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Conserved domains on  [gi|198278551|ref|NP_083332|]
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ATP-dependent RNA helicase TDRD9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
134-317 6.03e-97

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


The actual alignment was detected with superfamily member cd17988:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 180  Bit Score: 308.28  E-value: 6.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160
                         170       180
                  ....*....|....*....|....
gi 198278551  294 CKQFADYFAVPVqnkmNPAYVFEV 317
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
132-706 4.90e-92

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: 317.02  E-value: 4.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  132 PDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHytQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 291
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  292 INCKQFADYFavpvqnkmNPAYVFEVEGKPHAIEEYYLNDLGHiyhsglPYRLEEPVITkdvyevAVsliqmfDDLDMKE 371
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVEVRYRPLPAD------ERDLEDAVAD------AV------REALAEE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  372 SGnktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAES 451
Cdd:COG1643   220 PG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAET 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  452 SVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCP 531
Cdd:COG1643   286 SLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRAD 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  532 LGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKL 611
Cdd:COG1643   365 LASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARM 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  612 VVLGHVFGCLDECLIIAAALSLKNfftmPFRQhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwg 691
Cdd:COG1643   433 LLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQRE------------- 482
                         570
                  ....*....|....*
gi 198278551  692 RLNYIQIKRIREVAE 706
Cdd:COG1643   483 FLSYLRLREWRDLAR 497
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
906-1006 6.73e-55

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: 186.05  E-value: 6.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  906 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 985
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80
                          90       100
                  ....*....|....*....|.
gi 198278551  986 NRSHVDLDLLREIPCQFLELP 1006
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 ...
134-317 6.03e-97

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: 308.28  E-value: 6.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160
                         170       180
                  ....*....|....*....|....
gi 198278551  294 CKQFADYFAVPVqnkmNPAYVFEV 317
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
132-706 4.90e-92

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 317.02  E-value: 4.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  132 PDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHytQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 291
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  292 INCKQFADYFavpvqnkmNPAYVFEVEGKPHAIEEYYLNDLGHiyhsglPYRLEEPVITkdvyevAVsliqmfDDLDMKE 371
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVEVRYRPLPAD------ERDLEDAVAD------AV------REALAEE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  372 SGnktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAES 451
Cdd:COG1643   220 PG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAET 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  452 SVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCP 531
Cdd:COG1643   286 SLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRAD 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  532 LGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKL 611
Cdd:COG1643   365 LASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARM 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  612 VVLGHVFGCLDECLIIAAALSLKNfftmPFRQhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwg 691
Cdd:COG1643   433 LLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQRE------------- 482
                         570
                  ....*....|....*
gi 198278551  692 RLNYIQIKRIREVAE 706
Cdd:COG1643   483 FLSYLRLREWRDLAR 497
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
128-737 1.10e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 263.84  E-value: 1.10e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  128 TYKYPD-LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDhyTQRSAFCNIVVTQPRKIGASSIARWISKERS 206
Cdd:PRK11131   66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  207 WTLGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 286
Cdd:PRK11131  144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  287 LMSATINCKQFADYFavpvqnkmNPAYVFEVEGKPHAIEeyylndlghiyhsgLPYRleePVITKDVYEVAVSLIQMFDD 366
Cdd:PRK11131  223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVE--------------VRYR---PIVEEADDTERDQLQAIFDA 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  367 LDmkESGNKTwsgaqfvseRSSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPvpGYRKIILST 446
Cdd:PRK11131  278 VD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLAT 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  447 NIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPE 526
Cdd:PRK11131  345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR-PEFTDPE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  527 MLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPVSQ 606
Cdd:PRK11131  424 ILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPVDP 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  607 QLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPF--RQHLDGYRNKVHfsgSSRSDCLALVEAFRAWQAcrQRGELR-- 682
Cdd:PRK11131  497 RLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFVNLWNYLQE--QQKALSsn 571
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 198278551  683 --RPKDELDWgrLNYIqikRIREVAELYEELKNRISQFNMfvgphhPVLDQEYPYKQ 737
Cdd:PRK11131  572 qfRRLCRTDY--LNYL---RVREWQDIYTQLRQVVKELGI------PVNSEPAEYRE 617
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
322-509 2.51e-61

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: 207.00  E-value: 2.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  322 HAIEEYYLNDLGHIYHSglpyrlEEPVITKDVYEVAVSLIqmFDDLDMKESGnktwsgaqfvsersSVLVFLPGLGEINY 401
Cdd:cd18791     1 FPVEVYYLEDILELLGI------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIER 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  402 MHELLTNMIH----KRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTN 477
Cdd:cd18791    59 LCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTG 138
                         170       180       190
                  ....*....|....*....|....*....|..
gi 198278551  478 YQSLRLSWASKTSCDQRKGRAGRVSKGYCYRL 509
Cdd:cd18791   139 LSSLVTVWISKASAEQRAGRAGRTRPGKCYRL 170
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
134-690 2.44e-55

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: 208.47  E-value: 2.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHytqRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDA---PGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:TIGR01970   78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   294 CKQfadyfavpVQNKMNPAYVFEVEGKPHAIEEYYLndlghiyhsglPYRLEEPVITKDVYEVAVSLIQmfddldmkESG 373
Cdd:TIGR01970  158 GER--------LSSLLPDAPVVESEGRSFPVEIRYL-----------PLRGDQRLEDAVSRAVEHALAS--------ETG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   374 nktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSV 453
Cdd:TIGR01970  211 --------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSL 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   454 TVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLG 533
Cdd:TIGR01970  277 TIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRL-PAQDEPEILQADLS 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   534 STILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVSQQLGKLVV 613
Cdd:TIGR01970  356 GLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRLAAMLL 423
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551   614 LGHVFGCLDECLIIAAALSLKNfftmPFRQHLDGYRNKVHFSGSSRSDCLAlveafRAWQACRQ-RGELRRPKDELDW 690
Cdd:TIGR01970  424 SAHSTGLAALACDLAALLEERG----LPRQGGADLMNRLHRLQQGRQGRGQ-----RAQQLAKKlRRRLRFSQADSGA 492
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
906-1006 6.73e-55

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: 186.05  E-value: 6.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  906 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 985
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80
                          90       100
                  ....*....|....*....|.
gi 198278551  986 NRSHVDLDLLREIPCQFLELP 1006
Cdd:cd20431    81 NTSQVPSSLLREIPETLLTLP 101
DEXDc smart00487
DEAD-like helicases superfamily;
146-293 4.92e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.08  E-value: 4.92e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551    146 LIESNSVVIIHGATGSGKSTQLPQYVLDHYtQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVG------L 219
Cdd:smart00487   20 LLSGLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGdskreqL 98
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198278551    220 EKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIFIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSATIN 293
Cdd:smart00487   99 RKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKN-VQLLLLSATPP 171
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
589-666 1.75e-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: 75.38  E-value: 1.75e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551    589 DGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHfsgSSRSDCLALV 666
Cdd:smart00847    8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRRFA---DPESDHLTLL 82
TUDOR pfam00567
Tudor domain;
905-1014 2.94e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 76.24  E-value: 2.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   905 VTEVVEVGHFWgyRIDERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDynKESYFRAQILY-VSGNSAEVFF 981
Cdd:pfam00567    7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 198278551   982 VDYGNRSHVDLDLLREIPCQFLELPFQALEFKI 1014
Cdd:pfam00567   83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
567-647 7.03e-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: 74.58  E-value: 7.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   567 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLD 646
Cdd:pfam04408    2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPR 71

                   .
gi 198278551   647 G 647
Cdd:pfam04408   72 S 72
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
141-293 1.27e-07

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: 52.63  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   141 EEVISLIESNSVVIIHGATGSGKST--QLPqyVLDHYTQRSAFCNIVVTQPRKIGASSIARWIsKERSWTLGGLVGYQVG 218
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   219 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 291
Cdd:pfam00270   82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157

                   ..
gi 198278551   292 IN 293
Cdd:pfam00270  158 LP 159
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
951-1002 2.42e-07

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: 48.81  E-value: 2.42e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 198278551    951 VCLAPFTDYNkesYFRAQILYVSGN-SAEVFFVDYGNRSHVDLDLLREIPCQF 1002
Cdd:smart00333    8 KVAARWEDGE---WYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 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 ...
134-317 6.03e-97

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: 308.28  E-value: 6.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17988     1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:cd17988    81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160
                         170       180
                  ....*....|....*....|....
gi 198278551  294 CKQFADYFAVPVqnkmNPAYVFEV 317
Cdd:cd17988   161 CKEFADYFTTPN----NPAYVFEV 180
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
132-706 4.90e-92

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


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 317.02  E-value: 4.90e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  132 PDLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHytQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:COG1643     8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 291
Cdd:COG1643    86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  292 INCKQFADYFavpvqnkmNPAYVFEVEGKPHAIEEYYLNDLGHiyhsglPYRLEEPVITkdvyevAVsliqmfDDLDMKE 371
Cdd:COG1643   166 LDAERFARLL--------GDAPVIESSGRTYPVEVRYRPLPAD------ERDLEDAVAD------AV------REALAEE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  372 SGnktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAES 451
Cdd:COG1643   220 PG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAET 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  452 SVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCP 531
Cdd:COG1643   286 SLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARR-PAFTDPEILRAD 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  532 LGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKL 611
Cdd:COG1643   365 LASLILELAAWGLGDPEDL--PFLDPPPARAIADARALLQELGAL-------DA---DGRLTPLGRALARLPLDPRLARM 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  612 VVLGHVFGCLDECLIIAAALSLKNfftmPFRQhldgyrnkvhfsgSSRSDCLALVEAFRAWQACRQRgelrrpkdeldwg 691
Cdd:COG1643   433 LLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQRE------------- 482
                         570
                  ....*....|....*
gi 198278551  692 RLNYIQIKRIREVAE 706
Cdd:COG1643   483 FLSYLRLREWRDLAR 497
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
128-737 1.10e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 263.84  E-value: 1.10e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  128 TYKYPD-LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDhyTQRSAFCNIVVTQPRKIGASSIARWISKERS 206
Cdd:PRK11131   66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  207 WTLGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 286
Cdd:PRK11131  144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  287 LMSATINCKQFADYFavpvqnkmNPAYVFEVEGKPHAIEeyylndlghiyhsgLPYRleePVITKDVYEVAVSLIQMFDD 366
Cdd:PRK11131  223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVE--------------VRYR---PIVEEADDTERDQLQAIFDA 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  367 LDmkESGNKTwsgaqfvseRSSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPvpGYRKIILST 446
Cdd:PRK11131  278 VD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQSH--SGRRIVLAT 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  447 NIAESSVTVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPE 526
Cdd:PRK11131  345 NVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSR-PEFTDPE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  527 MLRCPLGSTILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPVSQ 606
Cdd:PRK11131  424 ILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPVDP 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  607 QLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPF--RQHLDGYRNKVHfsgSSRSDCLALVEAFRAWQAcrQRGELR-- 682
Cdd:PRK11131  497 RLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFVNLWNYLQE--QQKALSsn 571
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 198278551  683 --RPKDELDWgrLNYIqikRIREVAELYEELKNRISQFNMfvgphhPVLDQEYPYKQ 737
Cdd:PRK11131  572 qfRRLCRTDY--LNYL---RVREWQDIYTQLRQVVKELGI------PVNSEPAEYRE 617
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
150-301 5.84e-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: 5.84e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  150 NSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVGLEKIATEDTRL 229
Cdd:cd17917     1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278551  230 IYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATINCKQFADYF 301
Cdd:cd17917    81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDL-KVILMSATLDAEKFSSYF 151
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
322-509 2.51e-61

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: 207.00  E-value: 2.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  322 HAIEEYYLNDLGHIYHSglpyrlEEPVITKDVYEVAVSLIqmFDDLDMKESGnktwsgaqfvsersSVLVFLPGLGEINY 401
Cdd:cd18791     1 FPVEVYYLEDILELLGI------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIER 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  402 MHELLTNMIH----KRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLTRTLVCDEDTN 477
Cdd:cd18791    59 LCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTG 138
                         170       180       190
                  ....*....|....*....|....*....|..
gi 198278551  478 YQSLRLSWASKTSCDQRKGRAGRVSKGYCYRL 509
Cdd:cd18791   139 LSSLVTVWISKASAEQRAGRAGRTRPGKCYRL 170
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
134-690 2.44e-55

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: 208.47  E-value: 2.44e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHytqRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDA---PGIGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:TIGR01970   78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   294 CKQfadyfavpVQNKMNPAYVFEVEGKPHAIEEYYLndlghiyhsglPYRLEEPVITKDVYEVAVSLIQmfddldmkESG 373
Cdd:TIGR01970  158 GER--------LSSLLPDAPVVESEGRSFPVEIRYL-----------PLRGDQRLEDAVSRAVEHALAS--------ETG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   374 nktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSV 453
Cdd:TIGR01970  211 --------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSL 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   454 TVPDVKYVIDFCLTRTLVCDEDTNYQSLRLSWASKTSCDQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLRCPLG 533
Cdd:TIGR01970  277 TIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRL-PAQDEPEILQADLS 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   534 STILKVKLLDMGEPRALlaTALSPPSLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVSQQLGKLVV 613
Cdd:TIGR01970  356 GLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRLAAMLL 423
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551   614 LGHVFGCLDECLIIAAALSLKNfftmPFRQHLDGYRNKVHFSGSSRSDCLAlveafRAWQACRQ-RGELRRPKDELDW 690
Cdd:TIGR01970  424 SAHSTGLAALACDLAALLEERG----LPRQGGADLMNRLHRLQQGRQGRGQ-----RAQQLAKKlRRRLRFSQADSGA 492
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
906-1006 6.73e-55

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: 186.05  E-value: 6.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  906 TEVVEVGHFWGYRIDERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKESYFRAQILYVSGNSAEVFFVDYG 985
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80
                          90       100
                  ....*....|....*....|.
gi 198278551  986 NRSHVDLDLLREIPCQFLELP 1006
Cdd:cd20431    81 NTSQVPSSLLREIPETLLTLP 101
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
134-301 3.15e-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: 155.38  E-value: 3.15e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRS--AFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:cd17985     1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPplPVANIICTQPRRISAISVAERVAQERAERVGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 291
Cdd:cd17985    81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD-LKVILMSAT 159
                         170
                  ....*....|
gi 198278551  292 INCKQFADYF 301
Cdd:cd17985   160 LNAELFSDYF 169
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
134-602 5.71e-41

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 163.56  E-value: 5.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLdhytQRSAFC-NIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:PRK11664    4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL----QHGGINgKIIMLEPRRLAARNVAQRLAEQLGEKPGET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATI 292
Cdd:PRK11664   80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDDLKLLIMSATL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  293 NCKQfadyfavpVQNKMNPAYVFEVEGKPHAIEEYYLNDLGHiyhsglpYRLEEpvitkdvyEVAVSLIQMFDdldmKES 372
Cdd:PRK11664  160 DNDR--------LQQLLPDAPVIVSEGRSFPVERRYQPLPAH-------QRFDE--------AVARATAELLR----QES 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  373 GnktwsgaqfvsersSVLVFLPGLGEINYMHELLTNMIHKRLQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESS 452
Cdd:PRK11664  213 G--------------SLLLFLPGVGEIQRVQEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETS 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  453 VTVPDVKYVIDFCLTRTLVCDEDTNYQSL---RLSWASKTscdQRKGRAGRVSKGYCYRLIPRDFWDSAiPDHVVPEMLR 529
Cdd:PRK11664  279 LTIEGIRLVVDSGLERVARFDPKTGLTRLvtqRISQASMT---QRAGRAGRLEPGICLHLYSKEQAERA-AAQSEPEILH 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 198278551  530 CPLGSTILkvKLLDMGEPRALLATALSPPSLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQL 602
Cdd:PRK11664  355 SDLSGLLL--ELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGR----------LTARGRKMAAL 415
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
134-301 2.25e-40

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: 147.68  E-value: 2.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQR--SAFCNIVVTQPRKIGASSIARWISKER--SWTL 209
Cdd:cd17981     1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERgkGSSCRIVCTQPRRISAISVAERVAAERaeSCGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  210 GGLVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLM 288
Cdd:cd17981    81 GNSTGYQIRLEsRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDV-LMGIVKDLLPFRSDLKVILM 159
                         170
                  ....*....|...
gi 198278551  289 SATINCKQFADYF 301
Cdd:cd17981   160 SATLNAEKFSDYF 172
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
134-305 4.59e-40

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: 146.35  E-value: 4.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFcnIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17978     1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM--IGITQPRRVAAVSVAKRVAEEMGVELGQLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRF----VKVVLMS 289
Cdd:cd17978    79 GYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQklspLKVIIMS 158
                         170
                  ....*....|....*..
gi 198278551  290 ATINCKQFADYFA-VPV 305
Cdd:cd17978   159 ATLDADLFSEYFNgAPV 175
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
134-301 2.58e-39

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: 144.55  E-value: 2.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYT--QRSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:cd17976     1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVlrGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSA 290
Cdd:cd17976    81 NVGYQVRLEsRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE-LRVVLMSA 159
                         170
                  ....*....|.
gi 198278551  291 TINCKQFADYF 301
Cdd:cd17976   160 TGDNQRLSRYF 170
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
134-301 3.85e-38

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: 143.05  E-value: 3.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQ--RSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:cd17972    59 LPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQndRAAECNIVVTQPRRISAVSVAERVAFERGEEVGK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  212 LVGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAksLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTnSRFVKVVLMSA 290
Cdd:cd17972   139 SCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQA-YPDLRVILMSA 215
                         170
                  ....*....|.
gi 198278551  291 TINCKQFADYF 301
Cdd:cd17972   216 TIDTSMFCEYF 226
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
134-302 1.24e-37

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: 139.66  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYT---QRSAFCNIVVTQPRKIGASSIARWISKERSWTLG 210
Cdd:cd17975     1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlngGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  211 -----GLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKV 285
Cdd:cd17975    81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSD-LHL 159
                         170
                  ....*....|....*..
gi 198278551  286 VLMSATINCKQFADYFA 302
Cdd:cd17975   160 ILMSATVDCEKFSSYFT 176
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
134-301 1.80e-36

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: 136.11  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17987     1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKS-LMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATI 292
Cdd:cd17987    81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPN-LKLILSSAAL 159

                  ....*....
gi 198278551  293 NCKQFADYF 301
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 ...
134-302 2.29e-35

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: 132.57  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDhytqrSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17979     1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-----AGFRHIACTQPRRIACISLAKRVAFESLNQYGSKV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATIN 293
Cdd:cd17979    76 AYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD-LKLILMSATIN 154

                  ....*....
gi 198278551  294 CKQFADYFA 302
Cdd:cd17979   155 IELFSGYFE 163
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
134-305 3.20e-34

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: 129.50  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVL-DHYTQRSAfcnIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:cd17983     1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGYTDYGM---IGCTQPRRVAAMSVAKRVSEEMGVELGEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATI 292
Cdd:cd17983    78 VGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDL-KLIVTSATM 156
                         170
                  ....*....|....
gi 198278551  293 NCKQFADYFA-VPV 305
Cdd:cd17983   157 DADKFADFFGnVPI 170
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
134-301 2.56e-32

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: 124.20  E-value: 2.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFcnIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17984     1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGM--IGVTQPRRVAAISVAQRVAEEMKCTLGSKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSR----FVKVVLMS 289
Cdd:cd17984    79 GYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkeHLKVVVMS 158
                         170
                  ....*....|..
gi 198278551  290 ATINCKQFADYF 301
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 ...
133-301 7.03e-32

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: 123.29  E-value: 7.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  133 DLPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:cd17973    12 ELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDVKLGEE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLMSATI 292
Cdd:cd17973    92 VGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDI-LMGLLKEVVRRRPDLKLIVMSATL 170

                  ....*....
gi 198278551  293 NCKQFADYF 301
Cdd:cd17973   171 DAGKFQKYF 179
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
134-301 1.73e-30

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: 118.76  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDH-YTQRSAfcNIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:cd17974     1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAgYTKGGG--KIGCTQPRRVAAMSVAARVAEEMGVKLGNE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLlrtnSRF---VKVVLMS 289
Cdd:cd17974    79 VGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDI----ARFrpdLKLLISS 154
                         170
                  ....*....|..
gi 198278551  290 ATINCKQFADYF 301
Cdd:cd17974   155 ATMDAEKFSAFF 166
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
134-302 2.09e-30

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: 118.71  E-value: 2.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDhyTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17989     1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRtNSRFVKVVLMSATIN 293
Cdd:cd17989    79 GYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKVIITSATID 157

                  ....*....
gi 198278551  294 CKQFADYFA 302
Cdd:cd17989   158 AERFSRHFN 166
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
134-304 3.05e-28

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: 113.22  E-value: 3.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDH-YTQR--SAFCNIVVTQPRKIGASSIARWISKERSwTLG 210
Cdd:cd17982     1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAgFGSPesDNPGMIGITQPRRVAAVSMAKRVAEELN-VFG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  211 GLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDF---------LLLVVRKLLRTNSR 281
Cdd:cd17982    80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDIligmlsrivPLRAKLYLQDQTVK 159
                         170       180
                  ....*....|....*....|....*.
gi 198278551  282 FVKVVLMSATINCKQFAD---YFAVP 304
Cdd:cd17982   160 PLKLVIMSATLRVEDFTEnklLFPRP 185
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
134-301 2.36e-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: 110.26  E-value: 2.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDH-YTQRSAfcnIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:cd17971     6 LPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAgYTSRGK---IGCTQPRRVAAMSVAKRVAEEFGCCLGQE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATI 292
Cdd:cd17971    83 VGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDL-KLIVTSATL 161

                  ....*....
gi 198278551  293 NCKQFADYF 301
Cdd:cd17971   162 DAVKFSQYF 170
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
134-310 1.34e-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: 108.33  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDH-YTqrSAFCNIVVTQPRKIGASSIARWISKERSWTLGGL 212
Cdd:cd17980     1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAgWT--AGGRVVGCTQPRRVAAVTVAGRVAEEMGAVLGHE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  213 VGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 291
Cdd:cd17980    79 VGYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD-LRLIVASAT 157
                         170
                  ....*....|....*....
gi 198278551  292 INCKQFADYFAvpvQNKMN 310
Cdd:cd17980   158 LDAEKFRDFFN---QNETN 173
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
134-302 8.06e-25

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: 102.80  E-value: 8.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQYVLDHYTQRSAfcNIVVTQPRKIGASSIARWISKERSWTLGGLV 213
Cdd:cd17990     1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG--KIIVLEPRRVAARAAARRLATLLGEAPGETV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  214 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIN 293
Cdd:cd17990    79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLLRDDLRLLAMSATLD 158

                  ....*....
gi 198278551  294 CKQFADYFA 302
Cdd:cd17990   159 GDGLAALLP 167
DEXDc smart00487
DEAD-like helicases superfamily;
146-293 4.92e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.08  E-value: 4.92e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551    146 LIESNSVVIIHGATGSGKSTQLPQYVLDHYtQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGGLVGYQVG------L 219
Cdd:smart00487   20 LLSGLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGdskreqL 98
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198278551    220 EKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIFIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSATIN 293
Cdd:smart00487   99 RKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLPKN-VQLLLLSATPP 171
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
589-666 1.75e-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: 75.38  E-value: 1.75e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551    589 DGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLDGYRNKVHfsgSSRSDCLALV 666
Cdd:smart00847    8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRRFA---DPESDHLTLL 82
TUDOR pfam00567
Tudor domain;
905-1014 2.94e-16

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 76.24  E-value: 2.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   905 VTEVVEVGHFWgyRIDERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDynKESYFRAQILY-VSGNSAEVFF 981
Cdd:pfam00567    7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 198278551   982 VDYGNRSHVDLDLLREIPCQFLELPFQALEFKI 1014
Cdd:pfam00567   83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
567-647 7.03e-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: 74.58  E-value: 7.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   567 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVSQQLGKLVVLGHVFGCLDECLIIAAALSLKNFFTMPFRQHLD 646
Cdd:pfam04408    2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPR 71

                   .
gi 198278551   647 G 647
Cdd:pfam04408   72 S 72
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
134-266 3.34e-14

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: 72.24  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNS-VVIIHGATGSGKSTQLPQYVLDH-YTQRSAFCNIVVTQPRKIGASSIARWISKERSWTLGG 211
Cdd:cd17986     1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFaLSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 198278551  212 LVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMD 266
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 ...
134-266 1.03e-13

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: 70.62  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  134 LPINRCKEEVISLIESNSVVIIHGATGSGKSTQLPQ----YVL-DHYTQRSAFCnivvTQPRKIGASSIARWISKERSWT 208
Cdd:cd17977     1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLsAHYQHGVVVC----TQVHKQTAVWLALRVADEMDVN 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551  209 LGGLVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHERTEEMD 266
Cdd:cd17977    77 IGHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTD 134
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
905-1031 4.13e-13

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: 67.92  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  905 VTEVVEVGHFWgYRIDERN---AELLKQLTA---EINRLELVPLpiHPHPDLVCLAPFTDynkESYFRAQILYVSGNSAE 978
Cdd:cd20422     6 VEFVKDPSEFW-IRLGEHAvpfSKLMRSMTAfysQASKLDGVVL--KPQPGQLCCAKWKE---DRYYRAIVTAVKGKMVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 198278551  979 VFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPsaksliCGEHWS 1031
Cdd:cd20422    80 VFLVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP------LGERWS 126
HELICc smart00490
helicase superfamily c-terminal domain;
404-500 7.02e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 62.61  E-value: 7.02e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551    404 ELLTNMIHKR-LQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYVIDFCLtrtlvcdedtnyqslr 482
Cdd:smart00490    1 EELAELLKELgIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL---------------- 64
                            90
                    ....*....|....*...
gi 198278551    483 lsWASKTSCDQRKGRAGR 500
Cdd:smart00490   65 --PWSPASYIQRIGRAGR 80
Tudor_TDRD6_rpt5 cd20424
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
921-1014 6.46e-11

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: 61.37  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  921 ERNAELLKQLTAEINRL--ELVPLPIHPHPDLVCLAPFTDYNkesYFRAQILYVSgNSAEVFFVDYGNRSHVDLDLLREI 998
Cdd:cd20424    32 ARNAGVLDQLASAISRLssEIRKLELSVNPGTLCLAKYSDQH---WYRGIIITNK-NSTEVFFVDYGNTEKVEKEDMLPI 107
                          90
                  ....*....|....*....
gi 198278551  999 P---CQFLELPFQALEFKI 1014
Cdd:cd20424   108 PsdaYELLLLPMQAIKCSL 126
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
384-501 1.27e-10

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: 59.92  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   384 SERSSVLVFLpglgeiNYMHELLTNMIHKR--LQVYPLHSSVTLEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKYV 461
Cdd:pfam00271   13 ERGGKVLIFS------QTKKTLEAELLLEKegIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLV 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 198278551   462 IDFCLTRTLvcdedtnyqslrlswaskTSCDQRKGRAGRV 501
Cdd:pfam00271   87 INYDLPWNP------------------ASYIQRIGRAGRA 108
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
942-1011 4.79e-10

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: 57.22  E-value: 4.79e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278551  942 LPIHPHPDLVCLAPFTDynkeSYFRAQILYVSG--NSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 1011
Cdd:cd20407     1 LPEPIEVGVICAAPVMN----AWYRAQVVGVFEetDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATE 68
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
150-291 6.38e-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: 6.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  150 NSVVIIHGATGSGKSTQLPQYVLDHYTQRSafCNIVVTQPRKIGASSIARWISKERSW--TLGGLVGYQ--VGLEKIATE 225
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAERLRELFGPgiRVAVLVGGSsaEEREKNKLG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551  226 DTRLIYMTTGVLLQKIVSAK--SLMEFTHIFIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSAT 291
Cdd:cd00046    79 DADIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
Tudor_TDRD1_rpt2 cd20409
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
924-1003 3.45e-09

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: 54.77  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  924 AELLKQLTAEINRLELVPLpIHPHPDLVCLAPFTDYNkeSYFRAQIL-YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQF 1002
Cdd:cd20409     5 AELQESLSAYCKVAPASSD-FSPAVGEVCCAQFTEDN--QWYRASVLaYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSL 81

                  .
gi 198278551 1003 L 1003
Cdd:cd20409    82 L 82
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
149-507 4.44e-09

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 61.15  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  149 SNSVVIIHGATGSGKSTQLPQ------YVLDHYTQRSAFC------NIVVTQPRKigasSIARWISKE--RSWTLGGLVG 214
Cdd:PHA02653  178 SRKPVVLTGGTGVGKTSQVPKlllwfnYLFGGFDNLDKIDpnfierPIVLSLPRV----ALVRLHSITllKSLGFDEIDG 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  215 YQVGLE--KIATEDTRLIYMTTGVLL--QKIVSAKsLMEFTHIFIDEVHERTEEMDFLLLVVRKLLrtnSRFVKVVLMSA 290
Cdd:PHA02653  254 SPISLKygSIPDELINTNPKPYGLVFstHKLTLNK-LFDYGTVIIDEVHEHDQIGDIIIAVARKHI---DKIRSLFLMTA 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  291 TI-----NCKQFADyfavpvqnkmNPAYVFEVEGKPHAIEEYYLNDLGHIYHSgLPYRLEEpviTKDVyevaVSLIQMFd 365
Cdd:PHA02653  330 TLeddrdRIKEFFP----------NPAFVHIPGGTLFPISEVYVKNKYNPKNK-RAYIEEE---KKNI----VTALKKY- 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  366 dldMKESGnktwsgaqfvserSSVLVFLPGLGEINYMHELLTNmIHKRLQVYPLHSSVTLEEQ--NNVFLSPVPgyrKII 443
Cdd:PHA02653  391 ---TPPKG-------------SSGIVFVASVSQCEEYKKYLEK-RLPIYDFYIIHGKVPNIDEilEKVYSSKNP---SII 450
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198278551  444 LSTNIAESSVTVPDVKYVIDfcLTRTLVCDEDTNYQSLrlswASKTSCDQRKGRAGRVSKG-YCY 507
Cdd:PHA02653  451 ISTPYLESSVTIRNATHVYD--TGRVYVPEPFGGKEMF----ISKSMRTQRKGRVGRVSPGtYVY 509
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
948-998 5.80e-09

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: 53.29  E-value: 5.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 198278551  948 PDLVCLAPFTDYNKesYFRAQILYV-SGNSAEVFFVDYGNRSHVDLDLLREI 998
Cdd:cd20379     1 VGDLCAAKYEEDGK--WYRARVLEVlSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD1_rpt4 cd20411
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
905-1008 1.57e-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: 53.99  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  905 VTEVVEVGHFWGYRIDER-NAELLKQLTAEINRL---ELVPLPIHPHPDLVCLAPFTDYNkeSYFRAQILYVSGNSAEVF 980
Cdd:cd20411     3 VLEVISPDLFYALPKTGQvNVEKLKALMTELAEYcskQSVPQQFRPRIGDACCARFTGDK--NWYRAVVLETSDSEVKVL 80
                          90       100
                  ....*....|....*....|....*...
gi 198278551  981 FVDYGNRSHVDLDLLREIPCQFLELPFQ 1008
Cdd:cd20411    81 YADYGNTETLPLSRILPITKSHLELPFQ 108
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
892-1015 2.84e-08

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: 53.65  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  892 RPRTVADllltIDVTEVVEVGHFWGYRidERNAELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNKesYFRAQIL- 970
Cdd:cd20439     7 KPGSVVD----VKCSYVNSPGDFWCQL--QTKSSELKSLMKQIQSYYLIHNDPYKHGQIACVAKYSKDGK--WYRAAVLk 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 198278551  971 YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQAleFKIC 1015
Cdd:cd20439    79 QVSAKEVDVIFVDYGNQERVLISDLRAIKPQFLLLEGQA--FRCS 121
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
948-1024 5.68e-08

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: 52.03  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  948 PDLVCLAPFTDynkESYFRAQILYVSG-NSAEVF--FVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRPSAKSL 1024
Cdd:cd20418     6 PEMPCLAEYSD---GKWYRAKLLSILEfNPVKILvrHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDS 82
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
949-1019 5.79e-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: 5.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551  949 DLVCLapftDYNKESYFRAQILYVSGNS-------AEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 1019
Cdd:cd20435    54 DLCAV----EDENNLYHRVKVLEITEKDdktkpreVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKP 127
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
949-1011 5.89e-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: 51.91  E-value: 5.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 198278551  949 DLVClAPFTDYNkeSYFRAQILYVSGNS-AEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 1011
Cdd:cd20412    33 DIVA-APFRHDG--SWYRARVLGFLENGnLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIE 93
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
141-293 1.27e-07

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: 52.63  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   141 EEVISLIESNSVVIIHGATGSGKST--QLPqyVLDHYTQRSAFCNIVVTQPRKIGASSIARWIsKERSWTLGGLVGYQVG 218
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551   219 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIFIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 291
Cdd:pfam00270   82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157

                   ..
gi 198278551   292 IN 293
Cdd:pfam00270  158 LP 159
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
951-1002 2.42e-07

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: 48.81  E-value: 2.42e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 198278551    951 VCLAPFTDYNkesYFRAQILYVSGN-SAEVFFVDYGNRSHVDLDLLREIPCQF 1002
Cdd:smart00333    8 KVAARWEDGE---WYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD15_rpt5 cd20440
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
905-1012 4.94e-07

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: 50.15  E-value: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  905 VTEVVEVGHFwgYRIDERNAELLKQLTAEINrlELVPLPIHPHPDL----VCLAPFtdYNKESYFRAQILYVSGNS-AEV 979
Cdd:cd20440    16 ITHVYSPAKF--YCQLDRNTEILEALMEKIA--EISKLFNSQILDNcktrLCLAKY--FEDGQWYRALAHPVESSShLSV 89
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 198278551  980 FFVDYGNRSHVDLDLLREIPCQFLEL---PFQALEF 1012
Cdd:cd20440    90 YFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKC 125
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
945-1011 5.77e-07

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: 48.63  E-value: 5.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 198278551  945 HPHPDLVCLAPFTDYNKesYFRAQILYVSGN--SAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALE 1011
Cdd:cd20423     2 HSLPNPVCLAKYSEDGK--WCRALIDNVYEPveMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFR 68
Tudor_TDRD1_rpt3 cd20410
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
946-1003 1.91e-06

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: 46.18  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 198278551  946 PHPDLVCLAPFTDYNkeSYFRAQILYV-SGNSAEVFFVDYGNRSHVDLDLLREIPCQFL 1003
Cdd:cd20410     3 PIVGEPCCAFFSGDG--NWYRAMVKEIlPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
946-1019 1.95e-06

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: 47.43  E-value: 1.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 198278551  946 PHPDLVCLAPFTDYNkesYFRAQILYVSGNSA-EVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 1019
Cdd:cd20415    25 PVQGQACVALFEDGA---WYRARIIGLPGHREvEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
962-1019 2.24e-06

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: 47.42  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 198278551  962 ESYFRAQILYVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 1019
Cdd:cd20427    36 DAWLRAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLAGLEP 93
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
152-291 4.96e-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: 47.93  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  152 VVIIHGATGSGKSTQ-LPQYVLDHYTQRSafcNIVVTQPRKIGASSIARWISKERswtlgglVGYQVGLEKIATEDTRLI 230
Cdd:cd17931     3 LTVLDLHPGAGKTTRvLPQIIREAIKKRL---RTLVLAPTRVVAAEMYEALRGLP-------IRYRTGAVKEEHGGNEIV 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198278551  231 -YMTTGVLLQKIVSAKSLMEFTHIFIDEVHerteemdFLLLVVRKLLRTNSRFVK-----VVLMSAT 291
Cdd:cd17931    73 dYMCHGTFTCRLLSPKRVPNYNLIIMDEAH-------FTDPASIAARGYIHTRVEmgeaaVIFMTAT 132
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
905-1010 1.83e-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: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  905 VTEVVEVGHFWgYRIDERNAE---LLKQLTAEINRLELVPLPIH-PHPDLVCLApftDYNKES-YFRAQILYVSGNSAEV 979
Cdd:cd20438    11 VEYVLNPSNFW-IRTDEYNNEfqaLMKNIADIYNLCGNDEELLKkPEPGLLCCA---RYSKDRhYYRAVITEVLDLKVSV 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 198278551  980 FFVDYGNRSHVDLDLLREIPCQFLELPFQAL 1010
Cdd:cd20438    87 YFLDFGNTDTVPFYDVKTLLPEFSELPALAM 117
Tudor_TDRD11 cd20433
Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, ...
924-1002 8.76e-05

Tudor domain found in Tudor domain-containing protein 11 (TDRD11) and similar proteins; TDRD11, also called Staphylococcal nuclease domain-containing protein 1 (SND1), 100 kDa coactivator, EBNA2 coactivator p100, or p100 co-activator, is a multifunctional protein that is reportedly associated with different types of RNA molecules, including mRNA, miRNA, pre-miRNA, and dsRNA. It has been implicated in a number of biological processes in eukaryotic cells, including the cell cycle, DNA damage repair, proliferation, and apoptosis. TDRD11 is overexpressed in multiple cancers and functions as an oncogene. It contains multiple Staphylococcal nuclease (SN) domains and 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: 410504 [Multi-domain]  Cd Length: 84  Bit Score: 42.29  E-value: 8.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  924 AELLKQLTAEINRLELVPLPIHPHPDLVCLAPFTDYNkeSYFRAQILYVSGNS-AEVFFVDYGNRSHVDLDLLREIPCQF 1002
Cdd:cd20433     6 EKLMEKLRFEIASNPPLPGSYTPRKGDLCAAKFVEDG--EWYRAKVEKVEGDKkVHVLYIDYGNREVLPSTRLAALPPAF 83
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
913-1042 2.61e-04

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: 42.49  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  913 HFWgYRIDERNAELLKQLTAEINRLELVPLPIHPHPDL--VCLAPFTDYNKesYFRAQILYVSGNSAEVFFVDYGNRSHV 990
Cdd:cd20426    13 YFW-CQFATEKIQCLAVKVQEAGEQVADRGNFIPSIYVgdPCIVKYSEDNH--WYRALVTKINDNLVSVRFVDYGNEEDV 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 198278551  991 DLDLLREIPCQFLELPFQALEFKICKMRPSAKSlicgehWSGGAHGRFAALV 1042
Cdd:cd20426    90 VREQVRALPSELLKIPVQAFPCCLSGFNLSEGL------WSDEANDYFYEIV 135
Tudor_TDRD15_rpt6 cd20441
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
949-1006 4.68e-04

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: 40.88  E-value: 4.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 198278551  949 DLVcLAPFTDYNkeSYFRAQIL-YVSGNSAEVFFVDYGNRSHVDLDLLREIPCQFLELP 1006
Cdd:cd20441    42 DLV-AAEYDEDL--ALYRAVITaVLPGKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
Tudor_TDRD3 cd20413
Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is ...
952-998 1.98e-03

Tudor domain found in Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In the nucleus, it acts as a coactivator; it recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In the cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 contains 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: 410484  Cd Length: 53  Bit Score: 37.71  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 198278551  952 CLAPFTDYNKesYFRAQI--LYVSGNSAEVFFVDYGNRSHVDLDLLREI 998
Cdd:cd20413     7 CLAKYWEDNK--FYRAEVtaVHPSGKTAVVKFMEYGNYEEVLLSDIKPI 53
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
905-1019 3.15e-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: 39.28  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278551  905 VTEVVEVGHFWGYRIDERNAELLKQLTAEinrLELVPLPIHPHPDL------VCLAPFT-DYNkesYFRAQILYVSGN-- 975
Cdd:cd20408     3 VTEFKNPGEFYIQIYTLEVLESLVKLTSQ---LKKTYASVNNHKEYipevgeVCVAKYSeDQN---WYRALVQTVDVQqk 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 198278551  976 SAEVFFVDYGNRSHVDLDLLREIPCQFLELPFQALEFKICKMRP 1019
Cdd:cd20408    77 KAGVFYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKP 120
 
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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