|
Name |
Accession |
Description |
Interval |
E-value |
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
45-224 |
3.70e-108 |
|
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: 325.70 E-value: 3.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESnPTGVVLVSGEPGSGKSTQIPQWCAEFALARGFQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17986 1 LPIWAAKFTFLEQLES-PSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGDLRVVVVT 204
Cdd:cd17986 80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQR--PELRVVVVT 157
|
170 180
....*....|....*....|
gi 163914394 205 DPALEPKLRAFWGNPPIVHI 224
Cdd:cd17986 158 SPALEPKLRAFWGNPPVVHV 177
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
44-615 |
3.13e-55 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 203.00 E-value: 3.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 44 ALPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEfaLARGfQKGQVTVTQPYPLAARSLALRVADEMDLTL 123
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQ--VVVLAAPPGAGKTTQLPLALLE--LGWG-AGGRIGMLEPRRLAARAAAERMAEELGEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 124 GHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARlEKLPGDLRVVVV 203
Cdd:COG1643 84 GETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQ-PALRPDLKLLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 204 --T-DPAlepKLRAFWGNPPIV------------HIPREPGERpspiywdtippDRVEAACQAVLELCRKElPGDVLVFL 268
Cdd:COG1643 163 saTlDAE---RFARLLGDAPVIessgrtypvevrYRPLPADER-----------DLEDAVADAVREALAEE-PGDILVFL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 269 PSEEEIslcceslsREVESLLLQGLPP--RVLPLHPDCGRAVQ-AVYEDMDA--RKVVVTHWLADFSFSLPSIQHVIDSG 343
Cdd:COG1643 228 PGEREI--------RRTAEALRGRLPPdtEILPLYGRLSAAEQdRAFAPAPHgrRRIVLATNIAETSLTVPGIRYVIDSG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 344 LELRSVYNPRIRAEFQVLRPISKCQAEARRLRA-R-GfpPGSCLCLYPKS-FLELeaPPLPQPRVCEENLSSLVLLLKRR 420
Cdd:COG1643 300 LARIPRYDPRSGVTRLPTERISQASANQRAGRAgRlA--PGICYRLWSEEdFARR--PAFTDPEILRADLASLILELAAW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 421 QIAEPGECHFLDQPAPEALMQALEDLDYLAALDDDGDLSDLGVILSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAa 500
Cdd:COG1643 376 GLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 501 pgftRPPL-SAEEAALRRALEHTDGDHSsliqvyeafiqsgadeawCQARGLNWAALCQAHKLRGELLELmqrielpLSL 579
Cdd:COG1643 455 ----RDPRrGAAGSDLLARLNLWRRLRE------------------QQREFLSYLRLREWRDLARQLRRL-------LGE 505
|
570 580 590
....*....|....*....|....*....|....*.
gi 163914394 580 PAFGSEQNRRDLQKALVSGYFLKVARDTDGTGNYLL 615
Cdd:COG1643 506 GANEEPADYEAIGLLLALAYPDRIARRRGEGGRYLL 541
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
240-388 |
7.73e-48 |
|
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: 166.55 E-value: 7.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 240 IPPDRVEAACQAVLELCRKELPGDVLVFLPSEEEISLCCESLSREVESLLLQGLppRVLPLHPD-CGRAVQAVYEDMDA- 317
Cdd:cd18791 22 EDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLGKL--LVLPLHSSlPPEEQQRVFEPPPPg 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163914394 318 -RKVVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAEFQVLRPISKCQAEARRLRARGFPPGSCLCLY 388
Cdd:cd18791 100 vRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
65-498 |
3.75e-47 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 180.64 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 65 VVLVSGEPGSGKSTQIPQWCAEfaLARGfQKGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSIPQEDCTGPNTLLR 144
Cdd:PRK11131 91 VVIVAGETGSGKTTQLPKICLE--LGRG-VKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 145 FCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEKLPgDLRvVVVTDPALEPKL--RAFwGNPPIV 222
Cdd:PRK11131 168 LMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKEL-LPRRP-DLK-VIITSATIDPERfsRHF-NNAPII 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 223 HI-----PREPGERPSPIYWDTIPPDRVEAACQAVLELCRkELPGDVLVFLPSEEEISLCCESLSReveslllQGLP-PR 296
Cdd:PRK11131 244 EVsgrtyPVEVRYRPIVEEADDTERDQLQAIFDAVDELGR-EGPGDILIFMSGEREIRDTADALNK-------LNLRhTE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 297 VLPLHPDCGRAVQ-AVYEDMDARKVVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAEFQVLRPISKCQAEARRLR 375
Cdd:PRK11131 316 ILPLYARLSNSEQnRVFQSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 376 ARGFPPGSCLCLYPKS-FleLEAPPLPQPRVCEENLSSLVLLLKRRQIAEPGECHFLDQPAPEALMQALEDLDYLAALDD 454
Cdd:PRK11131 396 CGRVSEGICIRLYSEDdF--LSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITT 473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 163914394 455 DGDLSDLGVI-----LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLT 498
Cdd:PRK11131 474 DEQASAYKLTplgrqLAQLPVDPRLARMVLEAQKHGCVREVMIITSALS 522
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
591-674 |
5.15e-16 |
|
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.
Pssm-ID: 400182 [Multi-domain] Cd Length: 82 Bit Score: 73.44 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 591 LQKALVSGYFLKVARDTDGTGNYLLLTHKHVAQLSSYCCYRSrrAPARPPPWVLYHNFTISKDNCLSIVSEIQPQMLVEL 670
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFN--EKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLF 78
|
....
gi 163914394 671 APPY 674
Cdd:pfam07717 79 APHI 82
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
465-530 |
2.08e-11 |
|
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: 60.36 E-value: 2.08e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163914394 465 LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAAPGftRPPLSAEEAAL-RRALEHTDGDHSSLI 530
Cdd:smart00847 18 MAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDP--RPKEKREDADAaRRRFADPESDHLTLL 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
465-521 |
2.49e-11 |
|
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: 60.71 E-value: 2.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 163914394 465 LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAAPGFTRPPLSAEEAALRRALEH 521
Cdd:pfam04408 24 MAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
41-231 |
3.13e-07 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 51.34 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 41 QRQALPIWAARFtfleqlesnptGVVLVSGEPGSGKSTQIPQWCAEFALARGfqKGQVTVTQPYplaaRSLALRVADEMD 120
Cdd:smart00487 13 QKEAIEALLSGL-----------RDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPT----RELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 121 LTLGHE--------VGYSIPQED-----------CTGPNTLLRFC-WDRLLLQEvastrgtgaWGVLVLDEAQERSVAS- 179
Cdd:smart00487 76 KLGPSLglkvvglyGGDSKREQLrklesgktdilVTTPGRLLDLLeNDKLSLSN---------VDLVILDEAHRLLDGGf 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 163914394 180 -DSLQGLLQdarleKLPGDLRVVVVT---DPALEPKLRAFWGNPPIVHIPREPGER 231
Cdd:smart00487 147 gDQLEKLLK-----LLPKNVQLLLLSatpPEEIENLLELFLNDPVFIDVGFTPLEP 197
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
64-212 |
8.85e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.02 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 64 GVVLVSGEPGSGKSTQIpQWCAEFALARGFqkGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSipqedctgpnTLL 143
Cdd:pfam13401 6 GILVLTGESGTGKTTLL-RRLLEQLPEVRD--SVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKE----------ELL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163914394 144 RFCWDRLllqevastRGTGAWGVLVLDEAQersvasdslqgLLQDARLEKL-------PGDLRVVVVTDPALEPKL 212
Cdd:pfam13401 73 AALQQLL--------LALAVAVVLIIDEAQ-----------HLSLEALEELrdllnlsSKLLQLILVGTPELRELL 129
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
21-213 |
1.08e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 21 LAVNPFDGLPFSSRYYELLKQRQALpiwaARFTFLeqLESNPtGVVLVSGEPGSGKSTQIpQWCAEfALARGFQKGQVTV 100
Cdd:COG3267 8 LKEKPFSLTPDPRFLFLSPSHREAL----ARLEYA--LAQGG-GFVVLTGEVGTGKTTLL-RRLLE-RLPDDVKVAYIPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 101 TQpypLAARSLALRVADEMDLTLGHEvgysipqedctGPNTLLRfcwdRL---LLQEVASTRGTgawgVLVLDEAQerSV 177
Cdd:COG3267 79 PQ---LSPAELLRAIADELGLEPKGA-----------SKADLLR----QLqefLLELAAAGRRV----VLIIDEAQ--NL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 163914394 178 ASDSLQGL-----LQDARlEKLpgdLRVVVVTDPALEPKLR 213
Cdd:COG3267 135 PPETLEELrllsnLETDS-RKL---LQIVLVGQPELRERLA 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
45-224 |
3.70e-108 |
|
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: 325.70 E-value: 3.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESnPTGVVLVSGEPGSGKSTQIPQWCAEFALARGFQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17986 1 LPIWAAKFTFLEQLES-PSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQKGQVTVTQPHPLAARSLALRVADEMDLNLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGDLRVVVVT 204
Cdd:cd17986 80 HEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQR--PELRVVVVT 157
|
170 180
....*....|....*....|
gi 163914394 205 DPALEPKLRAFWGNPPIVHI 224
Cdd:cd17986 158 SPALEPKLRAFWGNPPVVHV 177
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
65-224 |
1.91e-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: 205.39 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 65 VVLVSGEPGSGKSTQIPQWCAEFALARGfQKGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSIPQEDCTGPNTLLR 144
Cdd:cd17917 3 VVVIVGETGSGKTTQVPQFLLEDGLAKG-GKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 145 FCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDaRLEKLPgDLRVVVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17917 82 FCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKD-LLRKRP-DLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
44-615 |
3.13e-55 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 203.00 E-value: 3.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 44 ALPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEfaLARGfQKGQVTVTQPYPLAARSLALRVADEMDLTL 123
Cdd:COG1643 9 DLPVSAVLPELLAALRAHQ--VVVLAAPPGAGKTTQLPLALLE--LGWG-AGGRIGMLEPRRLAARAAAERMAEELGEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 124 GHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARlEKLPGDLRVVVV 203
Cdd:COG1643 84 GETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQ-PALRPDLKLLVM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 204 --T-DPAlepKLRAFWGNPPIV------------HIPREPGERpspiywdtippDRVEAACQAVLELCRKElPGDVLVFL 268
Cdd:COG1643 163 saTlDAE---RFARLLGDAPVIessgrtypvevrYRPLPADER-----------DLEDAVADAVREALAEE-PGDILVFL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 269 PSEEEIslcceslsREVESLLLQGLPP--RVLPLHPDCGRAVQ-AVYEDMDA--RKVVVTHWLADFSFSLPSIQHVIDSG 343
Cdd:COG1643 228 PGEREI--------RRTAEALRGRLPPdtEILPLYGRLSAAEQdRAFAPAPHgrRRIVLATNIAETSLTVPGIRYVIDSG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 344 LELRSVYNPRIRAEFQVLRPISKCQAEARRLRA-R-GfpPGSCLCLYPKS-FLELeaPPLPQPRVCEENLSSLVLLLKRR 420
Cdd:COG1643 300 LARIPRYDPRSGVTRLPTERISQASANQRAGRAgRlA--PGICYRLWSEEdFARR--PAFTDPEILRADLASLILELAAW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 421 QIAEPGECHFLDQPAPEALMQALEDLDYLAALDDDGDLSDLGVILSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAa 500
Cdd:COG1643 376 GLGDPEDLPFLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSE- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 501 pgftRPPL-SAEEAALRRALEHTDGDHSsliqvyeafiqsgadeawCQARGLNWAALCQAHKLRGELLELmqrielpLSL 579
Cdd:COG1643 455 ----RDPRrGAAGSDLLARLNLWRRLRE------------------QQREFLSYLRLREWRDLARQLRRL-------LGE 505
|
570 580 590
....*....|....*....|....*....|....*.
gi 163914394 580 PAFGSEQNRRDLQKALVSGYFLKVARDTDGTGNYLL 615
Cdd:COG1643 506 GANEEPADYEAIGLLLALAYPDRIARRRGEGGRYLL 541
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
45-224 |
7.18e-55 |
|
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: 185.80 E-value: 7.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGFQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQ--IVIVSGDAKTGKSSQIPQWCAEYCLSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGDLRVVVVT 204
Cdd:cd17977 79 HEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSR--PELKLVIIT 156
|
170 180
....*....|....*....|
gi 163914394 205 DPALEPKLRAFWGNPPIVHI 224
Cdd:cd17977 157 CPHLSSKLLSYYGNVPLIEV 176
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
34-224 |
1.72e-51 |
|
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: 177.22 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 34 RYYELLKQRQALPIWAARFTFLEQLESNPTgVVLVsGEPGSGKSTQIPQWCAEFALARgFQKGQVTVTQPYPLAARSLAL 113
Cdd:cd17973 2 RYFEILEKRRELPVWEQKEDFLKLLKNNQI-LVLV-GETGSGKTTQIPQFVLDDELPH-QPKKLVACTQPRRVAAMSVAQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 114 RVADEMDLTLGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEK 193
Cdd:cd17973 79 RVAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEV-VRR 157
|
170 180 190
....*....|....*....|....*....|.
gi 163914394 194 LPgDLRVVVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17973 158 RP-DLKLIVMSATLDAGKFQKYFDNAPLLKV 187
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
240-388 |
7.73e-48 |
|
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: 166.55 E-value: 7.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 240 IPPDRVEAACQAVLELCRKELPGDVLVFLPSEEEISLCCESLSREVESLLLQGLppRVLPLHPD-CGRAVQAVYEDMDA- 317
Cdd:cd18791 22 EDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLGKL--LVLPLHSSlPPEEQQRVFEPPPPg 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163914394 318 -RKVVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAEFQVLRPISKCQAEARRLRARGFPPGSCLCLY 388
Cdd:cd18791 100 vRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
65-498 |
3.75e-47 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 180.64 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 65 VVLVSGEPGSGKSTQIPQWCAEfaLARGfQKGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSIPQEDCTGPNTLLR 144
Cdd:PRK11131 91 VVIVAGETGSGKTTQLPKICLE--LGRG-VKGLIGHTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 145 FCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEKLPgDLRvVVVTDPALEPKL--RAFwGNPPIV 222
Cdd:PRK11131 168 LMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKEL-LPRRP-DLK-VIITSATIDPERfsRHF-NNAPII 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 223 HI-----PREPGERPSPIYWDTIPPDRVEAACQAVLELCRkELPGDVLVFLPSEEEISLCCESLSReveslllQGLP-PR 296
Cdd:PRK11131 244 EVsgrtyPVEVRYRPIVEEADDTERDQLQAIFDAVDELGR-EGPGDILIFMSGEREIRDTADALNK-------LNLRhTE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 297 VLPLHPDCGRAVQ-AVYEDMDARKVVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAEFQVLRPISKCQAEARRLR 375
Cdd:PRK11131 316 ILPLYARLSNSEQnRVFQSHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 376 ARGFPPGSCLCLYPKS-FleLEAPPLPQPRVCEENLSSLVLLLKRRQIAEPGECHFLDQPAPEALMQALEDLDYLAALDD 454
Cdd:PRK11131 396 CGRVSEGICIRLYSEDdF--LSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITT 473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 163914394 455 DGDLSDLGVI-----LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLT 498
Cdd:PRK11131 474 DEQASAYKLTplgrqLAQLPVDPRLARMVLEAQKHGCVREVMIITSALS 522
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
41-225 |
2.60e-38 |
|
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: 140.31 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 41 QRQALPIWAARFTFLEQLESNPTGVVLvsGEPGSGKSTQIPQWCAEFALARgfqKGQVTVTQPYPLAARSLALRVADEMD 120
Cdd:cd17971 2 QRESLPIYKLKEQLIQAVHDNQILVVI--GETGSGKTTQITQYLAEAGYTS---RGKIGCTQPRRVAAMSVAKRVAEEFG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 121 LTLGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEKLPgDLRV 200
Cdd:cd17971 77 CCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKT-VQKRP-DLKL 154
|
170 180
....*....|....*....|....*
gi 163914394 201 VVVTDPALEPKLRAFWGNPPIVHIP 225
Cdd:cd17971 155 IVTSATLDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
45-224 |
2.85e-38 |
|
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: 140.18 E-value: 2.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPTgvVLVSGEPGSGKSTQIPQWCAEFALARGfqkGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17978 1 LPIYSARKRLLEELRKHDT--VIIIGETGSGKTTQIPQYLYEAGFARG---GMIGITQPRRVAAVSVAKRVAEEMGVELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDA---RLEKLPGDLRVV 201
Cdd:cd17978 76 QLVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAqrrRKEQKLSPLKVI 155
|
170 180
....*....|....*....|....
gi 163914394 202 VVTdPALEPKLRA-FWGNPPIVHI 224
Cdd:cd17978 156 IMS-ATLDADLFSeYFNGAPVLYI 178
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
45-224 |
3.54e-36 |
|
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: 134.17 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGfqKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQ--VLIIVGETGSGKTTQIPQYLHEAGYTKG--GGKIGCTQPRRVAAMSVAARVAEEMGVKLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQD-ARLEKlpgDLRVVVV 203
Cdd:cd17974 77 NEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDiARFRP---DLKLLIS 153
|
170 180
....*....|....*....|.
gi 163914394 204 TDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17974 154 SATMDAEKFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
45-224 |
3.00e-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: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALArgfQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNS--FLIVTGNTGSGKTTQLPKYLYEAGFS---QHGMIGVTQPRRVAAISVAQRVAEEMKCTLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKLPG---DLRVV 201
Cdd:cd17984 76 SKVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPNrkeHLKVV 155
|
170 180
....*....|....*....|...
gi 163914394 202 VVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17984 156 VMSATLELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
45-220 |
4.35e-35 |
|
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: 131.44 E-value: 4.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPTgVVLVsGEPGSGKSTQIPQWCAEFALARGFQkgQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17980 1 LPVFKLRNHILYLVENYQT-IVIV-GETGCGKSTQIPQYLAEAGWTAGGR--VVGCTQPRRVAAVTVAGRVAEEMGAVLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGP-NTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQdaRLEKLPGDLRVVVV 203
Cdd:cd17980 77 HEVGYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLK--KIQKKRGDLRLIVA 154
|
170 180
....*....|....*....|..
gi 163914394 204 TDPALEPKLRAFW-----GNPP 220
Cdd:cd17980 155 SATLDAEKFRDFFnqnetNDPS 176
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
45-224 |
5.40e-35 |
|
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: 130.66 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNptGVVLVSGEPGSGKSTQIPQWCAEfalaRGFQK-GQVTVTQPYPLAARSLALRVADEMDLTL 123
Cdd:cd17983 1 LPIFAVRQELLNVIRDN--NVVIVVGETGSGKTTQLTQYLHE----DGYTDyGMIGCTQPRRVAAMSVAKRVSEEMGVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 124 GHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGDLRVVVV 203
Cdd:cd17983 75 GEEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARR--RDLKLIVT 152
|
170 180
....*....|....*....|.
gi 163914394 204 TDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17983 153 SATMDADKFADFFGNVPIFTI 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
45-224 |
3.67e-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: 117.46 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQ--WCAEFALARGFQKGQVTVTQPYPLAARSLALRVADEMDLt 122
Cdd:cd17982 1 LPILAEEQEIMEAINENP--VVIICGETGSGKTTQVPQflYEAGFGSPESDNPGMIGITQPRRVAAVSMAKRVAEELNV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 123 LGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQ---DARLEKLPGD-- 197
Cdd:cd17982 78 FGKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSrivPLRAKLYLQDqt 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 163914394 198 ---LRVVV------VTDPALEPKLraFWGNPPIVHI 224
Cdd:cd17982 158 vkpLKLVImsatlrVEDFTENKLL--FPRPPPVIKV 191
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
45-224 |
1.52e-28 |
|
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: 112.55 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEfaLARGfQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQ--VVIIAGETGSGKTTQLPKICLE--LGRG-IRGLIGHTQPRRLAARSVAERIAEELKTELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEKLPgDLRvVVVT 204
Cdd:cd17989 76 GAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQL-LPRRP-DLK-VIIT 152
|
170 180
....*....|....*....|.
gi 163914394 205 DPALEP-KLRAFWGNPPIVHI 224
Cdd:cd17989 153 SATIDAeRFSRHFNNAPIIEV 173
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
45-499 |
7.22e-25 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 110.40 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPTgvVLVSGEPGSGKSTQIPqwcAEFALARGFQkGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:PRK11664 4 LPVAAVLPELLTALKTAPQ--VLLKAPTGAGKSTWLP---LQLLQHGGIN-GKIIMLEPRRLAARNVAQRLAEQLGEKPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLL---LQEVASTRGTGawgVLVLDEAQERSVASDSLQGLLQDARlEKLPGDLRVV 201
Cdd:PRK11664 78 ETVGYRMRAESKVGPNTRLEVVTEGILtrmIQRDPELSGVG---LVILDEFHERSLQADLALALLLDVQ-QGLRDDLKLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 202 VVTDPALEPKLRAFWGNPPIVhiprEPGERPSPI---YWDTIPPDR-VEAACQAVLELCRKElPGDVLVFLPSEEEIslc 277
Cdd:PRK11664 154 IMSATLDNDRLQQLLPDAPVI----VSEGRSFPVerrYQPLPAHQRfDEAVARATAELLRQE-SGSLLLFLPGVGEI--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 278 ceslsREVESLLLQGLPPRVL--PLH-----PDCGRAVQAVYEDMdaRKVVVTHWLADFSFSLPSIQHVIDSGLELRSVY 350
Cdd:PRK11664 226 -----QRVQEQLASRVASDVLlcPLYgalslAEQQKAILPAPAGR--RKVVLATNIAETSLTIEGIRLVVDSGLERVARF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 351 NPR---IRAEFQvlRpISKCQAEARRLRARGFPPGSCLCLYPKSFLElEAPPLPQPRVCEENLSSLVLLLKRRQIAEPGE 427
Cdd:PRK11664 299 DPKtglTRLVTQ--R-ISQASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLELLQWGCHDPAQ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 163914394 428 CHFLDQPAPEALMQALEDLDYLAALDDDGDLSDLGVILSEFPLAPELAKALLASCEFDcvDEMLTLAAMLTA 499
Cdd:PRK11664 375 LSWLDQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAKEDD--EAALATAAKLAA 444
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
45-224 |
2.95e-22 |
|
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: 94.52 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGFQK-GQVTVTQPYPLAARSLALRVADEMDLTL 123
Cdd:cd17985 1 LPAWQERETILELLEKHQ--VLVISGMTGCGKTTQIPQFILDNSLQGPPLPvANIICTQPRRISAISVAERVAQERAERV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 124 GHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGDLRVVVV 203
Cdd:cd17985 79 GQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQR--PDLKVILM 156
|
170 180
....*....|....*....|.
gi 163914394 204 TDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17985 157 SATLNAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
45-224 |
1.90e-21 |
|
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: 92.29 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGF--QKGQVTVTQPYPLAARSLALRVADEMDLT 122
Cdd:cd17975 1 LPVFKHRESILETLKRHR--VVVVAGETGSGKSTQVPQFLLEDLLLNGGtaQKCNIVCTQPRRISAMSLATRVCEELGCE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 123 LG-----HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKlpGD 197
Cdd:cd17975 79 SGpggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKR--SD 156
|
170 180
....*....|....*....|....*..
gi 163914394 198 LRVVVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17975 157 LHLILMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
45-224 |
2.78e-21 |
|
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: 91.35 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQwcaeFALARGFqkGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17979 1 LPIAQYREKIIELLKTHQ--VVIVAGDTGCGKSTQVPQ----YLLAAGF--RHIACTQPRRIACISLAKRVAFESLNQYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDarLEKLPGDLRVVVVT 204
Cdd:cd17979 73 SKVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRC--LLRLRPDLKLILMS 150
|
170 180
....*....|....*....|
gi 163914394 205 DPALEPKLRAFWGNPPIVHI 224
Cdd:cd17979 151 ATINIELFSGYFEGAPVVQV 170
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
45-224 |
5.91e-21 |
|
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: 90.66 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQwcaeFALARGFQKG---QVTVTQPYPLAARSLALRVADEMDL 121
Cdd:cd17987 1 LPVFEKQEQIVRIIKENK--VVLIVGETGSGKTTQIPQ----FLLDDCYANGipcRIFCTQPRRLAAIAVAERVAAERGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 122 TLGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEV-ASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDArLEKLPgDLRv 200
Cdd:cd17987 75 KIGQTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDI-LQKHP-NLK- 151
|
170 180
....*....|....*....|....*
gi 163914394 201 VVVTDPALEPKLRA-FWGNPPIVHI 224
Cdd:cd17987 152 LILSSAALDVNLFIrYFGSCPVIYI 176
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
45-224 |
2.46e-20 |
|
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: 89.08 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGfqKG---QVTVTQPYPLAARSLALRVADEMDL 121
Cdd:cd17976 1 LPVDSHKESILSAIEQNP--VVVISGDTGCGKTTRIPQFILEDYVLRG--RGarcNVVITQPRRISAVSVAQRVAHELGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 122 TLGHEVGYSIPQEDCTGPN-TLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDarLEKLPGDLRV 200
Cdd:cd17976 77 NLRRNVGYQVRLESRPPPRgGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKG--VLQLNPELRV 154
|
170 180
....*....|....*....|....
gi 163914394 201 VVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17976 155 VLMSATGDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
45-224 |
9.06e-20 |
|
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: 87.59 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGfqKG---QVTVTQPYPLAARSLALRVADEM-- 119
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQ--VTVISGETGCGKTTQVTQFILDDAIERG--KGsscRIVCTQPRRISAISVAERVAAERae 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 120 DLTLGHEVGYSI------PQEDCTgpntlLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDarLEK 193
Cdd:cd17981 77 SCGLGNSTGYQIrlesrkPRKQGS-----ILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKD--LLP 149
|
170 180 190
....*....|....*....|....*....|.
gi 163914394 194 LPGDLRVVVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17981 150 FRSDLKVILMSATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
45-182 |
2.11e-18 |
|
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: 83.32 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEFALARGfQKGQVTVTQPYPLAARSLALRVADEMDLTLG 124
Cdd:cd17988 1 LPIYAKREEILSLIEANS--VVIIKGATGCGKTTQLPQFILDHYYKRG-KYCNIVVTQPRRIAAISIARRVSQEREWTLG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 163914394 125 HEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSL 182
Cdd:cd17988 78 SLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFL 135
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
35-224 |
7.06e-18 |
|
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: 83.35 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 35 YYELLKQRQALPIWAARFTFLEQLESNPtgVVLVSGEPGSGKSTQIPQWCAEfALARGFQKGQ--VTVTQPYPLAARSLA 112
Cdd:cd17972 49 LQQILQERELLPVKKFREEILEAISNNP--VVIIRGATGCGKTTQVPQYILD-DFIQNDRAAEcnIVVTQPRRISAVSVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 113 LRVADEMDLTLGHEVGYSIPQEDCTG-PNTLLRFCWDRLLLQEVAStrgtGAWGV--LVLDEAQERSVASDSLQGLLQDA 189
Cdd:cd17972 126 ERVAFERGEEVGKSCGYSVRFESVLPrPHASILFCTVGVLLRKLEA----GIRGIshVIVDEIHERDINTDFLLVVLRDV 201
|
170 180 190
....*....|....*....|....*....|....*
gi 163914394 190 rLEKLPgDLRVVVVTDPALEPKLRAFWGNPPIVHI 224
Cdd:cd17972 202 -VQAYP-DLRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
45-222 |
1.33e-17 |
|
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: 80.84 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 45 LPIWAARFTFLEQLESNptGVVLVSGEPGSGKSTQIP----QWCAEFAlargfqkGQVTVTQPYPLAARSLALRVADEMD 120
Cdd:cd17990 1 LPIAAVLPALRAALDAG--GQVVLEAPPGAGKTTRVPlallAELWIAG-------GKIIVLEPRRVAARAAARRLATLLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 121 LTLGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGAWGVLVLDEAQERSVASDSLQGLLQDARLEKLPgDLRV 200
Cdd:cd17990 72 EAPGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLLRD-DLRL 150
|
170 180
....*....|....*....|..
gi 163914394 201 VVVTDPALEPKLRAFWGNPPIV 222
Cdd:cd17990 151 LAMSATLDGDGLAALLPEAPVV 172
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
591-674 |
5.15e-16 |
|
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.
Pssm-ID: 400182 [Multi-domain] Cd Length: 82 Bit Score: 73.44 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 591 LQKALVSGYFLKVARDTDGTGNYLLLTHKHVAQLSSYCCYRSrrAPARPPPWVLYHNFTISKDNCLSIVSEIQPQMLVEL 670
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGKGYTTLSDNQRVFIHPSSVLFN--EKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLF 78
|
....
gi 163914394 671 APPY 674
Cdd:pfam07717 79 APHI 82
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
465-530 |
2.08e-11 |
|
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: 60.36 E-value: 2.08e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 163914394 465 LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAAPGftRPPLSAEEAAL-RRALEHTDGDHSSLI 530
Cdd:smart00847 18 MAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDP--RPKEKREDADAaRRRFADPESDHLTLL 82
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
465-521 |
2.49e-11 |
|
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: 60.71 E-value: 2.49e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 163914394 465 LSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAAPGFTRPPLSAEEAALRRALEH 521
Cdd:pfam04408 24 MAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFLDPRSAAKAARRR 80
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
41-231 |
3.13e-07 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 51.34 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 41 QRQALPIWAARFtfleqlesnptGVVLVSGEPGSGKSTQIPQWCAEFALARGfqKGQVTVTQPYplaaRSLALRVADEMD 120
Cdd:smart00487 13 QKEAIEALLSGL-----------RDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPT----RELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 121 LTLGHE--------VGYSIPQED-----------CTGPNTLLRFC-WDRLLLQEvastrgtgaWGVLVLDEAQERSVAS- 179
Cdd:smart00487 76 KLGPSLglkvvglyGGDSKREQLrklesgktdilVTTPGRLLDLLeNDKLSLSN---------VDLVILDEAHRLLDGGf 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 163914394 180 -DSLQGLLQdarleKLPGDLRVVVVT---DPALEPKLRAFWGNPPIVHIPREPGER 231
Cdd:smart00487 147 gDQLEKLLK-----LLPKNVQLLLLSatpPEEIENLLELFLNDPVFIDVGFTPLEP 197
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
64-212 |
8.85e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.02 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 64 GVVLVSGEPGSGKSTQIpQWCAEFALARGFqkGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSipqedctgpnTLL 143
Cdd:pfam13401 6 GILVLTGESGTGKTTLL-RRLLEQLPEVRD--SVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKE----------ELL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163914394 144 RFCWDRLllqevastRGTGAWGVLVLDEAQersvasdslqgLLQDARLEKL-------PGDLRVVVVTDPALEPKL 212
Cdd:pfam13401 73 AALQQLL--------LALAVAVVLIIDEAQ-----------HLSLEALEELrdllnlsSKLLQLILVGTPELRELL 129
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
21-213 |
1.08e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 21 LAVNPFDGLPFSSRYYELLKQRQALpiwaARFTFLeqLESNPtGVVLVSGEPGSGKSTQIpQWCAEfALARGFQKGQVTV 100
Cdd:COG3267 8 LKEKPFSLTPDPRFLFLSPSHREAL----ARLEYA--LAQGG-GFVVLTGEVGTGKTTLL-RRLLE-RLPDDVKVAYIPN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 101 TQpypLAARSLALRVADEMDLTLGHEvgysipqedctGPNTLLRfcwdRL---LLQEVASTRGTgawgVLVLDEAQerSV 177
Cdd:COG3267 79 PQ---LSPAELLRAIADELGLEPKGA-----------SKADLLR----QLqefLLELAAAGRRV----VLIIDEAQ--NL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 163914394 178 ASDSLQGL-----LQDARlEKLpgdLRVVVVTDPALEPKLR 213
Cdd:COG3267 135 PPETLEELrllsnLETDS-RKL---LQIVLVGQPELRERLA 171
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
8-89 |
1.16e-03 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 42.25 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163914394 8 LAEEYGPS-----PGESELAVNPFDGLPfssRYYELLKQRQALPIWAA----------------RFTFLEQLESNPTGVV 66
Cdd:cd14895 7 LAQRYGVDqvycrSGAVLIAVNPFKHIP---GLYDLHKYREEMPGWTAlpphvfsiaegayrslRRRLHEPGASKKNQTI 83
|
90 100
....*....|....*....|....*.
gi 163914394 67 LVSGEPGSGK--STQ-IPQWCAEFAL 89
Cdd:cd14895 84 LVSGESGAGKteTTKfIMNYLAESSK 109
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| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
21-77 |
3.49e-03 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 40.83 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 163914394 21 LAVNPFDGLP-FSSRYYE----LLKQRQALP--IWAARFTFLEQLESNPTGVVLVSGEPGSGKS 77
Cdd:cd14897 25 VAVNPCKPLPiFDKKHHEeysnLSVRSQRPPhlFWIADQAYRRLLETGRNQCILVSGESGAGKT 88
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|
| DAP3 |
pfam10236 |
Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins ... |
53-105 |
5.63e-03 |
|
Mitochondrial ribosomal death-associated protein 3; This is a family of conserved proteins which were originally described as death-associated-protein-3 (DAP-3). The proteins carry a P-loop DNA-binding motif, and induce apoptosis. DAP3 has been shown to be a pro-apoptotic factor in the mitochondrial matrix and to be crucial for mitochondrial biogenesis and so has also been designated as MRP-S29 (mitochondrial ribosomal protein subunit 29).
Pssm-ID: 431160 Cd Length: 310 Bit Score: 39.59 E-value: 5.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 163914394 53 TFLEQLESNPTGVVLVSGEPGSGKSTQIPQwcaefALARGFQKGQVTVTQPYP 105
Cdd:pfam10236 13 KLKAADKSKKVVRFVLTGEPGSGKSVLLLQ-----AMAYALEKGWVVLHVPEA 60
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