|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
132-315 |
1.10e-99 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350746 [Multi-domain] Cd Length: 180 Bit Score: 315.60 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160
|
170 180
....*....|....*....|....
gi 767979637 292 CKEFADYFAVPVqnkmNPAYIFEV 315
Cdd:cd17988 161 CKEFADYFTTPN----NPAYVFEV 180
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
130-681 |
3.82e-81 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 285.44 E-value: 3.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 130 PDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHyvQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:COG1643 8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 289
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 290 ISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHlleepviTKDIYEVAVSLIqmfDDLDMK 369
Cdd:COG1643 166 LDAERFARLL--------GDAPVIESSGRTYPVE---------VRYRPLPAD-------ERDLEDAVADAV---REALAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:COG1643 219 EPG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 450 SSVTVPDVKY-----------------------------------GRAGRVSRGYCYRLVHK-DFwdNSIPDHVVPEMLR 493
Cdd:COG1643 285 TSLTVPGIRYvidsglariprydprsgvtrlpterisqasanqraGRAGRLAPGICYRLWSEeDF--ARRPAFTDPEILR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 494 CPLGSTILKVKLLDMGEPRAL-LATALSPPGLSDIERtilLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQL 572
Cdd:COG1643 363 ADLASLILELAAWGLGDPEDLpFLDPPPARAIADARA---LLQELGAL-------DA---DGRLTPLGRALARLPLDPRL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 573 GKLIVLGHVFGCLDECLIIAAALSLKNffamPFRQhldgyrnkvnfsgSSKSDCIALVEAFKTWKACRQtgelrypkdel 652
Cdd:COG1643 430 ARMLLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQR----------- 481
|
570 580
....*....|....*....|....*....
gi 767979637 653 nwgrlNYIQIKRIREVAELYEELKTRISQ 681
Cdd:COG1643 482 -----EFLSYLRLREWRDLARQLRRLLGE 505
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
126-688 |
1.31e-65 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 244.58 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 126 TYKYPD-LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:PRK11131 66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 205 WTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 284
Cdd:PRK11131 144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 285 LMSATISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEEYYlndlehihhsklsphlleEPVITKDIYEVAVSLIQMFD 364
Cdd:PRK11131 223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVEVRY------------------RPIVEEADDTERDQLQAIFD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 365 DLDmkESGNKAwsgaqfvleRSSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSpvPGYRKIILS 444
Cdd:PRK11131 277 AVD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQS--HSGRRIVLA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 445 TNIAESSVTVPDVKY-----------------------------------GRAGRVSRGYCYRLV-HKDFwdNSIPDHVV 488
Cdd:PRK11131 344 TNVAETSLTVPGIKYvidpgtarisrysyrtkvqrlpiepisqasanqrkGRCGRVSEGICIRLYsEDDF--LSRPEFTD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 489 PEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPV 568
Cdd:PRK11131 422 PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 569 NQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF--RQHLDGYRNKVNfsgSSKSDCIALVeafKTW-------KAC 639
Cdd:PRK11131 495 DPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFV---NLWnylqeqqKAL 568
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 767979637 640 RQTGELRYPKDELnwgrLNYIqikRIREVAELYEELKTRISQFNMHVDS 688
Cdd:PRK11131 569 SSNQFRRLCRTDY----LNYL---RVREWQDIYTQLRQVVKELGIPVNS 610
|
|
| Tudor_TDRD9 |
cd20431 |
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ... |
870-970 |
4.31e-59 |
|
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410502 Cd Length: 101 Bit Score: 198.00 E-value: 4.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 870 TEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYG 949
Cdd:cd20431 1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80
|
90 100
....*....|....*....|.
gi 767979637 950 NKSHVDLHLLMEIPCQFLELP 970
Cdd:cd20431 81 NTSQVPSSLLREIPETLLTLP 101
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
132-595 |
9.40e-44 |
|
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: 172.26 E-value: 9.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVqrsAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPG---IGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:TIGR01970 78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 292 CKEfadyfavpVQNKMNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHLLEEPVITKDIYEVAVSliqmfddldmkES 371
Cdd:TIGR01970 158 GER--------LSSLLPDAPVVESEGRSFPVE---------IRYLPLRGDQRLEDAVSRAVEHALAS-----------ET 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 372 GnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESS 451
Cdd:TIGR01970 210 G--------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 452 VTVPDVKY-----------------------------------GRAGRVSRGYCYRLvhkdfWD----NSIPDHVVPEML 492
Cdd:TIGR01970 276 LTIEGIRVvidsglarvarfdpktgitrletvrisqasatqraGRAGRLEPGVCYRL-----WSeeqhQRLPAQDEPEIL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 493 RCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQL 572
Cdd:TIGR01970 351 QADLSGLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRL 418
|
490 500
....*....|....*....|...
gi 767979637 573 GKLIVLGHVFGCLDECLIIAAAL 595
Cdd:TIGR01970 419 AAMLLSAHSTGLAALACDLAALL 441
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
320-474 |
3.59e-40 |
|
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: 146.52 E-value: 3.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 320 HSVEEYYLNDLEHIHHSklsphllEEPVITKDIYEVAVSLIqmFDDLDMKESGnkawsgaqfvlersSVLVFLPGLGEIN 399
Cdd:cd18791 1 FPVEVYYLEDILELLGI-------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 400 YMHELLTSLVH----KRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKY---------------- 459
Cdd:cd18791 58 RLCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYvidsglvkekvydprt 137
|
170 180 190
....*....|....*....|....*....|....
gi 767979637 460 -------------------GRAGRVSRGYCYRLV 474
Cdd:cd18791 138 glsslvtvwiskasaeqraGRAGRTRPGKCYRLY 171
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
126-299 |
1.75e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.01 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 126 TYKYPDLPISRYKEEVVSLIESN-SVVIIHGATGSGKSTQLPQYILDHyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA-LKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 205 WTLGGVVGYQVG------LEKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTN 277
Cdd:smart00487 80 SLGLKVVGLYGGdskreqLRKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLP 158
|
170 180
....*....|....*....|....
gi 767979637 278 SRfVKVVLMSATISC--KEFADYF 299
Cdd:smart00487 159 KN-VQLLLLSATPPEeiENLLELF 181
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
531-629 |
5.97e-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: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 531 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF----- 605
Cdd:pfam04408 2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldpr 71
|
90 100 110
....*....|....*....|....*....|...
gi 767979637 606 --------RQHLDGYRNKVNFSGSS-KSDCIAL 629
Cdd:pfam04408 72 saakaarrRRRAADEKARAKFARLDlEGDHLTL 104
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
553-630 |
6.81e-16 |
|
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.
Pssm-ID: 214852 [Multi-domain] Cd Length: 82 Bit Score: 73.84 E-value: 6.81e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979637 553 DGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPFRQHLDGYRNKvnFSgSSKSDCIALV 630
Cdd:smart00847 8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRR--FA-DPESDHLTLL 82
|
|
| TUDOR |
pfam00567 |
Tudor domain; |
869-978 |
7.82e-14 |
|
Tudor domain;
Pssm-ID: 425754 [Multi-domain] Cd Length: 117 Bit Score: 69.31 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWgyRIDENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdKQRYFRAQVLY-VSGNSAEVFF 945
Cdd:pfam00567 7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82
|
90 100 110
....*....|....*....|....*....|...
gi 767979637 946 VDYGNKSHVDLHLLMEIPCQFLELPFQALEFKI 978
Cdd:pfam00567 83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
139-291 |
1.84e-10 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 61.10 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 139 EEVVSLIESNSVVIIHGATGSGKST--QLPqyILDHYVQRSAYCSIVVTQPRKIGASSIARWIsKERAWTLGGVVGYQVG 216
Cdd:pfam00270 5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 217 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:pfam00270 82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157
|
..
gi 767979637 290 IS 291
Cdd:pfam00270 158 LP 159
|
|
| TUDOR |
smart00333 |
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ... |
915-966 |
1.57e-05 |
|
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).
Pssm-ID: 197660 Cd Length: 57 Bit Score: 43.80 E-value: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767979637 915 VCLAPFADfdkQRYFRAQVLYVSGN-SAEVFFVDYGNKSHVDLHLLMEIPCQF 966
Cdd:smart00333 8 KVAARWED---GEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
147-471 |
9.48e-04 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 43.43 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 147 SNSVVIIHGATGSGKSTQLPQ------YILDHYVQRSAYCS------IVVTQPRKigasSIARWISKERAWTLG--GVVG 212
Cdd:PHA02653 178 SRKPVVLTGGTGVGKTSQVPKlllwfnYLFGGFDNLDKIDPnfierpIVLSLPRV----ALVRLHSITLLKSLGfdEIDG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 213 YQVGLE--KIATEDTRLIYMTTGVLL--QKIVSAKsLMEFTHIIIDEVHERTEEMDFLLLVVRKLLrtnSRFVKVVLMSA 288
Cdd:PHA02653 254 SPISLKygSIPDELINTNPKPYGLVFstHKLTLNK-LFDYGTVIIDEVHEHDQIGDIIIAVARKHI---DKIRSLFLMTA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 289 TIS-----CKEFADyfavpvqnkmNPAYIFEVEGKPHSVEEYYLNDlehIHHSKLSPHLLEEPVitKDIyevaVSLIQMF 363
Cdd:PHA02653 330 TLEddrdrIKEFFP----------NPAFVHIPGGTLFPISEVYVKN---KYNPKNKRAYIEEEK--KNI----VTALKKY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 364 ddldMKESGnkawsgaqfvlerSSVLVFLPGLGEINYMHELLTSLvHKRLQVYPLHSSV--ALEEQNNVFLSPVPgyrKI 441
Cdd:PHA02653 391 ----TPPKG-------------SSGIVFVASVSQCEEYKKYLEKR-LPIYDFYIIHGKVpnIDEILEKVYSSKNP---SI 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 442 ILSTNIAESSVTVPDVKY-----------------------------GRAGRVSRG-YCY 471
Cdd:PHA02653 450 IISTPYLESSVTIRNATHvydtgrvyvpepfggkemfisksmrtqrkGRVGRVSPGtYVY 509
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
132-315 |
1.10e-99 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350746 [Multi-domain] Cd Length: 180 Bit Score: 315.60 E-value: 1.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGKYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRHVKIILMSATIS 160
|
170 180
....*....|....*....|....
gi 767979637 292 CKEFADYFAVPVqnkmNPAYIFEV 315
Cdd:cd17988 161 CKEFADYFTTPN----NPAYVFEV 180
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
130-681 |
3.82e-81 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 285.44 E-value: 3.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 130 PDLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHyvQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:COG1643 8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLEL--GWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlllvvrkllrtnsrfvKVVLMSAT 289
Cdd:COG1643 86 TVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpalrpdlKLLVMSAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 290 ISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHlleepviTKDIYEVAVSLIqmfDDLDMK 369
Cdd:COG1643 166 LDAERFARLL--------GDAPVIESSGRTYPVE---------VRYRPLPAD-------ERDLEDAVADAV---REALAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:COG1643 219 EPG--------------DILVFLPGEREIRRTAEALRGRLPPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 450 SSVTVPDVKY-----------------------------------GRAGRVSRGYCYRLVHK-DFwdNSIPDHVVPEMLR 493
Cdd:COG1643 285 TSLTVPGIRYvidsglariprydprsgvtrlpterisqasanqraGRAGRLAPGICYRLWSEeDF--ARRPAFTDPEILR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 494 CPLGSTILKVKLLDMGEPRAL-LATALSPPGLSDIERtilLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQL 572
Cdd:COG1643 363 ADLASLILELAAWGLGDPEDLpFLDPPPARAIADARA---LLQELGAL-------DA---DGRLTPLGRALARLPLDPRL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 573 GKLIVLGHVFGCLDECLIIAAALSLKNffamPFRQhldgyrnkvnfsgSSKSDCIALVEAFKTWKACRQtgelrypkdel 652
Cdd:COG1643 430 ARMLLAAAELGCLREAAILAALLSERD----PRRG-------------AAGSDLLARLNLWRRLREQQR----------- 481
|
570 580
....*....|....*....|....*....
gi 767979637 653 nwgrlNYIQIKRIREVAELYEELKTRISQ 681
Cdd:COG1643 482 -----EFLSYLRLREWRDLARQLRRLLGE 505
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
126-688 |
1.31e-65 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 244.58 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 126 TYKYPD-LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:PRK11131 66 EITYPEnLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGLIGHTQPRRLAARTVANRIAEELE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 205 WTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVV 284
Cdd:PRK11131 144 TELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD-LKVI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 285 LMSATISCKEFADYFavpvqnkmNPAYIFEVEGKPHSVEEYYlndlehihhsklsphlleEPVITKDIYEVAVSLIQMFD 364
Cdd:PRK11131 223 ITSATIDPERFSRHF--------NNAPIIEVSGRTYPVEVRY------------------RPIVEEADDTERDQLQAIFD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 365 DLDmkESGNKAwsgaqfvleRSSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSpvPGYRKIILS 444
Cdd:PRK11131 277 AVD--ELGREG---------PGDILIFMSGEREIRDTADALNKLNLRHTEILPLYARLSNSEQNRVFQS--HSGRRIVLA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 445 TNIAESSVTVPDVKY-----------------------------------GRAGRVSRGYCYRLV-HKDFwdNSIPDHVV 488
Cdd:PRK11131 344 TNVAETSLTVPGIKYvidpgtarisrysyrtkvqrlpiepisqasanqrkGRCGRVSEGICIRLYsEDDF--LSRPEFTD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 489 PEMLRCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALavsgqREDENPHDGELTFLGRVLAQLPV 568
Cdd:PRK11131 422 PEILRTNLASVILQMTALGLGDIAAF--PFVEAPDKRNIQDGVRLLEELGAI-----TTDEQASAYKLTPLGRQLAQLPV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 569 NQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF--RQHLDGYRNKVNfsgSSKSDCIALVeafKTW-------KAC 639
Cdd:PRK11131 495 DPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMdkQQASDEKHRRFA---DKESDFLAFV---NLWnylqeqqKAL 568
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 767979637 640 RQTGELRYPKDELnwgrLNYIqikRIREVAELYEELKTRISQFNMHVDS 688
Cdd:PRK11131 569 SSNQFRRLCRTDY----LNYL---RVREWQDIYTQLRQVVKELGIPVNS 610
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
148-299 |
5.55e-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: 5.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 148 NSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVVGYQVGLEKIATEDTRL 227
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979637 228 IYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATISCKEFADYF 299
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDL-KVILMSATLDAEKFSSYF 151
|
|
| Tudor_TDRD9 |
cd20431 |
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ... |
870-970 |
4.31e-59 |
|
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410502 Cd Length: 101 Bit Score: 198.00 E-value: 4.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 870 TEVVEVGHFWGYRIDENNSEILKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKQRYFRAQVLYVSGNSAEVFFVDYG 949
Cdd:cd20431 1 TEVVEVGHFWGYRIDENSSEILQQLTAEINQRQLVPLTTKPVPNLLCLAPFTDADMKKYYRAKILYVSGSSAEVFFVDYG 80
|
90 100
....*....|....*....|.
gi 767979637 950 NKSHVDLHLLMEIPCQFLELP 970
Cdd:cd20431 81 NTSQVPSSLLREIPETLLTLP 101
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
132-595 |
9.40e-44 |
|
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: 172.26 E-value: 9.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVqrsAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLDAPG---IGGKIIMLEPRRLAARSAAQRLASQLGEAVGQTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:TIGR01970 78 GYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSLREDLKILAMSATLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 292 CKEfadyfavpVQNKMNPAYIFEVEGKPHSVEeyylndlehIHHSKLSPHLLEEPVITKDIYEVAVSliqmfddldmkES 371
Cdd:TIGR01970 158 GER--------LSSLLPDAPVVESEGRSFPVE---------IRYLPLRGDQRLEDAVSRAVEHALAS-----------ET 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 372 GnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESS 451
Cdd:TIGR01970 210 G--------------SILVFLPGQAEIRRVQEQLAERLDSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 452 VTVPDVKY-----------------------------------GRAGRVSRGYCYRLvhkdfWD----NSIPDHVVPEML 492
Cdd:TIGR01970 276 LTIEGIRVvidsglarvarfdpktgitrletvrisqasatqraGRAGRLEPGVCYRL-----WSeeqhQRLPAQDEPEIL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 493 RCPLGSTILKVKLLDMGEPRALlaTALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQL 572
Cdd:TIGR01970 351 QADLSGLALELAQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDAQGR----------LTAHGKAMAALGCHPRL 418
|
490 500
....*....|....*....|...
gi 767979637 573 GKLIVLGHVFGCLDECLIIAAAL 595
Cdd:TIGR01970 419 AAMLLSAHSTGLAALACDLAALL 441
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
132-299 |
1.78e-43 |
|
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350743 [Multi-domain] Cd Length: 177 Bit Score: 156.15 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRS--AYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPplPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD-LKVILMSAT 159
|
170
....*....|
gi 767979637 290 ISCKEFADYF 299
Cdd:cd17985 160 LNAELFSDYF 169
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
132-299 |
3.88e-42 |
|
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350739 [Multi-domain] Cd Length: 180 Bit Score: 152.69 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQR--SAYCSIVVTQPRKIGASSIARWISKERA--WTL 207
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERgkGSSCRIVCTQPRRISAISVAERVAAERAesCGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 208 GGVVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLM 286
Cdd:cd17981 81 GNSTGYQIRLEsRKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDV-LMGIVKDLLPFRSDLKVILM 159
|
170
....*....|...
gi 767979637 287 SATISCKEFADYF 299
Cdd:cd17981 160 SATLNAEKFSDYF 172
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
132-299 |
4.26e-41 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350730 [Multi-domain] Cd Length: 234 Bit Score: 151.53 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQ--RSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17972 59 LPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQndRAAECNIVVTQPRRISAVSVAERVAFERGEEVGK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 210 VVGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAksLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTnSRFVKVVLMSA 288
Cdd:cd17972 139 SCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTDFLLVVLRDVVQA-YPDLRVILMSA 215
|
170
....*....|.
gi 767979637 289 TISCKEFADYF 299
Cdd:cd17972 216 TIDTSMFCEYF 226
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
132-299 |
6.24e-41 |
|
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350734 [Multi-domain] Cd Length: 178 Bit Score: 148.79 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYV--QRSAYCSIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVlrGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 210 VVGYQVGLE-KIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSA 288
Cdd:cd17976 81 NVGYQVRLEsRPPPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE-LRVVLMSA 159
|
170
....*....|.
gi 767979637 289 TISCKEFADYF 299
Cdd:cd17976 160 TGDNQRLSRYF 170
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
320-474 |
3.59e-40 |
|
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: 146.52 E-value: 3.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 320 HSVEEYYLNDLEHIHHSklsphllEEPVITKDIYEVAVSLIqmFDDLDMKESGnkawsgaqfvlersSVLVFLPGLGEIN 399
Cdd:cd18791 1 FPVEVYYLEDILELLGI-------SSEKEDPDYVDAAVRLI--LQIHRTEEPG--------------DILVFLPGQEEIE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 400 YMHELLTSLVH----KRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKY---------------- 459
Cdd:cd18791 58 RLCELLREELLspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYvidsglvkekvydprt 137
|
170 180 190
....*....|....*....|....*....|....
gi 767979637 460 -------------------GRAGRVSRGYCYRLV 474
Cdd:cd18791 138 glsslvtvwiskasaeqraGRAGRTRPGKCYRLY 171
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
132-303 |
5.25e-39 |
|
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438710 [Multi-domain] Cd Length: 178 Bit Score: 143.26 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYcsIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM--IGITQPRRVAAVSVAKRVAEEMGVELGQLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRF----VKVVLMS 287
Cdd:cd17978 79 GYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQklspLKVIIMS 158
|
170
....*....|....*..
gi 767979637 288 ATISCKEFADYFA-VPV 303
Cdd:cd17978 159 ATLDADLFSEYFNgAPV 175
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
132-300 |
9.16e-39 |
|
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: 143.13 E-value: 9.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYV---QRSAYCSIVVTQPRKIGASSIARWISKERAWTLG 208
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlngGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 209 -----GVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKV 283
Cdd:cd17975 81 pggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSD-LHL 159
|
170
....*....|....*..
gi 767979637 284 VLMSATISCKEFADYFA 300
Cdd:cd17975 160 ILMSATVDCEKFSSYFT 176
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
132-299 |
1.37e-37 |
|
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350745 [Multi-domain] Cd Length: 176 Bit Score: 139.19 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKS-LMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATI 290
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSaLSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPN-LKLILSSAAL 159
|
....*....
gi 767979637 291 SCKEFADYF 299
Cdd:cd17987 160 DVNLFIRYF 168
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
132-300 |
1.09e-36 |
|
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350737 [Multi-domain] Cd Length: 170 Bit Score: 136.42 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-----AGFRHIACTQPRRIACISLAKRVAFESLNQYGSKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLMSATIS 291
Cdd:cd17979 76 AYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD-LKLILMSATIN 154
|
....*....
gi 767979637 292 CKEFADYFA 300
Cdd:cd17979 155 IELFSGYFE 163
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
132-299 |
8.07e-35 |
|
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350742 [Multi-domain] Cd Length: 178 Bit Score: 131.52 E-value: 8.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAycSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHG--MIGVTQPRRVAAISVAQRVAEEMKCTLGSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSR----FVKVVLMS 287
Cdd:cd17984 79 GYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnrkeHLKVVVMS 158
|
170
....*....|..
gi 767979637 288 ATISCKEFADYF 299
Cdd:cd17984 159 ATLELAKLSAFF 170
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
132-595 |
3.19e-33 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 139.29 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILdhyvQRSAYCS-IVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:PRK11664 4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPLQLL----QHGGINGkIIMLEPRRLAARNVAQRLAEQLGEKPGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATI 290
Cdd:PRK11664 80 VGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGLRDDLKLLIMSATL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 291 sckefaDYFAvpVQNKMNPAYIFEVEGKPHSVEEYYLndlehihhsKLSPHL-LEEpvitkdiyEVAVSLIQMFDdldmK 369
Cdd:PRK11664 160 ------DNDR--LQQLLPDAPVIVSEGRSFPVERRYQ---------PLPAHQrFDE--------AVARATAELLR----Q 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 370 ESGnkawsgaqfvlersSVLVFLPGLGEINYMHELLTSLVHKRLQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAE 449
Cdd:PRK11664 211 ESG--------------SLLLFLPGVGEIQRVQEQLASRVASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 450 SSVTVP----------------DVKY-------------------GRAGRVSRGYCYRLVHKDFWDNSiPDHVVPEMLRC 494
Cdd:PRK11664 277 TSLTIEgirlvvdsglervarfDPKTgltrlvtqrisqasmtqraGRAGRLEPGICLHLYSKEQAERA-AAQSEPEILHS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 495 PLGSTILkvKLLDMGEPRALLATALSPPGLSDIERTILLLKEVGALAVSGQredenphdgeLTFLGRVLAQLPVNQQLGK 574
Cdd:PRK11664 356 DLSGLLL--ELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQLGALDGQGR----------LTARGRKMAALGNDPRLAA 423
|
490 500
....*....|....*....|.
gi 767979637 575 LIVLGHVFGclDECLIIAAAL 595
Cdd:PRK11664 424 MLVAAKEDD--EAALATAAKL 442
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
131-299 |
3.63e-33 |
|
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438709 [Multi-domain] Cd Length: 187 Bit Score: 127.15 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 131 DLPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:cd17973 12 ELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKKLVACTQPRRVAAMSVAQRVAEEMDVKLGEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFlLLVVRKLLRTNSRFVKVVLMSATI 290
Cdd:cd17973 92 VGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDI-LMGLLKEVVRRRPDLKLIVMSATL 170
|
....*....
gi 767979637 291 SCKEFADYF 299
Cdd:cd17973 171 DAGKFQKYF 179
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
132-315 |
7.10e-33 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350747 [Multi-domain] Cd Length: 173 Bit Score: 125.65 E-value: 7.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE--LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRtNSRFVKVVLMSATIS 291
Cdd:cd17989 79 GYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLP-RRPDLKVIITSATID 157
|
170 180
....*....|....*....|....
gi 767979637 292 CKEFADYFavpvqnkmNPAYIFEV 315
Cdd:cd17989 158 AERFSRHF--------NNAPIIEV 173
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
132-303 |
1.91e-32 |
|
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350741 [Multi-domain] Cd Length: 173 Bit Score: 124.50 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYIL-DHYvqrSAYCSIVVTQPRKIGASSIARWISKERAWTLGGV 210
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHeDGY---TDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 211 VGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATI 290
Cdd:cd17983 78 VGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDL-KLIVTSATM 156
|
170
....*....|....
gi 767979637 291 SCKEFADYFA-VPV 303
Cdd:cd17983 157 DADKFADFFGnVPI 170
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
132-299 |
2.51e-31 |
|
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350732 [Multi-domain] Cd Length: 174 Bit Score: 121.46 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS----IVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHE-----AGYTKgggkIGCTQPRRVAAMSVAARVAEEMGVKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 208 GGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLlrtnSRF---VKVV 284
Cdd:cd17974 76 GNEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDI----ARFrpdLKLL 151
|
170
....*....|....*
gi 767979637 285 LMSATISCKEFADYF 299
Cdd:cd17974 152 ISSATMDAEKFSAFF 166
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
132-302 |
3.72e-30 |
|
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350740 [Multi-domain] Cd Length: 191 Bit Score: 118.61 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS--------IVVTQPRKIGASSIARWISKER 203
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYE-----AGFGSpesdnpgmIGITQPRRVAAVSMAKRVAEEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 204 AwTLGGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDF---------LLLVVRKLL 274
Cdd:cd17982 76 N-VFGKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDIligmlsrivPLRAKLYLQ 154
|
170 180 190
....*....|....*....|....*....|.
gi 767979637 275 RTNSRFVKVVLMSATISCKEFAD---YFAVP 302
Cdd:cd17982 155 DQTVKPLKLVIMSATLRVEDFTEnklLFPRP 185
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
132-299 |
7.66e-27 |
|
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350729 [Multi-domain] Cd Length: 179 Bit Score: 108.72 E-value: 7.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyVQRSAYCSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17971 6 LPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAE--AGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLGQEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFvKVVLMSATIS 291
Cdd:cd17971 84 GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDL-KLIVTSATLD 162
|
....*...
gi 767979637 292 CKEFADYF 299
Cdd:cd17971 163 AVKFSQYF 170
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
132-308 |
1.52e-26 |
|
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350738 [Multi-domain] Cd Length: 185 Bit Score: 107.94 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDhyvqrSAYCS----IVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAE-----AGWTAggrvVGCTQPRRVAAVTVAGRVAEEMGAVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 208 GGVVGYQVGLEKIATED-TRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRfVKVVLM 286
Cdd:cd17980 76 GHEVGYCIRFDDCTDPQaTRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD-LRLIVA 154
|
170 180
....*....|....*....|..
gi 767979637 287 SATISCKEFADYFAvpvQNKMN 308
Cdd:cd17980 155 SATLDAEKFRDFFN---QNETN 173
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
132-300 |
2.06e-26 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 107.03 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQYILDHYVQRSAycSIVVTQPRKIGASSIARWISKERAWTLGGVV 211
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGG--KIIVLEPRRVAARAAARRLATLLGEAPGETV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 212 GYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSATIS 291
Cdd:cd17990 79 GYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLLRDDLRLLAMSATLD 158
|
....*....
gi 767979637 292 CKEFADYFA 300
Cdd:cd17990 159 GDGLAALLP 167
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
126-299 |
1.75e-20 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 91.01 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 126 TYKYPDLPISRYKEEVVSLIESN-SVVIIHGATGSGKSTQLPQYILDHyVQRSAYCSIVVTQPRKIGASSIARWISKERA 204
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA-LKRGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 205 WTLGGVVGYQVG------LEKIATEDTRLIYMTTGVLLQKIVS-AKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTN 277
Cdd:smart00487 80 SLGLKVVGLYGGdskreqLRKLESGKTDILVTTPGRLLDLLENdKLSLSNVDLVILDEAH-RLLDGGFGDQLEKLLKLLP 158
|
170 180
....*....|....*....|....
gi 767979637 278 SRfVKVVLMSATISC--KEFADYF 299
Cdd:smart00487 159 KN-VQLLLLSATPPEeiENLLELF 181
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
531-629 |
5.97e-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: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 531 ILLLKEVGALavsgqreDEnphDGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPF----- 605
Cdd:pfam04408 2 LELLYYLGAL-------DE---DGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNfldpr 71
|
90 100 110
....*....|....*....|....*....|...
gi 767979637 606 --------RQHLDGYRNKVNFSGSS-KSDCIAL 629
Cdd:pfam04408 72 saakaarrRRRAADEKARAKFARLDlEGDHLTL 104
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
553-630 |
6.81e-16 |
|
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.
Pssm-ID: 214852 [Multi-domain] Cd Length: 82 Bit Score: 73.84 E-value: 6.81e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979637 553 DGELTFLGRVLAQLPVNQQLGKLIVLGHVFGCLDECLIIAAALSLKNFFAMPFRQHLDGYRNKvnFSgSSKSDCIALV 630
Cdd:smart00847 8 DGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRPKEKREDADAARRR--FA-DPESDHLTLL 82
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
132-264 |
2.21e-15 |
|
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350744 [Multi-domain] Cd Length: 177 Bit Score: 75.70 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNS-VVIIHGATGSGKSTQLPQYILDHYVQRSAYC-SIVVTQPRKIGASSIARWISKERAWTLGG 209
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKgQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767979637 210 VVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMD 264
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASD 135
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
132-303 |
1.90e-14 |
|
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350735 [Multi-domain] Cd Length: 176 Bit Score: 72.94 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 132 LPISRYKEEVVSLIESNSVVIIHGATGSGKSTQLPQ----YILDHYVQRSAycsIVVTQPRKIGASSIARWISKERAWTL 207
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV---VVCTQVHKQTAVWLALRVADEMDVNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 208 GGVVGYQVGLEKIATEDTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMS 287
Cdd:cd17977 78 GHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITC 157
|
170
....*....|....*.
gi 767979637 288 ATISCKEFADYFAVPV 303
Cdd:cd17977 158 PHLSSKLLSYYGNVPL 173
|
|
| Tudor_TDRD6_rpt3 |
cd20422 |
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ... |
869-1002 |
4.17e-14 |
|
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410493 Cd Length: 135 Bit Score: 70.62 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWgYRIDENN---SEILKKLTAEINQLT-LVPLPTHPHPDLVCLAPFADfdkQRYFRAQVLYVSGNSAEVF 944
Cdd:cd20422 6 VEFVKDPSEFW-IRLGEHAvpfSKLMRSMTAFYSQASkLDGVVLKPQPGQLCCAKWKE---DRYYRAIVTAVKGKMVEVF 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767979637 945 FVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPsakslvCGKHWSDGASQWF 1002
Cdd:cd20422 82 LVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICP------LGERWSPEAISAF 133
|
|
| TUDOR |
pfam00567 |
Tudor domain; |
869-978 |
7.82e-14 |
|
Tudor domain;
Pssm-ID: 425754 [Multi-domain] Cd Length: 117 Bit Score: 69.31 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWgyRIDENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdKQRYFRAQVLY-VSGNSAEVFF 945
Cdd:pfam00567 7 VSHIESPSTFY--IQPKSDSKKLEKLTEELQEYyaSKPPESLPPAVGDGCVAAFSE--DGKWYRAKITEsLDDGLVEVLF 82
|
90 100 110
....*....|....*....|....*....|...
gi 767979637 946 VDYGNKSHVDLHLLMEIPCQFLELPFQALEFKI 978
Cdd:pfam00567 83 IDYGNTETVPLSDLRPLPPELESLPPQAIKCQL 115
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
139-291 |
1.84e-10 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 61.10 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 139 EEVVSLIESNSVVIIHGATGSGKST--QLPqyILDHYVQRSAYCSIVVTQPRKIGASSIARWIsKERAWTLGGVVGYQVG 216
Cdd:pfam00270 5 AEAIPAILEGRDVLVQAPTGSGKTLafLLP--ALEALDKLDNGPQALVLAPTRELAEQIYEEL-KKLGKGLGLKVASLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 217 -------LEKIATedTRLIYMTTGVLLQKIVSAKSLMEFTHIIIDEVHeRTEEMDFLLLVVRKLLRTNSRfVKVVLMSAT 289
Cdd:pfam00270 82 gdsrkeqLEKLKG--PDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKK-RQILLLSAT 157
|
..
gi 767979637 290 IS 291
Cdd:pfam00270 158 LP 159
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
148-289 |
6.70e-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: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 148 NSVVIIHGATGSGKSTQLPQYILDHYVQRSayCSIVVTQPRKIGASSIARWISKERAWtlGGVVGYQVG------LEKIA 221
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALQTAERLRELFGP--GIRVAVLVGgssaeeREKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 222 TEDTRLIYMTTGVLLQKIVSAK--SLMEFTHIIIDEVHERTEEMDFLLLVVRKLLRTNSRFVKVVLMSAT 289
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| Tudor_TDRD6_rpt5 |
cd20424 |
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ... |
885-978 |
4.04e-09 |
|
fifth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410495 Cd Length: 126 Bit Score: 55.97 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 885 ENNSEILKKLTAEINQL--TLVPLPTHPHPDLVCLAPFADfdkQRYFRAQVLYVSgNSAEVFFVDYGNKSHVDLHLLMEI 962
Cdd:cd20424 32 ARNAGVLDQLASAISRLssEIRKLELSVNPGTLCLAKYSD---QHWYRGIIITNK-NSTEVFFVDYGNTEKVEKEDMLPI 107
|
90
....*....|....*....
gi 767979637 963 P---CQFLELPFQALEFKI 978
Cdd:cd20424 108 PsdaYELLLLPMQAIKCSL 126
|
|
| Tudor_TDRD1_rpt4 |
cd20411 |
fourth Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ... |
869-981 |
2.60e-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: 53.22 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWGYRIDEN-NSEILKKLTAEINQL---TLVPLPTHPHPDLVCLAPFADfDKQRYfRAQVLYVSGNSAEVF 944
Cdd:cd20411 3 VLEVISPDLFYALPKTGQvNVEKLKALMTELAEYcskQSVPQQFRPRIGDACCARFTG-DKNWY-RAVVLETSDSEVKVL 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 767979637 945 FVDYGNKSHVDLHLLMEIPCQFLELPFQALefkICKM 981
Cdd:cd20411 81 YADYGNTETLPLSRILPITKSHLELPFQII---RCSL 114
|
|
| Tudor_TDRD2 |
cd20412 |
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ... |
913-975 |
3.22e-08 |
|
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410483 Cd Length: 95 Bit Score: 52.30 E-value: 3.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767979637 913 DLVClAPFADFDkqRYFRAQVLYVSGNS-AEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 975
Cdd:cd20412 33 DIVA-APFRHDG--SWYRARVLGFLENGnLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIE 93
|
|
| Tudor_TDRD15_rpt5 |
cd20440 |
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ... |
869-976 |
4.90e-08 |
|
fifth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410511 Cd Length: 127 Bit Score: 52.84 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWgYRIDENNsEILKKLTAEINQLtlVPLPTHPHPDL----VCLAPFadFDKQRYFRAQVLYVSGNS-AEV 943
Cdd:cd20440 16 ITHVYSPAKFY-CQLDRNT-EILEALMEKIAEI--SKLFNSQILDNcktrLCLAKY--FEDGQWYRALAHPVESSShLSV 89
|
90 100 110
....*....|....*....|....*....|....*.
gi 767979637 944 FFVDYGNKSHVDLHLLMEIPCQFLEL---PFQALEF 976
Cdd:cd20440 90 YFVDYGNKQIVEKNEVLPIPDTAVDLlltPMQAIKC 125
|
|
| Tudor_AKAP1 |
cd20407 |
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ... |
906-975 |
5.39e-08 |
|
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410478 Cd Length: 76 Bit Score: 51.05 E-value: 5.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979637 906 LPTHPHPDLVCLAPFADfdkqRYFRAQVLYVSG--NSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 975
Cdd:cd20407 1 LPEPIEVGVICAAPVMN----AWYRAQVVGVFEetDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATE 68
|
|
| Tudor_TDRD12_rpt2 |
cd20435 |
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ... |
928-983 |
6.03e-08 |
|
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410506 Cd Length: 134 Bit Score: 53.02 E-value: 6.03e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979637 928 YFRAQVLYVSGNS-------AEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 983
Cdd:cd20435 65 YHRVKVLEITEKDdktkpreVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKP 127
|
|
| Tudor_TDRD4_rpt5 |
cd20418 |
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ... |
912-988 |
1.74e-07 |
|
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410489 Cd Length: 105 Bit Score: 50.87 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 912 PDLVCLAPFADfdkQRYFRAQVLYVSG-NSAEVF--FVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPSAKSL 988
Cdd:cd20418 6 PEMPCLAEYSD---GKWYRAKLLSILEfNPVKILvrHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPLNDS 82
|
|
| Tudor_dTUD-like |
cd20379 |
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ... |
912-962 |
3.04e-07 |
|
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410450 Cd Length: 50 Bit Score: 48.28 E-value: 3.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767979637 912 PDLVCLAPFADFDKqrYFRAQVLYV-SGNSAEVFFVDYGNKSHVDLHLLMEI 962
Cdd:cd20379 1 VGDLCAAKYEEDGK--WYRARVLEVlSNDKVEVFFVDYGNTETVPLSDLRPL 50
|
|
| Tudor_TDRD15_rpt4 |
cd20439 |
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ... |
866-979 |
1.24e-06 |
|
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410510 Cd Length: 125 Bit Score: 49.03 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 866 TIDV--TEVVEVGHFWgYRIDENNSEiLKKLTAEINQLTLVPLPTHPHPDLVCLAPFADFDKqrYFRAQVL-YVSGNSAE 942
Cdd:cd20439 11 VVDVkcSYVNSPGDFW-CQLQTKSSE-LKSLMKQIQSYYLIHNDPYKHGQIACVAKYSKDGK--WYRAAVLkQVSAKEVD 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 767979637 943 VFFVDYGNKSHVDLHLLMEIPCQFLELPFQAleFKIC 979
Cdd:cd20439 87 VIFVDYGNQERVLISDLRAIKPQFLLLEGQA--FRCS 121
|
|
| Tudor_TDRD1_rpt2 |
cd20409 |
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ... |
889-967 |
3.82e-06 |
|
second Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410480 Cd Length: 82 Bit Score: 46.29 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 889 EILKKLTAEINQLTLVPLpTHPHPDLVCLAPFADfDKQRYfRAQVL-YVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFL 967
Cdd:cd20409 6 ELQESLSAYCKVAPASSD-FSPAVGEVCCAQFTE-DNQWY-RASVLaYSSEDSVLVGYIDFGNSEEVALSRLRPIPPSLL 82
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
150-289 |
5.84e-06 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 47.54 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 150 VVIIHGATGSGKSTQ-LPQYILDHYVQRSaycSIVVTQPRKIGASSIARWISKERawtlggvVGYQVGLEKIATEDTRLI 228
Cdd:cd17931 3 LTVLDLHPGAGKTTRvLPQIIREAIKKRL---RTLVLAPTRVVAAEMYEALRGLP-------IRYRTGAVKEEHGGNEIV 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979637 229 -YMTTGVLLQKIVSAKSLMEFTHIIIDEVHerteemdFLLLVVRKLLRTNSRFVK-----VVLMSAT 289
Cdd:cd17931 73 dYMCHGTFTCRLLSPKRVPNYNLIIMDEAH-------FTDPASIAARGYIHTRVEmgeaaVIFMTAT 132
|
|
| TUDOR |
smart00333 |
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ... |
915-966 |
1.57e-05 |
|
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).
Pssm-ID: 197660 Cd Length: 57 Bit Score: 43.80 E-value: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767979637 915 VCLAPFADfdkQRYFRAQVLYVSGN-SAEVFFVDYGNKSHVDLHLLMEIPCQF 966
Cdd:smart00333 8 KVAARWED---GEWYRARIVKVDGEqLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
|
|
| Tudor_TDRD15_rpt3 |
cd20438 |
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ... |
869-974 |
1.98e-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: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWgYRIDENNSE---ILKKLTAEINQLTLVP-LPTHPHPDLVCLAPFADfdKQRYFRAQVLYVSGNSAEVF 944
Cdd:cd20438 11 VEYVLNPSNFW-IRTDEYNNEfqaLMKNIADIYNLCGNDEeLLKKPEPGLLCCARYSK--DRHYYRAVITEVLDLKVSVY 87
|
90 100 110
....*....|....*....|....*....|
gi 767979637 945 FVDYGNKSHVDLHLLMEIPCQFLELPFQAL 974
Cdd:cd20438 88 FLDFGNTDTVPFYDVKTLLPEFSELPALAM 117
|
|
| Tudor_TDRD7_rpt1 |
cd20427 |
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ... |
930-983 |
3.51e-05 |
|
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410498 Cd Length: 98 Bit Score: 43.96 E-value: 3.51e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767979637 930 RAQVLYVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 983
Cdd:cd20427 40 RAQVIEVEEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLAGLEP 93
|
|
| Tudor_TDRD6_rpt4 |
cd20423 |
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ... |
909-975 |
4.25e-05 |
|
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410494 Cd Length: 80 Bit Score: 43.24 E-value: 4.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979637 909 HPHPDLVCLAPFADFDKqrYFRAQVLYVSGN--SAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALE 975
Cdd:cd20423 2 HSLPNPVCLAKYSEDGK--WCRALIDNVYEPveMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFR 68
|
|
| Tudor_TDRD6_rpt7 |
cd20426 |
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ... |
924-1007 |
4.70e-05 |
|
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410497 Cd Length: 140 Bit Score: 44.80 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 924 DKQRYFRAQVLYVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELPFQAleFKICKmrpSAKSLVCGkHWSDGASQWFA 1003
Cdd:cd20426 59 EDNHWYRALVTKINDNLVSVRFVDYGNEEDVVREQVRALPSELLKIPVQA--FPCCL---SGFNLSEG-LWSDEANDYFY 132
|
....
gi 767979637 1004 SLVS 1007
Cdd:cd20426 133 EIVT 136
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
400-464 |
6.88e-05 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 42.58 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 400 YMHELLTSLVHKrlqVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKY-----------------GRA 462
Cdd:smart00490 2 ELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLviiydlpwspasyiqriGRA 78
|
..
gi 767979637 463 GR 464
Cdd:smart00490 79 GR 80
|
|
| Tudor_TDRD4_rpt2 |
cd20415 |
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ... |
910-983 |
2.11e-04 |
|
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410486 Cd Length: 96 Bit Score: 41.65 E-value: 2.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767979637 910 PHPDLVCLAPFADfdkQRYFRAQVLYVSGNSA-EVFFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRP 983
Cdd:cd20415 25 PVQGQACVALFED---GAWYRARIIGLPGHREvEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
|
|
| Tudor_TDRD1_rpt3 |
cd20410 |
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ... |
910-967 |
4.83e-04 |
|
third Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410481 [Multi-domain] Cd Length: 59 Bit Score: 39.63 E-value: 4.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979637 910 PHPDLVCLAPFADfdKQRYFRAQVLYV-SGNSAEVFFVDYGNKSHVDLHLLMEIPCQFL 967
Cdd:cd20410 3 PIVGEPCCAFFSG--DGNWYRAMVKEIlPGGAVKVHFVDYGNVEEVTLDKLRKITSTFL 59
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
388-465 |
7.13e-04 |
|
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: 40.66 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 388 VLVFLpglgeiNYMHELLTSLVHKR--LQVYPLHSSVALEEQNNVFLSPVPGYRKIILSTNIAESSVTVPDVKY------ 459
Cdd:pfam00271 18 VLIFS------QTKKTLEAELLLEKegIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLvinydl 91
|
90
....*....|....*..
gi 767979637 460 -----------GRAGRV 465
Cdd:pfam00271 92 pwnpasyiqriGRAGRA 108
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
147-471 |
9.48e-04 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 43.43 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 147 SNSVVIIHGATGSGKSTQLPQ------YILDHYVQRSAYCS------IVVTQPRKigasSIARWISKERAWTLG--GVVG 212
Cdd:PHA02653 178 SRKPVVLTGGTGVGKTSQVPKlllwfnYLFGGFDNLDKIDPnfierpIVLSLPRV----ALVRLHSITLLKSLGfdEIDG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 213 YQVGLE--KIATEDTRLIYMTTGVLL--QKIVSAKsLMEFTHIIIDEVHERTEEMDFLLLVVRKLLrtnSRFVKVVLMSA 288
Cdd:PHA02653 254 SPISLKygSIPDELINTNPKPYGLVFstHKLTLNK-LFDYGTVIIDEVHEHDQIGDIIIAVARKHI---DKIRSLFLMTA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 289 TIS-----CKEFADyfavpvqnkmNPAYIFEVEGKPHSVEEYYLNDlehIHHSKLSPHLLEEPVitKDIyevaVSLIQMF 363
Cdd:PHA02653 330 TLEddrdrIKEFFP----------NPAFVHIPGGTLFPISEVYVKN---KYNPKNKRAYIEEEK--KNI----VTALKKY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 364 ddldMKESGnkawsgaqfvlerSSVLVFLPGLGEINYMHELLTSLvHKRLQVYPLHSSV--ALEEQNNVFLSPVPgyrKI 441
Cdd:PHA02653 391 ----TPPKG-------------SSGIVFVASVSQCEEYKKYLEKR-LPIYDFYIIHGKVpnIDEILEKVYSSKNP---SI 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 442 ILSTNIAESSVTVPDVKY-----------------------------GRAGRVSRG-YCY 471
Cdd:PHA02653 450 IISTPYLESSVTIRNATHvydtgrvyvpepfggkemfisksmrtqrkGRVGRVSPGtYVY 509
|
|
| Tudor_TDRD15_rpt6 |
cd20441 |
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ... |
929-970 |
2.15e-03 |
|
sixth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the sixth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410512 Cd Length: 108 Bit Score: 38.95 E-value: 2.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767979637 929 FRAQVL-YVSGNSAEVFFVDYGNKSHVDLHLLMEIPCQFLELP 970
Cdd:cd20441 55 YRAVITaVLPGKSFKVEFIDYGNTAVVDKSNIYTLQEKFLSLP 97
|
|
| Tudor_TDRD1_rpt1 |
cd20408 |
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ... |
869-996 |
8.47e-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: 38.12 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979637 869 VTEVVEVGHFWGYRIDENNSEILKKLTA---EINQLTLVPLPTHPHPDLVCLAPFADfdKQRYFRA--QVLYVSGNSAEV 943
Cdd:cd20408 3 VTEFKNPGEFYIQIYTLEVLESLVKLTSqlkKTYASVNNHKEYIPEVGEVCVAKYSE--DQNWYRAlvQTVDVQQKKAGV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767979637 944 FFVDYGNKSHVDLHLLMEIPCQFLELPFQALEFKICKMRPsaksLVCGkhWSD 996
Cdd:cd20408 81 FYIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKP----PSGS--WSE 127
|
|
| |
