|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
248-1036 |
1.40e-131 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 421.80 E-value: 1.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEmnLSHRV--- 324
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIG-MLEPRRLAARAAAERMAEE--LGEPVget 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 325 VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIV-ALRakrhlP-LKLLI 402
Cdd:COG1643 87 VGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQpALR-----PdLKLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 403 MSATLRVEDFtqnQRLFTtPPPVIKVESRQFPVTVHFNKRTPLD-DYSGECFRKVCKIHRMlPAGGILVFLTGQAEVHAL 481
Cdd:COG1643 162 MSATLDAERF---ARLLG-DAPVIESSGRTYPVEVRYRPLPADErDLEDAVADAVREALAE-EPGDILVFLPGEREIRRT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 482 CRRLRKAfpfrcsqpqekeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeeaLGSDLD 561
Cdd:COG1643 237 AEALRGR-------------------------------------------------------------------LPPDTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 562 ldlgdseanegeqpdaslplhVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:COG1643 250 ---------------------ILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRrpvEDL---ILQMKALSIEKVINFPF 718
Cdd:COG1643 309 RSGVTRLPTERISQASANQRAGRAGRLAPGICYRLWSEEDFARRPAFTDPEILR---ADLaslILELAAWGLGDPEDLPF 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 719 PTPPSVEALVAAEELLVALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:COG1643 386 LDPPPARAIADARALLQELGALDADGR---------------LTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAA 450
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 799 AMTVRELFeeldRPAASekelaelkgrrarvaqmkrtwagqgpslklGDLMVLLGAVGACEYAgcspqfcQANGLRYKAM 878
Cdd:COG1643 451 LLSERDPR----RGAAG------------------------------SDLLARLNLWRRLREQ-------QREFLSYLRL 489
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 879 LEIRRLRGQLTTAVNavcpeaglfldpkmQPPTESQVTYLR--QIMAAGLGDHLARRVQsedlldpkwknayktpllDDP 956
Cdd:COG1643 490 REWRDLARQLRRLLG--------------EGANEEPADYEAigLLLALAYPDRIARRRG------------------EGG 537
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 957 VF---------IHPSSVLFKElpEFVVYQEIVET---TKMYMkgVSTVEIQWIPSLLPSYCQfdaplEEPAPSYCPESGQ 1024
Cdd:COG1643 538 RYllargrgaaLFPGSPLAKK--EWLVAAELVGGaaeARIRL--AAPIDPEWLEELAAHLIK-----RYSEPHWDKKRGR 608
|
810
....*....|..
gi 1039770916 1025 VLCHRASVFYRV 1036
Cdd:COG1643 609 VVARERVRLGAL 620
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
248-428 |
3.68e-118 |
|
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: 363.21 E-value: 3.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDS----IIGVTEPRRVAAVAMSQRVAKEMNLSHR 323
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESdnpgMIGITQPRRVAAVSMAKRVAEELNVFGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 324 VVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK------RHLP 397
Cdd:cd17982 81 EVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqTVKP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1039770916 398 LKLLIMSATLRVEDFTQNQRLFTTPPPVIKV 428
Cdd:cd17982 161 LKLVIMSATLRVEDFTENKLLFPRPPPVIKV 191
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
248-1034 |
2.08e-100 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 346.76 E-value: 2.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:TIGR01967 66 LPVSAKREDIAEAIAENQVVIIAGETGSGKTTQLPKICLELGRGSH-GLIGHTQPRRLAARTVAQRIAEELGTPlGEKVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSAT 406
Cdd:TIGR01967 145 YKVRFHDQVSSNTLVKLMTDGILLAETQQDRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPDLKIIITSAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 407 LRVEDFTqnqRLFTTPPpVIKVESRQFPVTVHFNkrtPLDDYSGE--------CFRKVCKIHRMLPaGGILVFLTGQAEV 478
Cdd:TIGR01967 221 IDPERFS---RHFNNAP-IIEVSGRTYPVEVRYR---PLVEEQEDddldqleaILDAVDELFAEGP-GDILIFLPGEREI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 479 halcrrlrkafpfrcsqpqekeEDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgs 558
Cdd:TIGR01967 293 ----------------------RDAAEILRK------------------------------------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 559 dldLDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKPppEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRY 638
Cdd:TIGR01967 302 ---RNLRHTE--------------ILPLYARLSNKEQQRVFQP--HSGRRIVLATNVAETSLTVPGIHYVIDTGTARISR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 639 YDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALSIEKVINFPF 718
Cdd:TIGR01967 363 YSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLALRLGDIAAFPF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 719 PTPPSVEALVAAEELLVALGALQappKQERMKKLqmsqlscpiTALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVA 798
Cdd:TIGR01967 443 IEAPDPRAIRDGFRLLEELGALD---DDEAEPQL---------TPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIAS 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 799 AMTVRELFEE-LDRPAASEKELAELKGRRARVAQMKRTWAGqgpslklgdlmvllgaVGACEYAGCSPQFCQANGLRYKA 877
Cdd:TIGR01967 511 ALSIQDPRERpMEKQQAADQAHARFKDPRSDFLSRVNLWRH----------------IEEQRQALSANQFRNACRKQYLN 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 878 MLEIRRLRgQLTTAVNAVCPEAGLFLDpkmQPPTESQVtyLRQIMAAGLGDHLARRVQSEDLLDPKWKNayktpllddpV 957
Cdd:TIGR01967 575 YLRVREWQ-DIYRQLTQVVKELGLKLN---EEPADYDA--IHKALLSGLLSQIGMKDEKHEYDGARGRK----------F 638
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770916 958 FIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSLLPSYCQfDAPLEepaPSYCPESGQVLCHRASVFY 1034
Cdd:TIGR01967 639 HIFPGSPLFKKPPKWVMAAELVETSKLYARLVAKIEPEWVEPVAGHLIK-KNYFE---PHWEKKRGQVMAYEKVTLY 711
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
248-1000 |
8.87e-97 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 336.65 E-value: 8.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:PRK11131 73 LPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVK-GLIGHTQPRRLAARTVANRIAEELETElGGCVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:PRK11131 152 YKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDFILGYLKELLPRRPD----LKVIITSAT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 407 LRVEDFTqnqRLFTTpPPVIKVESRQFPVTVHFNKRTPLDDYSGE-----CFRKVCKIHRMLPaGGILVFLTGQAEVhal 481
Cdd:PRK11131 228 IDPERFS---RHFNN-APIIEVSGRTYPVEVRYRPIVEEADDTERdqlqaIFDAVDELGREGP-GDILIFMSGEREI--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 482 crrlrkafpfrcsqpqekeEDSAEGMRRfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgsdld 561
Cdd:PRK11131 300 -------------------RDTADALNK---------------------------------------------------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 562 LDLGDSEanegeqpdaslplhVLPLYSLLAPEKQAQVFKppPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDR 641
Cdd:PRK11131 309 LNLRHTE--------------ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKYVIDPGTARISRYSY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 642 VTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALSIEKVINFPFPTP 721
Cdd:PRK11131 373 RTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTALGLGDIAAFPFVEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 722 PSVEALVAAEELLVALGALQAPPKQERMKklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMT 801
Cdd:PRK11131 453 PDKRNIQDGVRLLEELGAITTDEQASAYK----------LTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 802 VRELFEeldRPaASEKELAELKGRRArvaqmkrtwagqgpSLKLGDLMVLLGA---VGACEYAGCSPQF---CQANGLRY 875
Cdd:PRK11131 523 IQDPRE---RP-MDKQQASDEKHRRF--------------ADKESDFLAFVNLwnyLQEQQKALSSNQFrrlCRTDYLNY 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 876 KAMLEIRRLRGQLTTAVNavcpEAGLfldpkmqpPTESQVTYLRQIMAA---GLGDHLARRVQSedlldpkwKNAYkTPL 952
Cdd:PRK11131 585 LRVREWQDIYTQLRQVVK----ELGI--------PVNSEPAEYREIHTAlltGLLSHIGMKDAE--------KQEY-TGA 643
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1039770916 953 LDDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSTVEIQWIPSL 1000
Cdd:PRK11131 644 RNARFSIFPGSGLFKKPPKWVMVAELVETSRLWGRIAARIEPEWIEPL 691
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
264-428 |
8.73e-68 |
|
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: 224.65 E-value: 8.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 264 HPIVIVCGETGSGKTTQVPQFLYEAGYSS-EDSIIGVTEPRRVAAVAMSQRVAKEMNLSH-RVVSYQIRYEGNVTEETRI 341
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKgGKGRIVCTQPRRIAAISVAERVAEERGEKLgEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 342 KFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSATLRVEDFTQnqrlFTT 421
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLL----RKRPDLKVILMSATLDAEKFSS----YFG 152
|
....*..
gi 1039770916 422 PPPVIKV 428
Cdd:cd17917 153 GAPVIHI 159
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
248-414 |
6.54e-66 |
|
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: 219.92 E-value: 6.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSsEDSIIGVTEPRRVAAVAMSQRVAKEMNLSH-RVVS 326
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFA-RGGMIGITQPRRVAAVSVAKRVAEEMGVELgQLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHL-PLKLLIMSA 405
Cdd:cd17978 80 YSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEQKLsPLKVIIMSA 159
|
....*....
gi 1039770916 406 TLRVEDFTQ 414
Cdd:cd17978 160 TLDADLFSE 168
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
433-677 |
8.42e-61 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 205.46 E-value: 8.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 433 FPVTVHFNKRT----------PLDDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCRRLRKAFPFrcsqpqekeed 502
Cdd:cd18791 1 FPVEVYYLEDIlellgissekEDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLS----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 503 saegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeealgsdldldlgdseanegeqpDASLPLH 582
Cdd:cd18791 70 -------------------------------------------------------------------------PDLGKLL 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 583 VLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRA 662
Cdd:cd18791 77 VLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRA 156
|
250
....*....|....*
gi 1039770916 663 GRAGRTEPGHCYRLY 677
Cdd:cd18791 157 GRAGRTRPGKCYRLY 171
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
248-800 |
2.74e-59 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 219.41 E-value: 2.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVP-QFLYEAGYSSEdsIIgVTEPRRVAAVAMSQRVAKEMNlsHRV-- 324
Cdd:PRK11664 4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGINGK--II-MLEPRRLAARNVAQRLAEQLG--EKPge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 325 -VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRI-VALRAKrhlpLKLLI 402
Cdd:PRK11664 79 tVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDD----LKLLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 403 MSATLrvedftQNQRLFTTPP--PVIKVESRQFPVTVHF---NKRTPLDDysgecfrKVCK-IHRML--PAGGILVFLTG 474
Cdd:PRK11664 155 MSATL------DNDRLQQLLPdaPVIVSEGRSFPVERRYqplPAHQRFDE-------AVARaTAELLrqESGSLLLFLPG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 475 QAEVHALCRRLRkafpfrcsqpqekeedsaegmrrfkksrtrarkaqamalpqinldnysvlpagegdedreaemddeeE 554
Cdd:PRK11664 222 VGEIQRVQEQLA-------------------------------------------------------------------S 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 555 ALGSDLDLdlgdseanegeqpdaslplhvLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKV 634
Cdd:PRK11664 235 RVASDVLL---------------------CPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 635 KKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALSIEKVI 714
Cdd:PRK11664 294 RVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAERAAAQSEPEILHSDLSGLLLELLQWGCHDPA 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 715 NFPFPTPPSVEALVAAEELLVALGALQappkqermkklQMSQLscpiTALGRTMSTFPVAPRYAKMLALSQQHG-CLPYT 793
Cdd:PRK11664 374 QLSWLDQPPAAALAAAKRLLQQLGALD-----------GQGRL----TARGRKMAALGNDPRLAAMLVAAKEDDeAALAT 438
|
....*..
gi 1039770916 794 IAIVAAM 800
Cdd:PRK11664 439 AAKLAAI 445
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
248-412 |
2.02e-54 |
|
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: 187.68 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEM--NLSHRvV 325
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGRVVGCTQPRRVAAVTVAGRVAEEMgaVLGHE-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 326 SYQIRYEGNVTE-ETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMS 404
Cdd:cd17980 80 GYCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGD----LRLIVAS 155
|
....*...
gi 1039770916 405 ATLRVEDF 412
Cdd:cd17980 156 ATLDAEKF 163
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
248-410 |
3.31e-54 |
|
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: 186.98 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSsEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFS-QHGMIGVTQPRRVAAISVAQRVAEEMKCTlGSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK-RHLPLKLLIMSA 405
Cdd:cd17984 80 YQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSPnRKEHLKVVVMSA 159
|
....*
gi 1039770916 406 TLRVE 410
Cdd:cd17984 160 TLELA 164
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
243-422 |
4.21e-52 |
|
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: 180.76 E-value: 4.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 243 EERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMN--L 320
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSR-GKIGCTQPRRVAAMSVAKRVAEEFGccL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 321 SHRVvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKL 400
Cdd:cd17971 80 GQEV-GYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTV----QKRPDLKL 154
|
170 180
....*....|....*....|....*
gi 1039770916 401 LIMSATLRVEDFTQ---NQRLFTTP 422
Cdd:cd17971 155 IVTSATLDAVKFSQyfyEAPIFTIP 179
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
248-413 |
7.52e-52 |
|
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: 180.01 E-value: 7.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMN--LSHRvV 325
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIGCTQPRRVAAMSVAARVAEEMGvkLGNE-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSA 405
Cdd:cd17974 80 GYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPD----LKLLISSA 155
|
....*...
gi 1039770916 406 TLRVEDFT 413
Cdd:cd17974 156 TMDAEKFS 163
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
236-423 |
1.75e-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: 179.53 E-value: 1.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 236 NRTPEMQEERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYS-SEDSIIGVTEPRRVAAVAMSQRV 314
Cdd:cd17973 1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPhQPKKLVACTQPRRVAAMSVAQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 315 AKEMNLS-HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAK 393
Cdd:cd17973 81 AEEMDVKlGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPD 160
|
170 180 190
....*....|....*....|....*....|
gi 1039770916 394 rhlpLKLLIMSATLRVEDFtqnQRLFTTPP 423
Cdd:cd17973 161 ----LKLIVMSATLDAGKF---QKYFDNAP 183
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
248-413 |
2.77e-51 |
|
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: 178.04 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSeDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTD-YGMIGCTQPRRVAAMSVAKRVSEEMGVElGEEVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:cd17983 80 YAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRD----LKLIVTSAT 155
|
....*..
gi 1039770916 407 LRVEDFT 413
Cdd:cd17983 156 MDADKFA 162
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
248-428 |
2.09e-47 |
|
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: 167.25 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEdSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIR-GLIGHTQPRRLAARSVAERIAEELKTElGGAVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMSAT 406
Cdd:cd17989 80 YKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLL----PRRPDLKVIITSAT 155
|
170 180
....*....|....*....|..
gi 1039770916 407 LRVEDFTQNqrlFTTpPPVIKV 428
Cdd:cd17989 156 IDAERFSRH---FNN-APIIEV 173
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
248-413 |
2.91e-47 |
|
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: 166.46 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSedsiIGVTEPRRVAAVAMSQRVAKE-MNLSHRVVS 326
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH----IACTQPRRIACISLAKRVAFEsLNQYGSKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIMSAT 406
Cdd:cd17979 77 YQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPD----LKLILMSAT 152
|
....*..
gi 1039770916 407 LRVEDFT 413
Cdd:cd17979 153 INIELFS 159
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
248-428 |
2.21e-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: 144.67 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-- 321
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEdlllNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCEsg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 322 ----HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHlp 397
Cdd:cd17975 81 pggkNSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLH-- 158
|
170 180 190
....*....|....*....|....*....|.
gi 1039770916 398 lkLLIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17975 159 --LILMSATVDCEKFSS----YFTHCPILRI 183
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
248-414 |
1.46e-36 |
|
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: 136.51 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLY----EAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLSH- 322
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILddaiERGKGSSCRIV-CTQPRRISAISVAERVAAERAESCg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 323 --RVVSYQIRYEGNVT-EETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRakrhLPLK 399
Cdd:cd17981 80 lgNSTGYQIRLESRKPrKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFR----SDLK 155
|
170
....*....|....*
gi 1039770916 400 LLIMSATLRVEDFTQ 414
Cdd:cd17981 156 VILMSATLNAEKFSD 170
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
248-428 |
9.93e-35 |
|
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: 131.08 E-value: 9.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGY-SSEDSIIGVTEPRRVAAVAMSQRVAKEMNLS-HRVV 325
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYkRGKYCNIVVTQPRRIAAISIARRVSQEREWTlGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAkRHlpLKLLIMSA 405
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNS-RH--VKIILMSA 157
|
170 180
....*....|....*....|...
gi 1039770916 406 TLRVEDFTQNQRLFTTPPPVIKV 428
Cdd:cd17988 158 TISCKEFADYFTTPNNPAYVFEV 180
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
248-414 |
1.51e-34 |
|
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: 130.35 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEA---GYSSEDSIIGVTEPRRVAAVAMSQRVAKEMnlSHRV 324
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqGPPLPVANIICTQPRRISAISVAERVAQER--AERV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 325 ---VSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLL 401
Cdd:cd17985 79 gqsVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPD----LKVI 154
|
170
....*....|...
gi 1039770916 402 IMSATLRVEDFTQ 414
Cdd:cd17985 155 LMSATLNAELFSD 167
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
248-428 |
2.56e-33 |
|
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: 126.87 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSI-IGVTEPRRVAAVAMSQRVAKEMNLS-HRVV 325
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIPCrIFCTQPRRLAAIAVAERVAAERGEKiGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 326 SYQIRYEGNVTEETRIKFMTDGVLLKEIQ-KDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIValraKRHLPLKLLIMS 404
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDIL----QKHPNLKLILSS 156
|
170 180
....*....|....*....|....
gi 1039770916 405 ATLRVEDFTqnqRLFTTpPPVIKV 428
Cdd:cd17987 157 AALDVNLFI---RYFGS-CPVIYI 176
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
248-428 |
4.56e-33 |
|
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: 126.06 E-value: 4.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIgVTEPRRVAAVAMSQRVAKEM--NLS 321
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEdyvlRGRGARCNVV-ITQPRRISAVSVAQRVAHELgpNLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 322 HRvVSYQIRYEGNVTEE-TRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKL 400
Cdd:cd17976 80 RN-VGYQVRLESRPPPRgGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPE----LRV 154
|
170 180
....*....|....*....|....*...
gi 1039770916 401 LIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17976 155 VLMSATGDNQRLSR----YFGGCPVVRV 178
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
248-410 |
1.56e-30 |
|
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: 118.97 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLS-HRVVS 326
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKII-VLEPRRVAARAAARRLATLLGEApGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRivaLRAKRHLPLKLLIMSAT 406
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLE---VQQLLRDDLRLLAMSAT 156
|
....
gi 1039770916 407 LRVE 410
Cdd:cd17990 157 LDGD 160
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
730-851 |
3.68e-29 |
|
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: 112.33 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 730 AEELLVALGALQAPPKqermkklqmsqlscpITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMTVRELFEEL 809
Cdd:pfam04408 1 ALELLYYLGALDEDGE---------------LTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQP 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039770916 810 DRPAASEKELAELKGRRARVAQMKRTWAGQGpslKLGDLMVL 851
Cdd:pfam04408 66 NFLDPRSAAKAARRRRRAADEKARAKFARLD---LEGDHLTL 104
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
248-405 |
6.48e-29 |
|
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: 114.15 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSS--EDSIIGVTEPRRVAAVAMSQRVAKEM--NLSHR 323
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEYCLSAhyQHGVVVCTQVHKQTAVWLALRVADEMdvNIGHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 324 VvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLIM 403
Cdd:cd17977 81 V-GYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPE----LKLVII 155
|
..
gi 1039770916 404 SA 405
Cdd:cd17977 156 TC 157
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
243-428 |
1.15e-28 |
|
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: 115.32 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 243 EERLKLPILAEEQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE----AGYSSEDSIIgVTEPRRVAAVAMSQRVAKEM 318
Cdd:cd17972 54 QERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDdfiqNDRAAECNIV-VTQPRRISAVSVAERVAFER 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 319 NLS-HRVVSYQIRYEGNVTE-ETRIKFMTDGVLLKEIQKDFLLLKYkvVIIDEAHERSVYTDILLGLLSRIValraKRHL 396
Cdd:cd17972 133 GEEvGKSCGYSVRFESVLPRpHASILFCTVGVLLRKLEAGIRGISH--VIVDEIHERDINTDFLLVVLRDVV----QAYP 206
|
170 180 190
....*....|....*....|....*....|..
gi 1039770916 397 PLKLLIMSATLRVEDFTQnqrlFTTPPPVIKV 428
Cdd:cd17972 207 DLRVILMSATIDTSMFCE----YFFNCPVIEV 234
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
254-414 |
2.37e-25 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 104.88 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 254 EQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSHRVV-------S 326
Cdd:smart00487 14 KEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVvglyggdS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 327 YQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLL-KYKVVIIDEAHERS--VYTDILLGLLSRivaLRAKRHlplkLLIM 403
Cdd:smart00487 94 KREQLRKLESGKTDILVTTPGRLLDLLENDKLSLsNVDLVILDEAHRLLdgGFGDQLEKLLKL---LPKNVQ----LLLL 166
|
170
....*....|...
gi 1039770916 404 SATL--RVEDFTQ 414
Cdd:smart00487 167 SATPpeEIENLLE 179
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
248-428 |
3.59e-25 |
|
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: 103.44 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 248 LPILAEEQAIMEAV-AEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDS--IIGVTEPRRVAAVAMSQRVAKEM--NLSH 322
Cdd:cd17986 1 LPIWAAKFTFLEQLeSPSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQkgQVTVTQPHPLAARSLALRVADEMdlNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 323 RVvSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlpLKLLI 402
Cdd:cd17986 81 EV-GYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPE----LRVVV 155
|
170 180
....*....|....*....|....*.
gi 1039770916 403 MSATLRVEDFtqnqRLFTTPPPVIKV 428
Cdd:cd17986 156 VTSPALEPKL----RAFWGNPPVVHV 177
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
918-1004 |
3.11e-22 |
|
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: 91.55 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 918 LRQIMAAGLGDHLARRvqsedllDPKWKNaYKTPLLDDPVFIHPSSVLFKEL---PEFVVYQEIVETTKMYMKGVSTVEI 994
Cdd:pfam07717 1 LRAALAAGLYPNVARR-------DPKGKG-YTTLSDNQRVFIHPSSVLFNEKtfpPEWVVYQELVETTKVYIRTVTAISP 72
|
90
....*....|
gi 1039770916 995 QWIPSLLPSY 1004
Cdd:pfam07717 73 EWLLLFAPHI 82
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
761-852 |
2.86e-15 |
|
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: 71.92 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 761 ITALGRTMSTFPVAPRYAKMLALSQQHGCLPYTIAIVAAMTVRELFEeldrpaasekelaelKGRRARVAQMKRTWAGQG 840
Cdd:smart00847 11 LTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPRP---------------KEKREDADAARRRFADPE 75
|
90
....*....|..
gi 1039770916 841 pslklGDLMVLL 852
Cdd:smart00847 76 -----SDHLTLL 82
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
578-667 |
9.94e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.84 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 578 SLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGkvkkryydrvtgvssfrvTWVSQAS 657
Cdd:smart00490 9 ELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------------LPWSPAS 70
|
90
....*....|
gi 1039770916 658 ADQRAGRAGR 667
Cdd:smart00490 71 YIQRIGRAGR 80
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
581-667 |
2.57e-09 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 55.68 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 581 LHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDcgkvkkryYDRVTGVSSFRvtwvsqasadQ 660
Cdd:pfam00271 39 IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVIN--------YDLPWNPASYI----------Q 100
|
....*..
gi 1039770916 661 RAGRAGR 667
Cdd:pfam00271 101 RIGRAGR 107
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
254-407 |
8.00e-09 |
|
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: 56.10 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 254 EQAIMEAVAEHPiVIVCGETGSGKTT--QVPqFLYEAGYSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSHRVVSY---- 327
Cdd:pfam00270 5 AEAIPAILEGRD-VLVQAPTGSGKTLafLLP-ALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASllgg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 328 -QIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLKYKVVIIDEAHErsvytdiLLGLLSRIVALRAKRHLPLK--LLIMS 404
Cdd:pfam00270 83 dSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHR-------LLDMGFGPDLEEILRRLPKKrqILLLS 155
|
...
gi 1039770916 405 ATL 407
Cdd:pfam00270 156 ATL 158
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
267-406 |
1.28e-08 |
|
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: 55.10 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 267 VIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRVAKEMNLSHRV------VSYQIRYEgNVTEETR 340
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKALALQTAERLRELFGPGIRVavlvggSSAEEREK-NKLGDAD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770916 341 IKFMTDGVLLKEIQKD--FLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKrhlPLKLLIMSAT 406
Cdd:cd00046 82 IIIATPDMLLNLLLREdrLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLK---NAQVILLSAT 146
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
254-678 |
2.21e-05 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 48.82 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 254 EQAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYE-----AGYSSEDSIIGVTEPR-------RVAAV-AMSQRVAKEM-- 318
Cdd:PHA02653 169 QLKIFEAWISRKPVVLTGGTGVGKTSQVPKLLLWfnylfGGFDNLDKIDPNFIERpivlslpRVALVrLHSITLLKSLgf 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 319 -NLSHRVVSyqIRYeGNVTEETR-IKFMTDGVLLK----EIQKdflLLKYKVVIIDEAHERSVYTDILlgllsrIVALRA 392
Cdd:PHA02653 249 dEIDGSPIS--LKY-GSIPDELInTNPKPYGLVFSthklTLNK---LFDYGTVIIDEVHEHDQIGDII------IAVARK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 393 KRHLPLKLLIMSATLrvEDFTQNQRLFTTPPPVIKVE-SRQFPVTVHF--NKRTPLDDYS-GECFRK-VCKIHRML--PA 465
Cdd:PHA02653 317 HIDKIRSLFLMTATL--EDDRDRIKEFFPNPAFVHIPgGTLFPISEVYvkNKYNPKNKRAyIEEEKKnIVTALKKYtpPK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 466 G--GIlVFLTGQAEVHALCRRLRKAFPfrcsqpqekeedsaegmrrfkksrtrarkaqamalpqiNLDNYSVLpagegde 543
Cdd:PHA02653 395 GssGI-VFVASVSQCEEYKKYLEKRLP--------------------------------------IYDFYIIH------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 544 dreaemddeeealGSDLDLD--LGDSEANEGeqpdaslpLHVLplysllapekqaqvfkpppegtrlcvVATNVAETSLT 621
Cdd:PHA02653 429 -------------GKVPNIDeiLEKVYSSKN--------PSII--------------------------ISTPYLESSVT 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770916 622 IPGIKYVVDCGKV--KKRYydrvTGvssfRVTWVSQASADQRAGRAGRTEPGHCYRLYS 678
Cdd:PHA02653 462 IRNATHVYDTGRVyvPEPF----GG----KEMFISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
266-434 |
9.10e-05 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 46.27 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 266 IVIVCGETGSGKTTQVPQF-LYEAGYSSEDSIIgVTEPRRVAAVAMSQR---VAKEMNLSHRVVSYQIRYEGNVTEE--- 338
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWaLHSLKSQKADRVI-IALPTRATINAMYRRakeAFGETGLYHSSILSSRIKEMGDSEEfeh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 339 --------------TRIKFMTDGVLLKEIQKDF-------LLLKYKVVIIDEAHersVYTDILLGLLsrIVALRAKRHLP 397
Cdd:cd09639 80 lfplyihsndtlflDPITVCTIDQVLKSVFGEFghyeftlASIANSLLIFDEVH---FYDEYTLALI--LAVLEVLKDND 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039770916 398 LKLLIMSATL--RVEDFTQNQRL--FTTPPPVIKVESRQFP 434
Cdd:cd09639 155 VPILLMSATLpkFLKEYAEKIGYveENEPLDLKPNERAPFI 195
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
610-670 |
2.82e-04 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 40.38 E-value: 2.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770916 610 VVATNVAETSLTIPGIKYVVDCGKVKkryydrvtgvssfrvtwvSQASADQRAGRAGRTEP 670
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPS------------------SAASYIQRVGRAGRGGK 68
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
264-412 |
5.34e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 264 HPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIGVTEPRRvaavamsqrvakemnlshrvvsYQIRYEGNVTEETRIKF 343
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDIL----------------------EEVLDQLLLIIVGGKKA 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 344 MTDGVLLKEIQKDFLL-LKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRHLPLKLLIMSATLRVEDF 412
Cdd:smart00382 60 SGSGELRLRLALALARkLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
266-407 |
7.82e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 43.21 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 266 IVIVCGETGSGKTTQVPQF-LYEAGYSSEDSIIgVTEPRRVAAVAMSQRvAKEMNLSHRVV----SYQIRYEGNVTEE-- 338
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAALLWaLHSIKSQKADRVI-IALPTRATINAMYRR-AKELFGSELVGlhhsSSFSRIKEMGDSEef 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 339 ----------------TRIKFMTDGVLLKEIQKDF-------LLLKYKVVIIDEAHersVYTDILLGLLsrIVALRAKRH 395
Cdd:TIGR01587 79 ehlfplyihsndklflDPITVCTIDQVLKSVFGEFghyeftlASIANSLLIFDEVH---FYDEYTLALI--LAVLEVLKD 153
|
170
....*....|..
gi 1039770916 396 LPLKLLIMSATL 407
Cdd:TIGR01587 154 NDVPILLMSATL 165
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
273-406 |
8.87e-04 |
|
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: 41.00 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 273 TGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRVAAVAMSQRvakemnLSHRVVSYQIryeGNVTEETR----IKFMTDGV 348
Cdd:cd17931 10 PGAGKTTRVLPQIIREAIKKRLRTL-VLAPTRVVAAEMYEA------LRGLPIRYRT---GAVKEEHGgneiVDYMCHGT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770916 349 LLKEIQKDFLLLKYKVVIIDEAHERSVYTDILLGLLSRIVALRAKRhlplkLLIMSAT 406
Cdd:cd17931 80 FTCRLLSPKRVPNYNLIIMDEAHFTDPASIAARGYIHTRVEMGEAA-----VIFMTAT 132
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
252-434 |
1.29e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 42.76 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 252 AEEQAIMEAVAEHPIVIVCGETGSGKTtqvpqflyEAGYS---------SEDSIIgVTEPRRVAAVAMSQRVAKEMNLS- 321
Cdd:COG1203 135 ALELALEAAEEEPGLFILTAPTGGGKT--------EAALLfalrlaakhGGRRII-YALPFTSIINQTYDRLRDLFGEDv 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 322 ----HRVVSYQIRYEGNVTEETRIKFMTDGVLLKEI------Q-------------KDFLLLKYKVVIIDEAHersVYTD 378
Cdd:COG1203 206 llhhSLADLDLLEEEEEYESEARWLKLLKELWDAPVvvttidQlfeslfsnrkgqeRRLHNLANSVIILDEVQ---AYPP 282
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770916 379 ILLGLLSRivALRAKRHLPLKLLIMSATL---RVEDFTQNQRLFTTPPPVIKVESRQFP 434
Cdd:COG1203 283 YMLALLLR--LLEWLKNLGGSVILMTATLpplLREELLEAYELIPDEPEELPEYFRAFV 339
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
253-387 |
1.39e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 40.62 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 253 EEQAIMEAVAEHPIVIVCGETGSGKTTQVpQFLYEAGYSSEDSIIGVTePRRVAAVAMSQRVAKEMNLSHRVVsyqirye 332
Cdd:cd17933 1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTL-KALLAALEAEGKRVVLAA-PTGKAAKRLSESTGIEASTIHRLL------- 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770916 333 gnvteetRIKFMTDGVLLKEIQkdflLLKYKVVIIDEAherS-VYTDILLGLLSRI 387
Cdd:cd17933 72 -------GINPGGGGFYYNEEN----PLDADLLIVDEA---SmVDTRLMAALLSAI 113
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
266-371 |
2.21e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.25 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 266 IVIVCGETGSGKTTQVPQFLYEAGySSEDSIIGVTEPRRVAAVAMSQRVAKEmnlshrvvsYQIRYEGNVTEETRIKFMT 345
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLP-EVRDSVVFVDLPSGTSPKDLLRALLRA---------LGLPLSGRLSKEELLAALQ 76
|
90 100
....*....|....*....|....*.
gi 1039770916 346 DgvLLKEIQKDflllkyKVVIIDEAH 371
Cdd:pfam13401 77 Q--LLLALAVA------VVLIIDEAQ 94
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
255-414 |
2.80e-03 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 39.94 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 255 QAIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGYSSEDSIIgVTEPRRvaavAMSQRvaKEMNLSHRVVSYQ---IRY 331
Cdd:cd17921 8 EALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKAV-YIAPTR----ALVNQ--KEADLRERFGPLGknvGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 332 EGNVTE------ETRIKFMT----DGVLLKEIQKDFLLLKYkvVIIDEAH-----ERSVytdILLGLLSRIvaLRAKRHl 396
Cdd:cd17921 81 TGDPSVnklllaEADILVATpeklDLLLRNGGERLIQDVRL--VVVDEAHligdgERGV---VLELLLSRL--LRINKN- 152
|
170
....*....|....*....
gi 1039770916 397 pLKLLIMSATLR-VEDFTQ 414
Cdd:cd17921 153 -ARFVGLSATLPnAEDLAE 170
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
265-407 |
5.60e-03 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 39.20 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 265 PIVIVCGETGSGKTtqvpqflyEAGY---------SSEDSIIgVTEPRRVAAVAMSQRVAKemNLSHRVVSYQIR-YEGN 334
Cdd:cd17930 2 GLVILEAPTGSGKT--------EAALlwalklaarGGKRRII-YALPTRATINQMYERIRE--ILGRLDDEDKVLlLHSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770916 335 VTEETRIKFMTDGVLLKEIQKDFLLLK---------------------------------YKVVIIDEAHERSV-YTDIL 380
Cdd:cd17930 71 AALELLESDEEPDDDPVEAVDWALLLKrswlapivvttidqllesllkykhferrlhglaNSVVVLDEVQAYDPeYMALL 150
|
170 180
....*....|....*....|....*..
gi 1039770916 381 LGLLSRIValrakRHLPLKLLIMSATL 407
Cdd:cd17930 151 LKALLELL-----GELGGPVVLMTATL 172
|
|
| |
