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Conserved domains on  [gi|166851804|ref|NP_694591|]
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ATP-dependent RNA helicase TDRD9 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 132-315 1.46e-99

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 315.60  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160

                         170       180
                  ....*....|....*....|....
gi 166851804  292 CKEFADYFAVPVqnkmNPAYIFEV 315
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
130-716 1.66e-93

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 321.26  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  130 PDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHyvQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 289
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  290 ISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHlleepviTKDIYEVAVSLIqmfDDLDMK 369
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVE---------VRYRPLPAD-------ERDLEDAVADAV---REALAE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:COG1643   219 EPG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAE 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  450 SSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLVHK-DFwdNSIPDHVVPEMLR 528
Cdd:COG1643   285 TSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEeDF--ARRPAFTDPEILR 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  529 CPLGSTILKVKLLDMGEPRAL-LATALSPPGLSDIERtilLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQL 607
Cdd:COG1643   363 ADLASLILELAAWGLGDPEDLpFLDPPPARAIADARA---LLQELGAL-------DA---DGRLTPLGRALARLPLDPRL 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  608 GKLIVLGHVFGCLDECLIIAAALSLKNffamPFRQhldgyrnkvnfsgSSKSDCIALVEAFKTWKACRQtgelrypkdel 687
Cdd:COG1643   430 ARMLLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQR----------- 481

                         570       580
                  ....*....|....*....|....*....
gi 166851804  688 nwgrlNYIQIKRIREVAELYEELKTRISQ 716
Cdd:COG1643   482 -----EFLSYLRLREWRDLARQLRRLLGE 505
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 905-1005 4.06e-59

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410502  Cd Length: 101  Bit Score: 198.00  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  905 TEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYG 984
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                          90       100
                  ....*....|....*....|.
gi 166851804  985 NKSHVDLHLLMEIPCQFLELP 1005
Cdd:cd20431    81 NTSQVPSSLLREIPETLLTLP 101
 
Name Accession Description Interval E-value
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 132-315 1.46e-99

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 315.60  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160

                         170       180
                  ....*....|....*....|....
gi 166851804  292 CKEFADYFAVPVqnkmNPAYIFEV 315
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
130-716 1.66e-93

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 321.26  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  130 PDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHyvQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 289
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  290 ISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHlleepviTKDIYEVAVSLIqmfDDLDMK 369
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVE---------VRYRPLPAD-------ERDLEDAVADAV---REALAE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:COG1643   219 EPG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAE 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  450 SSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLVHK-DFwdNSIPDHVVPEMLR 528
Cdd:COG1643   285 TSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEeDF--ARRPAFTDPEILR 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  529 CPLGSTILKVKLLDMGEPRAL-LATALSPPGLSDIERtilLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQL 607
Cdd:COG1643   363 ADLASLILELAAWGLGDPEDLpFLDPPPARAIADARA---LLQELGAL-------DA---DGRLTPLGRALARLPLDPRL 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  608 GKLIVLGHVFGCLDECLIIAAALSLKNffamPFRQhldgyrnkvnfsgSSKSDCIALVEAFKTWKACRQtgelrypkdel 687
Cdd:COG1643   430 ARMLLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQR----------- 481

                         570       580
                  ....*....|....*....|....*....
gi 166851804  688 nwgrlNYIQIKRIREVAELYEELKTRISQ 716
Cdd:COG1643   482 -----EFLSYLRLREWRDLARQLRRLLGE 505
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 126-723 8.08e-76

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 276.56  E-value: 8.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  126 TYKYPD-LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:PRK11131   66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  205 WTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 284
Cdd:PRK11131  144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  285 LMSATISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEEYYlndlehihhsklsphlleEPVITKDIYEVAVSLIQMFD 364
Cdd:PRK11131  223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVEVRY------------------RPIVEEADDTERDQLQAIFD 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  365 DLDmkESGNKAwsgaqfvleRSSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPvpGYRKIILS 444
Cdd:PRK11131  277 AVD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLA 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  445 TNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLV-HKDFwdNSIPDHVV 523
Cdd:PRK11131  344 TNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYsEDDF--LSRPEFTD 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  524 PEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPV 603
Cdd:PRK11131  422 PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPV 494

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  604 NQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF--RQHLDGYRNKVNfsgSSKSDCIALVeafKTW-------KAC 674
Cdd:PRK11131  495 DPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFV---NLWnylqeqqKAL 568

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 166851804  675 RQTGELRYPKDELnwgrLNYIqikRIREVAELYEELKTRISQFNMHVDS 723
Cdd:PRK11131  569 SSNQFRRLCRTDY----LNYL---RVREWQDIYTQLRQVVKELGIPVNS 610
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 320-509 1.31e-62

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 210.85  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  320 HSVEEYYLNDLEHIHHSklsphllEEPVITKDIYEVAVSLIqmFDDLDMKESGnkawsgaqfvlersSVLVFLPGLGEIN 399
Cdd:cd18791     1 FPVEVYYLEDILELLGI-------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  400 YMHELLTSLVH----KRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDT 475
Cdd:cd18791    58 RLCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRT 137

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166851804  476 NYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLV 509
Cdd:cd18791   138 GLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 905-1005 4.06e-59

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 198.00  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  905 TEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYG 984
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                          90       100
                  ....*....|....*....|.
gi 166851804  985 NKSHVDLHLLMEIPCQFLELP 1005
Cdd:cd20431    81 NTSQVPSSLLREIPETLLTLP 101
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 132-630 1.53e-53

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 202.69  E-value: 1.53e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVqrsAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPG---IGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:TIGR01970   78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   292 CKEfadyfavpVQNKMNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHLLEEPVITKDIYEVAVSliqmfddldmkES 371
Cdd:TIGR01970  158 GER--------LSSLLPDAPVVESEGRSFPVE---------IRYLPLRGDQRLEDAVSRAVEHALAS-----------ET 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   372 GnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESS 451
Cdd:TIGR01970  210 G--------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETS 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   452 VTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLvhkdfWD----NSIPDHVVPEML 527
Cdd:TIGR01970  276 LTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRL-----WSeeqhQRLPAQDEPEIL 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   528 RCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQL 607
Cdd:TIGR01970  351 QADLSGLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRL 418

                          490       500
                   ....*....|....*....|...
gi 166851804   608 GKLIVLGHVFGCLDECLIIAAAL 630
Cdd:TIGR01970  419 AAMLLSAHSTGLAALACDLAALL 441
DEXDc smart00487
DEAD-like helicases superfamily;
126-299 1.55e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 91.01  E-value: 1.55e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804    126 TYKYPDLPISRYKEEVVSLIESN-SVVIIHGATGSGKSTQLPQYILDHyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA-LKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804    205 WTLGGVVGYQVG------LEKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTN 277
Cdd:smart00487   80 SLGLKVVGLYGGdskreqLRKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLP 158

                           170       180
                    ....*....|....*....|....
gi 166851804    278 SRfVKVVLMSATISC--KEFADYF 299
Cdd:smart00487  159 KN-VQLLLLSATPPEeiENLLELF 181
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 566-664 5.61e-16

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 74.97  E-value: 5.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   566 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF----- 640
Cdd:pfam04408    2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldpr 71

                           90       100       110
                   ....*....|....*....|....*....|...
gi 166851804   641 --------RQHLDGYRNKVNFSGSS-KSDCIAL 664
Cdd:pfam04408   72 saakaarrRRRAADEKARAKFARLDlEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 588-665 6.99e-16

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 73.84  E-value: 6.99e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166851804    588 DGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPFRQHLDGYRNKvnFSgSSKSDCIALV 665
Cdd:smart00847    8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRR--FA-DPESDHLTLL 82
TUDOR pfam00567
Tudor domain;
904-1013 8.52e-14

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 69.31  E-value: 8.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   904 VTEVVEVGHFWgyRIDENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdKQRYFRAQVLY-VSGNSAEVFF 980
Cdd:pfam00567    7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 166851804   981 VDYGNKSHVDLHLLMEIPCQFLELPFQALEFKI 1013
Cdd:pfam00567   83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 139-291 1.79e-10

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 61.10  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   139 EEVVSLIESNSVVIIHGATGSGKST--QLPqyILDHYVQRSAYCSIVVTQPRKIGASSIARWIsKERAWTLGGVVGYQVG 216
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   217 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:pfam00270   82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157


                   ..
gi 166851804   290 IS 291
Cdd:pfam00270  158 LP 159
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 950-1001 1.73e-05

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 43.42  E-value: 1.73e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 166851804    950 VCLAPFADfdkQRYFRAQVLYVSGN-SAEVFFVDYGNKSHVDLHLLMEIPCQF 1001
Cdd:smart00333    8 KVAARWED---GEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
 
Name Accession Description Interval E-value
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
 132-315 1.46e-99

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 315.60  E-value: 1.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160

                         170       180
                  ....*....|....*....|....
gi 166851804  292 CKEFADYFAVPVqnkmNPAYIFEV 315
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
130-716 1.66e-93

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 321.26  E-value: 1.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  130 PDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHyvQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 289
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  290 ISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHlleepviTKDIYEVAVSLIqmfDDLDMK 369
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVE---------VRYRPLPAD-------ERDLEDAVADAV---REALAE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:COG1643   219 EPG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAE 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  450 SSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLVHK-DFwdNSIPDHVVPEMLR 528
Cdd:COG1643   285 TSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEeDF--ARRPAFTDPEILR 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  529 CPLGSTILKVKLLDMGEPRAL-LATALSPPGLSDIERtilLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQL 607
Cdd:COG1643   363 ADLASLILELAAWGLGDPEDLpFLDPPPARAIADARA---LLQELGAL-------DA---DGRLTPLGRALARLPLDPRL 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  608 GKLIVLGHVFGCLDECLIIAAALSLKNffamPFRQhldgyrnkvnfsgSSKSDCIALVEAFKTWKACRQtgelrypkdel 687
Cdd:COG1643   430 ARMLLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQR----------- 481

                         570       580
                  ....*....|....*....|....*....
gi 166851804  688 nwgrlNYIQIKRIREVAELYEELKTRISQ 716
Cdd:COG1643   482 -----EFLSYLRLREWRDLARQLRRLLGE 505
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
 126-723 8.08e-76

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 276.56  E-value: 8.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  126 TYKYPD-LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:PRK11131   66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  205 WTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 284
Cdd:PRK11131  144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  285 LMSATISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEEYYlndlehihhsklsphlleEPVITKDIYEVAVSLIQMFD 364
Cdd:PRK11131  223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVEVRY------------------RPIVEEADDTERDQLQAIFD 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  365 DLDmkESGNKAwsgaqfvleRSSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPvpGYRKIILS 444
Cdd:PRK11131  277 AVD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLA 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  445 TNIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLV-HKDFwdNSIPDHVV 523
Cdd:PRK11131  344 TNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYsEDDF--LSRPEFTD 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  524 PEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPV 603
Cdd:PRK11131  422 PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPV 494

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  604 NQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF--RQHLDGYRNKVNfsgSSKSDCIALVeafKTW-------KAC 674
Cdd:PRK11131  495 DPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFV---NLWnylqeqqKAL 568

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 166851804  675 RQTGELRYPKDELnwgrLNYIqikRIREVAELYEELKTRISQFNMHVDS 723
Cdd:PRK11131  569 SSNQFRRLCRTDY----LNYL---RVREWQDIYTQLRQVVKELGIPVNS 610
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
 320-509 1.31e-62

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 210.85  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  320 HSVEEYYLNDLEHIHHSklsphllEEPVITKDIYEVAVSLIqmFDDLDMKESGnkawsgaqfvlersSVLVFLPGLGEIN 399
Cdd:cd18791     1 FPVEVYYLEDILELLGI-------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  400 YMHELLTSLVH----KRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDT 475
Cdd:cd18791    58 RLCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRT 137

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166851804  476 NYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLV 509
Cdd:cd18791   138 GLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
 148-299 5.83e-62

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 208.47  E-value: 5.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  148 NSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVVGYQVGLEKIATEDTRL 227
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166851804  228 IYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATISCKEFADYF 299
Cdd:cd17917    81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDL-KVILMSATLDAEKFSSYF 151
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 905-1005 4.06e-59

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410502  Cd Length: 101  Bit Score: 198.00  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  905 TEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYG 984
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80

                          90       100
                  ....*....|....*....|.
gi 166851804  985 NKSHVDLHLLMEIPCQFLELP 1005
Cdd:cd20431    81 NTSQVPSSLLREIPETLLTLP 101
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
 132-630 1.53e-53

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 202.69  E-value: 1.53e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVqrsAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPG---IGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:TIGR01970   78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   292 CKEfadyfavpVQNKMNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHLLEEPVITKDIYEVAVSliqmfddldmkES 371
Cdd:TIGR01970  158 GER--------LSSLLPDAPVVESEGRSFPVE---------IRYLPLRGDQRLEDAVSRAVEHALAS-----------ET 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   372 GnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESS 451
Cdd:TIGR01970  210 G--------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETS 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   452 VTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCNQRKGRAGRVSRGYCYRLvhkdfWD----NSIPDHVVPEML 527
Cdd:TIGR01970  276 LTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRL-----WSeeqhQRLPAQDEPEIL 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   528 RCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQL 607
Cdd:TIGR01970  351 QADLSGLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRL 418

                          490       500
                   ....*....|....*....|...
gi 166851804   608 GKLIVLGHVFGCLDECLIIAAAL 630
Cdd:TIGR01970  419 AAMLLSAHSTGLAALACDLAALL 441
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
 132-299 1.94e-43

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 156.15  E-value: 1.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRS--AYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPplPVANIICTQPRRISAISVAERVAQERAERVGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD-LKVILMSAT 159

                         170
                  ....*....|
gi 166851804  290 ISCKEFADYF 299
Cdd:cd17985   160 LNAELFSDYF 169
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
 132-299 4.89e-42

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 152.30  E-value: 4.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQR--SAYCSIVVTQPRKIGASSIARWISKERA--WTL 207
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERgkGSSCRIVCTQPRRISAISVAERVAAERAesCGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  208 GGVVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLM 286
Cdd:cd17981    81 GNSTGYQIRLEsRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDV-LMGIVKDLLPFRSDLKVILM 159

                         170
                  ....*....|...
gi 166851804  287 SATISCKEFADYF 299
Cdd:cd17981   160 SATLNAEKFSDYF 172
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
 132-630 1.67e-41

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 165.48  E-value: 1.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILdhyvQRSAYCS-IVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL----QHGGINGkIIMLEPRRLAARNVAQRLAEQLGEKPGET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATI 290
Cdd:PRK11664   80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDDLKLLIMSATL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  291 sckefaDYFAVpvQNKMNPAYIFEVEGKPHSVEEYYLndlehihhsKLSPHL-LEEpvitkdiyEVAVSLIQMFDdldmK 369
Cdd:PRK11664  160 ------DNDRL--QQLLPDAPVIVSEGRSFPVERRYQ---------PLPAHQrFDE--------AVARATAELLR----Q 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:PRK11664  211 ESG--------------SLLLFLPGVGEIQRVQEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAE 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  450 SSVTVPDVKYVIDFCLTRTLVCDEDTNYQSL---RLSWASKTscnQRKGRAGRVSRGYCYRLVHKDFWDNSiPDHVVPEM 526
Cdd:PRK11664  277 TSLTIEGIRLVVDSGLERVARFDPKTGLTRLvtqRISQASMT---QRAGRAGRLEPGICLHLYSKEQAERA-AAQSEPEI 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  527 LRCPLGSTILkvKLLDMGEPRALLATALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQ 606
Cdd:PRK11664  353 LHSDLSGLLL--ELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGR----------LTARGRKMAALGNDPR 420

                         490       500
                  ....*....|....*....|....
gi 166851804  607 LGKLIVLGHVFGclDECLIIAAAL 630
Cdd:PRK11664  421 LAAMLVAAKEDD--EAALATAAKL 442
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
 132-299 4.42e-41

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 151.53  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQ--RSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17972    59 LPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQndRAAECNIVVTQPRRISAVSVAERVAFERGEEVGK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAksLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTnSRFVKVVLMSA 288
Cdd:cd17972   139 SCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQA-YPDLRVILMSA 215

                         170
                  ....*....|.
gi 166851804  289 TISCKEFADYF 299
Cdd:cd17972   216 TIDTSMFCEYF 226
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
 132-299 5.66e-41

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 149.17  E-value: 5.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYV--QRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVlrGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  210 VVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSA 288
Cdd:cd17976    81 NVGYQVRLEsRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE-LRVVLMSA 159

                         170
                  ....*....|.
gi 166851804  289 TISCKEFADYF 299
Cdd:cd17976   160 TGDNQRLSRYF 170
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
 132-303 5.04e-39

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 143.65  E-value: 5.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYcsIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM--IGITQPRRVAAVSVAKRVAEEMGVELGQLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRF----VKVVLMS 287
Cdd:cd17978    79 GYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQklspLKVIIMS 158

                         170
                  ....*....|....*..
gi 166851804  288 ATISCKEFADYFA-VPV 303
Cdd:cd17978   159 ATLDADLFSEYFNgAPV 175
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
 132-300 1.17e-38

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 142.75  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYV---QRSAYCSIVVTQPRKIGASSIARWISKERAWTLG 208
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlngGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  209 -----GVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKV 283
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSD-LHL 159

                         170
                  ....*....|....*..
gi 166851804  284 VLMSATISCKEFADYFA 300
Cdd:cd17975   160 ILMSATVDCEKFSSYFT 176
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
 132-299 1.63e-37

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 139.19  E-value: 1.63e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKS-LMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATI 290
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPN-LKLILSSAAL 159


                  ....*....
gi 166851804  291 SCKEFADYF 299
Cdd:cd17987   160 DVNLFIRYF 168
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
 132-300 1.11e-36

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 136.42  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-----AGFRHIACTQPRRIACISLAKRVAFESLNQYGSKV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATIS 291
Cdd:cd17979    76 AYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD-LKLILMSATIN 154


                  ....*....
gi 166851804  292 CKEFADYFA 300
Cdd:cd17979   155 IELFSGYFE 163
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
 132-299 8.46e-35

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 131.52  E-value: 8.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAycSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG--MIGVTQPRRVAAISVAQRVAEEMKCTLGSKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSR----FVKVVLMS 287
Cdd:cd17984    79 GYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkeHLKVVVMS 158

                         170
                  ....*....|..
gi 166851804  288 ATISCKEFADYF 299
Cdd:cd17984   159 ATLELAKLSAFF 170
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
 131-299 3.80e-33

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 127.15  E-value: 3.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  131 DLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:cd17973    12 ELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDVKLGEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLMSATI 290
Cdd:cd17973    92 VGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDI-LMGLLKEVVRRRPDLKLIVMSATL 170


                  ....*....
gi 166851804  291 SCKEFADYF 299
Cdd:cd17973   171 DAGKFQKYF 179
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
 132-315 6.63e-33

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 125.65  E-value: 6.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRtNSRFVKVVLMSATIS 291
Cdd:cd17989    79 GYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKVIITSATID 157

                         170       180
                  ....*....|....*....|....
gi 166851804  292 CKEFADYFavpvqnkmNPAYIFEV 315
Cdd:cd17989   158 AERFSRHF--------NNAPIIEV 173
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
 132-303 1.99e-32

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 124.50  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYIL-DHYvqrSAYCSIVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGY---TDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATI 290
Cdd:cd17983    78 VGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDL-KLIVTSATM 156

                         170
                  ....*....|....
gi 166851804  291 SCKEFADYFA-VPV 303
Cdd:cd17983   157 DADKFADFFGnVPI 170
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
 132-299 2.58e-31

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 121.46  E-value: 2.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS----IVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHE-----AGYTKgggkIGCTQPRRVAAMSVAARVAEEMGVKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  208 GGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLlrtnSRF---VKVV 284
Cdd:cd17974    76 GNEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDI----ARFrpdLKLL 151

                         170
                  ....*....|....*
gi 166851804  285 LMSATISCKEFADYF 299
Cdd:cd17974   152 ISSATMDAEKFSAFF 166
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
 132-302 3.21e-30

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 118.61  E-value: 3.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS--------IVVTQPRKIGASSIARWISKER 203
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYE-----AGFGSpesdnpgmIGITQPRRVAAVSMAKRVAEEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  204 AwTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDF---------LLLVVRKLL 274
Cdd:cd17982    76 N-VFGKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDIligmlsrivPLRAKLYLQ 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 166851804  275 RTNSRFVKVVLMSATISCKEFAD---YFAVP 302
Cdd:cd17982   155 DQTVKPLKLVIMSATLRVEDFTEnklLFPRP 185
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
 132-299 7.80e-27

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 108.72  E-value: 7.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17971     6 LPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAE--AGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGQEV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATIS 291
Cdd:cd17971    84 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDL-KLIVTSATLD 162


                  ....*...
gi 166851804  292 CKEFADYF 299
Cdd:cd17971   163 AVKFSQYF 170
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
 132-308 1.55e-26

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 107.94  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS----IVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAE-----AGWTAggrvVGCTQPRRVAAVTVAGRVAEEMGAVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  208 GGVVGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLM 286
Cdd:cd17980    76 GHEVGYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD-LRLIVA 154

                         170       180
                  ....*....|....*....|..
gi 166851804  287 SATISCKEFADYFAvpvQNKMN 308
Cdd:cd17980   155 SATLDAEKFRDFFN---QNETN 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
 132-300 2.11e-26

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 107.03  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAycSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG--KIIVLEPRRVAARAAARRLATLLGEAPGETV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17990    79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLLRDDLRLLAMSATLD 158


                  ....*....
gi 166851804  292 CKEFADYFA 300
Cdd:cd17990   159 GDGLAALLP 167
DEXDc smart00487
DEAD-like helicases superfamily;
126-299 1.55e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 91.01  E-value: 1.55e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804    126 TYKYPDLPISRYKEEVVSLIESN-SVVIIHGATGSGKSTQLPQYILDHyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA-LKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804    205 WTLGGVVGYQVG------LEKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTN 277
Cdd:smart00487   80 SLGLKVVGLYGGdskreqLRKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLP 158

                           170       180
                    ....*....|....*....|....
gi 166851804    278 SRfVKVVLMSATISC--KEFADYF 299
Cdd:smart00487  159 KN-VQLLLLSATPPEeiENLLELF 181
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
 566-664 5.61e-16

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 74.97  E-value: 5.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   566 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF----- 640
Cdd:pfam04408    2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldpr 71

                           90       100       110
                   ....*....|....*....|....*....|...
gi 166851804   641 --------RQHLDGYRNKVNFSGSS-KSDCIAL 664
Cdd:pfam04408   72 saakaarrRRRAADEKARAKFARLDlEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
 588-665 6.99e-16

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 73.84  E-value: 6.99e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166851804    588 DGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPFRQHLDGYRNKvnFSgSSKSDCIALV 665
Cdd:smart00847    8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRR--FA-DPESDHLTLL 82
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
 132-264 2.25e-15

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 75.70  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNS-VVIIHGATGSGKSTQLPQYILDHYVQRSAYC-SIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17986     1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLNLGH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 166851804  210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMD 264
Cdd:cd17986    81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASD 135
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
 132-303 1.93e-14

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 72.94  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQ----YILDHYVQRSAycsIVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV---VVCTQVHKQTAVWLALRVADEMDVNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  208 GGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMS 287
Cdd:cd17977    78 GHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157

                         170
                  ....*....|....*.
gi 166851804  288 ATISCKEFADYFAVPV 303
Cdd:cd17977   158 PHLSSKLLSYYGNVPL 173
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 904-1037 4.77e-14

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 70.62  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  904 VTEVVEVGHFWgYRIDENN---SEILKKLTAEINQLT-LVPLPTHPHPDLVCLAPFADfdkQRYFRAQVLYVSGNSAEVF 979
Cdd:cd20422     6 VEFVKDPSEFW-IRLGEHAvpfSKLMRSMTAFYSQASkLDGVVLKPQPGQLCCAKWKE---DRYYRAIVTAVKGKMVEVF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 166851804  980 FVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPsakslvCGKHWSDGASQWF 1037
Cdd:cd20422    82 LVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP------LGERWSPEAISAF 133
TUDOR pfam00567
Tudor domain;
904-1013 8.52e-14

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 69.31  E-value: 8.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   904 VTEVVEVGHFWgyRIDENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdKQRYFRAQVLY-VSGNSAEVFF 980
Cdd:pfam00567    7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 166851804   981 VDYGNKSHVDLHLLMEIPCQFLELPFQALEFKI 1013
Cdd:pfam00567   83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
HELICc smart00490
helicase superfamily c-terminal domain;
400-499 6.31e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 59.92  E-value: 6.31e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804    400 YMHELLTSLVHKrlqVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLtrtlvcdedtnyqs 479
Cdd:smart00490    2 ELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL-------------- 64

                            90       100
                    ....*....|....*....|
gi 166851804    480 lrlsWASKTSCNQRKGRAGR 499
Cdd:smart00490   65 ----PWSPASYIQRIGRAGR 80
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 139-291 1.79e-10

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 61.10  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   139 EEVVSLIESNSVVIIHGATGSGKST--QLPqyILDHYVQRSAYCSIVVTQPRKIGASSIARWIsKERAWTLGGVVGYQVG 216
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   217 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:pfam00270   82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157


                   ..
gi 166851804   290 IS 291
Cdd:pfam00270  158 LP 159
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 148-289 6.44e-10

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 58.95  E-value: 6.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  148 NSVVIIHGATGSGKSTQLPQYILDHYVQRSayCSIVVTQPRKIGASSIARWISKERAWtlGGVVGYQVG------LEKIA 221
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGgssaeeREKNK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  222 TEDTRLIYMTTGVLLQKIVSAK--SLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSAT 289
Cdd:cd00046    77 LGDADIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 388-500 2.83e-09

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 56.06  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804   388 VLVFLpglgeiNYMHELLTSLVHKR--LQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCL 465
Cdd:pfam00271   18 VLIFS------QTKKTLEAELLLEKegIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDL 91

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 166851804   466 TRTLvcdedtnyqslrlswaskTSCNQRKGRAGRV 500
Cdd:pfam00271   92 PWNP------------------ASYIQRIGRAGRA 108
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 920-1013 4.71e-09

fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410495  Cd Length: 126  Bit Score: 55.97  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  920 ENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdkQRYFRAQVLYVSgNSAEVFFVDYGNKSHVDLHLLMEI 997
Cdd:cd20424    32 ARNAGVLDQLASAISRLssEIRKLELSVNPGTLCLAKYSD---QHWYRGIIITNK-NSTEVFFVDYGNTEKVEKEDMLPI 107

                          90
                  ....*....|....*....
gi 166851804  998 P---CQFLELPFQALEFKI 1013
Cdd:cd20424   108 PsdaYELLLLPMQAIKCSL 126
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 904-1016 2.65e-08

fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410482  Cd Length: 116  Bit Score: 53.60  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  904 VTEVVEVGHFWGYRIDEN-NSEILKKLTAEINQL---TLVPLPTHPHPDLVCLAPFADfDKQRYfRAQVLYVSGNSAEVF 979
Cdd:cd20411     3 VLEVISPDLFYALPKTGQvNVEKLKALMTELAEYcskQSVPQQFRPRIGDACCARFTG-DKNWY-RAVVLETSDSEVKVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 166851804  980 FVDYGNKSHVDLHLLMEIPCQFLELPFQALefkICKM 1016
Cdd:cd20411    81 YADYGNTETLPLSRILPITKSHLELPFQII---RCSL 114
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 948-1010 3.31e-08

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 52.30  E-value: 3.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166851804  948 DLVClAPFADFDkqRYFRAQVLYVSGNS-AEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 1010
Cdd:cd20412    33 DIVA-APFRHDG--SWYRARVLGFLENGnLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIE 93
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 904-1011 5.24e-08

fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410511  Cd Length: 127  Bit Score: 52.84  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  904 VTEVVEVGHFWgYRIDENNsEILKKLTAEINQLtlVPLPTHPHPDL----VCLAPFadFDKQRYFRAQVLYVSGNS-AEV 978
Cdd:cd20440    16 ITHVYSPAKFY-CQLDRNT-EILEALMEKIAEI--SKLFNSQILDNcktrLCLAKY--FEDGQWYRALAHPVESSShLSV 89

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 166851804  979 FFVDYGNKSHVDLHLLMEIPCQFLEL---PFQALEF 1011
Cdd:cd20440    90 YFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKC 125
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 941-1010 5.43e-08

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 51.05  E-value: 5.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166851804  941 LPTHPHPDLVCLAPFADfdkqRYFRAQVLYVSG--NSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 1010
Cdd:cd20407     1 LPEPIEVGVICAAPVMN----AWYRAQVVGVFEetDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATE 68
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
 147-506 6.08e-08

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 57.29  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  147 SNSVVIIHGATGSGKSTQLPQ------YILDHYVQRSAYCS------IVVTQPRKigasSIARWISKERAWTLG--GVVG 212
Cdd:PHA02653  178 SRKPVVLTGGTGVGKTSQVPKlllwfnYLFGGFDNLDKIDPnfierpIVLSLPRV----ALVRLHSITLLKSLGfdEIDG 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  213 YQVGLE--KIATEDTRLIYMTTGVLL--QKIVSAKsLMEFTHIIIDEVHERTEEMDFLLLVVRKLLrtnSRFVKVVLMSA 288
Cdd:PHA02653  254 SPISLKygSIPDELINTNPKPYGLVFstHKLTLNK-LFDYGTVIIDEVHEHDQIGDIIIAVARKHI---DKIRSLFLMTA 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  289 TIS-----CKEFADyfavpvqnkmNPAYIFEVEGKPHSVEEYYLNDLehiHHSKLSPHLLEEPVitKDIyevaVSLIQMF 363
Cdd:PHA02653  330 TLEddrdrIKEFFP----------NPAFVHIPGGTLFPISEVYVKNK---YNPKNKRAYIEEEK--KNI----VTALKKY 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  364 ddldMKESGnkawsgaqfvlerSSVLVFLPGLGEINYMHELLTSLvHKRLQVYPLHSSV--ALEEQNNVFLSPVPgyrKI 441
Cdd:PHA02653  391 ----TPPKG-------------SSGIVFVASVSQCEEYKKYLEKR-LPIYDFYIIHGKVpnIDEILEKVYSSKNP---SI 449

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166851804  442 ILSTNIAESSVTVPDVKYVIDfcLTRTLVCDEDTNYQSLrlswASKTSCNQRKGRAGRVSRG-YCY 506
Cdd:PHA02653  450 IISTPYLESSVTIRNATHVYD--TGRVYVPEPFGGKEMF----ISKSMRTQRKGRVGRVSPGtYVY 509
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 963-1018 6.13e-08

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 53.02  E-value: 6.13e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 166851804  963 YFRAQVLYVSGNS-------AEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 1018
Cdd:cd20435    65 YHRVKVLEITEKDdktkpreVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKP 127
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 947-1023 1.79e-07

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 50.87  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  947 PDLVCLAPFADfdkQRYFRAQVLYVSG-NSAEVF--FVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPSAKSL 1023
Cdd:cd20418     6 PEMPCLAEYSD---GKWYRAKLLSILEfNPVKILvrHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDS 82
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 947-997 3.31e-07

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 48.28  E-value: 3.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166851804  947 PDLVCLAPFADFDKqrYFRAQVLYV-SGNSAEVFFVDYGNKSHVDLHLLMEI 997
Cdd:cd20379     1 VGDLCAAKYEEDGK--WYRARVLEVlSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 901-1014 1.44e-06

fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 48.64  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  901 TIDV--TEVVEVGHFWgYRIDENNSEiLKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKqrYFRAQVL-YVSGNSAE 977
Cdd:cd20439    11 VVDVkcSYVNSPGDFW-CQLQTKSSE-LKSLMKQIQSYYLIHNDPYKHGQIACVAKYSKDGK--WYRAAVLkQVSAKEVD 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 166851804  978 VFFVDYGNKSHVDLHLLMEIPCQFLELPFQAleFKIC 1014
Cdd:cd20439    87 VIFVDYGNQERVLISDLRAIKPQFLLLEGQA--FRCS 121
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 924-1002 3.96e-06

second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410480  Cd Length: 82  Bit Score: 46.29  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  924 EILKKLTAEINQLTLVPLpTHPHPDLVCLAPFADfDKQRYfRAQVL-YVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFL 1002
Cdd:cd20409     6 ELQESLSAYCKVAPASSD-FSPAVGEVCCAQFTE-DNQWY-RASVLaYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSLL 82
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
 150-289 6.00e-06

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 47.54  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  150 VVIIHGATGSGKSTQ-LPQYILDHYVQRSaycSIVVTQPRKIGASSIARWISKERawtlggvVGYQVGLEKIATEDTRLI 228
Cdd:cd17931     3 LTVLDLHPGAGKTTRvLPQIIREAIKKRL---RTLVLAPTRVVAAEMYEALRGLP-------IRYRTGAVKEEHGGNEIV 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166851804  229 -YMTTGVLLQKIVSAKSLMEFTHIIIDEVHerteemdFLLLVVRKLLRTNSRFVK-----VVLMSAT 289
Cdd:cd17931    73 dYMCHGTFTCRLLSPKRVPNYNLIIMDEAH-------FTDPASIAARGYIHTRVEmgeaaVIFMTAT 132
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 950-1001 1.73e-05

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 43.42  E-value: 1.73e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 166851804    950 VCLAPFADfdkQRYFRAQVLYVSGN-SAEVFFVDYGNKSHVDLHLLMEIPCQF 1001
Cdd:smart00333    8 KVAARWED---GEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 904-1009 2.11e-05

third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410509  Cd Length: 141  Bit Score: 45.93  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  904 VTEVVEVGHFWgYRIDENNSE---ILKKLTAEINQLTLVP-LPTHPHPDLVCLAPFADfdKQRYFRAQVLYVSGNSAEVF 979
Cdd:cd20438    11 VEYVLNPSNFW-IRTDEYNNEfqaLMKNIADIYNLCGNDEeLLKKPEPGLLCCARYSK--DRHYYRAVITEVLDLKVSVY 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 166851804  980 FVDYGNKSHVDLHLLMEIPCQFLELPFQAL 1009
Cdd:cd20438    88 FLDFGNTDTVPFYDVKTLLPEFSELPALAM 117
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 965-1018 3.64e-05

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410498  Cd Length: 98  Bit Score: 43.96  E-value: 3.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 166851804  965 RAQVLYVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 1018
Cdd:cd20427    40 RAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLAGLEP 93
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 944-1010 4.76e-05

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 43.24  E-value: 4.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 166851804  944 HPHPDLVCLAPFADFDKqrYFRAQVLYVSGN--SAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 1010
Cdd:cd20423     2 HSLPNPVCLAKYSEDGK--WCRALIDNVYEPveMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFR 68
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 959-1042 4.83e-05

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 44.80  E-value: 4.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  959 DKQRYFRAQVLYVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQAleFKICKmrpSAKSLVCGkHWSDGASQWFA 1038
Cdd:cd20426    59 EDNHWYRALVTKINDNLVSVRFVDYGNEEDVVREQVRALPSELLKIPVQA--FPCCL---SGFNLSEG-LWSDEANDYFY 132


                  ....
gi 166851804 1039 SLVS 1042
Cdd:cd20426   133 EIVT 136
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 945-1018 2.08e-04

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 41.65  E-value: 2.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166851804  945 PHPDLVCLAPFADfdkQRYFRAQVLYVSGNSA-EVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 1018
Cdd:cd20415    25 PVQGQACVALFED---GAWYRARIIGLPGHREvEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 945-1002 5.11e-04

third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410481 [Multi-domain]  Cd Length: 59  Bit Score: 39.63  E-value: 5.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 166851804  945 PHPDLVCLAPFADfdKQRYFRAQVLYV-SGNSAEVFFVDYGNKSHVDLHLLMEIPCQFL 1002
Cdd:cd20410     3 PIVGEPCCAFFSG--DGNWYRAMVKEIlPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 964-1005 2.03e-03

sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410512  Cd Length: 108  Bit Score: 39.34  E-value: 2.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 166851804  964 FRAQVL-YVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELP 1005
Cdd:cd20441    55 YRAVITaVLPGKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 904-1031 8.96e-03

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410479  Cd Length: 130  Bit Score: 37.73  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166851804  904 VTEVVEVGHFWGYRIDENNSEILKKLTA---EINQLTLVPLPTHPHPDLVCLAPFADfdKQRYFRA--QVLYVSGNSAEV 978
Cdd:cd20408     3 VTEFKNPGEFYIQIYTLEVLESLVKLTSqlkKTYASVNNHKEYIPEVGEVCVAKYSE--DQNWYRAlvQTVDVQQKKAGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 166851804  979 FFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPsaksLVCGkhWSD 1031
Cdd:cd20408    81 FYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKP----PSGS--WSE 127
 
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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