|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
564-1130 |
3.84e-111 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 370.18 E-value: 3.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 564 ESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmikRGLGGVANIICTQPRRISALGLADRVSDERCTSV 643
Cdd:COG1643 8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 644 GKEVGYIIRGDSRMRPGeTKITFVTTGVLLRRLQSGsgPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLP-YR 722
Cdd:COG1643 84 GETVGYRVRFEDKVSAA-TRIEVVTEGILLRELQRD--PE------LEGVDTVIFDEFHERSLNADLLLALLLDLQPaLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 723 PDIKVILMSATLDAEIFMDYFGGrekVGLVNIPGRTFPVSdyylddiVRYtgfapelaeRGLDEDVMSPPQGdeslgkll 802
Cdd:COG1643 155 PDLKLLVMSATLDAERFARLLGD---APVIESSGRTYPVE-------VRY---------RPLPADERDLEDA-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 803 rglgmginyelIASTVRYIdsqLGDQPGGILIFLPGTMEIERCLNAVRKI--PNVHPLPLHASLLPAEQKRVFLSPPKGK 880
Cdd:COG1643 208 -----------VADAVREA---LAEEPGDILVFLPGEREIRRTAEALRGRlpPDTEILPLYGRLSAAEQDRAFAPAPHGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 881 RKVIAATNVAETSITIEDVVAVIDTGRVKETSYDPKDNMVRLQEVWASQAACKQrrgragrvragsCYKLYTRKAESSMP 960
Cdd:COG1643 274 RRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQragragrlapgiCYRLWSEEDFARRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 961 QRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaSTITPPESVAVEGAIDFLHRVGALDHD-RLTALGRYLSMIPADLRCA 1039
Cdd:COG1643 354 AFTDPEILRADLASLILELAAW-GLGDPEDL--PFLDPPPARAIADARALLQELGALDADgRLTPLGRALARLPLDPRLA 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1040 KLMVYGSIFGCI-DACVtISAILTVKSPFisprdkRDEADAakasfskcdgDLLTDLAAYQQWSERtkaqgywqtqswcS 1118
Cdd:COG1643 431 RMLLAAAELGCLrEAAI-LAALLSERDPR------RGAAGS----------DLLARLNLWRRLREQ-------------Q 480
|
570
....*....|..
gi 2477806273 1119 ANFLSHQTLRDI 1130
Cdd:COG1643 481 REFLSYLRLREW 492
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
521-1261 |
2.26e-87 |
|
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: 311.32 E-value: 2.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 521 VRQSRKQSRKIdwnpgSPLGVSIREAWKARQSTTAQQEMT---RKRESLPAWKIQDAIIQAVNTHQVTIISGETGSGKST 597
Cdd:TIGR01967 23 LRKDHDQDRAI-----AALAKFRERIDAACDKVEARRQAVpeiRYPDNLPVSAKREDIAEAIAENQVVIIAGETGSGKTT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 598 QSVQFILDdmikRGLGGVANIICTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQ 677
Cdd:TIGR01967 98 QLPKICLE----LGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSS-NTLVKLMTDGILLAETQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 678 SGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMDYFGGrekVGLVNIPGR 757
Cdd:TIGR01967 173 QDR--------FLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNN---APIIEVSGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 758 TFPVSdyylddiVRYtgfapelaeRGLDEDvmsppQGDESLGKLlrglgmginyELIASTVryiDSQLGDQPGGILIFLP 837
Cdd:TIGR01967 242 TYPVE-------VRY---------RPLVEE-----QEDDDLDQL----------EAILDAV---DELFAEGPGDILIFLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 838 GTMEIERCLNAVRK--IPNVHPLPLHASLLPAEQKRVFlsPPKGKRKVIAATNVAETSITIEDVVAVIDTGRVKETSYDP 915
Cdd:TIGR01967 288 GEREIRDAAEILRKrnLRHTEILPLYARLSNKEQQRVF--QPHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 916 KDNMVRLQEVWASQAACKQRRGRAGRVRAGSCYKLYTRKAESSMPQRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaST 995
Cdd:TIGR01967 366 RTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLAL-RLGDIAAF--PF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 996 ITPPESVAVEGAIDFLHRVGALDHD----RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISPR 1071
Cdd:TIGR01967 443 IEAPDPRAIRDGFRLLEELGALDDDeaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPM 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1072 DKRDEADAAKASFSKCDGDLLTDLAAYQQWSERTKAQGYWQTQSWCSANFLSHQTLRDISSNRAQFISSLKDAGiLPVdy 1151
Cdd:TIGR01967 523 EKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFRNACRKQYLNYLRVREWQDIYRQLTQVVKELG-LKL-- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1152 sDSEPSSAwnrnngnRSLLRAIIAGAfqpqVAQISFPDKKFassvtgtveidpdartiKYFNQENGRVFIHPSSLLFSAQ 1231
Cdd:TIGR01967 600 -NEEPADY-------DAIHKALLSGL----LSQIGMKDEKH-----------------EYDGARGRKFHIFPGSPLFKKP 650
|
730 740 750
....*....|....*....|....*....|
gi 2477806273 1232 SYSGAAAYLsyftkMATSKVFIRDLTPFNP 1261
Cdd:TIGR01967 651 PKWVMAAEL-----VETSKLYARLVAKIEP 675
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
582-745 |
3.69e-79 |
|
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: 257.39 E-value: 3.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 582 HQVTIISGETGSGKSTQSVQFILDDMIKRGLGGvaNIICTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMRPgE 661
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKG--RIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSS-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 662 TKITFVTTGVLLRRLQSGsgpdgnvaGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMD 741
Cdd:cd17917 78 TRIKFCTDGILLRELLSD--------PLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSS 149
|
....
gi 2477806273 742 YFGG 745
Cdd:cd17917 150 YFGG 153
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
549-1254 |
5.99e-75 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 273.86 E-value: 5.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 549 ARQSTTAQQEMTRKR---------ESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmIKRGLGGVanII 619
Cdd:PRK11131 47 AKEIAQAAQRVLLREaarpeitypENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGL--IG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 620 CTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMrpGE-TKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVV 698
Cdd:PRK11131 123 HTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQV--SDnTMVKLMTDGILLAEIQQDR--------LLMQYDTIII 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 699 DEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMDYFGgreKVGLVNIPGRTFPVSdyylddiVRYtgfape 778
Cdd:PRK11131 193 DEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFN---NAPIIEVSGRTYPVE-------VRY------ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 779 laeRGLDEDvmsppqGDESLGKLLRGlgmginyelIASTVryidSQLGDQ-PGGILIFLPGTMEIERCLNAVRK--IPNV 855
Cdd:PRK11131 257 ---RPIVEE------ADDTERDQLQA---------IFDAV----DELGREgPGDILIFMSGEREIRDTADALNKlnLRHT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 856 HPLPLHASLLPAEQKRVFlsPPKGKRKVIAATNVAETSITIEDVVAVIDTG--RVKETSYDPKdnMVRLQEVWASQAACK 933
Cdd:PRK11131 315 EILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGtaRISRYSYRTK--VQRLPIEPISQASAN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 934 QRRGRAGRVRAGSCYKLYTRKAESSMPQRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaSTITPPESVAVEGAIDFLHR 1013
Cdd:PRK11131 391 QRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTAL-GLGDIAAF--PFVEAPDKRNIQDGVRLLEE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1014 VGALDHD------RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISPRDKRDEADAAKASFSKC 1087
Cdd:PRK11131 468 LGAITTDeqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1088 DGDLLTDLAAYQQWSERTKAQGYWQTQSWCSANFLSHQTLRDISSNRAQFISSLKDAGiLPVdysDSEPSSAwnrnngnR 1167
Cdd:PRK11131 548 ESDFLAFVNLWNYLQEQQKALSSNQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELG-IPV---NSEPAEY-------R 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1168 SLLRAIIAGAfqpqvaqISFPDKKfassvtgtveidpDARTIKYFNQENGRVFIHPSSLLFSAQSYSGAAAYLsyftkMA 1247
Cdd:PRK11131 617 EIHTALLTGL-------LSHIGMK-------------DAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAEL-----VE 671
|
....*..
gi 2477806273 1248 TSKVFIR 1254
Cdd:PRK11131 672 TSRLWGR 678
|
|
| RWD_YLR419W-like |
cd23827 |
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ... |
391-493 |
1.98e-36 |
|
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.
Pssm-ID: 467662 Cd Length: 104 Bit Score: 133.14 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 391 WVEEQDTLEAIFGERYKRLSSKVCEIKSEAPN-IPGSLSFRFQKPSaGYPSSVPVIAIQGTG-IPAYIRLSAIRQAVQFA 468
Cdd:cd23827 1 WDEEIEALEAIYGEKFEVISDDSCEITLNSPTkTKPSLKLKFYKSS-SYPNSLPGIFISSSDkLPAYIKLAIIRQLLQYA 79
|
90 100
....*....|....*....|....*
gi 2477806273 469 EENFLGESMIFNIMDWLETHLPGII 493
Cdd:cd23827 80 RDNLLGDPMIFSIVEWLEENIEEII 104
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
560-764 |
1.47e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.18 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 560 TRKRESLPAWKIQDAIIQAV-NTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVaniICTQPRRISALGLADRVSdE 638
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELK-K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 639 RCTSVGKEVGYIIRGDSRMRP------GETKITFVTTGVLLRRLQSGSgpdgnvaGSLADVTHVVVDEVHERsLDTDFLL 712
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQlrklesGKTDILVTTPGRLLDLLENDK-------LSLSNVDLVILDEAHRL-LDGGFGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2477806273 713 ALLRDVLPYRPDIKVILMSATLDAEI--FMDYFGgrekVGLVNIPGRTFPVSDY 764
Cdd:smart00487 149 QLEKLLKLLPKNVQLLLLSATPPEEIenLLELFL----NDPVFIDVGFTPLEPI 198
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
1007-1093 |
1.66e-18 |
|
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: 81.90 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1007 AIDFLHRVGALDHD-RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISP-------------RD 1072
Cdd:pfam04408 1 ALELLYYLGALDEDgELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarRR 80
|
90 100
....*....|....*....|...
gi 2477806273 1073 KRDEADAAKASFSKCD--GDLLT 1093
Cdd:pfam04408 81 RRAADEKARAKFARLDleGDHLT 103
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1170-1271 |
4.82e-15 |
|
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: 71.51 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1170 LRAIIAGAFQPQVAQIsfpdkkfassvtgtveiDPDARTIKyFNQENGRVFIHPSSLLFSAQSYsgAAAYLSYFTKMATS 1249
Cdd:pfam07717 1 LRAALAAGLYPNVARR-----------------DPKGKGYT-TLSDNQRVFIHPSSVLFNEKTF--PPEWVVYQELVETT 60
|
90 100
....*....|....*....|..
gi 2477806273 1250 KVFIRDLTPFNPYSLLLFCGSI 1271
Cdd:pfam07717 61 KVYIRTVTAISPEWLLLFAPHI 82
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
389-489 |
7.39e-14 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 68.89 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 389 DSWVEEQDTLEAIFGERYKRLSSKV-------CEIKSEAPNIPG----SLSFRFQKPSaGYPSSVPVIAIQGT-GIPAYI 456
Cdd:pfam05773 1 EEQEEELEALESIYPDEFEVISDSPyesleieIKLSLDSDESDSshlpPLVLKFTLPE-DYPDEPPKISLSSPwNLSDEQ 79
|
90 100 110
....*....|....*....|....*....|...
gi 2477806273 457 RLSAIRQAVQFAEENfLGESMIFNIMDWLETHL 489
Cdd:pfam05773 80 VLSLLEELEELAEEN-LGEVMIFELIEWLQENL 111
|
|
| RWD |
smart00591 |
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ... |
398-485 |
1.83e-04 |
|
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;
Pssm-ID: 214735 Cd Length: 107 Bit Score: 41.96 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 398 LEAIFGE--RYKRLSSKVCEIK-----SEAPNIPGSLSFRFQ-KPSAGYPSSVPVIAIQG-TGIPAYIRLSAIRQAVQFA 468
Cdd:smart00591 5 LESIYPEdfEVIDEDARIPEITiklspSSDEGEDQYVSLTLQvKLPENYPDEAPPISLLNsEGLSDEQLAELLKKLEEIA 84
|
90
....*....|....*..
gi 2477806273 469 EENfLGESMIFNIMDWL 485
Cdd:smart00591 85 EEN-LGEVMIFELVEKL 100
|
|
| DSRM_A1CF-like |
cd19872 |
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding ... |
60-136 |
1.89e-03 |
|
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding protein 46 (RBM46) and similar proteins; The family includes two dsRNA-binding motif-containing proteins, A1CF and RBM46. A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. RBM46 (also called cancer/testis antigen 68 (CT68), or RNA-binding motif protein 46) plays a novel role in the regulation of embryonic stem cell (ESC) differentiation by regulating the degradation of beta-catenin mRNA. It also regulates trophectoderm specification by stabilizing Cdx2 mRNA in early mouse embryos. Members of this family contain three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.
Pssm-ID: 380701 Cd Length: 75 Bit Score: 38.43 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 60 PVNMLAEHCQKQKWEKPEYTMMRTSDG-----YISSVILkridpktreltvlpPMKPPSshkHLAAQP-----TALEARH 129
Cdd:cd19872 2 PVQILEEICQKNGWGEPVYQLLSTSSNnevqlFIYKVTI--------------PNLPNG---RLTFQPdklcrTPEEAKV 64
|
....*..
gi 2477806273 130 FAAAYAL 136
Cdd:cd19872 65 LAAEFVL 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
564-1130 |
3.84e-111 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 370.18 E-value: 3.84e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 564 ESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmikRGLGGVANIICTQPRRISALGLADRVSDERCTSV 643
Cdd:COG1643 8 PDLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLE----LGWGAGGRIGMLEPRRLAARAAAERMAEELGEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 644 GKEVGYIIRGDSRMRPGeTKITFVTTGVLLRRLQSGsgPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLP-YR 722
Cdd:COG1643 84 GETVGYRVRFEDKVSAA-TRIEVVTEGILLRELQRD--PE------LEGVDTVIFDEFHERSLNADLLLALLLDLQPaLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 723 PDIKVILMSATLDAEIFMDYFGGrekVGLVNIPGRTFPVSdyylddiVRYtgfapelaeRGLDEDVMSPPQGdeslgkll 802
Cdd:COG1643 155 PDLKLLVMSATLDAERFARLLGD---APVIESSGRTYPVE-------VRY---------RPLPADERDLEDA-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 803 rglgmginyelIASTVRYIdsqLGDQPGGILIFLPGTMEIERCLNAVRKI--PNVHPLPLHASLLPAEQKRVFLSPPKGK 880
Cdd:COG1643 208 -----------VADAVREA---LAEEPGDILVFLPGEREIRRTAEALRGRlpPDTEILPLYGRLSAAEQDRAFAPAPHGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 881 RKVIAATNVAETSITIEDVVAVIDTGRVKETSYDPKDNMVRLQEVWASQAACKQrrgragrvragsCYKLYTRKAESSMP 960
Cdd:COG1643 274 RRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERISQASANQragragrlapgiCYRLWSEEDFARRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 961 QRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaSTITPPESVAVEGAIDFLHRVGALDHD-RLTALGRYLSMIPADLRCA 1039
Cdd:COG1643 354 AFTDPEILRADLASLILELAAW-GLGDPEDL--PFLDPPPARAIADARALLQELGALDADgRLTPLGRALARLPLDPRLA 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1040 KLMVYGSIFGCI-DACVtISAILTVKSPFisprdkRDEADAakasfskcdgDLLTDLAAYQQWSERtkaqgywqtqswcS 1118
Cdd:COG1643 431 RMLLAAAELGCLrEAAI-LAALLSERDPR------RGAAGS----------DLLARLNLWRRLREQ-------------Q 480
|
570
....*....|..
gi 2477806273 1119 ANFLSHQTLRDI 1130
Cdd:COG1643 481 REFLSYLRLREW 492
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
521-1261 |
2.26e-87 |
|
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: 311.32 E-value: 2.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 521 VRQSRKQSRKIdwnpgSPLGVSIREAWKARQSTTAQQEMT---RKRESLPAWKIQDAIIQAVNTHQVTIISGETGSGKST 597
Cdd:TIGR01967 23 LRKDHDQDRAI-----AALAKFRERIDAACDKVEARRQAVpeiRYPDNLPVSAKREDIAEAIAENQVVIIAGETGSGKTT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 598 QSVQFILDdmikRGLGGVANIICTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQ 677
Cdd:TIGR01967 98 QLPKICLE----LGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSS-NTLVKLMTDGILLAETQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 678 SGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMDYFGGrekVGLVNIPGR 757
Cdd:TIGR01967 173 QDR--------FLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNN---APIIEVSGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 758 TFPVSdyylddiVRYtgfapelaeRGLDEDvmsppQGDESLGKLlrglgmginyELIASTVryiDSQLGDQPGGILIFLP 837
Cdd:TIGR01967 242 TYPVE-------VRY---------RPLVEE-----QEDDDLDQL----------EAILDAV---DELFAEGPGDILIFLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 838 GTMEIERCLNAVRK--IPNVHPLPLHASLLPAEQKRVFlsPPKGKRKVIAATNVAETSITIEDVVAVIDTGRVKETSYDP 915
Cdd:TIGR01967 288 GEREIRDAAEILRKrnLRHTEILPLYARLSNKEQQRVF--QPHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 916 KDNMVRLQEVWASQAACKQRRGRAGRVRAGSCYKLYTRKAESSMPQRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaST 995
Cdd:TIGR01967 366 RTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDFNSRPEFTDPEILRTNLASVILQMLAL-RLGDIAAF--PF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 996 ITPPESVAVEGAIDFLHRVGALDHD----RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISPR 1071
Cdd:TIGR01967 443 IEAPDPRAIRDGFRLLEELGALDDDeaepQLTPIGRQLAQLPVDPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPM 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1072 DKRDEADAAKASFSKCDGDLLTDLAAYQQWSERTKAQGYWQTQSWCSANFLSHQTLRDISSNRAQFISSLKDAGiLPVdy 1151
Cdd:TIGR01967 523 EKQQAADQAHARFKDPRSDFLSRVNLWRHIEEQRQALSANQFRNACRKQYLNYLRVREWQDIYRQLTQVVKELG-LKL-- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1152 sDSEPSSAwnrnngnRSLLRAIIAGAfqpqVAQISFPDKKFassvtgtveidpdartiKYFNQENGRVFIHPSSLLFSAQ 1231
Cdd:TIGR01967 600 -NEEPADY-------DAIHKALLSGL----LSQIGMKDEKH-----------------EYDGARGRKFHIFPGSPLFKKP 650
|
730 740 750
....*....|....*....|....*....|
gi 2477806273 1232 SYSGAAAYLsyftkMATSKVFIRDLTPFNP 1261
Cdd:TIGR01967 651 PKWVMAAEL-----VETSKLYARLVAKIEP 675
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
582-745 |
3.69e-79 |
|
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: 257.39 E-value: 3.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 582 HQVTIISGETGSGKSTQSVQFILDDMIKRGLGGvaNIICTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMRPgE 661
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAKGGKG--RIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSS-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 662 TKITFVTTGVLLRRLQSGsgpdgnvaGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMD 741
Cdd:cd17917 78 TRIKFCTDGILLRELLSD--------PLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSS 149
|
....
gi 2477806273 742 YFGG 745
Cdd:cd17917 150 YFGG 153
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
549-1254 |
5.99e-75 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 273.86 E-value: 5.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 549 ARQSTTAQQEMTRKR---------ESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmIKRGLGGVanII 619
Cdd:PRK11131 47 AKEIAQAAQRVLLREaarpeitypENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE--LGRGVKGL--IG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 620 CTQPRRISALGLADRVSDERCTSVGKEVGYIIRGDSRMrpGE-TKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVV 698
Cdd:PRK11131 123 HTQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQV--SDnTMVKLMTDGILLAEIQQDR--------LLMQYDTIII 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 699 DEVHERSLDTDFLLALLRDVLPYRPDIKVILMSATLDAEIFMDYFGgreKVGLVNIPGRTFPVSdyylddiVRYtgfape 778
Cdd:PRK11131 193 DEAHERSLNIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFN---NAPIIEVSGRTYPVE-------VRY------ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 779 laeRGLDEDvmsppqGDESLGKLLRGlgmginyelIASTVryidSQLGDQ-PGGILIFLPGTMEIERCLNAVRK--IPNV 855
Cdd:PRK11131 257 ---RPIVEE------ADDTERDQLQA---------IFDAV----DELGREgPGDILIFMSGEREIRDTADALNKlnLRHT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 856 HPLPLHASLLPAEQKRVFlsPPKGKRKVIAATNVAETSITIEDVVAVIDTG--RVKETSYDPKdnMVRLQEVWASQAACK 933
Cdd:PRK11131 315 EILPLYARLSNSEQNRVF--QSHSGRRIVLATNVAETSLTVPGIKYVIDPGtaRISRYSYRTK--VQRLPIEPISQASAN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 934 QRRGRAGRVRAGSCYKLYTRKAESSMPQRPEPEIRRVPLEQLCLSVKAMkGIDDVATFlaSTITPPESVAVEGAIDFLHR 1013
Cdd:PRK11131 391 QRKGRCGRVSEGICIRLYSEDDFLSRPEFTDPEILRTNLASVILQMTAL-GLGDIAAF--PFVEAPDKRNIQDGVRLLEE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1014 VGALDHD------RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISPRDKRDEADAAKASFSKC 1087
Cdd:PRK11131 468 LGAITTDeqasayKLTPLGRQLAQLPVDPRLARMVLEAQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1088 DGDLLTDLAAYQQWSERTKAQGYWQTQSWCSANFLSHQTLRDISSNRAQFISSLKDAGiLPVdysDSEPSSAwnrnngnR 1167
Cdd:PRK11131 548 ESDFLAFVNLWNYLQEQQKALSSNQFRRLCRTDYLNYLRVREWQDIYTQLRQVVKELG-IPV---NSEPAEY-------R 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1168 SLLRAIIAGAfqpqvaqISFPDKKfassvtgtveidpDARTIKYFNQENGRVFIHPSSLLFSAQSYSGAAAYLsyftkMA 1247
Cdd:PRK11131 617 EIHTALLTGL-------LSHIGMK-------------DAEKQEYTGARNARFSIFPGSGLFKKPPKWVMVAEL-----VE 671
|
....*..
gi 2477806273 1248 TSKVFIR 1254
Cdd:PRK11131 672 TSRLWGR 678
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
566-1066 |
9.42e-69 |
|
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273901 [Multi-domain] Cd Length: 819 Bit Score: 248.91 E-value: 9.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmiKRGLGGvaNIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLD---APGIGG--KIIMLEPRRLAARSAAQRLASQLGEAVGQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSGPDGnvagsladVTHVVVDEVHERSLDTDFLLALLRDVLP-YRPD 724
Cdd:TIGR01970 76 TVGYRVRGENKVSR-RTRLEVVTEGILTRMIQDDPELDG--------VGALIFDEFHERSLDADLGLALALDVQSsLRED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 725 IKVILMSATLDAEI---FMDYfggrekVGLVNIPGRTFPVSdyylddiVRYTGFAPElaERGLDEdvmsppqgdeslgkl 801
Cdd:TIGR01970 147 LKILAMSATLDGERlssLLPD------APVVESEGRSFPVE-------IRYLPLRGD--QRLEDA--------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 802 lrglgmginyeliasTVRYIDSQLGDQPGGILIFLPGTMEIERCLNAV--RKIPNVHPLPLHASLLPAEQKRVFLSPPKG 879
Cdd:TIGR01970 197 ---------------VSRAVEHALASETGSILVFLPGQAEIRRVQEQLaeRLDSDVLICPLYGELSLAAQDRAIKPDPQG 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 880 KRKVIAATNVAETSITIEDVVAVIDTGRVKETSYDPKDNMVRLQEVWASQAACKQRRGRAGRVRAGSCYKLYTRKAESSM 959
Cdd:TIGR01970 262 RRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQRL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 960 PQRPEPEIRRVPLEQLCLSVkAMKGIDDVATFlaSTITPPESVAVEGAIDFLHRVGALD-HDRLTALGRYLSMIPADLRC 1038
Cdd:TIGR01970 342 PAQDEPEILQADLSGLALEL-AQWGAKDPSDL--RWLDAPPSVALAAARQLLQRLGALDaQGRLTAHGKAMAALGCHPRL 418
|
490 500
....*....|....*....|....*...
gi 2477806273 1039 AKLMVYGSIFGCIDACVTISAILTVKSP 1066
Cdd:TIGR01970 419 AAMLLSAHSTGLAALACDLAALLEERGL 446
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
566-744 |
1.25e-67 |
|
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: 225.49 E-value: 1.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANIICTQPRRISALGLADRVSDERCTSV-- 643
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCRIVCTQPRRISAISVAERVAAERAESCgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 644 GKEVGYIIRGDSRMRPGETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRP 723
Cdd:cd17981 81 GNSTGYQIRLESRKPRKQGSILYCTTGIVLQWLQSDP--------HLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRS 152
|
170 180
....*....|....*....|.
gi 2477806273 724 DIKVILMSATLDAEIFMDYFG 744
Cdd:cd17981 153 DLKVILMSATLNAEKFSDYFN 173
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
566-745 |
1.23e-63 |
|
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: 213.93 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSrMRPGETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17985 81 SVGYQIRLES-VKSSATRLLYCTTGVLLRRLEGDP--------TLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDL 151
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17985 152 KVILMSATLNAELFSDYFNS 171
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
550-744 |
6.05e-61 |
|
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: 208.53 E-value: 6.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 550 RQSTTAQQEMTRKRESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANIICTQPRRISAL 629
Cdd:cd17972 43 REQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRAAECNIVVTQPRRISAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 630 GLADRVSDERCTSVGKEVGYIIRGDSRMRPGETKITFVTTGVLLRRLQSGsgpdgnvagsLADVTHVVVDEVHERSLDTD 709
Cdd:cd17972 123 SVAERVAFERGEEVGKSCGYSVRFESVLPRPHASILFCTVGVLLRKLEAG----------IRGISHVIVDEIHERDINTD 192
|
170 180 190
....*....|....*....|....*....|....*
gi 2477806273 710 FLLALLRDVLPYRPDIKVILMSATLDAEIFMDYFG 744
Cdd:cd17972 193 FLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFF 227
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
566-745 |
2.84e-56 |
|
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: 192.74 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGgvANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIP--CRIFCTQPRRLAAIAVAERVAAERGEKIGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSGpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17987 79 TVGYQIRLESRVSP-KTLLTFCTNGVLLRTLMAGDS-------ALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNL 150
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17987 151 KLILSSAALDVNLFIRYFGS 170
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
565-1046 |
4.81e-54 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 204.00 E-value: 4.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 565 SLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQsvqFILDDMIKRGLGGvaNIICTQPRRISALGLADRVSDERCTSVG 644
Cdd:PRK11664 3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTW---LPLQLLQHGGING--KIIMLEPRRLAARNVAQRLAEQLGEKPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 645 KEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGsgPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDV---Lpy 721
Cdd:PRK11664 78 ETVGYRMRAESKVGP-NTRLEVVTEGILTRMIQRD--PE------LSGVGLVILDEFHERSLQADLALALLLDVqqgL-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 722 RPDIKVILMSATLDAEifmdyfggREKVGLVNIP-----GRTFPVSDYYLDdivrytgfapelaergldedvmsppqgde 796
Cdd:PRK11664 147 RDDLKLLIMSATLDND--------RLQQLLPDAPvivseGRSFPVERRYQP----------------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 797 slgkllrglgMGINYELIASTVRYIDSQLGDQPGGILIFLPGTMEIERCLNAVR-KIP-NVHPLPLHASLLPAEQKRVFL 874
Cdd:PRK11664 190 ----------LPAHQRFDEAVARATAELLRQESGSLLLFLPGVGEIQRVQEQLAsRVAsDVLLCPLYGALSLAEQQKAIL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 875 SPPKGKRKVIAATNVAETSITIEDVVAVIDTGRVKETSYDPKDNMVRLQEVWASQAACKQRRGRAGRVRAGSCYKLYTRK 954
Cdd:PRK11664 260 PAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 955 AESSMPQRPEPEIRRVPLEQLCLSVkAMKGIDDVATFlaSTITPPESVAVEGAIDFLHRVGALD-HDRLTALGRYLSMIP 1033
Cdd:PRK11664 340 QAERAAAQSEPEILHSDLSGLLLEL-LQWGCHDPAQL--SWLDQPPAAALAAAKRLLQQLGALDgQGRLTARGRKMAALG 416
|
490
....*....|...
gi 2477806273 1034 ADLRCAKLMVYGS 1046
Cdd:PRK11664 417 NDPRLAAMLVAAK 429
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
759-934 |
1.32e-53 |
|
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: 185.04 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 759 FPVSDYYLDDIVRYTGFAPELAERgldedvmsppqgdeslgkllrglgmgINYELIASTVRYIDSQLGdqPGGILIFLPG 838
Cdd:cd18791 1 FPVEVYYLEDILELLGISSEKEDP--------------------------DYVDAAVRLILQIHRTEE--PGDILVFLPG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 839 TMEIERCLNAVRKI------PNVHPLPLHASLLPAEQKRVFLSPPKGKRKVIAATNVAETSITIEDVVAVIDTGRVKETS 912
Cdd:cd18791 53 QEEIERLCELLREEllspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKV 132
|
170 180
....*....|....*....|..
gi 2477806273 913 YDPKDNMVRLQEVWASQAACKQ 934
Cdd:cd18791 133 YDPRTGLSSLVTVWISKASAEQ 154
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
566-745 |
1.29e-52 |
|
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: 182.30 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCNVVITQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPGETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17976 81 NVGYQVRLESRPPPRGGALLFCTVGVLLKKLQSNP--------RLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPEL 152
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17976 153 RVVLMSATGDNQRLSRYFGG 172
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
566-743 |
2.25e-50 |
|
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: 176.26 E-value: 2.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMI-KRGLGGVANIICTQPRRISALGLADRVSDERCTSVG 644
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLlNGGTAQKCNIVCTQPRRISAMSLATRVCEELGCESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 645 -----KEVGYIIRGDSRMrpGE-TKITFVTTGVLLRRLQSGsgpdgnvaGSLADVTHVVVDEVHERSLDTDFLLALLRDV 718
Cdd:cd17975 81 pggknSLCGYQIRMESRT--GEaTRLLYCTTGVLLRKLQED--------GLLSSISHIIVDEVHERSVQSDFLLIILKEI 150
|
170 180
....*....|....*....|....*
gi 2477806273 719 LPYRPDIKVILMSATLDAEIFMDYF 743
Cdd:cd17975 151 LHKRSDLHLILMSATVDCEKFSSYF 175
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
566-745 |
3.42e-48 |
|
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: 169.55 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmikrglGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLA-------AGFRHIACTQPRRIACISLAKRVAFESLNQYGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDsRMRPGETKITFVTTGVLLRRLQsgsgpdgnVAGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17979 74 KVAYQIRFE-RTRTLATKLLFLTEGLLLRQIQ--------RDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDL 144
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17979 145 KLILMSATINIELFSGYFEG 164
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
557-743 |
1.46e-45 |
|
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: 162.58 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 557 QEMTRKRESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLG-GVAniiCTQPRRISALGLADRV 635
Cdd:cd17973 4 FEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPKkLVA---CTQPRRVAAMSVAQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 636 SDERCTSVGKEVGYIIRGDSRMRPgETKITFVTTGVLLRrlQSGSGPDgnvagsLADVTHVVVDEVHERSLDTDFLLALL 715
Cdd:cd17973 81 AEEMDVKLGEEVGYSIRFEDCSSA-KTILKYMTDGMLLR--EAMSDPL------LSRYSVIILDEAHERTLATDILMGLL 151
|
170 180
....*....|....*....|....*...
gi 2477806273 716 RDVLPYRPDIKVILMSATLDAEIFMDYF 743
Cdd:cd17973 152 KEVVRRRPDLKLIVMSATLDAGKFQKYF 179
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
566-744 |
2.86e-45 |
|
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: 161.52 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLggVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRGK--YCNIVVTQPRRIAAISIARRVSQEREWTLGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIrGDSRMRPGETKITFVTTGVLLRRLQSgsgpdgnvAGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPD- 724
Cdd:cd17988 79 LVGYQV-GLERPASEETRLIYCTTGVLLQKLIN--------NKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRh 149
|
170 180
....*....|....*....|
gi 2477806273 725 IKVILMSATLDAEIFMDYFG 744
Cdd:cd17988 150 VKIILMSATISCKEFADYFT 169
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
566-745 |
3.15e-45 |
|
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: 161.37 E-value: 3.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRglGGVANIicTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFAR--GGMIGI--TQPRRVAAVSVAKRVAEEMGVELGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYR--- 722
Cdd:cd17978 77 LVGYSVRFDDVTSE-ETRIKYMTDGMLLREAIGDP--------LLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeq 147
|
170 180
....*....|....*....|....*
gi 2477806273 723 --PDIKVILMSATLDAEIFMDYFGG 745
Cdd:cd17978 148 klSPLKVIIMSATLDADLFSEYFNG 172
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
562-743 |
4.29e-44 |
|
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: 158.03 E-value: 4.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 562 KRESLPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFilddMIKRGLGGVANIICTQPRRISALGLADRVSDERCT 641
Cdd:cd17971 2 QRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQY----LAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 642 SVGKEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQsgsgpdgnVAGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPY 721
Cdd:cd17971 78 CLGQEVGYTIRFEDCTSP-ETVIKYMTDGMLLRECL--------IDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQK 148
|
170 180
....*....|....*....|..
gi 2477806273 722 RPDIKVILMSATLDAEIFMDYF 743
Cdd:cd17971 149 RPDLKLIVTSATLDAVKFSQYF 170
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
566-743 |
1.30e-43 |
|
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: 156.51 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVAniiCTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGGKIG---CTQPRRVAAMSVAARVAEEMGVKLGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGsgPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17974 78 EVGYSIRFEDCTSE-KTVLKYMTDGMLLREFLTE--PD------LASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDL 148
|
170
....*....|....*...
gi 2477806273 726 KVILMSATLDAEIFMDYF 743
Cdd:cd17974 149 KLLISSATMDAEKFSAFF 166
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
566-743 |
3.03e-43 |
|
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: 155.70 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGlGGVanIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAG-GRV--VGCTQPRRVAAVTVAGRVAEEMGAVLGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPGETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17980 78 EVGYCIRFDDCTDPQATRIKFLTDGMLVREMMLDP--------LLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDL 149
|
170
....*....|....*...
gi 2477806273 726 KVILMSATLDAEIFMDYF 743
Cdd:cd17980 150 RLIVASATLDAEKFRDFF 167
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
566-745 |
7.68e-43 |
|
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: 154.16 E-value: 7.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDmikrGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHED----GYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRrlQSGSGPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17983 77 EVGYAIRFEDCTSE-NTVIKYMTDGILLR--ESLRDPD------LDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDL 147
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17983 148 KLIVTSATMDADKFADFFGN 167
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
566-745 |
4.94e-40 |
|
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: 146.06 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDdmikRGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE----LGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPDI 725
Cdd:cd17989 77 AVGYKVRFTDQTSD-ETCVKLMTDGILLAETQTDR--------YLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDL 147
|
170 180
....*....|....*....|
gi 2477806273 726 KVILMSATLDAEIFMDYFGG 745
Cdd:cd17989 148 KVIITSATIDAERFSRHFNN 167
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
566-745 |
3.58e-37 |
|
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: 137.85 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTqsvqFILDDMIKRGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTT----RVPLALLAELWIAGGKIIVLEPRRVAARAAARRLATLLGEAPGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGsgPDgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLP-YRPD 724
Cdd:cd17990 77 TVGYRVRGESRVGR-RTRVEVVTEGVLLRRLQRD--PE------LSGVGAVILDEFHERSLDADLALALLLEVQQlLRDD 147
|
170 180
....*....|....*....|.
gi 2477806273 725 IKVILMSATLDAEIFMDYFGG 745
Cdd:cd17990 148 LRLLAMSATLDGDGLAALLPE 168
|
|
| RWD_YLR419W-like |
cd23827 |
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ... |
391-493 |
1.98e-36 |
|
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.
Pssm-ID: 467662 Cd Length: 104 Bit Score: 133.14 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 391 WVEEQDTLEAIFGERYKRLSSKVCEIKSEAPN-IPGSLSFRFQKPSaGYPSSVPVIAIQGTG-IPAYIRLSAIRQAVQFA 468
Cdd:cd23827 1 WDEEIEALEAIYGEKFEVISDDSCEITLNSPTkTKPSLKLKFYKSS-SYPNSLPGIFISSSDkLPAYIKLAIIRQLLQYA 79
|
90 100
....*....|....*....|....*
gi 2477806273 469 EENFLGESMIFNIMDWLETHLPGII 493
Cdd:cd23827 80 RDNLLGDPMIFSIVEWLEENIEEII 104
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
566-741 |
3.08e-35 |
|
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: 133.25 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANII-CTQPRRISALGLADRVSDErCTSVG 644
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPESDNPGMIgITQPRRVAAVSMAKRVAEE-LNVFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 645 KEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPD 724
Cdd:cd17982 80 KEVSYQIRYDSTVSE-NTKIKFMTDGVLLKEIQTDF--------LLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAK 150
|
170 180
....*....|....*....|....*..
gi 2477806273 725 ----------IKVILMSATLDAEIFMD 741
Cdd:cd17982 151 lylqdqtvkpLKLVIMSATLRVEDFTE 177
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
566-744 |
4.07e-30 |
|
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: 118.03 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFilddMIKRGLGGVANIICTQPRRISALGLADRVSDERCTSVGK 645
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKY----LYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 646 EVGYIIRGDSrMRPGETKITFVTTGVLLRRLQSGSgpdgnvagSLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRP-- 723
Cdd:cd17984 77 KVGYQVRFDD-CSSKETAIKYMTDGCLLRHILADP--------NLTKYSVIILDEAHERSLTTDILFGLLKKLFQEKSpn 147
|
170 180
....*....|....*....|....
gi 2477806273 724 ---DIKVILMSATLDAEIFMDYFG 744
Cdd:cd17984 148 rkeHLKVVVMSATLELAKLSAFFG 171
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
566-744 |
3.71e-26 |
|
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: 106.45 E-value: 3.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQ----FILDDMIKRGLggvanIICTQPRRISALGLADRVSDERCT 641
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQwcaeYCLSAHYQHGV-----VVCTQVHKQTAVWLALRVADEMDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 642 SVGKEVGYIIRGDSRMrPGETKITFVTTGVLLRRLQSgsgpdgnvAGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPY 721
Cdd:cd17977 76 NIGHEVGYVIPFENCC-TNETILRYCTDDMLLREMMS--------DPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLS 146
|
170 180
....*....|....*....|...
gi 2477806273 722 RPDIKVILMSATLDAEIFMDYFG 744
Cdd:cd17977 147 RPELKLVIITCPHLSSKLLSYYG 169
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
560-764 |
1.47e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.18 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 560 TRKRESLPAWKIQDAIIQAV-NTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVaniICTQPRRISALGLADRVSdE 638
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRV---LVLVPTRELAEQWAEELK-K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 639 RCTSVGKEVGYIIRGDSRMRP------GETKITFVTTGVLLRRLQSGSgpdgnvaGSLADVTHVVVDEVHERsLDTDFLL 712
Cdd:smart00487 77 LGPSLGLKVVGLYGGDSKREQlrklesGKTDILVTTPGRLLDLLENDK-------LSLSNVDLVILDEAHRL-LDGGFGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2477806273 713 ALLRDVLPYRPDIKVILMSATLDAEI--FMDYFGgrekVGLVNIPGRTFPVSDY 764
Cdd:smart00487 149 QLEKLLKLLPKNVQLLLLSATPPEEIenLLELFL----NDPVFIDVGFTPLEPI 198
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
1015-1095 |
1.77e-20 |
|
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: 86.94 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1015 GALDHD-RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFisPRDKRDEADAAKASFSKCDGDLLT 1093
Cdd:smart00847 3 GALDDDgRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHLT 80
|
..
gi 2477806273 1094 DL 1095
Cdd:smart00847 81 LL 82
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
566-732 |
1.13e-19 |
|
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: 88.03 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 566 LPAWKIQDAIIQAVNTHQ-VTIISGETGSGKSTQSVQFILDDMIKRGLGgVANIICTQPRRISALGLADRVSDERCTSVG 644
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSRGFQ-KGQVTVTQPHPLAARSLALRVADEMDLNLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 645 KEVGYIIRGDSRMRPgETKITFVTTGVLLRRLQSGSGpdgnvagsLADVTHVVVDEVHERSLDTDFLLALLRDVLPYRPD 724
Cdd:cd17986 80 HEVGYSIPQEDCTGP-NTILRFCWDRLLLQEMTSTPL--------LGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPE 150
|
....*...
gi 2477806273 725 IKVILMSA 732
Cdd:cd17986 151 LRVVVVTS 158
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
1007-1093 |
1.66e-18 |
|
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: 81.90 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1007 AIDFLHRVGALDHD-RLTALGRYLSMIPADLRCAKLMVYGSIFGCIDACVTISAILTVKSPFISP-------------RD 1072
Cdd:pfam04408 1 ALELLYYLGALDEDgELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarRR 80
|
90 100
....*....|....*....|...
gi 2477806273 1073 KRDEADAAKASFSKCD--GDLLT 1093
Cdd:pfam04408 81 RRAADEKARAKFARLDleGDHLT 103
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
585-733 |
2.95e-17 |
|
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: 80.14 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 585 TIISGETGSGKSTQSVQFILDDMIKRGLGGVanIICtqPRRISALGLADRVSDERctSVGKEVGYIIRGDS-----RMRP 659
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGKKVL--VLV--PTKALALQTAERLRELF--GPGIRVAVLVGGSSaeereKNKL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2477806273 660 GETKITFVTTGVLLRRLQSgsgpdgNVAGSLADVTHVVVDEVHERSLDTDFLLALLRDVLPY-RPDIKVILMSAT 733
Cdd:cd00046 78 GDADIIIATPDMLLNLLLR------EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAgLKNAQVILLSAT 146
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1170-1271 |
4.82e-15 |
|
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: 71.51 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 1170 LRAIIAGAFQPQVAQIsfpdkkfassvtgtveiDPDARTIKyFNQENGRVFIHPSSLLFSAQSYsgAAAYLSYFTKMATS 1249
Cdd:pfam07717 1 LRAALAAGLYPNVARR-----------------DPKGKGYT-TLSDNQRVFIHPSSVLFNEKTF--PPEWVVYQELVETT 60
|
90 100
....*....|....*....|..
gi 2477806273 1250 KVFIRDLTPFNPYSLLLFCGSI 1271
Cdd:pfam07717 61 KVYIRTVTAISPEWLLLFAPHI 82
|
|
| RWD |
pfam05773 |
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ... |
389-489 |
7.39e-14 |
|
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.
Pssm-ID: 399058 Cd Length: 111 Bit Score: 68.89 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 389 DSWVEEQDTLEAIFGERYKRLSSKV-------CEIKSEAPNIPG----SLSFRFQKPSaGYPSSVPVIAIQGT-GIPAYI 456
Cdd:pfam05773 1 EEQEEELEALESIYPDEFEVISDSPyesleieIKLSLDSDESDSshlpPLVLKFTLPE-DYPDEPPKISLSSPwNLSDEQ 79
|
90 100 110
....*....|....*....|....*....|...
gi 2477806273 457 RLSAIRQAVQFAEENfLGESMIFNIMDWLETHL 489
Cdd:pfam05773 80 VLSLLEELEELAEEN-LGEVMIFELIEWLQENL 111
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
569-738 |
3.99e-12 |
|
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: 65.73 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 569 WKIQDAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGLGGVANIICtqPRRISALGLADRVSdERCTSVGKEVG 648
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLA--PTRELAEQIYEELK-KLGKGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 649 YIIRGDSRM----RPGETKITFVTTGVLLRRLQSgsgpdgnvAGSLADVTHVVVDEVHeRSLDTDF---LLALLRDVlpy 721
Cdd:pfam00270 78 SLLGGDSRKeqleKLKGPDILVGTPGRLLDLLQE--------RKLLKNLKLLVLDEAH-RLLDMGFgpdLEEILRRL--- 145
|
170
....*....|....*..
gi 2477806273 722 RPDIKVILMSATLDAEI 738
Cdd:pfam00270 146 PKKRQILLLSATLPRNL 162
|
|
| RWD_DRWD_ELF-like |
cd11605 |
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ... |
398-485 |
7.12e-11 |
|
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.
Pssm-ID: 467641 Cd Length: 94 Bit Score: 59.89 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 398 LEAIFGERYKRLSSK-----VCEIKSEAPNIPGSLSFRFQKPSAGYPSSVPVIAIQGTGIPAYIRLSAIRQAVQFAEENF 472
Cdd:cd11605 2 LESIYGDELEVLSDDsplrfSIRLSPEEEEDDPPLELEFTLPPGYPPEEPPLITLRSPKLSSAERLSLLKLELEEAAEEN 81
|
90
....*....|...
gi 2477806273 473 LGESMIFNIMDWL 485
Cdd:cd11605 82 LGEPMLFDLVEAL 94
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
818-922 |
2.09e-09 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 56.45 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 818 VRYIDSQLGDQPGG-ILIFLPGTMEIErcLNAVRKIPNVHPLPLHASLLPAEQKRVFLSPPKGKRKVIAATNVAETSITI 896
Cdd:pfam00271 3 LEALLELLKKERGGkVLIFSQTKKTLE--AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*.
gi 2477806273 897 EDVVAVIDtgrvketsYDPKDNMVRL 922
Cdd:pfam00271 81 PDVDLVIN--------YDLPWNPASY 98
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
858-906 |
8.86e-08 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 50.67 E-value: 8.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2477806273 858 LPLHASLLPAEQKRVFLSPPKGKRKVIAATNVAETSITIEDVVAVIDTG 906
Cdd:smart00490 15 ARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD 63
|
|
| RWD_RWDD3 |
cd23819 |
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ... |
393-489 |
3.74e-06 |
|
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.
Pssm-ID: 467655 Cd Length: 106 Bit Score: 46.93 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 393 EEQDTLEAIF---GE----RYKRLSSKVCE---IKSEAPNIPGSLSFRFQKPSaGYPSSVPVIAIQGTgipayiRLSAIR 462
Cdd:cd23819 1 DELSVLQAIFcgpGEfevlSSSETSDGVSFkiqISVEGFDEDIVLKLTFHLSP-NYPSSLPDISVSSE------QLTRAQ 73
|
90 100 110
....*....|....*....|....*....|...
gi 2477806273 463 QA------VQFAEENfLGESMIFNIMDWLETHL 489
Cdd:cd23819 74 CNdlqdslLEYANSL-LGEPMVLELVLWLQENL 105
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
688-908 |
1.46e-05 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 49.59 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 688 GSLADVTHVVVDEVHERSLDTDFLLALLRdVLPYRPDiKVILMSATL--DAEIFMDYFggrEKVGLVNIPGRT-FPVSDY 764
Cdd:PHA02653 287 NKLFDYGTVIIDEVHEHDQIGDIIIAVAR-KHIDKIR-SLFLMTATLedDRDRIKEFF---PNPAFVHIPGGTlFPISEV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 765 YLddivrytgfapelaergldEDVMSPPQgdeslgkllrglgmgiNYELIASTVRYIDSQLGD-----QPGGIlIFLPgt 839
Cdd:PHA02653 362 YV-------------------KNKYNPKN----------------KRAYIEEEKKNIVTALKKytppkGSSGI-VFVA-- 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2477806273 840 mEIERCLNAVRKIPNVHPL----PLHASLLPAEQ--KRVFLSPpkgKRKVIAATNVAETSITIEDVVAVIDTGRV 908
Cdd:PHA02653 404 -SVSQCEEYKKYLEKRLPIydfyIIHGKVPNIDEilEKVYSSK---NPSIIISTPYLESSVTIRNATHVYDTGRV 474
|
|
| RWD_GCN2 |
cd23823 |
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ... |
393-488 |
2.31e-05 |
|
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.
Pssm-ID: 467659 Cd Length: 117 Bit Score: 44.90 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 393 EEQDTLEAIFGERYKRLSSKV-------CEIK-----SEAPNIPGSLSFRFQKPsAGYPSSVPVIAIQGT-GIPaYIRLS 459
Cdd:cd23823 6 EELEALQSIYGDDFEDLSSKKavwsppeFRIRlrpqeGESEENHVSVDLHVKFP-PTYPDVPPEIELENVkGLS-DEQLE 83
|
90 100 110
....*....|....*....|....*....|....
gi 2477806273 460 AIRQAV-QFAEENfLGESMIFN----IMDWLETH 488
Cdd:cd23823 84 ELLKELeELAKEL-LGEEMIFElaeaVQEFLEEH 116
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
569-755 |
5.42e-05 |
|
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: 45.33 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 569 WKIQ-DAIIQAVNTHQVTIISGETGSGKSTQSVQFILDDMIKRGlggvANIICTQPRRisalGLADRVSD---ERCTSVG 644
Cdd:cd17921 3 NPIQrEALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG----GKAVYIAPTR----ALVNQKEAdlrERFGPLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 645 KEVGYIIrGDSRMRP---GETKItFVTT----GVLLRRLQSGSgpdgnvagsLADVTHVVVDEVH-----ERSLDTDFLL 712
Cdd:cd17921 75 KNVGLLT-GDPSVNKlllAEADI-LVATpeklDLLLRNGGERL---------IQDVRLVVVDEAHligdgERGVVLELLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2477806273 713 ALLRDVLPYrpdIKVILMSATLD-AEIFMDYFGgreKVGLVNIP 755
Cdd:cd17921 144 SRLLRINKN---ARFVGLSATLPnAEDLAEWLG---VEDLIRFD 181
|
|
| RWD |
smart00591 |
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ... |
398-485 |
1.83e-04 |
|
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;
Pssm-ID: 214735 Cd Length: 107 Bit Score: 41.96 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 398 LEAIFGE--RYKRLSSKVCEIK-----SEAPNIPGSLSFRFQ-KPSAGYPSSVPVIAIQG-TGIPAYIRLSAIRQAVQFA 468
Cdd:smart00591 5 LESIYPEdfEVIDEDARIPEITiklspSSDEGEDQYVSLTLQvKLPENYPDEAPPISLLNsEGLSDEQLAELLKKLEEIA 84
|
90
....*....|....*..
gi 2477806273 469 EENfLGESMIFNIMDWL 485
Cdd:smart00591 85 EEN-LGEVMIFELVEKL 100
|
|
| RWD_DHX57 |
cd23825 |
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ... |
393-486 |
2.35e-04 |
|
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.
Pssm-ID: 467661 Cd Length: 115 Bit Score: 42.18 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 393 EEQDTLEAIFGERYK-RLSSKVCEIKSEAPNIPGS-LSFRFQKPSAgYPSSVPVIAIQGT--GIPAYIRLSA----IRQA 464
Cdd:cd23825 9 EEAMALESIYGEAFSeRIPNKVWTIKLDLPYLPWFeLEIRFPKGNK-YPYEPPIVAFSSTneNFPKAVCLNIterlMEEA 87
|
90 100
....*....|....*....|..
gi 2477806273 465 VQFAEEnflGESMIFNIMDWLE 486
Cdd:cd23825 88 LELAED---GEPVVFSLVSLLE 106
|
|
| DSRM_A1CF-like |
cd19872 |
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding ... |
60-136 |
1.89e-03 |
|
double-stranded RNA binding motif of APOBEC1 complementation factor (A1CF), RNA-binding protein 46 (RBM46) and similar proteins; The family includes two dsRNA-binding motif-containing proteins, A1CF and RBM46. A1CF (also known as APOBEC1-stimulating protein) is an essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the posttranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. A1CF binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. RBM46 (also called cancer/testis antigen 68 (CT68), or RNA-binding motif protein 46) plays a novel role in the regulation of embryonic stem cell (ESC) differentiation by regulating the degradation of beta-catenin mRNA. It also regulates trophectoderm specification by stabilizing Cdx2 mRNA in early mouse embryos. Members of this family contain three RNA recognition motifs (RRMs) and a C-terminal double-stranded RNA binding motif (DSRM) that is not sequence specific, but highly specific for dsRNAs of various origin and structure.
Pssm-ID: 380701 Cd Length: 75 Bit Score: 38.43 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477806273 60 PVNMLAEHCQKQKWEKPEYTMMRTSDG-----YISSVILkridpktreltvlpPMKPPSshkHLAAQP-----TALEARH 129
Cdd:cd19872 2 PVQILEEICQKNGWGEPVYQLLSTSSNnevqlFIYKVTI--------------PNLPNG---RLTFQPdklcrTPEEAKV 64
|
....*..
gi 2477806273 130 FAAAYAL 136
Cdd:cd19872 65 LAAEFVL 71
|
|
| DSRM_SON-like |
cd19870 |
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known ... |
57-84 |
4.44e-03 |
|
double-stranded RNA binding motif of protein SON and similar proteins; Protein SON (also known as Bax antagonist selected in saccharomyces 1 (BASS1), negative regulatory element-binding protein (NRE-binding protein), or protein DBP-5, or SON3) is an RNA-binding protein which acts as an mRNA splicing cofactor by promoting efficient splicing of transcripts that possess weak splice sites. It specifically promotes splicing of many cell-cycle and DNA-repair transcripts that possess weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Members of this group contain a double-stranded RNA binding motif (DSRM) at the C-terminus. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.
Pssm-ID: 380699 Cd Length: 75 Bit Score: 37.26 E-value: 4.44e-03
10 20
....*....|....*....|....*...
gi 2477806273 57 GKLPVNMLAEHCQKQKWEKPEYTMMRTS 84
Cdd:cd19870 1 GKHPVSALMELCNKRKWGPPEFRLVEES 28
|
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