFLDESWSPKFTVIVAQKNHHTKFFQAGSPDNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGF 817
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  808 SPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQFTKFEGISEDGK------------VPELPRLHENVEGNM 875
Cdd:PLN03202 818 SADDLQELVHSLSYVYQRSTTAISVVAPVCYAHLAAAQMGQFMKFEDMSETSSshggitsagavpVPELPRLHENVASSM 897

                 ...
gi 42569579  876 FFC 878
Cdd:PLN03202 898 FFC 900
 
Name Accession Description Interval E-value
PLN03202 PLN03202
protein argonaute; Provisional
15-878 0e+00

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 1661.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   15 EPEQPSHRDYDITTRRGVGTTGNPIELCTNHFNVSVRQPDVVFYQYTVSITTENGDAVDGTGISRKLMDQLFKTYSSDLD 94
Cdd:PLN03202  22 PTKKPSKPKRLPMARRGFGSKGQKIQLLTNHFKVSVNNPDGHFFHYSVSLTYEDGRPVDGKGIGRKVIDKVQETYSSDLA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   95 GKRLAYDGEKTLYTVGPLPQNEFDFLVIVEGSFSKRDCGVSDGGS----SSGTCKRSKRSFLPRSYKVQIHYAAEIPLKT 170
Cdd:PLN03202 102 GKDFAYDGEKSLFTVGALPQNKLEFTVVLEDVSSNRNNGNGSPVGngspNGGDRKRSRRPYQSKTFKVEISFAAKIPMQA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  171 VLGTQRGayTPDKSAQDALRVLDIVLRQQAAERGCLLVRQAFFHSDGHPM-KVGGGVIGIRGLHSSFRPTHGGLSLNIDV 249
Cdd:PLN03202 182 IANALRG--QESENSQDALRVLDIILRQHAAKQGCLLVRQSFFHNDPKNFvDLGGGVLGCRGFHSSFRTTQGGLSLNIDV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  250 STTMILEPGPVIEFLKANQSVETPRQIDWIKAAKMLKHMRVKATHRNMEFKIIGLSSKPCNQQLFSMKIKDGER-EVPIR 328
Cdd:PLN03202 260 STTMIVQPGPVVDFLIANQNVRDPFQIDWSKAKRMLKNLRVKVSPSNQEYKITGLSEKPCKEQTFSLKQRNGNGnEVETV 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  329 EITVYDYF-KQTYTEPISSAYFPCLDVGKPDRPNYLPLEFCNLVSLQRYTKPLSGRQRVLLVESSRQKPLERIKTLNDAM 407
Cdd:PLN03202 340 EITVYDYFvKHRGIELRYSGDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  408 HTYCYDKDPFLAGCGISIEKEMTQVEGRVLKPPMLKFGKNEDFQPCNGRWNFNNKMLLEPRAIKSWAIVNFSFPCDSSHI 487
Cdd:PLN03202 420 KSSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPTKIERWAVVNFSARCDIRHL 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  488 SRELISCGMRKGIEIDRPFALVEEDPQYKKAGPVERVEKMIATMKLKFPDPPHFILCILPERKTSDIYGPWKKICLTEEG 567
Cdd:PLN03202 500 VRDLIKCGEMKGINIEPPFDVFEENPQFRRAPPPVRVEKMFEQIQSKLPGPPQFLLCILPERKNSDIYGPWKKKNLSEFG 579
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  568 IHTQCICPIKISDQYLTNVLLKINSKLGGINSLLGIEYSYNIPLINKIPTLILGMDVSHGPPGRADVPSVAAVVGSKCWP 647
Cdd:PLN03202 580 IVTQCIAPTRVNDQYLTNVLLKINAKLGGLNSLLAIEHSPSIPLVSKVPTIILGMDVSHGSPGQSDVPSIAAVVSSRQWP 659
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  648 LISRYRAAVRTQSPRLEMIDSLFQPIENTEkgDNGIMNELFVEFYRTSRARKPKQIIIFRDGVSESQFEQVLKIEVDQII 727
Cdd:PLN03202 660 LISRYRASVRTQSPKVEMIDSLFKPVGDKD--DDGIIRELLLDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQII 737
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  728 KAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPENVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGF 807
Cdd:PLN03202 738 EACKFLDESWSPKFTVIVAQKNHHTKFFQAGSPDNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGF 817
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  808 SPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQFTKFEGISEDGK------------VPELPRLHENVEGNM 875
Cdd:PLN03202 818 SADDLQELVHSLSYVYQRSTTAISVVAPVCYAHLAAAQMGQFMKFEDMSETSSshggitsagavpVPELPRLHENVASSM 897

                 ...
gi 42569579  876 FFC 878
Cdd:PLN03202 898 FFC 900
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
416-845 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: 539.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 416 PFLAGCGISIEKEMTQVEGRVLKPPMLKFG-KNEDFQPCNGRWNFNNKMLLEPRAIKSWAIVNFSFPCDSshisrelisc 494
Cdd:cd04657   1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGdSSKTVPPRNGSWNLRGKKFLEGGPIRSWAVLNFAGPRRS---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 495 gmRKGIEIDRPFALVEED--------PQYKKAGPVERVEKMIATMKLKFPDPPHFILCILPeRKTSDIYGPWKKICLTEE 566
Cdd:cd04657  71 --REERADLRNFVDQLVKtvigaginITTAIASVEGRVEELFAKLKQAKGEGPQLVLVILP-KKDSDIYGRIKRLADTEL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 567 GIHTQCICPIKI----SDQYLTNVLLKINSKLGGINSLLGIEYsynIPLINKIPTLILGMDVSHGPPG-RADVPSVAAVV 641
Cdd:cd04657 148 GIHTQCVLAKKVtkkgNPQYFANVALKINLKLGGINHSLEPDI---RPLLTKEPTMVLGADVTHPSPGdPAGAPSIAAVV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 642 GSKCWPLiSRYRAAVRTQSPRLEMIDSLfqpientekgdNGIMNELFVEFYRTSRArKPKQIIIFRDGVSESQFEQVLKI 721
Cdd:cd04657 225 ASVDWHL-AQYPASVRLQSHRQEIIDDL-----------ESMVRELLRAFKKATGK-LPERIIYYRDGVSEGQFAQVLNE 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 722 EVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPE------NVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRP 795
Cdd:cd04657 292 ELPAIRKACAKLYPGYKPKITFIVVQKRHHTRFFPTDEDDadgkngNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARP 371
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 42569579 796 AHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQ 845
Cdd:cd04657 372 THYHVLWDEIGFTADELQTLTYNLCYTYARCTRSVSIPPPAYYAHLAAAR 421
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
541-851 2.13e-124

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: 377.06  E-value: 2.13e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   541 FILCILPErKTSDIYGPWKKICLTEEGIHTQCICPIKIS----DQYLTNVLLKINSKLGGINSLLgIEYSYNIPLInkip 616
Cdd:pfam02171   1 LILVILPE-KNKDLYHSIKKYLETDLGIPSQCILSKTILkrtlKQTLTNVLLKINVKLGGINYWI-VEIKPKVDVI---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   617 tliLGMDVSHGPPGRADVPSVAAVVGSKCwPLISRYRAAVRTQSPRLEMIDSLfqpientekgdNGIMNELFVEFYRTSR 696
Cdd:pfam02171  75 ---IGFDISHGTAGTDDNPSVAAVVASFD-KGNSRYFGTVRTQASGQELLEPL-----------KDIIKELLRSFQKSSR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   697 ArKPKQIIIFRDGVSESQFEQVLKIEVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPE---NVPAGTVVDTKI 773
Cdd:pfam02171 140 K-KPERIIVYRDGVSEGQFPQVLNYEVNQIKEACKSLGPGYNPKLTVIVVQKRHHTRFFANDKPDgdqNPPPGTVVDDVI 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42569579   774 VHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQFTK 851
Cdd:pfam02171 219 TLPEYYDFYLCSHAGLQGTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
541-851 1.52e-110

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: 341.24  E-value: 1.52e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    541 FILCILPERKTSDIYGPWKKICLTEEGIHTQCICPIKIS--------DQYLTNVLLKINSKLGGINsllgieYSYNIPLI 612
Cdd:smart00950   1 LIVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTLDkvskrrklKQYLTNVALKINAKLGGIN------WVLDVPPI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    613 NKIPTLILGMDVSHGPPGRA--DVPSVAAVVGSKCWPLISRYRAAVRTQSPRlemidslfqpientekGDNGIMNELFVE 690
Cdd:smart00950  75 PLKPTLIIGIDVSHPSAGKGgsVAPSVAAFVASGNYLSGNFYQAFVREQGSR----------------QLKEILREALKK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    691 FYRTSRARKPKQIIIFRDGVSESQFEQVLKIEVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQA--KGPENVPAGTV 768
Cdd:smart00950 139 YYKSNRKRLPDRIVVYRDGVSEGQFKQVLEYEVKAIKKACKELGPDYKPKLTVIVVQKRHHTRFFPEdgNGRVNVPPGTV 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    769 VDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQ 848
Cdd:smart00950 219 VDSVITSPEWYDFYLVSHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQ 298

                   ...
gi 42569579    849 FTK 851
Cdd:smart00950 299 LLH 301
 
Name Accession Description Interval E-value
PLN03202 PLN03202
protein argonaute; Provisional
15-878 0e+00

protein argonaute; Provisional


Pssm-ID: 215631 [Multi-domain]  Cd Length: 900  Bit Score: 1661.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   15 EPEQPSHRDYDITTRRGVGTTGNPIELCTNHFNVSVRQPDVVFYQYTVSITTENGDAVDGTGISRKLMDQLFKTYSSDLD 94
Cdd:PLN03202  22 PTKKPSKPKRLPMARRGFGSKGQKIQLLTNHFKVSVNNPDGHFFHYSVSLTYEDGRPVDGKGIGRKVIDKVQETYSSDLA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   95 GKRLAYDGEKTLYTVGPLPQNEFDFLVIVEGSFSKRDCGVSDGGS----SSGTCKRSKRSFLPRSYKVQIHYAAEIPLKT 170
Cdd:PLN03202 102 GKDFAYDGEKSLFTVGALPQNKLEFTVVLEDVSSNRNNGNGSPVGngspNGGDRKRSRRPYQSKTFKVEISFAAKIPMQA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  171 VLGTQRGayTPDKSAQDALRVLDIVLRQQAAERGCLLVRQAFFHSDGHPM-KVGGGVIGIRGLHSSFRPTHGGLSLNIDV 249
Cdd:PLN03202 182 IANALRG--QESENSQDALRVLDIILRQHAAKQGCLLVRQSFFHNDPKNFvDLGGGVLGCRGFHSSFRTTQGGLSLNIDV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  250 STTMILEPGPVIEFLKANQSVETPRQIDWIKAAKMLKHMRVKATHRNMEFKIIGLSSKPCNQQLFSMKIKDGER-EVPIR 328
Cdd:PLN03202 260 STTMIVQPGPVVDFLIANQNVRDPFQIDWSKAKRMLKNLRVKVSPSNQEYKITGLSEKPCKEQTFSLKQRNGNGnEVETV 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  329 EITVYDYF-KQTYTEPISSAYFPCLDVGKPDRPNYLPLEFCNLVSLQRYTKPLSGRQRVLLVESSRQKPLERIKTLNDAM 407
Cdd:PLN03202 340 EITVYDYFvKHRGIELRYSGDLPCINVGKPKRPTYFPIELCSLVSLQRYTKALSTLQRSSLVEKSRQKPQERMKVLTDAL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  408 HTYCYDKDPFLAGCGISIEKEMTQVEGRVLKPPMLKFGKNEDFQPCNGRWNFNNKMLLEPRAIKSWAIVNFSFPCDSSHI 487
Cdd:PLN03202 420 KSSNYDADPMLRSCGISISSQFTQVEGRVLPAPKLKVGNGEDFFPRNGRWNFNNKKLVEPTKIERWAVVNFSARCDIRHL 499
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  488 SRELISCGMRKGIEIDRPFALVEEDPQYKKAGPVERVEKMIATMKLKFPDPPHFILCILPERKTSDIYGPWKKICLTEEG 567
Cdd:PLN03202 500 VRDLIKCGEMKGINIEPPFDVFEENPQFRRAPPPVRVEKMFEQIQSKLPGPPQFLLCILPERKNSDIYGPWKKKNLSEFG 579
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  568 IHTQCICPIKISDQYLTNVLLKINSKLGGINSLLGIEYSYNIPLINKIPTLILGMDVSHGPPGRADVPSVAAVVGSKCWP 647
Cdd:PLN03202 580 IVTQCIAPTRVNDQYLTNVLLKINAKLGGLNSLLAIEHSPSIPLVSKVPTIILGMDVSHGSPGQSDVPSIAAVVSSRQWP 659
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  648 LISRYRAAVRTQSPRLEMIDSLFQPIENTEkgDNGIMNELFVEFYRTSRARKPKQIIIFRDGVSESQFEQVLKIEVDQII 727
Cdd:PLN03202 660 LISRYRASVRTQSPKVEMIDSLFKPVGDKD--DDGIIRELLLDFYTSSGKRKPEQIIIFRDGVSESQFNQVLNIELDQII 737
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  728 KAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPENVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGF 807
Cdd:PLN03202 738 EACKFLDESWSPKFTVIVAQKNHHTKFFQAGSPDNVPPGTVVDNKICHPRNNDFYMCAHAGMIGTTRPTHYHVLLDEIGF 817
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579  808 SPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQFTKFEGISEDGK------------VPELPRLHENVEGNM 875
Cdd:PLN03202 818 SADDLQELVHSLSYVYQRSTTAISVVAPVCYAHLAAAQMGQFMKFEDMSETSSshggitsagavpVPELPRLHENVASSM 897

                 ...
gi 42569579  876 FFC 878
Cdd:PLN03202 898 FFC 900
Piwi_ago-like cd04657
Piwi_ago-like: PIWI domain, Argonaute-like subfamily. Argonaute is the central component of ...
416-845 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: 539.51  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 416 PFLAGCGISIEKEMTQVEGRVLKPPMLKFG-KNEDFQPCNGRWNFNNKMLLEPRAIKSWAIVNFSFPCDSshisrelisc 494
Cdd:cd04657   1 PYLKEFGISVSKEMITVPGRVLPPPKLKYGdSSKTVPPRNGSWNLRGKKFLEGGPIRSWAVLNFAGPRRS---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 495 gmRKGIEIDRPFALVEED--------PQYKKAGPVERVEKMIATMKLKFPDPPHFILCILPeRKTSDIYGPWKKICLTEE 566
Cdd:cd04657  71 --REERADLRNFVDQLVKtvigaginITTAIASVEGRVEELFAKLKQAKGEGPQLVLVILP-KKDSDIYGRIKRLADTEL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 567 GIHTQCICPIKI----SDQYLTNVLLKINSKLGGINSLLGIEYsynIPLINKIPTLILGMDVSHGPPG-RADVPSVAAVV 641
Cdd:cd04657 148 GIHTQCVLAKKVtkkgNPQYFANVALKINLKLGGINHSLEPDI---RPLLTKEPTMVLGADVTHPSPGdPAGAPSIAAVV 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 642 GSKCWPLiSRYRAAVRTQSPRLEMIDSLfqpientekgdNGIMNELFVEFYRTSRArKPKQIIIFRDGVSESQFEQVLKI 721
Cdd:cd04657 225 ASVDWHL-AQYPASVRLQSHRQEIIDDL-----------ESMVRELLRAFKKATGK-LPERIIYYRDGVSEGQFAQVLNE 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 722 EVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPE------NVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRP 795
Cdd:cd04657 292 ELPAIRKACAKLYPGYKPKITFIVVQKRHHTRFFPTDEDDadgkngNVPPGTVVDRGITHPREFDFYLCSHAGIQGTARP 371
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 42569579 796 AHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQ 845
Cdd:cd04657 372 THYHVLWDEIGFTADELQTLTYNLCYTYARCTRSVSIPPPAYYAHLAAAR 421
Piwi pfam02171
Piwi domain; This domain is found in the protein Piwi and its relatives. The function of this ...
541-851 2.13e-124

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: 377.06  E-value: 2.13e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   541 FILCILPErKTSDIYGPWKKICLTEEGIHTQCICPIKIS----DQYLTNVLLKINSKLGGINSLLgIEYSYNIPLInkip 616
Cdd:pfam02171   1 LILVILPE-KNKDLYHSIKKYLETDLGIPSQCILSKTILkrtlKQTLTNVLLKINVKLGGINYWI-VEIKPKVDVI---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   617 tliLGMDVSHGPPGRADVPSVAAVVGSKCwPLISRYRAAVRTQSPRLEMIDSLfqpientekgdNGIMNELFVEFYRTSR 696
Cdd:pfam02171  75 ---IGFDISHGTAGTDDNPSVAAVVASFD-KGNSRYFGTVRTQASGQELLEPL-----------KDIIKELLRSFQKSSR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   697 ArKPKQIIIFRDGVSESQFEQVLKIEVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQAKGPE---NVPAGTVVDTKI 773
Cdd:pfam02171 140 K-KPERIIVYRDGVSEGQFPQVLNYEVNQIKEACKSLGPGYNPKLTVIVVQKRHHTRFFANDKPDgdqNPPPGTVVDDVI 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42569579   774 VHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQFTK 851
Cdd:pfam02171 219 TLPEYYDFYLCSHAGLQGTVKPTHYTVLYDEIGLSADELQNLTYKLCHMYYRSTRPISIPAPVYYAHLLAKRVRNNIK 296
Piwi smart00950
This domain is found in the protein Piwi and its relatives; The function of this domain is the ...
541-851 1.52e-110

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: 341.24  E-value: 1.52e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    541 FILCILPERKTSDIYGPWKKICLTEEGIHTQCICPIKIS--------DQYLTNVLLKINSKLGGINsllgieYSYNIPLI 612
Cdd:smart00950   1 LIVVILPGEKKTDLYHEIKKYLETKLGVPTQCVQAKTLDkvskrrklKQYLTNVALKINAKLGGIN------WVLDVPPI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    613 NKIPTLILGMDVSHGPPGRA--DVPSVAAVVGSKCWPLISRYRAAVRTQSPRlemidslfqpientekGDNGIMNELFVE 690
Cdd:smart00950  75 PLKPTLIIGIDVSHPSAGKGgsVAPSVAAFVASGNYLSGNFYQAFVREQGSR----------------QLKEILREALKK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    691 FYRTSRARKPKQIIIFRDGVSESQFEQVLKIEVDQIIKAYQRLGESDVPKFTVIVAQKNHHTKLFQA--KGPENVPAGTV 768
Cdd:smart00950 139 YYKSNRKRLPDRIVVYRDGVSEGQFKQVLEYEVKAIKKACKELGPDYKPKLTVIVVQKRHHTRFFPEdgNGRVNVPPGTV 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    769 VDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQ 848
Cdd:smart00950 219 VDSVITSPEWYDFYLVSHAGLQGTARPTHYTVLYDEGNLDPDELQRLTYKLCHLYYRSTRPVSLPAPVYYAHLLAKRARQ 298

                   ...
gi 42569579    849 FTK 851
Cdd:smart00950 299 LLH 301
Piwi_piwi-like_Euk cd04658
Piwi_piwi-like_Euk: PIWI domain, Piwi-like subfamily found in eukaryotes. This domain is found ...
422-848 2.25e-73

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: 247.95  E-value: 2.25e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 422 GISIEKEMTQVEGRVLKPPMLKFGKNEDFQPCNGRWNF--NNKMLLEPRAIKSWAIVNfsfPCDSSHISRELISC----G 495
Cdd:cd04658  42 GIELDSNPLKIQGRVLPPEQIIMGNVFVYANSNADWKReiRNQPLYDAVNLNNWVLIY---PSRDQREAESFLQTlkqvA 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 496 MRKGIEIDRPFALVEEDpqykkagpvERVEKMIATMKLKFPDPPHFILCILPERKTsDIYGPWKKICLTEEGIHTQCICP 575
Cdd:cd04658 119 GPMGIQISPPKIIKVKD---------DRIETYIRALKDAFRSDPQLVVIILPGNKK-DLYDAIKKFCCVECPVPSQVITS 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 576 IKISDQY-----LTNVLLKINSKLGGInsLLGIEysynIPLINKIPTLILGMDVSHGPPGRADvpSVAAVVGSKCwPLIS 650
Cdd:cd04658 189 RTLKKKKnlrsiASKIALQINAKLGGI--PWTVE----IPPFILKNTMIVGIDVYHDTITKKK--SVVGFVASLN-KSIT 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 651 RYRAAVRTQSPRLEM-IDSLFQPIE---NTEKGDNGIMnelfvefyrtsrarkPKQIIIFRDGVSESQFEQVLKIEVDQI 726
Cdd:cd04658 260 KWFSKYISQVRGQEEiIDSLGKSMKkalKAYKKENKKL---------------PSRIIIYRDGVGDGQLKKVKEYEVPQI 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 727 IKAYQRLGESDVPKFTVIVAQKNHHTKLFQAKG--PENVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDE 804
Cdd:cd04658 325 KKAIKQYSENYSPKLAYIVVNKRINTRFFNQGGnnFSNPPPGTVVDSEITKPEWYDFFLVSQSVRQGTVTPTHYNVLYDT 404
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 42569579 805 IGFSPDDLQNLIHSLSYVNQRSTTATSIVAPVRYAHLAAAQVAQ 848
Cdd:cd04658 405 TGLKPDHLQRLTYKLCHLYYNWSGSIRVPAPCQYAHKLAFLVGQ 448
Piwi-like cd02826
Piwi-like: PIWI domain. Domain found in proteins involved in RNA silencing. RNA silencing ...
432-843 1.83e-61

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: 213.40  E-value: 1.83e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 432 VEGRVLKPPMLKFGKNedfqpcngrWNFNNKMLLEPRAI-KSWAIVNFSFPcdSSHISRELISCGMRK-GIEIDR--PFA 507
Cdd:cd02826   5 LKGRVLPKPQILFKNK---------FLRNIGPFEKPAKItNPVAVIAFRNE--EVDDLVKRLADACRQlGMKIKEipIVS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 508 LVEEDPqykkagpvERVEKMIATMKLKFPDPPHFILCILPErKTSDIYGPWKKICLtEEGIHTQCI--CPIKIS---DQY 582
Cdd:cd02826  74 WIEDLN--------NSFKDLKSVFKNAIKAGVQLVIFILKE-KKPPLHDEIKRLEA-KSDIPSQVIqlKTAKKMrrlKQT 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 583 LTNVLLKINSKLGGINsllgieYSYNIPLINKIPTLILGMDVSHgpPGRADVPSVAAVVGSKC-WPLISRYRAAVRTQSP 661
Cdd:cd02826 144 LDNLLRKVNSKLGGIN------YILDSPVKLFKSDIFIGFDVSH--PDRRTVNGGPSAVGFAAnLSNHTFLGGFLYVQPS 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 662 RlEMIDSLFQPIentekgdngiMNELFVEFYRTSRARKPKQIIIFRDGVSESQFEQVLKiEVDQIIKAYQRLGESDVPKF 741
Cdd:cd02826 216 R-EVKLQDLGEV----------IKKCLDGFKKSTGEGLPEKIVIYRDGVSEGEFKRVKE-EVEEIIKEACEIEESYRPKL 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 742 TVIVAQKNHHTKLFQAKGPE---NVPAGTVVDTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEIGFSPDDLQNLIHS 818
Cdd:cd02826 284 VIIVVQKRHNTRFFPNEKNGgvqNPEPGTVVDHTITSPGLSEFYLASHVARQGTVKPTKYTVVFNDKNWSLNELEILTYI 363
                       410       420
                ....*....|....*....|....*
gi 42569579 819 LSYVNQRSTTATSIVAPVRYAHLAA 843
Cdd:cd02826 364 LCLTHQNVYSPISLPAPLYYAHKLA 388
PAZ_argonaute_like cd02846
PAZ domain, argonaute_like subfamily. Argonaute is part of the RNA-induced silencing complex ...
257-371 6.64e-32

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: 120.11  E-value: 6.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 257 PGPVIEFLKANQSVETPR---QIDWIKAAKMLKHMRVKATHR---NMEFKIIGLSSKPCNQQLFSMKIKDgerevpiREI 330
Cdd:cd02846   1 AQPVIEFLKEFLGFDTPLglsDNDRRKLKKALKGLKVEVTHRgntNRKYKIKGLSAEPASQQTFELKDGE-------KEI 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42569579 331 TVYDYFKQTYTEPISSAYFPCLDVGKPDRPNYLPLEFCNLV 371
Cdd:cd02846  74 SVADYFKEKYNIRLKYPNLPCLQVGRKGKPNYLPMELCNIV 114
PAZ pfam02170
PAZ domain; This domain is named PAZ after the proteins Piwi Argonaut and Zwille. This domain ...
261-389 2.39e-29

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: 113.06  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   261 IEFLKANQSVETPRqiDWIKAA-KMLKHMRVKATHRNM-EFKIIGLSSKPCNQQLFSMKikDGErevpirEITVYDYFKQ 338
Cdd:pfam02170   1 LDFLKRLQQQKDRR--DFRKEAkKALKGLKVYTTYNNPrTYRIDGITFDPTPESTFPLK--DGK------EITVVDYFKK 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42569579   339 TYTEPISSAYFPCLDVGKPDRPNYLPLEFCNLVSLQRYTKPL--SGRQRVLLV 389
Cdd:pfam02170  71 KYNIDLKYPDQPLLLVGKKRPKVYLPPELCNLVDGQRYTKKLmpSIAQRTRLL 123
ArgoL2 pfam16488
Argonaute linker 2 domain; ArgoL2 is the second linker domain in eukaryotic argonaute proteins. ...
398-444 5.23e-13

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


Pssm-ID: 465136 [Multi-domain]  Cd Length: 47  Bit Score: 63.97  E-value: 5.23e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 42569579   398 ERIKTLNDAMHTYCYDKDPFLAGCGISIEKEMTQVEGRVLKPPMLKF 444
Cdd:pfam16488   1 ERAESIVEGLKVLGYDQDPYLREFGISVDPQMITVPGRVLPPPKLKY 47
ArgoN pfam16486
N-terminal domain of argonaute; ArgoN is the N-terminal domain of argonaute proteins in ...
101-196 3.44e-10

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: 57.30  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   101 DGEKTLYTVGPLPQNEFDFLVIVEGSfskrdcgvsdggssSGTCKRSKRSFLPRSYKVQIHYAAEIPLKTVLGTQRGAYT 180
Cdd:pfam16486  14 DGRKNLYSAKKLPFGEEEFVVLDEEP--------------GRGARKRPGVRRPRTFKVTIKFTKTINLQDLLEYLRGKQD 79
                          90
                  ....*....|....*.
gi 42569579   181 PdkSAQDALRVLDIVL 196
Cdd:pfam16486  80 N--TPLEAIQALDIVL 93
Piwi_piwi-like_ProArk cd04659
Piwi_piwi-like_ProArk: PIWI domain, Piwi-like subfamily found in Archaea and Bacteria. RNA ...
537-843 2.06e-07

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: 54.31  E-value: 2.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 537 DPPHFILCILPERKT-----SDIYGPWKKIcLTEEGIHTQCICPIKISDQ-----YLTNVLLKINSKLGGinsllgieys 606
Cdd:cd04659 109 QGVDVVIVVLPEDLKelpeeFDLYDRLKAK-LLRLGIPTQFVREDTLKNRqdlayVAWNLALALYAKLGG---------- 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 607 ynIP-LINKIP---TLILGMDVSHGPPGRADVPSVAAVVGSKCWPLISRYRAA--VRTQSPRLEMIDSLFQPIentekgd 680
Cdd:cd04659 178 --IPwKLDADSdpaDLYIGIGFARSRDGEVRVTGCAQVFDSDGLGLILRGAPIeePTEDRSPADLKDLLKRVL------- 248
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 681 ngimnELFVEFYrtsRARKPKQIIIFRDGvsesqfeQVLKIEVDQIIKAYQRLGEsdvpKFTVIVAQKNHHTKLF---QA 757
Cdd:cd04659 249 -----EGYRESH---RGRDPKRLVLHKDG-------RFTDEEIEGLKEALEELGI----KVDLVEVIKSGPHRLFrfgTY 309
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 758 KGPENVPAGTVV---DTKIVHPTNYDFYMCAHAGKIGTSRPAHYHVLLDEigFSPDDLQNLIHSLSYVNQRSTTA-TSIV 833
Cdd:cd04659 310 PNGFPPRRGTYVklsDDEGLLWTHGSVPKYNTYPGMGTPRPLLLRRHSGN--TDLEQLASQILGLTKLNWNSFQFySRLP 387
                       330
                ....*....|
gi 42569579 834 APVRYAHLAA 843
Cdd:cd04659 388 VTIHYADRVA 397
ArgoL1 pfam08699
Argonaute linker 1 domain; ArgoL1 is a region found in argonaute proteins. It normally ...
233-256 5.97e-07

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: 46.75  E-value: 5.97e-07
                          10        20
                  ....*....|....*....|....
gi 42569579   233 HSSFRPTHGGLSLNIDVSTTMILE 256
Cdd:pfam08699  29 FQSVRPTQGGLLLNVDVSHTAFYK 52
PAZ smart00949
This domain is named PAZ after the proteins Piwi Argonaut and Zwille; This domain is found in ...
280-380 1.64e-06

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: 48.44  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579    280 KAAKMLKHMRVKATHRNMEFKIIGL--SSKPcnqqLFSMKIKDGErevpirEITVYDYFKQTYTEPISSAYFPCLDV--- 354
Cdd:smart00949  22 RCAKDLKGLIVLTRYNNKTYRIDDIdwNLAP----KSTFEKSDGS------EITFVEYYKQKYNITIRDPNQPLLVSrpk 91
                           90       100       110
                   ....*....|....*....|....*....|...
gi 42569579    355 ------GKPdRPNYLPLEFCNLVSL-QRYTKPL 380
Cdd:smart00949  92 rrrnqnGKG-EPVLLPPELCFITGLtDRMRKDF 123
ArgoMid pfam16487
Mid domain of argonaute; The ArgoMid domain is found to be part of the Piwi-lobe of the ...
452-532 3.28e-05

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: 43.00  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579   452 PCNGRWNFNNKMLLEPRAIKSWAIVNFSFP--CDSSHIS---RELISCGMRKGIEIDrpfalvEEDPQYKKAGPVERVEK 526
Cdd:pfam16487   2 PNNGSWDMRGKQFLEGIKIHKWAILCFASQrrVPENKLRdftRQLVRQSNDVGMPIE------EKPCICKYADGVRQVET 75

                  ....*.
gi 42569579   527 MIATMK 532
Cdd:pfam16487  76 LFRDLK 81
PAZ cd02825
PAZ domain, named PAZ after the proteins Piwi Argonaut and Zwille. PAZ is found in two ...
262-371 4.34e-04

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: 40.91  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42569579 262 EFLKANQSVETPRQIDWIKAAKMLKHMRVKATHR--NMEFKIIGLSSKPCNQQLFSmkiKDGErevpirEITVYDYFKQT 339
Cdd:cd02825  10 KFPKDREIDTPLLDSPREEFTKELKGLKVEDTHNplNRVYRPDGETRLKAPSQLKH---SDGK------EITFADYFKER 80
                        90       100       110
                ....*....|....*....|....*....|....*
gi 42569579 340 YTEPISSAYFPCLDVG---KPDRPNYLPLEFCNLV 371
Cdd:cd02825  81 YNLTLTDLNQPLLIVKfssKKSYSILLPPELCVIT 115
 
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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