|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1336-1525 |
6.84e-129 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 401.75 E-value: 6.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1336 HFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQRSsLGLKV 1415
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEK-LGKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1416 VELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISSHTGRAI 1495
Cdd:cd18022 80 VELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPV 159
|
170 180 190
....*....|....*....|....*....|
gi 24647182 1496 RIVGLSTALANAQDLANWLGINKMGLYNFK 1525
Cdd:cd18022 160 RLVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
486-683 |
5.34e-123 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 385.63 E-value: 5.34e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 486 ELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQ-GVINRDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRL 644
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 24647182 645 VESSQSMIRIVGLSATLPNYIDVAHFLRVNPMKGLFYFD 683
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
985-1298 |
8.46e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.19 E-value: 8.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 985 DMNITDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELKNAYCKIKPYGGSENVH 1064
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1065 GKVNILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTIN 1144
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1145 AETIDKLERRG-LSVYRLRDMEHRELKEWLRS-NTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRV 1222
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLlDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24647182 1223 HGKtCQSFWLWIEDPESNYIYHSELFQVTRKLVMsgQSQQLVMTIPLKEPLpPQYYIRVSSDNWLGSTTCIPLSFQ 1298
Cdd:smart00611 241 HGK-QEGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
989-1296 |
2.90e-112 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 359.59 E-value: 2.90e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 989 TDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELkNAYCKIKPYGGSENVHGKVN 1068
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKL-LEKVPIPVKGDIEDPHAKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1069 ILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTINAETI 1148
Cdd:pfam02889 81 ILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1149 DKLERRGLSVYR--LRDMEHRELKEWLRSNTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRVHGKT 1226
Cdd:pfam02889 161 KKLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1227 cQSFWLWIEDPESNYIYHSELFQVTRKLVMSgqSQQLVMTIPLKEPLPPQYYIRVSSDNWLGSTTCIPLS 1296
Cdd:pfam02889 241 -EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1334-1859 |
4.18e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 342.26 E-value: 4.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1334 FTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQnpKCKVVYIAPLKALVKERIADWEQRFqrSSLGL 1413
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDF--EELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1414 KVVELTGDVTPDIQAIRESQLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRtnfiSS 1489
Cdd:COG1204 96 KVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRngpSW-----LRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1490 HTGRAIRIVGLSTALANAQDLANWLGINkmglyNFKPSVRPVPLQ--VHING---FPGKHYCPRMATMNRptfqAIRTYS 1564
Cdd:COG1204 167 RLNPEAQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSKDPTLAL----ALDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1565 PCEPTIVFVSSRRQTRLTALDLITFVAGESNPkqflhIPEDEIELILQNIRE--------QNLKFCLAFGIGLHHAGLQE 1636
Cdd:COG1204 238 EGGQVLVFVSSRRDAESLAKKLADELKRRLTP-----EEREELEELAEELLEvseethtnEKLADCLEKGVAFHHAGLPS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1637 QDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkvkkyVDMPITDVLQMMGRAGRPQFDNEGVAVVLV 1716
Cdd:COG1204 313 ELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1717 --HDEKKNFYKKFLY-DPFPVESSLLG--VLPEHINAEIVAGTVQSKQAALDYLTWTYFfrrllrnpsYYQLQDIEPENV 1791
Cdd:COG1204 388 ksSDEADELFERYILgEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFY---------AYQYDKGDLEEV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647182 1792 nnfmsnlVERVVYELSAAACLVERDGCLIPTFLGRISSYYYL---SYRTMKHFLEDLQPGMNTKKVLLAIA 1859
Cdd:COG1204 459 -------VDDALEFLLENGFIEEDGDRLRATKLGKLVSRLYIdplTAAELVDGLRKADEEFTDLGLLHLIL 522
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1818-2176 |
2.26e-98 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 319.97 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1818 CLIPTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFRPPSSSWDSSY 1897
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1898 TKTFLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEFLTLPGVN 1977
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1978 EDNLDAFLNIphddyDYLTLPVLKELCKQEYEVLAKPLRdafeeHEIEKMYKVIQDLPEIAIQIFVEGRhmENEYAKRPL 2057
Cdd:smart00611 161 EEILKRLEKK-----KVLSLEDLLELEDEERGELLGLLD-----AEGERVYKVLSRLPKLNIEISLEPI--TRTVLGVEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 2058 SLSDDTRGEWMslhanedyvlivnlqrlnvsgqrrgggqsytvhcpkyPKPKNEAWFLTLGSQANDELLAMKRVSIRGQR 2137
Cdd:smart00611 229 TLTVDLTWDDE-------------------------------------IHGKQEGWWLVIGDSDGNELLHIERFSLNKKN 271
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24647182 2138 C--TNRISFQATPRLGRLQLTLYLMSDCLMGFDQQYDLQFE 2176
Cdd:smart00611 272 VseEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
485-1025 |
1.68e-87 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 296.81 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHtircHLEQGvinrdeFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:COG1204 21 EELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILK----ALLNG------GKALYIVPLRALASEKYREFKRDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGdvaLISLVELLIIDEVHLLH-GERGPVVEALVARTLR 643
Cdd:COG1204 91 EELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS---WLRDVDLVVVDEAHLIDdESRGPTLEVLLARLRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 644 LVESsqsmIRIVGLSATLPNYIDVAHFLRVNPmkglfyFDSRFRPVPLDTNFV--GI-----KSVKQLQQIADMdqccyq 716
Cdd:COG1204 168 LNPE----AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLNEGVLydGVlrfddGSRRSKDPTLAL------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 717 kCVEMVQEGHQIMVFVHARNATVRTAnviRELAQQ-NNTSALFLPKDSAAHGLATRSIQRSR--NKQLVELFSCGLAMHH 793
Cdd:COG1204 232 -ALDLLEEGGQVLVFVSSRRDAESLA---KKLADElKRRLTPEEREELEELAEELLEVSEEThtNEKLADCLEKGVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 794 AGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRgtdiyDAKHGSFVDLGILDVLQIFGRAGRPQFDKSGV 873
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGRAGRPGYDPYGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 874 GTIIT----SYDKL-NHYlsLLTNQFPIESNFVN--CLADNLNAEIGLGTITNVDEAIEWLSYTYLFVRMRINphvygie 946
Cdd:COG1204 383 AILVAkssdEADELfERY--ILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYAYQYDKG------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 947 yselekdpTLEARrralimsAAMSLDKARMMRF-NQRTMDMNITDLGRTASYFYIKYDTVETFNELMK---PFMTQAEIL 1022
Cdd:COG1204 454 --------DLEEV-------VDDALEFLLENGFiEEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLL 518
|
...
gi 24647182 1023 AMI 1025
Cdd:COG1204 519 HLI 521
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1821-2174 |
1.84e-74 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 250.97 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1821 PTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFrPPSSSWDSSYTKT 1900
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPI-PVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1901 FLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEFLTLPGVNEDN 1980
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1981 LDAFLNIPHDDYDYLtlpvLKELCKQEYEVLakplrdAFEEHEIEKMYKVIQDLPEIAIQIFVEgrhmeneyakrplsls 2060
Cdd:pfam02889 160 IKKLEKKGVESVRDI----LELDDAEELGEL------IRNPKMGKDIAQFVNRFPKIEIEAEVQ---------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 2061 ddtrgewmsLHANEDYVLIVNLQRLNVSGQRRGGgqsytvhcpkypkpKNEAWFLTLGSQANDELLAMKRVSIRGQRC-- 2138
Cdd:pfam02889 214 ---------PITRSVLRVEVTITPDFPWDKRVHG--------------KSEGFWLVVGDSDGNEILHIERFTLTKRTLag 270
|
330 340 350
....*....|....*....|....*....|....*..
gi 24647182 2139 TNRISFQATP-RLGRLQLTLYLMSDCLMGFDQQYDLQ 2174
Cdd:pfam02889 271 EHKLEFTVPPsDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1529-1717 |
3.18e-65 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 218.19 E-value: 3.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1529 RPVPLQVHINGFPGKHYCPRMATM-----NRPTFQAIRTYSPCEPTIVFVSSRRQTRLTALDLItfvagesnpkqflhip 1603
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1604 edeielilqnireqnlkfclafGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkv 1683
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG-- 120
|
170 180 190
....*....|....*....|....*....|....
gi 24647182 1684 KKYVDMPITDVLQMMGRAGRPQFDNEGVAVVLVH 1717
Cdd:cd18795 121 KGYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1354-1844 |
5.36e-55 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 206.73 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKCkvVYIAPLKALVKERiadwEQRFQR-SSLGLKVVELTGDVTPDIQAIRES 1432
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIARGGKA--LYIVPLRALASEK----FEEFERfEELGVRVGISTGDYDSRDEWLGDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1433 QLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRTNfissHTGRAIRIVGLSTALANAQ 1508
Cdd:PRK02362 115 DIIVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAKLR----RLNPDLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1509 DLANWLGIN-----------KMGLY-----NFKPSVRPVPLqvhingfPGKHYCPRMAtmnrptfqaIRTYSPCEPTIVF 1572
Cdd:PRK02362 186 ELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEV-------PSKDDTLNLV---------LDTLEEGGQCLVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1573 VSSRRQT-----RLTALDLITFVAGESNpkqflhipedEIELILQNIRE-------QNLKFCLAFGIGLHHAGLQEQDRK 1640
Cdd:PRK02362 250 VSSRRNAegfakRAASALKKTLTAAERA----------ELAELAEEIREvsdtetsKDLADCVAKGAAFHHAGLSREHRE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1641 CVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkvkKYVDMPItDVL---QMMGRAGRPQFDNEGVAVVLV- 1716
Cdd:PRK02362 320 LVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG---GAGMQPI-PVLeyhQMAGRAGRPGLDPYGEAVLLAk 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1717 -HDEKKNFYKKFLY-DPFPVESSLL--GVLPEHINAEIVAGTVQSKQAALDYLTWTYFFrrllrnpsyYQLQDiepenvN 1792
Cdd:PRK02362 396 sYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYA---------TQTDD------T 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24647182 1793 NFMSNLVERVVYELSAAACLVERDGCLIPTFLGRISSYYY---LSYRTMKHFLED 1844
Cdd:PRK02362 461 GRLERVVDDVLDFLERNGMIEEDGETLEATELGHLVSRLYidpLSAAEIIDGLEA 515
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
503-1047 |
6.71e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 191.18 E-value: 6.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGvinrdeFKIVYIAPMKALAAEMVDNFsKRLKSLQIAVRELTGDIQLTK 582
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYDSTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 583 AEMAATQILVTTPEKWDVVTRKGSgdvALISLVELLIIDEVHLLHG-ERGPVVEALVARTLrlvessqSMIRIVGLSATL 661
Cdd:PRK00254 110 EWLGKYDIIIATAEKFDSLLRHGS---SWIKDVKLVVADEIHLIGSyDRGATLEMILTHML-------GRAQILGLSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 662 PNYIDVAHFLRVNPMKglfyfdSRFRPVPLDTN-----FVGIKSVKQLQQIADMDQCCYqkcvEMVQEGHQIMVFVHARN 736
Cdd:PRK00254 180 GNAEELAEWLNAELVV------SDWRPVKLRKGvfyqgFLFWEDGKIERFPNSWESLVY----DAVKKGKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 737 ATVRTANVIRELAQqnntSALFLPKDSAAHGLATRSIQRSRNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVL 816
Cdd:PRK00254 250 SAEKEALELAKKIK----RFLTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 817 VCTATLAWGVNLPAHAVIIRGTDIYdAKHGsFVDLGILDVLQIFGRAGRPQFDKSGVGTIITSYDK----LNHYL----- 887
Cdd:PRK00254 326 TATPTLSAGINLPAFRVIIRDTKRY-SNFG-WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfgkpe 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 888 ---SLLTNqfpiESNF---VNCLADNLNaeiglgtITNVDEAIEWLSYTYlfvrmrinphvygieYSELEKDP-TLEARR 960
Cdd:PRK00254 404 klfSMLSN----ESAFrsqVLALITNFG-------VSNFKELVNFLERTF---------------YAHQRKDLySLEEKA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 961 RALImsaamsldkarMMRFNQRTMDMNITD------LGRTASYFYIKYDTVETFNELMKPFMTQAE---ILAMISQAQEF 1031
Cdd:PRK00254 458 KEIV-----------YFLLENEFIDIDLEDrfiplpLGIRTSQLYIDPLTAKKFKDAFPKIEKNPNplgIFQLIASTPDM 526
|
570
....*....|....*.
gi 24647182 1032 QQLKVRDDEMEELDEL 1047
Cdd:PRK00254 527 TPLNYSRKEMEDLLDE 542
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
687-878 |
4.89e-47 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 166.19 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 687 RPVPLDTNFVGIKSVKQLQQIADM----DQCCYQKCVEMVQEGHQIMVFVHARNATVRTANVIRelaqqnntsalflpkd 762
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 763 saahglatrsiqrsrnkqlvelfscGLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTDIYD 842
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 24647182 843 AKHgsFVDLGILDVLQIFGRAGRPQFDKSGVGTIIT 878
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1338-1510 |
6.13e-35 |
|
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: 131.98 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1338 NPIQTQIFHCLYhTDNNVLLGAPTGSGKTIVAEIAIFRALNQN-PKCKVVYIAPLKALVKERIADWEQRFqrSSLGLKVV 1416
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLdNGPQALVLAPTRELAEQIYEELKKLG--KGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1417 ELTGDVTPDIQ--AIRESQLIVTTPEKWDGIsrsWQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRTNFisshtgr 1493
Cdd:pfam00270 78 SLLGGDSRKEQleKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLPK------- 147
|
170
....*....|....*...
gi 24647182 1494 AIRIVGLS-TALANAQDL 1510
Cdd:pfam00270 148 KRQILLLSaTLPRNLEDL 165
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
488-666 |
2.54e-33 |
|
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: 127.36 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 488 NRIQSVVFPVAYhSNENMLVCAPTGAGKTNVAMLSIVHTIRchleqgvINRDEFKIVYIAPMKALAAEMVDNFSKRLKSL 567
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALD-------KLDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 568 QIAVRELTG--DIQLTKAEMAATQILVTTPEKWDVVTRKgsgdVALISLVELLIIDEVHLLHGE-RGPVVEALVARTlrl 644
Cdd:pfam00270 73 GLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE----RKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRL--- 145
|
170 180
....*....|....*....|..
gi 24647182 645 vessQSMIRIVGLSATLPNYID 666
Cdd:pfam00270 146 ----PKKRQILLLSATLPRNLE 163
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1332-1532 |
1.53e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 114.90 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1332 YKFTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVkeriADWEQRFQR--S 1409
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELA----EQWAEELKKlgP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1410 SLGLKVVELTGDVTPDIQ----AIRESQLIVTTPEKWDGISRSWqtREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRT 1484
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQlrklESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24647182 1485 NfisshtgRAIRIVGLS-TALANAQDLANWLGINKMGLYNFKPSVRPVP 1532
Cdd:smart00487 158 P-------KNVQLLLLSaTPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
485-690 |
1.49e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.12 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:smart00487 7 EPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRG--------KGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQI-AVRELTGD---IQLTKAEMAATQILVTTPEKWDVVTRKGSGDValiSLVELLIIDEVH-LLHGERGPVVEALVA 639
Cdd:smart00487 79 PSLGLkVVGLYGGDskrEQLRKLESGKTDILVTTPGRLLDLLENDKLSL---SNVDLVILDEAHrLLDGGFGDQLEKLLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24647182 640 RTLRlvessqsMIRIVGLSATLPNYIDVAHFLRvnpMKGLFYFDSRFRPVP 690
Cdd:smart00487 156 LLPK-------NVQLLLLSATPPEEIENLLELF---LNDPVFIDVGFTPLE 196
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
498-671 |
6.70e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMLSIV-----HTIRCHLEQGVinrdefKIVYIAPMKALA-----------AEMVDNFS 561
Cdd:COG1201 35 AIAAGESTLLIAPTGSGKTLAAFLPALdelarRPRPGELPDGL------RVLYISPLKALAndiernlraplEEIGEAAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 562 KRLKSLQIAVRelTGDiqlT----KAEMAAT--QILVTTPEkwdvvtrkgsgdvaliSL---------------VELLII 620
Cdd:COG1201 109 LPLPEIRVGVR--TGD---TpaseRQRQRRRppHILITTPE----------------SLallltspdarellrgVRTVIV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24647182 621 DEVH-LLHGERGpvveALVARTL-RLVESSQSMIRIVGLSATLPNYIDVAHFL 671
Cdd:COG1201 168 DEIHaLAGSKRG----VHLALSLeRLRALAPRPLQRIGLSATVGPLEEVARFL 216
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1356-1672 |
1.02e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.92 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1356 LLGAPTGSGKT------IVAEIAIFRALNQNPkCKVVYIAPLKALVKeriaDWEQRFQR--SSLGLKV-VEL-TGDvTPd 1425
Cdd:TIGR04121 32 LLIAPTGSGKTlagflpSLIDLAGPEAPKEKG-LHTLYITPLRALAV----DIARNLQApiEELGLPIrVETrTGD-TS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1426 iQAIRESQ------LIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRTNFISShtgrAIRIV 1498
Cdd:TIGR04121 105 -SSERARQrkkppdILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAP----GLRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1499 GLSTALANAQDLANWLginkMGLYNFKPSV------RPVPLQVHI---------NGFPGKHYCPRMAtmnrPTFQAIRTy 1563
Cdd:TIGR04121 180 GLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISLLpeseerfpwAGHLGLRALPEVY----AEIDQART- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1564 spcepTIVFVSSRRQTrltaldlitfvagesnpkqflhipedeiELILQNIREQNLKFCLAfgIGLHHAGLQEQDRKCVE 1643
Cdd:TIGR04121 251 -----TLVFTNTRSQA----------------------------ELWFQALWEANPEFALP--IALHHGSLDREQRRWVE 295
|
330 340 350
....*....|....*....|....*....|
gi 24647182 1644 ELFLNRKIQILVATATLAWGVN-LPAHLVV 1672
Cdd:TIGR04121 296 AAMAAGRLRAVVCTSSLDLGVDfGPVDLVI 325
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1333-1660 |
1.42e-17 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 89.78 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQIFHcLYHTDNNVLLGAPTGSGKT------IVAEIAiFRALNQNPK--CKVVYIAPLKALVkeriADWEQ 1404
Cdd:COG1201 21 RFGAPTPPQREAWP-AIAAGESTLLIAPTGSGKTlaaflpALDELA-RRPRPGELPdgLRVLYISPLKALA----NDIER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1405 RFQ------RSSLGLKVVEL-----TGDvTPdiQAIRESQL------IVTTPE---------KWdgisrswqtREYVQHV 1458
Cdd:COG1201 95 NLRapleeiGEAAGLPLPEIrvgvrTGD-TP--ASERQRQRrrpphiLITTPEslallltspDA---------RELLRGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1459 SLIVIDEIH-LLGEDRGPVIEVIVSRtnfISSHTGRAIRIVGLSTALANAQDLANWLGinkmGlynfKPSVRPVplqVHI 1537
Cdd:COG1201 163 RTVIVDEIHaLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFLV----G----YEDPRPV---TIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1538 NGFPGKHY-----CPRMATMNRPT-------------FQAI---RTyspcepTIVFVSSRRQTrltaldlitfvagesnp 1596
Cdd:COG1201 229 DAGAGKKPdlevlVPVEDLIERFPwaghlwphlyprvLDLIeahRT------TLVFTNTRSQA----------------- 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647182 1597 kqflhipedeiELILQNIREQNLKFCLAfgIGLHHAGL-QEQDRKcVEELFLNRKIQILVATATL 1660
Cdd:COG1201 286 -----------ERLFQRLNELNPEDALP--IAAHHGSLsREQRLE-VEEALKAGELRAVVATSSL 336
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
500-766 |
1.43e-14 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 79.93 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 500 HSNENMLVCAPTGAGKTNVAMLSIVHTI-----RCHLEQGVInrdefkIVYIAPMKALAAEMVDNFSKRLKSLQ------ 568
Cdd:PRK13767 45 HEGKNVLISSPTGSGKTLAAFLAIIDELfrlgrEGELEDKVY------CLYVSPLRALNNDIHRNLEEPLTEIReiaker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 569 --------IAVRelTGDI-QLTKAEMAAT--QILVTTPEkwdvvtrkgSGDVALIS--------LVELLIIDEVHLLHG- 628
Cdd:PRK13767 119 geelpeirVAIR--TGDTsSYEKQKMLKKppHILITTPE---------SLAILLNSpkfreklrTVKWVIVDEIHSLAEn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 629 ERGPVVEALVARTLRLVEssQSMIRIvGLSATLPNYIDVAHFLrvnpmkGLFYFDSRFRPVPL-DTNFVGIKSVKQLQQI 707
Cdd:PRK13767 188 KRGVHLSLSLERLEELAG--GEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIvDARFVKPFDIKVISPV 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 708 ADM--------DQCCYQKCVEMVQEGHQIMVFVHARNATVRTANVIRELAQQNntsalFLPKDSAAH 766
Cdd:PRK13767 259 DDLihtpaeeiSEALYETLHELIKEHRTTLIFTNTRSGAERVLYNLRKRFPEE-----YDEDNIGAH 320
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1605-1704 |
4.84e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1605 DEIELILQNireqnlkfcLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP-AHLVVIKGteyfdgkv 1683
Cdd:smart00490 1 EELAELLKE---------LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-------- 63
|
90 100
....*....|....*....|.
gi 24647182 1684 kkyVDMPITDVLQMMGRAGRP 1704
Cdd:smart00490 64 ---LPWSPASYIQRIGRAGRA 81
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
498-830 |
8.25e-14 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 77.21 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMLSIV---HTIRCHLEQGVinrdefKIVYIAPMKALAAEMvdnfskrLKSLQIAVREL 574
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLidlAGPEAPKEKGL------HTLYITPLRALAVDI-------ARNLQAPIEEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 575 ---------TGDiqlTKAEMAATQ------ILVTTPEKWDV-VTRKGSGDvaLISLVELLIIDEVH-LLHGERGPVVEAL 637
Cdd:TIGR04121 91 glpirvetrTGD---TSSSERARQrkkppdILLTTPESLALlLSYPDAAR--LFKDLRCVVVDEWHeLAGSKRGDQLELA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 638 VARTLRLvessQSMIRIVGLSATLPNYIDVAHFL-RVNPMKGLFYFDSRFRPVPLDT------------NFVGIKSVKQL 704
Cdd:TIGR04121 166 LARLRRL----APGLRRWGLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEVISllpeseerfpwaGHLGLRALPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 705 qqiadmdqccyqkcVEMVQEGHQIMVFVHARNATVRtanVIRELAQQNNTSALFlpkdsaahglatrsiqrsrnkqlvel 784
Cdd:TIGR04121 242 --------------YAEIDQARTTLVFTNTRSQAEL---WFQALWEANPEFALP-------------------------- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24647182 785 fscgLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPA 830
Cdd:TIGR04121 279 ----IALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGP 320
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
790-866 |
2.69e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.46 E-value: 2.69e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647182 790 AMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLP-AHAVIirgtdIYDAkhgsfvDLGILDVLQIFGRAGRP 866
Cdd:smart00490 15 ARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVI-----IYDL------PWSPASYIQRIGRAGRA 81
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1614-1703 |
1.16e-08 |
|
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: 54.91 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1614 IREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP-AHLVVIkgteyfdgkvkkyVDMP-- 1690
Cdd:pfam00271 28 LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-------------YDLPwn 94
|
90
....*....|...
gi 24647182 1691 ITDVLQMMGRAGR 1703
Cdd:pfam00271 95 PASYIQRIGRAGR 107
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
770-865 |
3.88e-08 |
|
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: 53.37 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 770 TRSIQRSRNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLP-AHAVIirgtdIYDAkhgsf 848
Cdd:pfam00271 22 SQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVI-----NYDL----- 91
|
90
....*....|....*..
gi 24647182 849 vDLGILDVLQIFGRAGR 865
Cdd:pfam00271 92 -PWNPASYIQRIGRAGR 107
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1333-1474 |
4.20e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 58.74 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQIFHcLYHTDNNVLLGAPTGSGKTIVAEIAI----FRALNQNP---KCKVVYIAPLKAL-------VKER 1398
Cdd:PRK13767 29 KFGTFTPPQRYAIP-LIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREGEledKVYCLYVSPLRALnndihrnLEEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1399 IADWEQRFQRssLGLKVVEL-----TGDVTPdiqAIRESQL------IVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH 1467
Cdd:PRK13767 108 LTEIREIAKE--RGEELPEIrvairTGDTSS---YEKQKMLkkpphiLITTPESLAILLNSPKFREKLRTVKWVIVDEIH 182
|
....*...
gi 24647182 1468 LLGED-RG 1474
Cdd:PRK13767 183 SLAENkRG 190
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
247-284 |
3.56e-04 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 42.21 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....*....
gi 24647182 247 DILGSQRSSEV-LQNELMEILGFDYFELVEKLLMERDKI 284
Cdd:pfam18149 38 DILESAADDLReCENQLVELLDYDKFDLVKLLLKNRDKI 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1336-1525 |
6.84e-129 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 401.75 E-value: 6.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1336 HFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQRSsLGLKV 1415
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEK-LGKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1416 VELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISSHTGRAI 1495
Cdd:cd18022 80 VELTGDVTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYISSQTEKPV 159
|
170 180 190
....*....|....*....|....*....|
gi 24647182 1496 RIVGLSTALANAQDLANWLGINKMGLYNFK 1525
Cdd:cd18022 160 RLVGLSTALANAGDLANWLGIKKMGLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
486-683 |
5.34e-123 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 385.63 E-value: 5.34e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 486 ELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQ-GVINRDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:cd18020 1 RLNRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQgGVIKKDDFKIVYIAPMKALAAEMVEKFSKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRL 644
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 24647182 645 VESSQSMIRIVGLSATLPNYIDVAHFLRVNPMKGLFYFD 683
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYKGLFFFD 199
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
985-1298 |
8.46e-113 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 361.19 E-value: 8.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 985 DMNITDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELKNAYCKIKPYGGSENVH 1064
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1065 GKVNILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTIN 1144
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1145 AETIDKLERRG-LSVYRLRDMEHRELKEWLRS-NTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRV 1222
Cdd:smart00611 161 EEILKRLEKKKvLSLEDLLELEDEERGELLGLlDAEGERVYKVLSRLPKLNIEISLEPITRTVLGVEVTLTVDLTWDDEI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24647182 1223 HGKtCQSFWLWIEDPESNYIYHSELFQVTRKLVMsgQSQQLVMTIPLKEPLpPQYYIRVSSDNWLGSTTCIPLSFQ 1298
Cdd:smart00611 241 HGK-QEGWWLVIGDSDGNELLHIERFSLNKKNVS--EEVKLDFTAPATEGN-YQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
989-1296 |
2.90e-112 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 359.59 E-value: 2.90e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 989 TDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELkNAYCKIKPYGGSENVHGKVN 1068
Cdd:pfam02889 2 TDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKL-LEKVPIPVKGDIEDPHAKVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1069 ILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCHLKQFPTINAETI 1148
Cdd:pfam02889 81 ILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1149 DKLERRGLSVYR--LRDMEHRELKEWLRSNTYADLVIRSAHELPLLEVEASLQPITRTVLRIKVDIWPSFTWNDRVHGKT 1226
Cdd:pfam02889 161 KKLEKKGVESVRdiLELDDAEELGELIRNPKMGKDIAQFVNRFPKIEIEAEVQPITRSVLRVEVTITPDFPWDKRVHGKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1227 cQSFWLWIEDPESNYIYHSELFQVTRKLVMSgqSQQLVMTIPLKEPLPPQYYIRVSSDNWLGSTTCIPLS 1296
Cdd:pfam02889 241 -EGFWLVVGDSDGNEILHIERFTLTKRTLAG--EHKLEFTVPPSDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
470-683 |
1.27e-110 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 350.90 E-value: 1.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 470 IEELDDVGRLAFANCKELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHL-EQGVINRDEFKIVYIAP 548
Cdd:cd18019 1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLDAFKIVYIAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 549 MKALAAEMVDNFSKRLKSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKgSGDVALISLVELLIIDEVHLLHG 628
Cdd:cd18019 81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRK-SGDRTYTQLVRLIIIDEIHLLHD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24647182 629 ERGPVVEALVARTLRLVESSQSMIRIVGLSATLPNYIDVAHFLRVNPMKGLFYFD 683
Cdd:cd18019 160 DRGPVLESIVARTIRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDPKKGLFYFD 214
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1334-1859 |
4.18e-103 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 342.26 E-value: 4.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1334 FTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQnpKCKVVYIAPLKALVKERIADWEQRFqrSSLGL 1413
Cdd:COG1204 20 IEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRDF--EELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1414 KVVELTGDVTPDIQAIRESQLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRtnfiSS 1489
Cdd:COG1204 96 KVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRngpSW-----LRDVDLVVVDEAHLIDdESRGPTLEVLLAR----LR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1490 HTGRAIRIVGLSTALANAQDLANWLGINkmglyNFKPSVRPVPLQ--VHING---FPGKHYCPRMATMNRptfqAIRTYS 1564
Cdd:COG1204 167 RLNPEAQIVALSATIGNAEEIAEWLDAE-----LVKSDWRPVPLNegVLYDGvlrFDDGSRRSKDPTLAL----ALDLLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1565 PCEPTIVFVSSRRQTRLTALDLITFVAGESNPkqflhIPEDEIELILQNIRE--------QNLKFCLAFGIGLHHAGLQE 1636
Cdd:COG1204 238 EGGQVLVFVSSRRDAESLAKKLADELKRRLTP-----EEREELEELAEELLEvseethtnEKLADCLEKGVAFHHAGLPS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1637 QDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkvkkyVDMPITDVLQMMGRAGRPQFDNEGVAVVLV 1716
Cdd:COG1204 313 ELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGM-----VPIPVLEFKQMAGRAGRPGYDPYGEAILVA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1717 --HDEKKNFYKKFLY-DPFPVESSLLG--VLPEHINAEIVAGTVQSKQAALDYLTWTYFfrrllrnpsYYQLQDIEPENV 1791
Cdd:COG1204 388 ksSDEADELFERYILgEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFY---------AYQYDKGDLEEV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647182 1792 nnfmsnlVERVVYELSAAACLVERDGCLIPTFLGRISSYYYL---SYRTMKHFLEDLQPGMNTKKVLLAIA 1859
Cdd:COG1204 459 -------VDDALEFLLENGFIEEDGDRLRATKLGKLVSRLYIdplTAAELVDGLRKADEEFTDLGLLHLIL 522
|
|
| SEC63 |
smart00611 |
Domain of unknown function in Sec63p, Brr2p and other proteins; |
1818-2176 |
2.26e-98 |
|
Domain of unknown function in Sec63p, Brr2p and other proteins;
Pssm-ID: 214744 Cd Length: 312 Bit Score: 319.97 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1818 CLIPTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFRPPSSSWDSSY 1897
Cdd:smart00611 1 GIWPTDLGRIASYYYISYTTIRTFNELLKPKMTTKDLLRILSMSSEFDQIPVRHEEDLLLEELAEKLPIRLENPSLDDPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1898 TKTFLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEFLTLPGVN 1977
Cdd:smart00611 81 VKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALERGWLSTALNALNLSQMIIQALWPTDSPLLQLPHLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1978 EDNLDAFLNIphddyDYLTLPVLKELCKQEYEVLAKPLRdafeeHEIEKMYKVIQDLPEIAIQIFVEGRhmENEYAKRPL 2057
Cdd:smart00611 161 EEILKRLEKK-----KVLSLEDLLELEDEERGELLGLLD-----AEGERVYKVLSRLPKLNIEISLEPI--TRTVLGVEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 2058 SLSDDTRGEWMslhanedyvlivnlqrlnvsgqrrgggqsytvhcpkyPKPKNEAWFLTLGSQANDELLAMKRVSIRGQR 2137
Cdd:smart00611 229 TLTVDLTWDDE-------------------------------------IHGKQEGWWLVIGDSDGNELLHIERFSLNKKN 271
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24647182 2138 C--TNRISFQATPRLGRLQLTLYLMSDCLMGFDQQYDLQFE 2176
Cdd:smart00611 272 VseEVKLDFTAPATEGNYQYTLRLVSDSYLGCDQEYPLSFD 312
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
989-1297 |
4.52e-93 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 304.67 E-value: 4.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 989 TDLGRTASYFYIKYDTVETFNELMKPFMTQAEILAMISQAQEFQQLKVRDDEMEELDELkNAYCKIKPYGGSEN-VHGKV 1067
Cdd:smart00973 2 TELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNEL-NKRVPIPVKEGIIDsPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1068 NILIQTYLSNGYVKSFSLSSDMSYITTNIGRISRALFSIVLRQNNAVLSGNMLQLCKMFERRQWDFDCH-LKQFPTINAE 1146
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDSDSpLKQLPHFLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1147 TI-DKLERRGL--SVYRLRDMEHRELKEWLRSN-TYADLVIRSAHELPLLEVEASLQPITRTV-LRIKVDIWPSFTWNDR 1221
Cdd:smart00973 161 DVyDKLELKDGsrSFELLLDMNAAELGEFLNRLpPNGRLIYELLRRFPKIEVEAEVLPITRDLtLRVELEITPVFAWDLP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24647182 1222 VHGKTCQSFWLWIEDPESNYIYHSELFQVTRKlvMSGQSQQLVMTIPLKEPLPPQYYIRVSSDNWLGSTTCIPLSF 1297
Cdd:smart00973 241 RHKGKSESWWLVVGDSDTNELLAIKRVTLRKK--KKSNEVKLDFTVPLSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
485-1025 |
1.68e-87 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 296.81 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHtircHLEQGvinrdeFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:COG1204 21 EELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILK----ALLNG------GKALYIVPLRALASEKYREFKRDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGdvaLISLVELLIIDEVHLLH-GERGPVVEALVARTLR 643
Cdd:COG1204 91 EELGIKVGVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPS---WLRDVDLVVVDEAHLIDdESRGPTLEVLLARLRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 644 LVESsqsmIRIVGLSATLPNYIDVAHFLRVNPmkglfyFDSRFRPVPLDTNFV--GI-----KSVKQLQQIADMdqccyq 716
Cdd:COG1204 168 LNPE----AQIVALSATIGNAEEIAEWLDAEL------VKSDWRPVPLNEGVLydGVlrfddGSRRSKDPTLAL------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 717 kCVEMVQEGHQIMVFVHARNATVRTAnviRELAQQ-NNTSALFLPKDSAAHGLATRSIQRSR--NKQLVELFSCGLAMHH 793
Cdd:COG1204 232 -ALDLLEEGGQVLVFVSSRRDAESLA---KKLADElKRRLTPEEREELEELAEELLEVSEEThtNEKLADCLEKGVAFHH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 794 AGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRgtdiyDAKHGSFVDLGILDVLQIFGRAGRPQFDKSGV 873
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIR-----DTKRGGMVPIPVLEFKQMAGRAGRPGYDPYGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 874 GTIIT----SYDKL-NHYlsLLTNQFPIESNFVN--CLADNLNAEIGLGTITNVDEAIEWLSYTYLFVRMRINphvygie 946
Cdd:COG1204 383 AILVAkssdEADELfERY--ILGEPEPIRSKLANesALRTHLLALIASGFANSREELLDFLENTFYAYQYDKG------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 947 yselekdpTLEARrralimsAAMSLDKARMMRF-NQRTMDMNITDLGRTASYFYIKYDTVETFNELMK---PFMTQAEIL 1022
Cdd:COG1204 454 --------DLEEV-------VDDALEFLLENGFiEEDGDRLRATKLGKLVSRLYIDPLTAAELVDGLRkadEEFTDLGLL 518
|
...
gi 24647182 1023 AMI 1025
Cdd:COG1204 519 HLI 521
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
1334-1524 |
6.46e-86 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 279.14 E-value: 6.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1334 FTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQrSSLGL 1413
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFG-PLLGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1414 KVVELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISSHTGR 1493
Cdd:cd18021 80 KVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYISSQLEK 159
|
170 180 190
....*....|....*....|....*....|.
gi 24647182 1494 AIRIVGLSTALANAQDLANWLGINKMGLYNF 1524
Cdd:cd18021 160 PIRIVGLSSSLANARDVGEWLGASKSTIFNF 190
|
|
| Sec63 |
smart00973 |
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ... |
1821-2175 |
2.91e-77 |
|
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.
Pssm-ID: 214946 Cd Length: 314 Bit Score: 259.21 E-value: 2.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1821 PTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFRPPSSSWDSSYTKT 1900
Cdd:smart00973 1 PTELGRIASYYYISYETIETFNQSLKPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKRVPIPVKEGIIDSPHAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1901 FLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEfltlpgvnedn 1980
Cdd:smart00973 81 NLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALSKGWLRTALNALDLSQMVVQRLWEDSDS----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1981 ldAFLNIPHddydyLTLPVLKELCKQEYEVLAKPLRDAFEEHEIEKMYKVIQDLPEIAIQIFVEGRHMENEYAKRPLsls 2060
Cdd:smart00973 150 --PLKQLPH-----FLIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPI--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 2061 ddTRGEWMSLHANEDYVLIVNLQRlnvsgqrrgggqsytvhcpkyPKPKNEAWFLTLGSQANDELLAMKRVSIRGQRCTN 2140
Cdd:smart00973 220 --TRDLTLRVELEITPVFAWDLPR---------------------HKGKSESWWLVVGDSDTNELLAIKRVTLRKKKKSN 276
|
330 340 350
....*....|....*....|....*....|....*...
gi 24647182 2141 RISFQAT---PRLGRLQLTLYLMSDCLMGFDQQYDLQF 2175
Cdd:smart00973 277 EVKLDFTvplSEPGPENYTVYLISDSYLGCDQEVSFSL 314
|
|
| Sec63 |
pfam02889 |
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ... |
1821-2174 |
1.84e-74 |
|
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.
Pssm-ID: 460740 Cd Length: 307 Bit Score: 250.97 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1821 PTFLGRISSYYYLSYRTMKHFLEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHNEEMAEVSRFrPPSSSWDSSYTKT 1900
Cdd:pfam02889 1 PTDLGRIASHYYISYETIETFNQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLLEKVPI-PVKGDIEDPHAKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1901 FLLLQAHFARQSLPNSDYLTDTKSALDNATRVMQAMVDYTAERGWLSTTLVVQQLMQSVIQARWFDGSEFLTLPGVNEDN 1980
Cdd:pfam02889 80 NILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLSKGWLSAALTALDLCKMIEQRMWDSDSPLRQFPGIPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1981 LDAFLNIPHDDYDYLtlpvLKELCKQEYEVLakplrdAFEEHEIEKMYKVIQDLPEIAIQIFVEgrhmeneyakrplsls 2060
Cdd:pfam02889 160 IKKLEKKGVESVRDI----LELDDAEELGEL------IRNPKMGKDIAQFVNRFPKIEIEAEVQ---------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 2061 ddtrgewmsLHANEDYVLIVNLQRLNVSGQRRGGgqsytvhcpkypkpKNEAWFLTLGSQANDELLAMKRVSIRGQRC-- 2138
Cdd:pfam02889 214 ---------PITRSVLRVEVTITPDFPWDKRVHG--------------KSEGFWLVVGDSDGNEILHIERFTLTKRTLag 270
|
330 340 350
....*....|....*....|....*....|....*..
gi 24647182 2139 TNRISFQATP-RLGRLQLTLYLMSDCLMGFDQQYDLQ 2174
Cdd:pfam02889 271 EHKLEFTVPPsDPGPPQLFVRLISDSWLGADQEVPIS 307
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
1336-1524 |
7.08e-69 |
|
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: 229.84 E-value: 7.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1336 HFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKcKVVYIAPLKALVKERIADWEQRFQRssLGLKV 1415
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-KAVYIAPTRALVNQKEADLRERFGP--LGKNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1416 VELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTReYVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRTNFISSHtgra 1494
Cdd:cd17921 78 GLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRINKN---- 152
|
170 180 190
....*....|....*....|....*....|
gi 24647182 1495 IRIVGLSTALANAQDLANWLGinKMGLYNF 1524
Cdd:cd17921 153 ARFVGLSATLPNAEDLAEWLG--VEDLIRF 180
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
1529-1717 |
3.18e-65 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 218.19 E-value: 3.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1529 RPVPLQVHINGFPGKHYCPRMATM-----NRPTFQAIRTYSPCEPTIVFVSSRRQTRLTALDLItfvagesnpkqflhip 1603
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdsDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1604 edeielilqnireqnlkfclafGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkv 1683
Cdd:cd18795 65 ----------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDG-- 120
|
170 180 190
....*....|....*....|....*....|....
gi 24647182 1684 KKYVDMPITDVLQMMGRAGRPQFDNEGVAVVLVH 1717
Cdd:cd18795 121 KGYRELSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
1337-1530 |
2.06e-64 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 217.99 E-value: 2.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1337 FNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNP-----KCKVVYIAPLKALVKERIADWEQRFqrSSL 1411
Cdd:cd18023 2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERNplpwgNRKVVYIAPIKALCSEKYDDWKEKF--GPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1412 GLKVVELTGD-VTPDIQAIRESQLIVTTPEKWDGISRSWQTRE-YVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFISS 1489
Cdd:cd18023 80 GLSCAELTGDtEMDDTFEIQDADIILTTPEKWDSMTRRWRDNGnLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24647182 1490 HTG------RAIRIVGLSTALANAQDLANWLGINKMGLYNFKPSVRP 1530
Cdd:cd18023 160 SSElrgstvRPMRFVAVSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
486-683 |
5.02e-61 |
|
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: 207.11 E-value: 5.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 486 ELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrdEFKIVYIAPMKALAAEMVDNFSKRLK 565
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS---------GGKAVYIAPTRALVNQKEADLRERFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 566 SLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGDvaLISLVELLIIDEVHLLH-GERGPVVEALVARTLRL 644
Cdd:cd17921 72 PLGKNVGLLTGDPSVNKLLLAEADILVATPEKLDLLLRNGGER--LIQDVRLVVVDEAHLIGdGERGVVLELLLSRLLRI 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 24647182 645 vessQSMIRIVGLSATLPNYIDVAHFLRVnpmKGLFYFD 683
Cdd:cd17921 150 ----NKNARFVGLSATLPNAEDLAEWLGV---EDLIRFD 181
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
488-688 |
8.05e-58 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 199.12 E-value: 8.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 488 NRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRchlEQGVINRDEFKIVYIAPMKALAAEMVDNFSKRLKSL 567
Cdd:cd18023 3 NRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLK---ERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 568 QIAVRELTGDIQLTKA-EMAATQILVTTPEKWDVVTRKGSGDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRLVE 646
Cdd:cd18023 80 GLSCAELTGDTEMDDTfEIQDADIILTTPEKWDSMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATLEVVVSRMKTLSS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24647182 647 SSQSM------IRIVGLSATLPNYIDVAHFLRVNPmKGLFYFDSRFRP 688
Cdd:cd18023 160 SSELRgstvrpMRFVAVSATIPNIEDLAEWLGDNP-AGCFSFGESFRP 206
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
1334-1524 |
7.79e-57 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 196.44 E-value: 7.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1334 FTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRAL--NQNPKC-------KVVYIAPLKALVKERIADWEQ 1404
Cdd:cd18019 15 FKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIgkHRNPDGtinldafKIVYIAPMKALVQEMVGNFSK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1405 RFqrSSLGLKVVELTGDVTPDIQAIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRT 1484
Cdd:cd18019 95 RL--APYGITVAELTGDQQLTKEQISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPVLESIVART 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24647182 1485 NFISSHTGRAIRIVGLSTALANAQDLANWLGIN-KMGLYNF 1524
Cdd:cd18019 173 IRQIEQTQEYVRLVGLSATLPNYEDVATFLRVDpKKGLFYF 213
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
1354-1844 |
5.36e-55 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 206.73 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKCkvVYIAPLKALVKERiadwEQRFQR-SSLGLKVVELTGDVTPDIQAIRES 1432
Cdd:PRK02362 41 NLLAAIPTASGKTLIAELAMLKAIARGGKA--LYIVPLRALASEK----FEEFERfEELGVRVGISTGDYDSRDEWLGDN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1433 QLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRTNfissHTGRAIRIVGLSTALANAQ 1508
Cdd:PRK02362 115 DIIVATSEKVDSLLRngaPW-----LDDITCVVVDEVHLIDsANRGPTLEVTLAKLR----RLNPDLQVVALSATIGNAD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1509 DLANWLGIN-----------KMGLY-----NFKPSVRPVPLqvhingfPGKHYCPRMAtmnrptfqaIRTYSPCEPTIVF 1572
Cdd:PRK02362 186 ELADWLDAElvdsewrpidlREGVFyggaiHFDDSQREVEV-------PSKDDTLNLV---------LDTLEEGGQCLVF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1573 VSSRRQT-----RLTALDLITFVAGESNpkqflhipedEIELILQNIRE-------QNLKFCLAFGIGLHHAGLQEQDRK 1640
Cdd:PRK02362 250 VSSRRNAegfakRAASALKKTLTAAERA----------ELAELAEEIREvsdtetsKDLADCVAKGAAFHHAGLSREHRE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1641 CVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkvkKYVDMPItDVL---QMMGRAGRPQFDNEGVAVVLV- 1716
Cdd:PRK02362 320 LVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDG---GAGMQPI-PVLeyhQMAGRAGRPGLDPYGEAVLLAk 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1717 -HDEKKNFYKKFLY-DPFPVESSLL--GVLPEHINAEIVAGTVQSKQAALDYLTWTYFFrrllrnpsyYQLQDiepenvN 1792
Cdd:PRK02362 396 sYDELDELFERYIWaDPEDVRSKLAtePALRTHVLSTIASGFARTRDGLLEFLEATFYA---------TQTDD------T 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24647182 1793 NFMSNLVERVVYELSAAACLVERDGCLIPTFLGRISSYYY---LSYRTMKHFLED 1844
Cdd:PRK02362 461 GRLERVVDDVLDFLERNGMIEEDGETLEATELGHLVSRLYidpLSAAEIIDGLEA 515
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1354-1881 |
4.81e-53 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 200.43 E-value: 4.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKcKVVYIAPLKALVKER---IADWEQrfqrssLGLKVVELTGDVTPDIQAIR 1430
Cdd:PRK00254 41 NLVLAIPTASGKTLVAEIVMVNKLLREGG-KAVYLVPLKALAEEKyreFKDWEK------LGLRVAMTTGDYDSTDEWLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1431 ESQLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLGE-DRGPVIEVIvsrtnfISSHTGRAiRIVGLSTALAN 1506
Cdd:PRK00254 114 KYDIIIATAEKFDSLLRhgsSW-----IKDVKLVVADEIHLIGSyDRGATLEMI------LTHMLGRA-QILGLSATVGN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1507 AQDLANWLGINKMglynfKPSVRPVPLQ--VHINGF----PGK--HYCPRMATMnrpTFQAIRTyspCEPTIVFVSSRRQ 1578
Cdd:PRK00254 182 AEELAEWLNAELV-----VSDWRPVKLRkgVFYQGFlfweDGKieRFPNSWESL---VYDAVKK---GKGALVFVNTRRS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1579 TRLTALDLITFVagesnpKQFLHIPE--------DEIElilQNIREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRK 1650
Cdd:PRK00254 251 AEKEALELAKKI------KRFLTKPElralkelaDSLE---ENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1651 IQILVATATLAWGVNLPAHLVVIKGTEYFDGkvKKYVDMPITDVLQMMGRAGRPQFDNEGVAVVLVH-DEKKNFYKKF-- 1727
Cdd:PRK00254 322 IKVITATPTLSAGINLPAFRVIIRDTKRYSN--FGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATtEEPSKLMERYif 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1728 -----LYDPFPVESSLLGvlpeHINAEIVAGTVQSKQAALDYLTWTYFfrrllrnpsYYQLQDIE--PENVNNFMSNLVE 1800
Cdd:PRK00254 400 gkpekLFSMLSNESAFRS----QVLALITNFGVSNFKELVNFLERTFY---------AHQRKDLYslEEKAKEIVYFLLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1801 RVVYELSaaacLVERdgcLIPTFLGRISSYYYLSYRTMKHF---LEDLQPGMNTKKVLLAIADSYEFDQLPVRHNEDKHN 1877
Cdd:PRK00254 467 NEFIDID----LEDR---FIPLPLGIRTSQLYIDPLTAKKFkdaFPKIEKNPNPLGIFQLIASTPDMTPLNYSRKEMEDL 539
|
....
gi 24647182 1878 EEMA 1881
Cdd:PRK00254 540 LDEA 543
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
1354-1738 |
7.74e-51 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 193.18 E-value: 7.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKCkvVYIAPLKALVKERiadWEQRFQRSSLGLKVVELTGDV--TPDIqaIRE 1431
Cdd:PRK01172 39 NVIVSVPTAAGKTLIAYSAIYETFLAGLKS--IYIVPLRSLAMEK---YEELSRLRSLGMRVKISIGDYddPPDF--IKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1432 SQLIVTTPEKWDgiSRSWQTREYVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRTNFISSHTgraiRIVGLSTALANAQDL 1510
Cdd:PRK01172 112 YDVVILTSEKAD--SLIHHDPYIINDVGLIVADEIHIIGdEDRGPTLETVLSSARYVNPDA----RILALSATVSNANEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1511 ANWLGINKMglynfKPSVRPVPLQVHINgFPGKHYCPRMATMNRPTFQAIR-TYSPCEPTIVFVSSRRQTRLTALDLITF 1589
Cdd:PRK01172 186 AQWLNASLI-----KSNFRPVPLKLGIL-YRKRLILDGYERSQVDINSLIKeTVNDGGQVLVFVSSRKNAEDYAEMLIQH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1590 VAGESNpkqfLHIPEDEielilQNIREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAH 1669
Cdd:PRK01172 260 FPEFND----FKVSSEN-----NNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPAR 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24647182 1670 LVVIKG-TEYFDGKVKKYVDMPITdvlQMMGRAGRPQFDNEGVAVVLVhdEKKNFY---KKFLY-DPFPVESSL 1738
Cdd:PRK01172 331 LVIVRDiTRYGNGGIRYLSNMEIK---QMIGRAGRPGYDQYGIGYIYA--ASPASYdaaKKYLSgEPEPVISYM 399
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
1352-1737 |
3.92e-50 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 192.46 E-value: 3.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCkvVYIAPLKALVKERIADWEQRFQRSSLGLkvveLTGDVTpdiqaI-R 1430
Cdd:COG4581 40 GRSVLVAAPTGSGKTLVAEFAIFLALARGRRS--FYTAPIKALSNQKFFDLVERFGAENVGL----LTGDAS-----VnP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1431 ESQLIVTTPEkwdgISRSW--QTREYVQHVSLIVIDEIHLLGE-DRGPVIEVIVsrtnfIssHTGRAIRIVGLSTALANA 1507
Cdd:COG4581 109 DAPIVVMTTE----ILRNMlyREGADLEDVGVVVMDEFHYLADpDRGWVWEEPI-----I--HLPARVQLVLLSATVGNA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1508 QDLANWLGinkmglynfkpSV-----------RPVPLQVhingfpgkHYC--PRMATMNRPTFQAIRTYSPCE------- 1567
Cdd:COG4581 178 EEFAEWLT-----------RVrgetavvvseeRPVPLEF--------HYLvtPRLFPLFRVNPELLRPPSRHEvieeldr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1568 ----PTIVFVSSRRQ-----TRLTALDLITfvagesnpkqflhipEDEIELILQNIREQNLKFCLAF----------GIG 1628
Cdd:COG4581 239 ggllPAIVFIFSRRGcdeaaQQLLSARLTT---------------KEERAEIREAIDEFAEDFSVLFgktlsrllrrGIA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1629 LHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKGTEYFDGkvKKYVDMPITDVLQMMGRAGRPQFDN 1708
Cdd:COG4581 304 VHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDG--ERHRPLTAREFHQIAGRAGRRGIDT 381
|
410 420 430
....*....|....*....|....*....|...
gi 24647182 1709 EGVAVVLVHDEKKnfYKKFLY----DPFPVESS 1737
Cdd:COG4581 382 EGHVVVLAPEHDD--PKKFARlasaRPEPLRSS 412
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
503-1047 |
6.71e-50 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 191.18 E-value: 6.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGvinrdeFKIVYIAPMKALAAEMVDNFsKRLKSLQIAVRELTGDIQLTK 582
Cdd:PRK00254 40 KNLVLAIPTASGKTLVAEIVMVNKL---LREG------GKAVYLVPLKALAEEKYREF-KDWEKLGLRVAMTTGDYDSTD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 583 AEMAATQILVTTPEKWDVVTRKGSgdvALISLVELLIIDEVHLLHG-ERGPVVEALVARTLrlvessqSMIRIVGLSATL 661
Cdd:PRK00254 110 EWLGKYDIIIATAEKFDSLLRHGS---SWIKDVKLVVADEIHLIGSyDRGATLEMILTHML-------GRAQILGLSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 662 PNYIDVAHFLRVNPMKglfyfdSRFRPVPLDTN-----FVGIKSVKQLQQIADMDQCCYqkcvEMVQEGHQIMVFVHARN 736
Cdd:PRK00254 180 GNAEELAEWLNAELVV------SDWRPVKLRKGvfyqgFLFWEDGKIERFPNSWESLVY----DAVKKGKGALVFVNTRR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 737 ATVRTANVIRELAQqnntSALFLPKDSAAHGLATRSIQRSRNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVL 816
Cdd:PRK00254 250 SAEKEALELAKKIK----RFLTKPELRALKELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 817 VCTATLAWGVNLPAHAVIIRGTDIYdAKHGsFVDLGILDVLQIFGRAGRPQFDKSGVGTIITSYDK----LNHYL----- 887
Cdd:PRK00254 326 TATPTLSAGINLPAFRVIIRDTKRY-SNFG-WEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEpsklMERYIfgkpe 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 888 ---SLLTNqfpiESNF---VNCLADNLNaeiglgtITNVDEAIEWLSYTYlfvrmrinphvygieYSELEKDP-TLEARR 960
Cdd:PRK00254 404 klfSMLSN----ESAFrsqVLALITNFG-------VSNFKELVNFLERTF---------------YAHQRKDLySLEEKA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 961 RALImsaamsldkarMMRFNQRTMDMNITD------LGRTASYFYIKYDTVETFNELMKPFMTQAE---ILAMISQAQEF 1031
Cdd:PRK00254 458 KEIV-----------YFLLENEFIDIDLEDrfiplpLGIRTSQLYIDPLTAKKFKDAFPKIEKNPNplgIFQLIASTPDM 526
|
570
....*....|....*.
gi 24647182 1032 QQLKVRDDEMEELDEL 1047
Cdd:PRK00254 527 TPLNYSRKEMEDLLDE 542
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
502-1047 |
3.84e-48 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 185.09 E-value: 3.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHTIRCHLeqgvinrdefKIVYIAPMKALAAEMVDNFSkRLKSLQIAVRELTGDIQLT 581
Cdd:PRK01172 37 GENVIVSVPTAAGKTLIAYSAIYETFLAGL----------KSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGDYDDP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 582 KAEMAATQILVTTPEKWDVVTRKgsgDVALISLVELLIIDEVHLLHGE-RGPVVEAlVARTLRLVESSqsmIRIVGLSAT 660
Cdd:PRK01172 106 PDFIKRYDVVILTSEKADSLIHH---DPYIINDVGLIVADEIHIIGDEdRGPTLET-VLSSARYVNPD---ARILALSAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 661 LPNYIDVAHFLRVNPMKglfyfdSRFRPVPLDTnfvGIKSVKQL----QQIADMDQCCYQKcvEMVQEGHQIMVFVHARN 736
Cdd:PRK01172 179 VSNANELAQWLNASLIK------SNFRPVPLKL---GILYRKRLildgYERSQVDINSLIK--ETVNDGGQVLVFVSSRK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 737 ATVRTAnviRELAQQNNTSALFLPKDSAAHGLatrsiqrsrNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVL 816
Cdd:PRK01172 248 NAEDYA---EMLIQHFPEFNDFKVSSENNNVY---------DDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 817 VCTATLAWGVNLPAHAVIIRgtDIYDAKHGSFVDLGILDVLQIFGRAGRPQFDKSGVGTII----TSYDKLNHYLSllTN 892
Cdd:PRK01172 316 VATPTLAAGVNLPARLVIVR--DITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYaaspASYDAAKKYLS--GE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 893 QFPIESNFVN--CLADNLNAEIGLGTITNVDEAIEWLSYTYLFVRMRINPHVYGIEYSE--LEKDPtlearrralimsaa 968
Cdd:PRK01172 392 PEPVISYMGSqrKVRFNTLAAISMGLASSMEDLILFYNETLMAIQNGVDEIDYYIESSLkfLKENG-------------- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 969 msldkarmmrFNQRTMDMNITDLGRTASYFYIKydtVETFNELMKPFMTQAEI---LAMISQAQEFQQLKVRDDE--MEE 1043
Cdd:PRK01172 458 ----------FIKGDVTLRATRLGKLTSDLYID---PESALILKSAFDHDYDEdlaLYYISLCREIIPANTRDDYyaMEF 524
|
....
gi 24647182 1044 LDEL 1047
Cdd:PRK01172 525 LEDI 528
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
486-683 |
2.53e-47 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 168.32 E-value: 2.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 486 ELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRchleqgviNRDEFKIVYIAPMKALAAEMVDNFSKRLK 565
Cdd:cd18022 1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFN--------KYPGSKVVYIAPLKALVRERVDDWKKRFE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 566 -SLQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSgDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRL 644
Cdd:cd18022 73 eKLGKKVVELTGDVTPDMKALADADIIITTPEKWDGISRSWQ-TREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYI 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 24647182 645 VESSQSMIRIVGLSATLPNYIDVAHFLRVNPMkGLFYFD 683
Cdd:cd18022 152 SSQTEKPVRLVGLSTALANAGDLANWLGIKKM-GLFNFR 189
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
1338-1524 |
3.34e-47 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 168.38 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1338 NPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQN---------PKCKVVYIAPLKALVKERIADWEQRFqr 1408
Cdd:cd18020 3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHvnqggvikkDDFKIVYIAPMKALAAEMVEKFSKRL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1409 SSLGLKVVELTGDVTPDIQAIRESQLIVTTPEKWDGISR-SWQTREYVQHVSLIVIDEIHLLGEDRGPVIEVIVSRTNFI 1487
Cdd:cd18020 81 APLGIKVKELTGDMQLTKKEIAETQIIVTTPEKWDVVTRkSSGDVALSQLVRLLIIDEVHLLHDDRGPVIESLVARTLRQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 24647182 1488 SSHTGRAIRIVGLSTALANAQDLANWLGINKM-GLYNF 1524
Cdd:cd18020 161 VESTQSMIRIVGLSATLPNYLDVADFLRVNPYkGLFFF 198
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
687-878 |
4.89e-47 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 166.19 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 687 RPVPLDTNFVGIKSVKQLQQIADM----DQCCYQKCVEMVQEGHQIMVFVHARNATVRTANVIRelaqqnntsalflpkd 762
Cdd:cd18795 1 RPVPLEEYVLGFNGLGIKLRVDVMnkfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 763 saahglatrsiqrsrnkqlvelfscGLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTDIYD 842
Cdd:cd18795 65 -------------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYD 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 24647182 843 AKHgsFVDLGILDVLQIFGRAGRPQFDKSGVGTIIT 878
Cdd:cd18795 120 GKG--YRELSPLEYLQMIGRAGRPGFDTRGEAIIMT 153
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
501-883 |
3.37e-43 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 170.91 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 501 SNENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGvinrdefKIVYIAPMKALAAEMVDNFSkRLKSLQIAVRELTGDIQL 580
Cdd:PRK02362 38 DGKNLLAAIPTASGKTLIAELAMLKAI---ARGG-------KALYIVPLRALASEKFEEFE-RFEELGVRVGISTGDYDS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 TKAEMAATQILVTTPEKWDVVTRKGSGDVALISLVellIIDEVHLL-HGERGPVVEALVARTLRLVESSQsmirIVGLSA 659
Cdd:PRK02362 107 RDEWLGDNDIIVATSEKVDSLLRNGAPWLDDITCV---VVDEVHLIdSANRGPTLEVTLAKLRRLNPDLQ----VVALSA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 660 TLPNYIDVAHFLR----------VNPMKGLFY-----FDSRFRPVPldtnfvgIKSVKQLQQIadmdqccyqkCVEMVQE 724
Cdd:PRK02362 180 TIGNADELADWLDaelvdsewrpIDLREGVFYggaihFDDSQREVE-------VPSKDDTLNL----------VLDTLEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 725 GHQIMVFVHAR-NATV---RTANVIRELAQQNNTSALflpkdsaaHGLATRSIQRSRNKQLVELFSC---GLAMHHAGML 797
Cdd:PRK02362 243 GGQCLVFVSSRrNAEGfakRAASALKKTLTAAERAEL--------AELAEEIREVSDTETSKDLADCvakGAAFHHAGLS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 798 RADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTDIYDAKHGSfVDLGILDVLQIFGRAGRPQFDKSGVGTII 877
Cdd:PRK02362 315 REHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAGM-QPIPVLEYHQMAGRAGRPGLDPYGEAVLL 393
|
....*..
gi 24647182 878 T-SYDKL 883
Cdd:PRK02362 394 AkSYDEL 400
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
485-683 |
1.51e-41 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 152.03 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHtircHLEQGvinrDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:cd18021 2 KFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLR----HWRQN----PKGRAVYIAPMQELVDARYKDWRAKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KS-LQIAVRELTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSGDVALISlVELLIIDEVHLLHGERGPVVEALVARTlR 643
Cdd:cd18021 74 GPlLGKKVVKLTGETSTDLKLLAKSDVILATPEQWDVLSRRWKQRKNVQS-VELFIADELHLIGGENGPVYEVVVSRM-R 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24647182 644 LVeSSQ--SMIRIVGLSATLPNYIDVAHFLRVNPmKGLFYFD 683
Cdd:cd18021 152 YI-SSQleKPIRIVGLSSSLANARDVGEWLGASK-STIFNFH 191
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
1337-1515 |
9.89e-37 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 137.47 E-value: 9.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1337 FNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPkcKVVYIAPLKALVKERIadweQRFQR-SSLGLKV 1415
Cdd:cd18028 2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG--KALYLVPLRALASEKY----EEFKKlEEIGLKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1416 VELTGDVTPDIQAIRESQLIVTTPEKWDGISR---SWqtreyVQHVSLIVIDEIHLLG-EDRGPVIEVIVSRTNfissHT 1491
Cdd:cd18028 76 GISTGDYDEDDEWLGDYDIIVATYEKFDSLLRhspSW-----LRDVGVVVVDEIHLISdEERGPTLESIVARLR----RL 146
|
170 180
....*....|....*....|....
gi 24647182 1492 GRAIRIVGLSTALANAQDLANWLG 1515
Cdd:cd18028 147 NPNTQIIGLSATIGNPDELAEWLN 170
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
1338-1510 |
6.13e-35 |
|
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: 131.98 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1338 NPIQTQIFHCLYhTDNNVLLGAPTGSGKTIVAEIAIFRALNQN-PKCKVVYIAPLKALVKERIADWEQRFqrSSLGLKVV 1416
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALDKLdNGPQALVLAPTRELAEQIYEELKKLG--KGLGLKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1417 ELTGDVTPDIQ--AIRESQLIVTTPEKWDGIsrsWQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRTNFisshtgr 1493
Cdd:pfam00270 78 SLLGGDSRKEQleKLKGPDILVGTPGRLLDL---LQERKLLKNLKLLVLDEAHrLLDMGFGPDLEEILRRLPK------- 147
|
170
....*....|....*...
gi 24647182 1494 AIRIVGLS-TALANAQDL 1510
Cdd:pfam00270 148 KRQILLLSaTLPRNLEDL 165
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
498-900 |
1.11e-34 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 144.31 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMlsivHTIRCHLEQGVinrdefKIVYIAPMKALAAEMVDNFSKRLKSlqIAVRELTGD 577
Cdd:COG4581 36 ALEAGRSVLVAAPTGSGKTLVAE----FAIFLALARGR------RSFYTAPIKALSNQKFFDLVERFGA--ENVGLLTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 578 IQL---------TkAEMAATQILVTTPEKWDVvtrkgsgdvalislvELLIIDEVHLL-HGERGPVVEALVartLRLVES 647
Cdd:COG4581 104 ASVnpdapivvmT-TEILRNMLYREGADLEDV---------------GVVVMDEFHYLaDPDRGWVWEEPI---IHLPAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 648 sqsmIRIVGLSATLPNYIDVAHFLR--------VnpmkglfyfDSRFRPVPLDTNFVGIKSVKQLQQIADMDQCCYQKC- 718
Cdd:COG4581 165 ----VQLVLLSATVGNAEEFAEWLTrvrgetavV---------VSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSRHe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 719 -VEMVQEGHQ--IMVFVHARNATVRTAnviRELAQQNNTSALflPKDSAAHGLATRSIQRS--RNKQLVELFSCGLAMHH 793
Cdd:COG4581 232 vIEELDRGGLlpAIVFIFSRRGCDEAA---QQLLSARLTTKE--ERAEIREAIDEFAEDFSvlFGKTLSRLLRRGIAVHH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 794 AGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTDIYDAKhgSFVDLGILDVLQIFGRAGRPQFDKSG- 872
Cdd:COG4581 307 AGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGE--RHRPLTAREFHQIAGRAGRRGIDTEGh 384
|
410 420
....*....|....*....|....*....
gi 24647182 873 VGTIITSYDKLNHYLSLLTNQ-FPIESNF 900
Cdd:COG4581 385 VVVLAPEHDDPKKFARLASARpEPLRSSF 413
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
488-666 |
2.54e-33 |
|
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: 127.36 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 488 NRIQSVVFPVAYhSNENMLVCAPTGAGKTNVAMLSIVHTIRchleqgvINRDEFKIVYIAPMKALAAEMVDNFSKRLKSL 567
Cdd:pfam00270 1 TPIQAEAIPAIL-EGRDVLVQAPTGSGKTLAFLLPALEALD-------KLDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 568 QIAVRELTG--DIQLTKAEMAATQILVTTPEKWDVVTRKgsgdVALISLVELLIIDEVHLLHGE-RGPVVEALVARTlrl 644
Cdd:pfam00270 73 GLKVASLLGgdSRKEQLEKLKGPDILVGTPGRLLDLLQE----RKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRL--- 145
|
170 180
....*....|....*....|..
gi 24647182 645 vessQSMIRIVGLSATLPNYID 666
Cdd:pfam00270 146 ----PKKRQILLLSATLPRNLE 163
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
486-671 |
3.26e-30 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type 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: 350786 [Multi-domain] Cd Length: 177 Bit Score: 118.98 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 486 ELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGvinrdefKIVYIAPMKALAAEMVDNFSKRLK 565
Cdd:cd18028 1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTL---LEGG-------KALYLVPLRALASEKYEEFKKLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 566 -SLQIAVRelTGDIQLTKAEMAATQILVTTPEKWDVVTRKGSgdvALISLVELLIIDEVHLLHG-ERGPVVEALVARTLR 643
Cdd:cd18028 71 iGLKVGIS--TGDYDEDDEWLGDYDIIVATYEKFDSLLRHSP---SWLRDVGVVVVDEIHLISDeERGPTLESIVARLRR 145
|
170 180
....*....|....*....|....*...
gi 24647182 644 LVESSQsmirIVGLSATLPNYIDVAHFL 671
Cdd:cd18028 146 LNPNTQ----IIGLSATIGNPDELAEWL 169
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1332-1532 |
1.53e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 114.90 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1332 YKFTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVkeriADWEQRFQR--S 1409
Cdd:smart00487 4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELA----EQWAEELKKlgP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1410 SLGLKVVELTGDVTPDIQ----AIRESQLIVTTPEKWDGISRSWqtREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRT 1484
Cdd:smart00487 80 SLGLKVVGLYGGDSKREQlrklESGKTDILVTTPGRLLDLLEND--KLSLSNVDLVILDEAHrLLDGGFGDQLEKLLKLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24647182 1485 NfisshtgRAIRIVGLS-TALANAQDLANWLGINKMGLYNFKPSVRPVP 1532
Cdd:smart00487 158 P-------KNVQLLLLSaTPPEEIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
1353-1716 |
2.75e-28 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 124.23 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1353 NNVLLGAPTGSGKTIVAEIA-IFRALNQnpKCKVVYIAPLKALVKERIADWEQRFQRsslGLKVVELTGDV---TPDIQA 1428
Cdd:COG1202 226 KDQLVVSATATGKTLIGELAgIKNALEG--KGKMLFLVPLVALANQKYEDFKDRYGD---GLDVSIRVGASrirDDGTRF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1429 IRESQLIVTTPEKWDGISRswqTREYVQHVSLIVIDEIHLLGE-DRGPVIEVIVSRTNFISSHTgraiRIVGLSTALANA 1507
Cdd:COG1202 301 DPNADIIVGTYEGIDHALR---TGRDLGDIGTVVIDEVHMLEDpERGHRLDGLIARLKYYCPGA----QWIYLSATVGNP 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1508 QDLANWLGInKMGLYNfkpsVRPVPLQVHINGFPGKHYCPRMATMNRPTFQAIRTYSPCEPTIVFVSSRRQTRLTAldli 1587
Cdd:COG1202 374 EELAKKLGA-KLVEYE----ERPVPLERHLTFADGREKIRIINKLVKREFDTKSSKGYRGQTIIFTNSRRRCHEIA---- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1588 tfvagesnpkQFLHIPEDEielilqnireqnlkfclafgiglHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP 1667
Cdd:COG1202 445 ----------RALGYKAAP-----------------------YHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFP 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24647182 1668 AHLVVikgteyFDGkvkkyVDMPI-----TDVLQMMGRAGRPQFDNEGVAVVLV 1716
Cdd:COG1202 492 ASQVI------FDS-----LAMGIewlsvQEFHQMLGRAGRPDYHDRGKVYLLV 534
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
485-690 |
1.49e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 109.12 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:smart00487 7 EPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRG--------KGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQI-AVRELTGD---IQLTKAEMAATQILVTTPEKWDVVTRKGSGDValiSLVELLIIDEVH-LLHGERGPVVEALVA 639
Cdd:smart00487 79 PSLGLkVVGLYGGDskrEQLRKLESGKTDILVTTPGRLLDLLENDKLSL---SNVDLVILDEAHrLLDGGFGDQLEKLLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24647182 640 RTLRlvessqsMIRIVGLSATLPNYIDVAHFLRvnpMKGLFYFDSRFRPVP 690
Cdd:smart00487 156 LLPK-------NVQLLLLSATPPEEIENLLELF---LNDPVFIDVGFTPLE 196
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
502-671 |
7.11e-26 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 106.13 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQGVinrdefKIVYIAPMKALAAEMVDNFSKRLKSLQ----IAVRelTGD 577
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGV------QVLYISPLKALINDQERRLEEPLDEIDleipVAVR--HGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 578 I-QLTKAEMAAT--QILVTTPEKWDV--VTRKGSGdvaLISLVELLIIDEVH-LLHGERGPVVEALVARTLRLVESSqsm 651
Cdd:cd17922 73 TsQSEKAKQLKNppGILITTPESLELllVNKKLRE---LFAGLRYVVVDEIHaLLGSKRGVQLELLLERLRKLTGRP--- 146
|
170 180
....*....|....*....|
gi 24647182 652 IRIVGLSATLPNYIDVAHFL 671
Cdd:cd17922 147 LRRIGLSATLGNLEEAAAFL 166
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
1352-1514 |
2.20e-24 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 101.51 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALNQNPK--CKVVYIAPLKALvkerIADWEQRFQR----SSLGLKVVELTGDVTpd 1425
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEkgVQVLYISPLKAL----INDQERRLEEpldeIDLEIPVAVRHGDTS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1426 iQAIRESQL------IVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRtnfISSHTGRAIRIV 1498
Cdd:cd17922 75 -QSEKAKQLknppgiLITTPESLELLLVNKKLRELFAGLRYVVVDEIHaLLGSKRGVQLELLLER---LRKLTGRPLRRI 150
|
170
....*....|....*.
gi 24647182 1499 GLSTALANAQDLANWL 1514
Cdd:cd17922 151 GLSATLGNLEEAAAFL 166
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1299-1719 |
1.32e-23 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 109.15 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1299 HLVLPEHHPPLTEL-LPLRPLPVSCLKNVVYESLYKFthfnpiQTQIFHcLYHTDNNVLLGAPTGSGKTIVAEIAIFRAL 1377
Cdd:COG1205 24 VRTIPAREARYAPWpDWLPPELRAALKKRGIERLYSH------QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1378 NQNPKCKVVYIAPLKALVKERIADWEQRFQRSSLGLKVVELTGDVTPDI-QAIRE-SQLIVTTPekwDGISRS------- 1448
Cdd:COG1205 97 LEDPGATALYLYPTKALARDQLRRLRELAEALGLGVRVATYDGDTPPEErRWIREhPDIVLTNP---DMLHYGllphhtr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1449 WqtREYVQHVSLIVIDEIHLLgedRGpvieV-------IVSRTNFISSHTGRAIRIVGLSTALANAQDLANWL-Ginkmg 1520
Cdd:COG1205 174 W--ARFFRNLRYVVIDEAHTY---RG----VfgshvanVLRRLRRICRHYGSDPQFILASATIGNPAEHAERLtG----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1521 lynfkpsvRPVplqVHI--NGFP--GKHY-----CPRMATMNRPTFQA------------IRtyspcepTIVFVSSRRQT 1579
Cdd:COG1205 240 --------RPV---TVVdeDGSPrgERTFvlwnpPLVDDGIRRSALAEaarlladlvregLR-------TLVFTRSRRGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1580 rltaldlitfvagesnpkqflhipedeiELILQNIREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATAT 1659
Cdd:COG1205 302 ----------------------------ELLARYARRALREPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNA 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24647182 1660 LAWGVNLPA-HLVVIKGteYfdgkvkkyvdmP--ITDVLQMMGRAGRpqfDNEGVAVVLVHDE 1719
Cdd:COG1205 354 LELGIDIGGlDAVVLAG--Y-----------PgtRASFWQQAGRAGR---RGQDSLVVLVAGD 400
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
1354-1526 |
8.87e-23 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 98.44 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKcKVVYIAPLKALVKERIaDWEQRFQrSSLGLKVVELTGDVTPDIQAIRES- 1432
Cdd:cd18026 35 NLVYSLPTSGGKTLVAEILMLKRLLERRK-KALFVLPYVSIVQEKV-DALSPLF-EELGFRVEGYAGNKGRSPPKRRKSl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1433 QLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLGE-DRGPVIEVIVSRtnfISSHTGRAIRIVGLSTALANAQDLA 1511
Cdd:cd18026 112 SVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDgHRGALLELLLTK---LLYAAQKNIQIVGMSATLPNLEELA 188
|
170
....*....|....*..
gi 24647182 1512 NWLginKMGLY--NFKP 1526
Cdd:cd18026 189 SWL---RAELYttNFRP 202
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
502-688 |
3.12e-19 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 88.04 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrdEFKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDI-QL 580
Cdd:cd18026 33 GRNLVYSLPTSGGKTLVAEILMLKRLLER---------RKKALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGNKgRS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 TKAEMAATQILVTTPEKWDVVTRKG--SGDVALISLVellIIDEVHLL-HGERGPVVEALVARtlrLVESSQSMIRIVGL 657
Cdd:cd18026 104 PPKRRKSLSVAVCTIEKANSLVNSLieEGRLDELGLV---VVDELHMLgDGHRGALLELLLTK---LLYAAQKNIQIVGM 177
|
170 180 190
....*....|....*....|....*....|.
gi 24647182 658 SATLPNYIDVAHFLRVnpmkglFYFDSRFRP 688
Cdd:cd18026 178 SATLPNLEELASWLRA------ELYTTNFRP 202
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
498-671 |
6.70e-19 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 94.01 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMLSIV-----HTIRCHLEQGVinrdefKIVYIAPMKALA-----------AEMVDNFS 561
Cdd:COG1201 35 AIAAGESTLLIAPTGSGKTLAAFLPALdelarRPRPGELPDGL------RVLYISPLKALAndiernlraplEEIGEAAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 562 KRLKSLQIAVRelTGDiqlT----KAEMAAT--QILVTTPEkwdvvtrkgsgdvaliSL---------------VELLII 620
Cdd:COG1201 109 LPLPEIRVGVR--TGD---TpaseRQRQRRRppHILITTPE----------------SLallltspdarellrgVRTVIV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24647182 621 DEVH-LLHGERGpvveALVARTL-RLVESSQSMIRIVGLSATLPNYIDVAHFL 671
Cdd:COG1201 168 DEIHaLAGSKRG----VHLALSLeRLRALAPRPLQRIGLSATVGPLEEVARFL 216
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
1293-1514 |
8.29e-19 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 87.11 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1293 IPLSFQHLVLPEHHPPLTellPLRPlpvsclknvvyeslYKFThFNPIQTQIFHCLyhtDNN--VLLGAPTGSGKTIVAE 1370
Cdd:cd18024 7 LPPDYDYTPISAHKPPGN---PART--------------YPFT-LDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1371 IAIFRALNQnpKCKVVYIAPLKALVKERIADWEQRFQrsSLGLkvveLTGDVTPDIQAireSQLIVTTPekwdgISRSWQ 1450
Cdd:cd18024 66 YAIAQSLRD--KQRVIYTSPIKALSNQKYRELQEEFG--DVGL----MTGDVTINPNA---SCLVMTTE-----ILRSML 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 1451 TR--EYVQHVSLIVIDEIHLLGE-DRGPVIEvivsRTNFISSHTgraIRIVGLSTALANAQDLANWL 1514
Cdd:cd18024 130 YRgsEIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPDK---VRYVFLSATIPNARQFAEWI 189
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
1356-1672 |
1.02e-17 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 89.92 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1356 LLGAPTGSGKT------IVAEIAIFRALNQNPkCKVVYIAPLKALVKeriaDWEQRFQR--SSLGLKV-VEL-TGDvTPd 1425
Cdd:TIGR04121 32 LLIAPTGSGKTlagflpSLIDLAGPEAPKEKG-LHTLYITPLRALAV----DIARNLQApiEELGLPIrVETrTGD-TS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1426 iQAIRESQ------LIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRTNFISShtgrAIRIV 1498
Cdd:TIGR04121 105 -SSERARQrkkppdILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHeLAGSKRGDQLELALARLRRLAP----GLRRW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1499 GLSTALANAQDLANWLginkMGLYNFKPSV------RPVPLQVHI---------NGFPGKHYCPRMAtmnrPTFQAIRTy 1563
Cdd:TIGR04121 180 GLSATIGNLEEARRVL----LGVGGAPAVLvrgklpKAIEVISLLpeseerfpwAGHLGLRALPEVY----AEIDQART- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1564 spcepTIVFVSSRRQTrltaldlitfvagesnpkqflhipedeiELILQNIREQNLKFCLAfgIGLHHAGLQEQDRKCVE 1643
Cdd:TIGR04121 251 -----TLVFTNTRSQA----------------------------ELWFQALWEANPEFALP--IALHHGSLDREQRRWVE 295
|
330 340 350
....*....|....*....|....*....|
gi 24647182 1644 ELFLNRKIQILVATATLAWGVN-LPAHLVV 1672
Cdd:TIGR04121 296 AAMAAGRLRAVVCTSSLDLGVDfGPVDLVI 325
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
1333-1660 |
1.42e-17 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 89.78 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQIFHcLYHTDNNVLLGAPTGSGKT------IVAEIAiFRALNQNPK--CKVVYIAPLKALVkeriADWEQ 1404
Cdd:COG1201 21 RFGAPTPPQREAWP-AIAAGESTLLIAPTGSGKTlaaflpALDELA-RRPRPGELPdgLRVLYISPLKALA----NDIER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1405 RFQ------RSSLGLKVVEL-----TGDvTPdiQAIRESQL------IVTTPE---------KWdgisrswqtREYVQHV 1458
Cdd:COG1201 95 NLRapleeiGEAAGLPLPEIrvgvrTGD-TP--ASERQRQRrrpphiLITTPEslallltspDA---------RELLRGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1459 SLIVIDEIH-LLGEDRGPVIEVIVSRtnfISSHTGRAIRIVGLSTALANAQDLANWLGinkmGlynfKPSVRPVplqVHI 1537
Cdd:COG1201 163 RTVIVDEIHaLAGSKRGVHLALSLER---LRALAPRPLQRIGLSATVGPLEEVARFLV----G----YEDPRPV---TIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1538 NGFPGKHY-----CPRMATMNRPT-------------FQAI---RTyspcepTIVFVSSRRQTrltaldlitfvagesnp 1596
Cdd:COG1201 229 DAGAGKKPdlevlVPVEDLIERFPwaghlwphlyprvLDLIeahRT------TLVFTNTRSQA----------------- 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647182 1597 kqflhipedeiELILQNIREQNLKFCLAfgIGLHHAGL-QEQDRKcVEELFLNRKIQILVATATL 1660
Cdd:COG1201 286 -----------ERLFQRLNELNPEDALP--IAAHHGSLsREQRLE-VEEALKAGELRAVVATSSL 336
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
502-868 |
4.49e-17 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 88.02 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSivhtirchleqGVIN--RDEFKIVYIAPMKALAAEMVDNFSKRL-KSLQIAVRELTGDI 578
Cdd:COG1202 225 GKDQLVVSATATGKTLIGELA-----------GIKNalEGKGKMLFLVPLVALANQKYEDFKDRYgDGLDVSIRVGASRI 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 579 QLTKAE--MAAtQILVTTPEKWDVVTRKGS--GDVALIslvellIIDEVHLLH-GERGPVVEALVARTLRLVESSQsmir 653
Cdd:COG1202 294 RDDGTRfdPNA-DIIVGTYEGIDHALRTGRdlGDIGTV------VIDEVHMLEdPERGHRLDGLIARLKYYCPGAQ---- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 654 IVGLSATLPNYIDVAHFLRVNPMKglfyFDSrfRPVPLDTNFVGIKSVKQLQQIAdmdqccyqkcvEMVQE--------G 725
Cdd:COG1202 363 WIYLSATVGNPEELAKKLGAKLVE----YEE--RPVPLERHLTFADGREKIRIIN-----------KLVKRefdtksskG 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 726 H--QIMVFVHARnatvRTANVIrelaqqnntsALFLPKDSAAhglatrsiqrsrnkqlvelfscglamHHAGMLRADRQM 803
Cdd:COG1202 426 YrgQTIIFTNSR----RRCHEI----------ARALGYKAAP--------------------------YHAGLDYGERKK 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24647182 804 VEKYFVEGHISVLVCTATLAWGVNLPAHAVIirgtdiydakhgsFVDL--GI--LDV---LQIFGRAGRPQF 868
Cdd:COG1202 466 VERRFADQELAAVVTTAALAAGVDFPASQVI-------------FDSLamGIewLSVqefHQMLGRAGRPDY 524
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
1353-1480 |
4.60e-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: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1353 NNVLLGAPTGSGKTIVAEIAIFRALNQNPKcKVVYIAPLKALVKeriaDWEQRFQ-RSSLGLKVVELTGDVTPDIQ---A 1428
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLKKGK-KVLVLVPTKALAL----QTAERLReLFGPGIRVAVLVGGSSAEEReknK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 24647182 1429 IRESQLIVTTPEKWDGISRSwQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVI 1480
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLR-EDRLFLKDLKLIIVDEAHaLLIDSRGALILDL 128
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
1338-1522 |
2.67e-15 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 76.15 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1338 NPIQTQIFHCLYHTDNnVLLGAPTGSGKTIVAEIAIfrALNQNPKCKVVYIAPLKALVKERIADWEQRFqrSSLGLkvve 1417
Cdd:cd18027 10 DVFQKQAILHLEAGDS-VFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNTF--GDVGL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1418 LTGDVTPDIQAireSQLIVTTPekwdgISRS--WQTREYVQHVSLIVIDEIHLLGE-DRGPVIEVIVSrtnFISSHtgra 1494
Cdd:cd18027 81 ITGDVQLNPEA---SCLIMTTE-----ILRSmlYNGSDVIRDLEWVIFDEVHYINDaERGVVWEEVLI---MLPDH---- 145
|
170 180
....*....|....*....|....*....
gi 24647182 1495 IRIVGLSTALANAQDLANWLG-INKMGLY 1522
Cdd:cd18027 146 VSIILLSATVPNTVEFADWIGrIKKKNIY 174
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
500-766 |
1.43e-14 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 79.93 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 500 HSNENMLVCAPTGAGKTNVAMLSIVHTI-----RCHLEQGVInrdefkIVYIAPMKALAAEMVDNFSKRLKSLQ------ 568
Cdd:PRK13767 45 HEGKNVLISSPTGSGKTLAAFLAIIDELfrlgrEGELEDKVY------CLYVSPLRALNNDIHRNLEEPLTEIReiaker 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 569 --------IAVRelTGDI-QLTKAEMAAT--QILVTTPEkwdvvtrkgSGDVALIS--------LVELLIIDEVHLLHG- 628
Cdd:PRK13767 119 geelpeirVAIR--TGDTsSYEKQKMLKKppHILITTPE---------SLAILLNSpkfreklrTVKWVIVDEIHSLAEn 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 629 ERGPVVEALVARTLRLVEssQSMIRIvGLSATLPNYIDVAHFLrvnpmkGLFYFDSRFRPVPL-DTNFVGIKSVKQLQQI 707
Cdd:PRK13767 188 KRGVHLSLSLERLEELAG--GEFVRI-GLSATIEPLEEVAKFL------VGYEDDGEPRDCEIvDARFVKPFDIKVISPV 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 708 ADM--------DQCCYQKCVEMVQEGHQIMVFVHARNATVRTANVIRELAQQNntsalFLPKDSAAH 766
Cdd:PRK13767 259 DDLihtpaeeiSEALYETLHELIKEHRTTLIFTNTRSGAERVLYNLRKRFPEE-----YDEDNIGAH 320
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
498-887 |
1.78e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 79.49 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrDEFKIVYIAPMKALAAEMVDNFSKRLKSLQIAVR--ELT 575
Cdd:COG1205 67 AARAGKNVVIATPTASGKSLAYLLPVLEALLED--------PGATALYLYPTKALARDQLRRLRELAEALGLGVRvaTYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 576 GDiqlTKAEM-----AATQILVTTP-----------EKWdvvtrkgsgdVALISLVELLIIDEVHLLHGERGPVVEALVA 639
Cdd:COG1205 139 GD---TPPEErrwirEHPDIVLTNPdmlhygllphhTRW----------ARFFRNLRYVVIDEAHTYRGVFGSHVANVLR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 640 RTLRLVESSQSMIRIVGLSATLPN--------------YIDV-------AHFLRVNPmkgLFYFDSRFRPVPLDTnfvgi 698
Cdd:COG1205 206 RLRRICRHYGSDPQFILASATIGNpaehaerltgrpvtVVDEdgsprgeRTFVLWNP---PLVDDGIRRSALAEA----- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 699 ksvkqlqqiADMdqccyqkCVEMVQEGHQIMVFVHARNATVRTANVIRELAQQnntsalflpkdsaaHGLATRsiqrsrn 778
Cdd:COG1205 278 ---------ARL-------LADLVREGLRTLVFTRSRRGAELLARYARRALRE--------------PDLADR------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 779 kqlvelfscgLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPA-HAVIIRGtdiYDAKHGSFvdlgildvL 857
Cdd:COG1205 321 ----------VAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVLAG---YPGTRASF--------W 379
|
410 420 430
....*....|....*....|....*....|
gi 24647182 858 QIFGRAGRPQfdKSGVGTIITSYDKLNHYL 887
Cdd:COG1205 380 QQAGRAGRRG--QDSLVVLVAGDDPLDQYY 407
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
1352-1514 |
3.84e-14 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 73.17 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFQRSSL--GLKVVE-LTGDVTpdIQA 1428
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYPpsGKSLWGvFTRDYR--HNN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1429 IRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIHLLG-EDRGPVIEVIVSrtnfisshtgrAIR--IVGLSTALA 1505
Cdd:cd18025 94 PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGqSEDGAVWEQLLL-----------LIPcpFLALSATIG 162
|
....*....
gi 24647182 1506 NAQDLANWL 1514
Cdd:cd18025 163 NPQKFHEWL 171
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1605-1704 |
4.84e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1605 DEIELILQNireqnlkfcLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP-AHLVVIKGteyfdgkv 1683
Cdd:smart00490 1 EELAELLKE---------LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYD-------- 63
|
90 100
....*....|....*....|.
gi 24647182 1684 kkyVDMPITDVLQMMGRAGRP 1704
Cdd:smart00490 64 ---LPWSPASYIQRIGRAGRA 81
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
498-830 |
8.25e-14 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 77.21 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 498 AYHSNENMLVCAPTGAGKTNVAMLSIV---HTIRCHLEQGVinrdefKIVYIAPMKALAAEMvdnfskrLKSLQIAVREL 574
Cdd:TIGR04121 24 AALEGRSGLLIAPTGSGKTLAGFLPSLidlAGPEAPKEKGL------HTLYITPLRALAVDI-------ARNLQAPIEEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 575 ---------TGDiqlTKAEMAATQ------ILVTTPEKWDV-VTRKGSGDvaLISLVELLIIDEVH-LLHGERGPVVEAL 637
Cdd:TIGR04121 91 glpirvetrTGD---TSSSERARQrkkppdILLTTPESLALlLSYPDAAR--LFKDLRCVVVDEWHeLAGSKRGDQLELA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 638 VARTLRLvessQSMIRIVGLSATLPNYIDVAHFL-RVNPMKGLFYFDSRFRPVPLDT------------NFVGIKSVKQL 704
Cdd:TIGR04121 166 LARLRRL----APGLRRWGLSATIGNLEEARRVLlGVGGAPAVLVRGKLPKAIEVISllpeseerfpwaGHLGLRALPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 705 qqiadmdqccyqkcVEMVQEGHQIMVFVHARNATVRtanVIRELAQQNNTSALFlpkdsaahglatrsiqrsrnkqlvel 784
Cdd:TIGR04121 242 --------------YAEIDQARTTLVFTNTRSQAEL---WFQALWEANPEFALP-------------------------- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24647182 785 fscgLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPA 830
Cdd:TIGR04121 279 ----IALHHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGP 320
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
502-660 |
3.72e-13 |
|
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: 68.97 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGvinrdeFKIVYIAPMKALAAEMVDNFSKRLK---SLQIAVRELTGDI 578
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLL---LKKG------KKVLVLVPTKALALQTAERLRELFGpgiRVAVLVGGSSAEE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 579 QLTKAEMAAtQILVTTPEKwdVVTRKGSGDVALISLVELLIIDEVH-LLHGERGPVVEALVARTLRLVESsqsmiRIVGL 657
Cdd:cd00046 72 REKNKLGDA-DIIIATPDM--LLNLLLREDRLFLKDLKLIIVDEAHaLLIDSRGALILDLAVRKAGLKNA-----QVILL 143
|
...
gi 24647182 658 SAT 660
Cdd:cd00046 144 SAT 146
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
503-660 |
1.46e-11 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 65.92 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHtircHLEQGVINRDEfKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIQLT- 581
Cdd:cd17927 18 KNTIICLPTGSGKTFVAVLICEH----HLKKFPAGRKG-KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 582 --KAEMAATQILVTTPEKwdVVTRKGSGDVALISLVELLIIDEVHLLHGErGPVVEALVARTLRLVESSQSMIRIVGLSA 659
Cdd:cd17927 93 svEQIVESSDVIIVTPQI--LVNDLKSGTIVSLSDFSLLVFDECHNTTKN-HPYNEIMFRYLDQKLGSSGPLPQILGLTA 169
|
.
gi 24647182 660 T 660
Cdd:cd17927 170 S 170
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
1359-1702 |
1.76e-11 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 69.95 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1359 APTGSGKTIVAEI-AIFRALNQ------NPK----CKVVYIAPLKAL---VKER-------IADWEQRFQRSSLGLKVVE 1417
Cdd:PRK09751 3 APTGSGKTLAAFLyALDRLFREggedtrEAHkrktSRILYISPIKALgtdVQRNlqiplkgIADERRRRGETEVNLRVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1418 LTGDVTPDIQA---IRESQLIVTTPEKWDGISRSwQTREYVQHVSLIVIDEIH-LLGEDRGPVIEVIVSRTNFIsSHTgR 1493
Cdd:PRK09751 83 RTGDTPAQERSkltRNPPDILITTPESLYLMLTS-RARETLRGVETVIIDEVHaVAGSKRGAHLALSLERLDAL-LHT-S 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1494 AIRIvGLSTALANAQDLANWLGINKMGLYNFKPSVR--------PVPLQVHINGFPGKHYCPRMATMNRPTFQAIRT--- 1562
Cdd:PRK09751 160 AQRI-GLSATVRSASDVAAFLGGDRPVTVVNPPAMRhpqirivvPVANMDDVSSVASGTGEDSHAGREGSIWPYIETgil 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1563 --YSPCEPTIVFVSSRRQT-----RLTALDLITFVAGESNPKQFLHIpeDEIELILQNiREQNLKFCLAFGiglHHAGLQ 1635
Cdd:PRK09751 239 deVLRHRSTIVFTNSRGLAekltaRLNELYAARLQRSPSIAVDAAHF--ESTSGATSN-RVQSSDVFIARS---HHGSVS 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647182 1636 EQDRKCVEELFLNRKIQILVATATLAWGVNLPAHLVVIKgteyfdgkvkkyVDMP--ITDVLQMMGRAG 1702
Cdd:PRK09751 313 KEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ------------VATPlsVASGLQRIGRAG 369
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1350-1467 |
1.99e-11 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 64.23 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1350 HTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKeriaDWEQRFQRssLGLKVVELTGDVTPD--IQ 1427
Cdd:pfam04851 21 NGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLE----QALEEFKK--FLPNYVEIGEIISGDkkDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 24647182 1428 AIRESQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH 1467
Cdd:pfam04851 95 SVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
790-866 |
2.69e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 61.46 E-value: 2.69e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647182 790 AMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLP-AHAVIirgtdIYDAkhgsfvDLGILDVLQIFGRAGRP 866
Cdd:smart00490 15 ARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVI-----IYDL------PWSPASYIQRIGRAGRA 81
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
1353-1467 |
3.82e-11 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 64.14 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1353 NNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALV---KERIADWEQRFqrsSLGLKVVELTGDvTP--DIQ 1427
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAqdqLRSLRELLEQL---GLGIRVATYDGD-TPreERR 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 24647182 1428 AIRES--QLIVTTP-----------EKWDGISRSWQtreyvqhvsLIVIDEIH 1467
Cdd:cd17923 92 AIIRNppRILLTNPdmlhyallphhDRWARFLRNLR---------YVVLDEAH 135
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
500-663 |
5.49e-11 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 63.76 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 500 HSNENMLVCAPTGAGKTNVAMLSIVhtirchleQGVINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLQ--IAVRELTGD 577
Cdd:cd17923 13 RAGRSVVVTTGTASGKSLCYQLPIL--------EALLRDPGSRALYLYPTKALAQDQLRSLRELLEQLGlgIRVATYDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 578 IQLTKAEMAATQ---ILVTTPEKWDV-VTRKGSGDVALISLVELLIIDEVHLLHGERGPVVEALVARTLRLVESSQSMIR 653
Cdd:cd17923 85 TPREERRAIIRNpprILLTNPDMLHYaLLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLCRRYGADPQ 164
|
170
....*....|
gi 24647182 654 IVGLSATLPN 663
Cdd:cd17923 165 FILTSATIGN 174
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
502-663 |
1.13e-10 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 62.77 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHTIRchleqgviNRDEFKIVYIAPMKAL----AAEMVDNFSKRL-KSLQIAVRELTG 576
Cdd:cd18025 16 RESALIVAPTSSGKTFISYYCMEKVLR--------ESDDGVVVYVAPTKALvnqvVAEVYARFSKKYpPSGKSLWGVFTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 577 DIQLTKAEmaATQILVTTPEKWDVVTRKgSGDVALISLVELLIIDEVHLLHG-ERGPVVEALVArtlrlvessqsMIR-- 653
Cdd:cd18025 88 DYRHNNPM--NCQVLITVPECLEILLLS-PHNASWVPRIKYVIFDEIHSIGQsEDGAVWEQLLL-----------LIPcp 153
|
170
....*....|
gi 24647182 654 IVGLSATLPN 663
Cdd:cd18025 154 FLALSATIGN 163
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
507-864 |
2.96e-10 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 66.10 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 507 VCAPTGAGKTNVAMLsivHTI-RCHLEQGVINRDEFK-----IVYIAPMKALAAEMVDNFSKRLKSLqIAVRELTGDIQL 580
Cdd:PRK09751 1 VIAPTGSGKTLAAFL---YALdRLFREGGEDTREAHKrktsrILYISPIKALGTDVQRNLQIPLKGI-ADERRRRGETEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 -----------TKAEMAA-----TQILVTTPEK-WDVVTRKGSgdvALISLVELLIIDEVHLLHG-ERGPVVEALVARTL 642
Cdd:PRK09751 77 nlrvgirtgdtPAQERSKltrnpPDILITTPESlYLMLTSRAR---ETLRGVETVIIDEVHAVAGsKRGAHLALSLERLD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 643 RLVESSQSMIrivGLSATLPNYIDVAHFLRVNpmkglfyfdsrfRPV----PLDTNFVGIKSVKQLQQIADMDQCCYQ-- 716
Cdd:PRK09751 154 ALLHTSAQRI---GLSATVRSASDVAAFLGGD------------RPVtvvnPPAMRHPQIRIVVPVANMDDVSSVASGtg 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 717 -----------------KCVEMVQEGHQIMVFVHARNATVRTANVIRELAQQNNTSALFLPKDSAAHGLATRSIQ-RSRN 778
Cdd:PRK09751 219 edshagregsiwpyietGILDEVLRHRSTIVFTNSRGLAEKLTARLNELYAARLQRSPSIAVDAAHFESTSGATSnRVQS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 779 KQLVELFScglamHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIRGTdiydakhgsfVDLGILDVLQ 858
Cdd:PRK09751 299 SDVFIARS-----HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVA----------TPLSVASGLQ 363
|
....*.
gi 24647182 859 IFGRAG 864
Cdd:PRK09751 364 RIGRAG 369
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
501-668 |
5.30e-10 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 belongs 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 61.31 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 501 SNENMLVCAPTGAGKTNVAMLSIVHTIRchleqgvinrDEFKIVYIAPMKALAAEMVDNFSKRLKSlqiaVRELTGDIQL 580
Cdd:cd18024 46 RNESVLVSAHTSAGKTVVAEYAIAQSLR----------DKQRVIYTSPIKALSNQKYRELQEEFGD----VGLMTGDVTI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 TkaemAATQILVTTPEKWDVVTRKGSgdvALISLVELLIIDEVHLLHG-ERGPVVEalvaRTLRLVESsqsMIRIVGLSA 659
Cdd:cd18024 112 N----PNASCLVMTTEILRSMLYRGS---EIMREVAWVIFDEIHYMRDkERGVVWE----ETIILLPD---KVRYVFLSA 177
|
....*....
gi 24647182 660 TLPNYIDVA 668
Cdd:cd18024 178 TIPNARQFA 186
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
1352-1467 |
1.33e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 63.60 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALnQNPKCKVVYIAPLKALVkeriadwEQ--RFQRSSLGL---KVVELTGDVTPDI 1426
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAERL-HKKGGKVLFLAPTKPLV-------EQhaEFFKEALNIpedEIVVFTGEVSPEK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24647182 1427 QAIR--ESQLIVTTPE--KWDGISRswqtREYVQHVSLIVIDEIH 1467
Cdd:COG1111 89 RKELweKARIIVATPQviENDLIAG----RIDLDDVSLLIFDEAH 129
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
1352-1468 |
1.88e-09 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain] Cd Length: 201 Bit Score: 59.75 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALNQNP---KCKVVYIAPLKALVKERIADWEQRFQRssLGLKVVELTGDVTPDI-- 1426
Cdd:cd17927 17 GKNTIICLPTGSGKTFVAVLICEHHLKKFPagrKGKVVFLANKVPLVEQQKEVFRKHFER--PGYKVTGLSGDTSENVsv 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24647182 1427 -QAIRESQLIVTTP-------EKWDGISRSwqtreyvqHVSLIVIDEIHL 1468
Cdd:cd17927 95 eQIVESSDVIIVTPqilvndlKSGTIVSLS--------DFSLLVFDECHN 136
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
478-622 |
6.56e-09 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 57.98 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 478 RLAFANCKELNRIQSVVFPVAyHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQGvinrdEFKIVYIAPMKALAAEMV 557
Cdd:cd17957 4 NLEESGYREPTPIQMQAIPIL-LHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKK-----GLRALILAPTRELASQIY 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647182 558 DNFSKRLKSLQIAVRELTGDIQLTKAEMAAT----QILVTTPEKWDVVTRKGSGDvalISLVELLIIDE 622
Cdd:cd17957 78 RELLKLSKGTGLRIVLLSKSLEAKAKDGPKSitkyDILVSTPLRLVFLLKQGPID---LSSVEYLVLDE 143
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1614-1703 |
1.16e-08 |
|
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: 54.91 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1614 IREQNLKFCLAFGIGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP-AHLVVIkgteyfdgkvkkyVDMP-- 1690
Cdd:pfam00271 28 LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN-------------YDLPwn 94
|
90
....*....|...
gi 24647182 1691 ITDVLQMMGRAGR 1703
Cdd:pfam00271 95 PASYIQRIGRAGR 107
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
1343-1470 |
2.52e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 59.27 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1343 QIFHCLYHTDNNVLLGAPTGSGKTIVAeIAIFRALNQNPkcKVVYIAPLKALVKeriaDWEQRFQRsslGLKVVELTGDV 1422
Cdd:COG1061 91 ALLAALERGGGRGLVVAPTGTGKTVLA-LALAAELLRGK--RVLVLVPRRELLE----QWAEELRR---FLGDPLAGGGK 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24647182 1423 TPdiqaiRESQLIVTTpekWDGISRSWQTREYVQHVSLIVIDEIHLLG 1470
Cdd:COG1061 161 KD-----SDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHAG 200
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
1354-1467 |
3.35e-08 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 55.74 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFR-----ALNQNPKCKVVYIAPLKALVK---ERIadweqrfqRSSLGLKVVELTGDVTPD 1425
Cdd:cd18034 18 NTIVVLPTGSGKTLIAVMLIKEmgelnRKEKNPKKRAVFLVPTVPLVAqqaEAI--------RSHTDLKVGEYSGEMGVD 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24647182 1426 IQA-------IRESQLIVTTPEkwdgISRSWQTREYVQ--HVSLIVIDEIH 1467
Cdd:cd18034 90 KWTkerwkeeLEKYDVLVMTAQ----ILLDALRHGFLSlsDINLLIFDECH 136
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
770-865 |
3.88e-08 |
|
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: 53.37 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 770 TRSIQRSRNKQLVELFSCGLAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLP-AHAVIirgtdIYDAkhgsf 848
Cdd:pfam00271 22 SQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVI-----NYDL----- 91
|
90
....*....|....*..
gi 24647182 849 vDLGILDVLQIFGRAGR 865
Cdd:pfam00271 92 -PWNPASYIQRIGRAGR 107
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
485-677 |
4.14e-08 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 55.53 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYhSNENMLVCAPTGAGKTNVAMLSIVHTIrchLEQGVINRDEFKIVYIAPMKALAAEMVDNFSKRL 564
Cdd:cd00268 11 EKPTPIQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPILEKL---LPEPKKKGRGPQALVLAPTRELAMQIAEVARKLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 565 KSLQIAVRELTG----DIQLtKAEMAATQILVTTPEK-WDVVTRkgsGDVALiSLVELLIIDEV-HLLHGERGPVVEALV 638
Cdd:cd00268 87 KGTGLKVAAIYGgapiKKQI-EALKKGPDIVVGTPGRlLDLIER---GKLDL-SNVKYLVLDEAdRMLDMGFEEDVEKIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24647182 639 ARTLRlveSSQSMIrivgLSATLPNYID--VAHFLRvNPMK 677
Cdd:cd00268 162 SALPK---DRQTLL----FSATLPEEVKelAKKFLK-NPVR 194
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
502-624 |
4.20e-08 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.59 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIVHtiRCHLEQGvinrdefKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIQLT 581
Cdd:COG1111 17 RKNTLVVLPTGLGKTAVALLVIAE--RLHKKGG-------KVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24647182 582 K--AEMAATQILVTTPE--KWDVVTRKgsgdvalISL--VELLIIDEVH 624
Cdd:COG1111 88 KrkELWEKARIIVATPQviENDLIAGR-------IDLddVSLLIFDEAH 129
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
1333-1474 |
4.20e-08 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 58.74 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQIFHcLYHTDNNVLLGAPTGSGKTIVAEIAI----FRALNQNP---KCKVVYIAPLKAL-------VKER 1398
Cdd:PRK13767 29 KFGTFTPPQRYAIP-LIHEGKNVLISSPTGSGKTLAAFLAIidelFRLGREGEledKVYCLYVSPLRALnndihrnLEEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1399 IADWEQRFQRssLGLKVVEL-----TGDVTPdiqAIRESQL------IVTTPEKWDGISRSWQTREYVQHVSLIVIDEIH 1467
Cdd:PRK13767 108 LTEIREIAKE--RGEELPEIrvairTGDTSS---YEKQKMLkkpphiLITTPESLAILLNSPKFREKLRTVKWVIVDEIH 182
|
....*...
gi 24647182 1468 LLGED-RG 1474
Cdd:PRK13767 183 SLAENkRG 190
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
503-660 |
5.08e-08 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 55.02 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHTIRChLEQGvinrdefKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIQLTK 582
Cdd:cd18033 17 QNTLVALPTGLGKTFIAAVVMLNYYRW-FPKG-------KIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 583 A--EMAATQILVTTPEkwdVVTRKGSGDVALISLVELLIIDEVHLLHGERG--PVVEALVARTLRLvessqsmiRIVGLS 658
Cdd:cd18033 89 RaeLWASKRVFFLTPQ---TLENDLKEGDCDPKSIVCLVIDEAHRATGNYAycQVVRELMRYNSHF--------RILALT 157
|
..
gi 24647182 659 AT 660
Cdd:cd18033 158 AT 159
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
500-975 |
5.43e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.11 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 500 HSNENMLVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrdefKIVYIAPMKALAAEMVDNFSKRLKSLQIAVREltgdiq 579
Cdd:COG1061 98 RGGGRGLVVAPTGTGKTVLALALAAELLRGK-----------RVLVLVPRRELLEQWAEELRRFLGDPLAGGGK------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 580 ltkaEMAATQILVTTpekWDVVTRKGSGDvALISLVELLIIDEVHLlhgergpvveaLVARTLRLVESSQSMIRIVGLSA 659
Cdd:COG1061 161 ----KDSDAPITVAT---YQSLARRAHLD-ELGDRFGLVIIDEAHH-----------AGAPSYRRILEAFPAAYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 660 T----------LPNYIDVAHFLRVNPM--KGL---FYFDSRFRPVPLDTNFVGIKSVKQLQQIADMDQCCYQKCVEMVQE 724
Cdd:COG1061 222 TpfrsdgreilLFLFDGIVYEYSLKEAieDGYlapPEYYGIRVDLTDERAEYDALSERLREALAADAERKDKILRELLRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 725 ---GHQIMVFVharnATVRTANVIRELAQQNNTSALFLpkdsaahglatrsiqrsrnkqlvelfscglamhHAGMLRADR 801
Cdd:COG1061 302 hpdDRKTLVFC----SSVDHAEALAELLNEAGIRAAVV---------------------------------TGDTPKKER 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 802 QMVEKYFVEGHISVLVCTATLAWGVNLPA--HAVIIRGTdiydakhGSfvdLGILdvLQIFGRAGRPQFDKSGVgtiits 879
Cdd:COG1061 345 EEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPT-------GS---PREF--IQRLGRGLRPAPGKEDA------ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 880 ydklnHYLSLLTNQFPIESNFVNCLADNLNAEIGLG-TITNVDEAIEWLSYTYLFVRMRINPHVYGIEYSELEKDPTLEA 958
Cdd:COG1061 407 -----LVYDFVGNDVPVLEELAKDLRDLAGYRVEFLdEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLA 481
|
490
....*....|....*..
gi 24647182 959 RRRALIMSAAMSLDKAR 975
Cdd:COG1061 482 ELLLLELLALALELLEL 498
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
1354-1467 |
6.44e-08 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 54.83 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAeIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQRFqrsSLGLKVVELTGDVTPDIQA--IRE 1431
Cdd:cd18035 18 NTLIVLPTGLGKTIIA-ILVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVL---NIPDKITSLTGEVKPEERAerWDA 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 24647182 1432 SQLIVTTPE--KWDGISrswqTREYVQHVSLIVIDEIH 1467
Cdd:cd18035 94 SKIIVATPQviENDLLA----GRITLDDVSLLIFDEAH 127
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
503-661 |
7.47e-08 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 54.83 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHtircHLEQgVINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIqltk 582
Cdd:cd18073 18 KNTIICAPTGCGKTFVSLLICEH----HLKK-FPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 583 AEMAATQ-------ILVTTPEKwdVVTRKGSGDVALISLVELLIIDEVHLLHGERgPvVEALVARTL--RLVESSQSMIR 653
Cdd:cd18073 89 AENVPVEqiienndIIILTPQI--LVNNLKKGTIPSLSIFTLMIFDECHNTSGNH-P-YNMIMFRYLdqKLGGSSGPLPQ 164
|
....*...
gi 24647182 654 IVGLSATL 661
Cdd:cd18073 165 IIGLTASV 172
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
1354-1469 |
1.06e-07 |
|
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: 54.22 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALV---KERIADWEQRFQRSslgLKVVELTGDVTPD--IQA 1428
Cdd:cd17930 3 LVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATInqmYERIREILGRLDDE---DKVLLLHSKAALEllESD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24647182 1429 IRESQLIVTTPEKWDGISRSWQtREYV----------------QHV-------SLIVIDEIHLL 1469
Cdd:cd17930 80 EEPDDDPVEAVDWALLLKRSWL-APIVvttidqllesllkykhFERrlhglanSVVVLDEVQAY 142
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
497-661 |
1.10e-07 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 53.08 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 497 VAYHSNENMLVCAPTGAGKTNVAMLSIVHtirchleqgvinRDEFKIVYIAPMKALAAEMVDNFSKrlKSLQIAVRELTG 576
Cdd:cd17926 13 LAHKNNRRGILVLPTGSGKTLTALALIAY------------LKELRTLIVVPTDALLDQWKERFED--FLGDSSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 577 DIqltKAEMAATQILVTTpekWDVVTRKGSGDVALISLVELLIIDEVHllhgeRGPvvealvARTLRLVESSQSMIRIVG 656
Cdd:cd17926 79 GK---KKDFDDANVVVAT---YQSLSNLAEEEKDLFDQFGLLIVDEAH-----HLP------AKTFSEILKELNAKYRLG 141
|
....*
gi 24647182 657 LSATL 661
Cdd:cd17926 142 LTATP 146
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
503-671 |
1.17e-07 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 53.81 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLSIVHTIRcHLEqgvinrdefKIVYIAPMKALAAEMVDNFSKRLKSLQIavreLTGDIQLTk 582
Cdd:cd18027 24 DSVFVAAHTSAGKTVVAEYAIALAQK-HMT---------RTIYTSPIKALSNQKFRDFKNTFGDVGL----ITGDVQLN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 583 aemAATQILVTTPEKWDVVTRKGSGdvaLISLVELLIIDEVHLLH-GERGPVVEALVartLRLVESsqsmIRIVGLSATL 661
Cdd:cd18027 89 ---PEASCLIMTTEILRSMLYNGSD---VIRDLEWVIFDEVHYINdAERGVVWEEVL---IMLPDH----VSIILLSATV 155
|
170
....*....|
gi 24647182 662 PNYIDVAHFL 671
Cdd:cd18027 156 PNTVEFADWI 165
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
1352-1467 |
1.41e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.81 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1352 DNNVLLGAPTGSGKTIVAEIAIFRALNQNPKcKVVYIAPLKALVkeriadwEQ--RFQRSSLGL---KVVELTGDVTPD- 1425
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIAERLHKKGG-KVLILAPTKPLV-------EQhaEFFRKFLNIpeeKIVVFTGEVSPEk 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24647182 1426 -IQAIRESQLIVTTPE--KWDGISRSWQTREyvqhVSLIVIDEIH 1467
Cdd:PRK13766 101 rAELWEKAKVIVATPQviENDLIAGRISLED----VSLLIFDEAH 141
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
503-662 |
2.02e-07 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 53.63 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAmlsiVHTIRCHLEQGVINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLqIAVRELTGDIQL-- 580
Cdd:cd18036 18 KNTIICAPTGSGKTRVA----VYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRKG-YKVTGLSGDSSHkv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 -TKAEMAATQILVTTPEKWDVVTRKGS-GDVALISLVELLIIDEVHllHGERGPVVEALVARTLR-LVESSQSMIRIVGL 657
Cdd:cd18036 93 sFGQIVKASDVIICTPQILINNLLSGReEERVYLSDFSLLIFDECH--HTQKEHPYNKIMRMYLDkKLSSQGPLPQILGL 170
|
....*
gi 24647182 658 SATLP 662
Cdd:cd18036 171 TASPG 175
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
1359-1486 |
2.34e-07 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 52.31 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1359 APTGSGKTIVAeIAIFRALnqnPKCKVVYIAPLKALVKERIADWEQRFQRSSLGLkvveLTGDvtpDIQAIRESQLIVTT 1438
Cdd:cd17926 25 LPTGSGKTLTA-LALIAYL---KELRTLIVVPTDALLDQWKERFEDFLGDSSIGL----IGGG---KKKDFDDANVVVAT 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24647182 1439 PEKWDGISRSWqtREYVQHVSLIVIDEIHLLGedrGPVIEVIVSRTNF 1486
Cdd:cd17926 94 YQSLSNLAEEE--KDLFDQFGLLIVDEAHHLP---AKTFSEILKELNA 136
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
504-624 |
2.67e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.04 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 504 NMLVCAPTGAGKTNVAMLSIVHtiRCHLEQGvinrdefKIVYIAPMKALAAEMVDNFSK--RLKSLQIAVreLTGDIQLT 581
Cdd:PRK13766 31 NTLVVLPTGLGKTAIALLVIAE--RLHKKGG-------KVLILAPTKPLVEQHAEFFRKflNIPEEKIVV--FTGEVSPE 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24647182 582 K-AEM-AATQILVTTPE--KWDVVTRKgsgdvalISL--VELLIIDEVH 624
Cdd:PRK13766 100 KrAELwEKAKVIVATPQviENDLIAGR-------ISLedVSLLIFDEAH 141
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
1321-1467 |
3.41e-07 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 52.92 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1321 SCLKNVvyeslYKFTHFNPIQTQ-IFHCLYHTDnnVLLGAPTGSGKTIVAEIAifrALNqNPKCKVVyIAPLKALVKERI 1399
Cdd:cd17920 2 QILKEV-----FGYDEFRPGQLEaINAVLAGRD--VLVVMPTGGGKSLCYQLP---ALL-LDGVTLV-VSPLISLMQDQV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 1400 adweQRFQRssLGLKVVELTGDVTPD-----IQAIRESQ--LIVTTPEK--WDGISRSWQTREYVQHVSLIVIDEIH 1467
Cdd:cd17920 70 ----DRLQQ--LGIRAAALNSTLSPEekrevLLRIKNGQykLLYVTPERllSPDFLELLQRLPERKRLALIVVDEAH 140
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
1335-1503 |
4.94e-07 |
|
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: 54.70 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1335 THFNPIQTQIF-HCLYHTDNN---VLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVkeriadwEQRFQR-- 1408
Cdd:COG1203 126 TPINPLQNEALeLALEAAEEEpglFILTAPTGGGKTEAALLFALRLAAKHGGRRIIYALPFTSII-------NQTYDRlr 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1409 SSLGLKVVELTGDVTPDIQAIRE-----------------SQLIVTTPEK-WDGISRSWQTREYVQHV---SLIVIDEIH 1467
Cdd:COG1203 199 DLFGEDVLLHHSLADLDLLEEEEeyesearwlkllkelwdAPVVVTTIDQlFESLFSNRKGQERRLHNlanSVIILDEVQ 278
|
170 180 190
....*....|....*....|....*....|....*.
gi 24647182 1468 LLGEDRGPVIEVIVsrtNFISSHTGRAIrivgLSTA 1503
Cdd:COG1203 279 AYPPYMLALLLRLL---EWLKNLGGSVI----LMTA 307
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
503-666 |
6.57e-07 |
|
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: 51.91 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 503 ENMLVCAPTGAGKTNVAMLsivhtirCHLEQGvINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLQIA--VRELTGDIQL 580
Cdd:cd17930 2 GLVILEAPTGSGKTEAALL-------WALKLA-ARGGKRRIIYALPTRATINQMYERIREILGRLDDEdkVLLLHSKAAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 581 TKAEMAATQILVTTPEKWDVVTRK---------GSGDVALISLVE--------------LLIIDEVHLLHGER-GPVVEA 636
Cdd:cd17930 74 ELLESDEEPDDDPVEAVDWALLLKrswlapivvTTIDQLLESLLKykhferrlhglansVVVLDEVQAYDPEYmALLLKA 153
|
170 180 190
....*....|....*....|....*....|
gi 24647182 637 LVARTLRLvessqsMIRIVGLSATLPNYID 666
Cdd:cd17930 154 LLELLGEL------GGPVVLMTATLPALLR 177
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
485-659 |
1.14e-06 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.50 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAyhSNENMLVCAPTGAGKTNVA-MLsivhtIRCHLEQGVINRDEFKI-VYIAPMKALA---AEMVDN 559
Cdd:cd18034 1 FTPRSYQLELFEAA--LKRNTIVVLPTGSGKTLIAvML-----IKEMGELNRKEKNPKKRaVFLVPTVPLVaqqAEAIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 560 FSKrLKslqiaVRELTGDI-------QLTKAEMAATQILVTTPEKW-DVVTRkgsgdvALISL--VELLIIDEVHllHGe 629
Cdd:cd18034 74 HTD-LK-----VGEYSGEMgvdkwtkERWKEELEKYDVLVMTAQILlDALRH------GFLSLsdINLLIFDECH--HA- 138
|
170 180 190
....*....|....*....|....*....|
gi 24647182 630 RGPVVEALVARTLRLVESSQSMIRIVGLSA 659
Cdd:cd18034 139 TGDHPYARIMKEFYHLEGRTSRPRILGLTA 168
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
490-660 |
5.01e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 48.82 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 490 IQSVVFPVAYHSNENMLVcAPTGAGKTNVaMLSIVHTIRchleqgvINRDEFKIVYIAPMKALAAEMVDNFSKRLKSLQI 569
Cdd:pfam04851 12 IENLLESIKNGQKRGLIV-MATGSGKTLT-AAKLIARLF-------KKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 570 AVRELTGDiqLTKAEMAATQILVTTPEKWDvVTRKGSGDVALISLVELLIIDEVHllHgergpvveaLVARTLRLVESSQ 649
Cdd:pfam04851 83 IGEIISGD--KKDESVDDNKIVVTTIQSLY-KALELASLELLPDFFDVIIIDEAH--R---------SGASSYRNILEYF 148
|
170
....*....|.
gi 24647182 650 SMIRIVGLSAT 660
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
1337-1467 |
7.53e-06 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 48.47 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1337 FNPIQTQIFHclyhtdnNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERIADWEQ--RFQRSSlglk 1414
Cdd:cd18033 8 FTIVQKALFQ-------NTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKitGIPSSQ---- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 24647182 1415 VVELTGDVTPDIQAI--RESQLIVTTPEKWDG-ISRSwqtREYVQHVSLIVIDEIH 1467
Cdd:cd18033 77 TAELTGSVPPTKRAElwASKRVFFLTPQTLENdLKEG---DCDPKSIVCLVIDEAH 129
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
1354-1467 |
1.04e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain] Cd Length: 204 Bit Score: 48.63 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNPKC----KVVYIAPLKALVKERIADWEQRFQRsslGLKVVELTGDVTPDI--- 1426
Cdd:cd18036 19 NTIICAPTGSGKTRVAVYICRHHLEKRRSAgekgRVVVLVNKVPLVEQQLEKFFKYFRK---GYKVTGLSGDSSHKVsfg 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24647182 1427 QAIRESQLIVTTPEKWDGISRS--WQTREYVQHVSLIVIDEIH 1467
Cdd:cd18036 96 QIVKASDVIICTPQILINNLLSgrEEERVYLSDFSLLIFDECH 138
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
506-764 |
2.41e-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: 48.97 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 506 LVCAPTGAGKTNVAMLSIVHTIRchleqgviNRDEFKIVYIAPMKALAAEMVDNFSKRLKSL--------------QIAV 571
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLK--------SQKADRVIIALPTRATINAMYRRAKEAFGETglyhssilssrikeMGDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 572 RELTGDIQL---TKAEMAATQILVTTPEKWdVVTRKGSGDVALISLVEL----LIIDEVHLLHGE-RGPVVEALvaRTLR 643
Cdd:cd09639 75 EEFEHLFPLyihSNDTLFLDPITVCTIDQV-LKSVFGEFGHYEFTLASIanslLIFDEVHFYDEYtLALILAVL--EVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 644 LVESSqsmirIVGLSATLPNYIDvahflRVNPMKGLFYFDSRFRPVPLDTNFVGI---KSVKQLQQIADMdqccyqkcVE 720
Cdd:cd09639 152 DNDVP-----ILLMSATLPKFLK-----EYAEKIGYVEENEPLDLKPNERAPFIKiesDKVGEISSLERL--------LE 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24647182 721 MVQEGHQIMVFVHarnaTVRTA----NVIRELAQQNNTSAL---FLPKDSA 764
Cdd:cd09639 214 FIKKGGSVAIIVN----TVDRAqefyQQLKEKGPEEEIMLIhsrFTEKDRA 260
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
1333-1465 |
2.92e-05 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 47.63 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQI----FHCLYHTDNN----VLLGAPTGSGKTIVAEIAIFRALNQNPKCKV--VYIAPLKALVKErIADW 1402
Cdd:cd17956 9 GITSAFPVQAAVipwlLPSSKSTPPYrpgdLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLraLIVVPTKELVQQ-VYKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1403 EQRFQRSSlGLKVVELTGD-----------VTPDIQAIRESQLIVTTP-------EKWDGISrswqtreyVQHVSLIVID 1464
Cdd:cd17956 88 FESLCKGT-GLKVVSLSGQksfkkeqklllVDTSGRYLSRVDILVATPgrlvdhlNSTPGFT--------LKHLRFLVID 158
|
.
gi 24647182 1465 E 1465
Cdd:cd17956 159 E 159
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
490-661 |
3.15e-05 |
|
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: 46.56 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 490 IQSVVFPV--AYHSNENMLVCAPTGAGKTNVAMLSIVHtiRCHLEQGvinrdefKIVYIAPMKaLAAEMVdnfSKRL-KS 566
Cdd:cd17990 3 IAAVLPALraALDAGGQVVLEAPPGAGKTTRVPLALLA--ELWIAGG-------KIIVLEPRR-VAARAA---ARRLaTL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 567 LQIAVRELTG-DIQLTKAEMAATQILVTTPekwDVVTRKGSGDVALiSLVELLIIDEVHllhgERGPVVEALVARTLRLV 645
Cdd:cd17990 70 LGEAPGETVGyRVRGESRVGRRTRVEVVTE---GVLLRRLQRDPEL-SGVGAVILDEFH----ERSLDADLALALLLEVQ 141
|
170
....*....|....*.
gi 24647182 646 ESSQSMIRIVGLSATL 661
Cdd:cd17990 142 QLLRDDLRLLAMSATL 157
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
1353-1467 |
4.16e-05 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain] Cd Length: 163 Bit Score: 46.02 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1353 NNVLLGAPTGSGKTIVAEIAIFRALNQNPKCKVVYIAPLKALVKERiadwEQRFQRsslgLKVVELTGDVTPDIQAIRES 1432
Cdd:cd18032 21 RRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQA----ERSFKE----VLPDGSFGNLKGGKKKPDDA 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 24647182 1433 QLIVTTpekWDGISRSWQTREY-VQHVSLIVIDEIH 1467
Cdd:cd18032 93 RVVFAT---VQTLNKRKRLEKFpPDYFDLIIIDEAH 125
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
502-624 |
5.64e-05 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain] Cd Length: 181 Bit Score: 45.97 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 502 NENMLVCAPTGAGKTNVAMLSIvhtirchleQGVINRDEFKIVYIAPMKALAAEMVDNFsKRLKSLQIAVRELTGDIQLT 581
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVA---------ADRLTKKGGKVLILAPSRPLVEQHAENL-KRVLNIPDKITSLTGEVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24647182 582 KAE--MAATQILVTTPEKWDVVTRKGSGDVALISlveLLIIDEVH 624
Cdd:cd18035 86 ERAerWDASKIIVATPQVIENDLLAGRITLDDVS---LLIFDEAH 127
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
1359-1491 |
8.76e-05 |
|
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350712 [Multi-domain] Cd Length: 203 Bit Score: 45.77 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1359 APTGSGKTIVAEIAIFRALNQNPKckvvyiaPLKALV----KERIADWEQRFQR--SSLGLKVVELTGDVTPDIQAIRES 1432
Cdd:cd17954 44 AETGSGKTAAFALPILQALLENPQ-------RFFALVlaptRELAQQISEQFEAlgSSIGLKSAVLVGGMDMMAQAIALA 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1433 Q---LIVTTPEK-WDGISRswqTREY-VQHVSLIVIDEI-HLLGEDRGPVIEVIV-----SRTNFISSHT 1491
Cdd:cd17954 117 KkphVIVATPGRlVDHLEN---TKGFsLKSLKFLVMDEAdRLLNMDFEPEIDKILkviprERTTYLFSAT 183
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
485-819 |
8.87e-05 |
|
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: 47.38 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 485 KELNRIQSVVFPVAYHSNEN----MLVCAPTGAGKTNVAMLSIVHtircHLEQGVINRdefkIVYIAPMKALAAEMVDnf 560
Cdd:COG1203 126 TPINPLQNEALELALEAAEEepglFILTAPTGGGKTEAALLFALR----LAAKHGGRR----IIYALPFTSIINQTYD-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 561 skRLKSLQ-IAVRELTGDIQLTKAEMA-----------------ATQILVTTPekwD-----VVTRKGSGDVALISLVE- 616
Cdd:COG1203 196 --RLRDLFgEDVLLHHSLADLDLLEEEeeyesearwlkllkelwDAPVVVTTI---DqlfesLFSNRKGQERRLHNLANs 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 617 LLIIDEVHLLhgergPVveALVARTLRLVESSQSM-IRIVGLSATLPNYIDVAHFLRVN-----PMKGLFYFDSRFRpvp 690
Cdd:COG1203 271 VIILDEVQAY-----PP--YMLALLLRLLEWLKNLgGSVILMTATLPPLLREELLEAYElipdePEELPEYFRAFVR--- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 691 ldtnfvgiKSVKQLQQIADMDQcCYQKCVEMVQEGHQIMVFVharnATVRTAnviRELAQqnntsalflpkdsaahglat 770
Cdd:COG1203 341 --------KRVELKEGPLSDEE-LAELILEALHKGKSVLVIV----NTVKDA---QELYE-------------------- 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 24647182 771 rsiqrsrnkQLVELFSCGLAMH-HAGMLRADRQMVEKY----FVEGHISVLVCT 819
Cdd:COG1203 385 ---------ALKEKLPDEEVYLlHSRFCPADRSEIEKEikerLERGKPCILVST 429
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
789-865 |
1.00e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 44.64 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 789 LAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIrgtdIYDAKHgsfvdLGILDVLQIFGRAGR 865
Cdd:cd18811 64 VGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMV----IEDAER-----FGLSQLHQLRGRVGR 131
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
506-666 |
1.40e-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: 46.68 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 506 LVCAPTGAGKTNVAMLSIVHTIRchleqgviNRDEFKIVYIAPMKALAAEMVDNFSKRLKS---------------LQIA 570
Cdd:TIGR01587 3 VIEAPTGYGKTEAALLWALHSIK--------SQKADRVIIALPTRATINAMYRRAKELFGSelvglhhsssfsrikEMGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 571 VRELTGDIQL---TKAEMAATQILVTTPEKWdVVTRKGSGDVALISLVEL----LIIDEVHLLHGE-RGPVVEALvaRTL 642
Cdd:TIGR01587 75 SEEFEHLFPLyihSNDKLFLDPITVCTIDQV-LKSVFGEFGHYEFTLASIanslLIFDEVHFYDEYtLALILAVL--EVL 151
|
170 180
....*....|....*....|....
gi 24647182 643 RLVESSqsmirIVGLSATLPNYID 666
Cdd:TIGR01587 152 KDNDVP-----ILLMSATLPKFLK 170
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
490-626 |
2.53e-04 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 44.50 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 490 IQSVVFPVAYhSNENMLVCAPTGAGKTNVAMLSIVHTIrCHLEQGVINRDEFKIVYIAPMKalaaEMVDNFSKRLKSLQI 569
Cdd:cd17961 20 IQSKAIPLAL-EGKDILARARTGSGKTAAYALPIIQKI-LKAKAESGEEQGTRALILVPTR----ELAQQVSKVLEQLTA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24647182 570 AVRELTGDIQLTKAEMAATQ---------ILVTTPEKwdVVTRKGSGDVALISLVELLIIDEVHLL 626
Cdd:cd17961 94 YCRKDVRVVNLSASSSDSVQrallaekpdIVVSTPAR--LLSHLESGSLLLLSTLKYLVIDEADLV 157
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
1334-1485 |
3.47e-04 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 43.97 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1334 FTHFNPIQTQIFHCLYhTDNNVLLGAPTGSGKTIVAEIAIFRALNQNPKCK-----VVYIAP-----------LKALVKe 1397
Cdd:cd00268 10 FEKPTPIQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKgrgpqALVLAPtrelamqiaevARKLGK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1398 riadweqrfqrsSLGLKVVELTG--DVTPDIQAIRE-SQLIVTTPEK-WDGISRswqTREYVQHVSLIVIDEI-HLLGED 1472
Cdd:cd00268 88 ------------GTGLKVAAIYGgaPIKKQIEALKKgPDIVVGTPGRlLDLIER---GKLDLSNVKYLVLDEAdRMLDMG 152
|
170
....*....|...
gi 24647182 1473 RGPVIEVIVSRTN 1485
Cdd:cd00268 153 FEEDVEKILSALP 165
|
|
| Helicase_PWI |
pfam18149 |
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 ... |
247-284 |
3.56e-04 |
|
N-terminal helicase PWI domain; This domain is found in spliceosomal RNA helicase Brr2. Brr2 is required for the assembly of a catalytically active spliceosome on a messenger RNA precursor. The domain is found in the N-terminal region and is non-canonically PWI-like. The PWI-like domain is thought to be involved in protein-protein interactions.
Pssm-ID: 436309 Cd Length: 111 Bit Score: 42.21 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....*....
gi 24647182 247 DILGSQRSSEV-LQNELMEILGFDYFELVEKLLMERDKI 284
Cdd:pfam18149 38 DILESAADDLReCENQLVELLDYDKFDLVKLLLKNRDKI 76
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
1354-1440 |
7.84e-04 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 42.89 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAeIAI----FRALNQNPKCKVVYIAPlKALVKERIAD-WEQRFQRSslGLKVVELTGDV---TPD 1425
Cdd:cd18073 19 NTIICAPTGCGKTFVS-LLIcehhLKKFPQGQKGKVVFFAT-KVPVYEQQKSvFSKYFERH--GYRVTGISGATaenVPV 94
|
90
....*....|....*
gi 24647182 1426 IQAIRESQLIVTTPE 1440
Cdd:cd18073 95 EQIIENNDIIILTPQ 109
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
1348-1469 |
8.45e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 42.55 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1348 LYHTDNNVLLGAPTGSGKTIVAeIAIFRAL--NQNPKCKVVYIAPLKALvkeriADWEQRFQRSSLGLKVVELTGDVTP- 1424
Cdd:cd17919 15 LYENGPGGILADEMGLGKTLQA-IAFLAYLlkEGKERGPVLVVCPLSVL-----ENWEREFEKWTPDLRVVVYHGSQREr 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24647182 1425 -DIQAIR---ESQLIVTTPEKWDGISRSWQtreyVQHVSLIVIDEIHLL 1469
Cdd:cd17919 89 aQIRAKEkldKFDVVLTTYETLRRDKASLR----KFRWDLVVVDEAHRL 133
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
1333-1439 |
9.91e-04 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 42.58 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1333 KFTHFNPIQTQIFHCLYHTdNNVLLGAPTGSGKTIVAEIAIFRAL---NQNPKCKVVYIAPLKALVKErIADWEQRFQRS 1409
Cdd:cd17957 9 GYREPTPIQMQAIPILLHG-RDLLACAPTGSGKTLAFLIPILQKLgkpRKKKGLRALILAPTRELASQ-IYRELLKLSKG 86
|
90 100 110
....*....|....*....|....*....|....
gi 24647182 1410 SlGLKVVELTGDVTP----DIQAIRESQLIVTTP 1439
Cdd:cd17957 87 T-GLRIVLLSKSLEAkakdGPKSITKYDILVSTP 119
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
506-624 |
1.61e-03 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350749 [Multi-domain] Cd Length: 193 Bit Score: 41.79 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 506 LVCAPTGAGKTNVAMLSIVHTIRCHleqgvinrdeFKIVYIAPMKALAAEMVDNFSKRLKSLQIAVRELTGDIqlTKAEm 585
Cdd:cd17991 40 LICGDVGFGKTEVAMRAAFKAVLSG----------KQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRFT--TAAE- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 24647182 586 aATQILVTTPE-KWDVV--TRK-GSGDVALISLvELLIIDEVH 624
Cdd:cd17991 107 -QREILEGLKEgKVDIVigTHRlLSKDVEFKNL-GLLIIDEEQ 147
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
478-661 |
4.20e-03 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 41.08 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 478 RLAFANCKELNRIQSVVFPVAYHSNE--------NMLVCAPTGAGKTNVAMLSIVHTIRchleQGVINRdeFKIVYIAPM 549
Cdd:cd17956 4 NLQNNGITSAFPVQAAVIPWLLPSSKstppyrpgDLCVSAPTGSGKTLAYVLPIVQALS----KRVVPR--LRALIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 550 KALAAEMVDNFSKRLKSLQIAVRELTGDIQLTKAEMA-----------ATQILVTTPEKW-DVVTRKGSgdvalISL--V 615
Cdd:cd17956 78 KELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLllvdtsgrylsRVDILVATPGRLvDHLNSTPG-----FTLkhL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647182 616 ELLIIDE-------------VHLLH--GERGPVVEALVARTLRLVESSQSMIRIVgLSATL 661
Cdd:cd17956 153 RFLVIDEadrllnqsfqdwlETVMKalGRPTAPDLGSFGDANLLERSVRPLQKLL-FSATL 212
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
479-622 |
4.59e-03 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 41.07 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 479 LAFANCKELNRIQSVVFPVAYHSNENMLVCAPTGAGKTNVAMLSIVHTIRCHLEQGVINRdEFKIVY---IAPMKALAAE 555
Cdd:cd17946 5 LADLGFSEPTPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGG-KQKPLRaliLTPTRELAVQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647182 556 MVDNFSKRLKSLQIAVRELTGDIQLTKAEMAATQ---ILVTTPEK-WDVVTRKGSGdVALISLVELLIIDE 622
Cdd:cd17946 84 VKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKrpeIVVATPGRlWELIQEGNEH-LANLKSLRFLVLDE 153
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
789-865 |
4.71e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.94 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647182 789 LAMHHAGMLRADRQMVEKYFVEGHISVLVCTATLAWGVNLPAHAVIIrgtdIYDAKHgsfvdLGILDVLQIFGRAGR 865
Cdd:cd18792 63 VALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMI----IEDADR-----FGLSQLHQLRGRVGR 130
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1627-1703 |
5.73e-03 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 41.62 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1627 IGLHHAGLQEQDRKCVEELFLNRKIQILVATATLAWGVNLP-AHLVVikgteyfdgkvkkYVDMP--ITDVLQMMGRAGR 1703
Cdd:PRK11057 263 AAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPnVRFVV-------------HFDIPrnIESYYQETGRAGR 329
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
1323-1483 |
6.55e-03 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 40.26 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1323 LKNVVYESLY--KFTHFNPIQTQIFHCLYHTDNNVLLGAPTGSGKTIVAEI-AIFRALN-----QNPKCKVVYIAPLKAL 1394
Cdd:cd17964 1 LDPSLLKALTrmGFETMTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLpAIQSLLNtkpagRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1395 VKErIADWEQRFQRSSLGLKVVELTGDvTPDIQAIRE-----SQLIVTTPEKWDGISRSWQTREYVQHVSLIVIDEI-HL 1468
Cdd:cd17964 81 ALQ-IAAEAKKLLQGLRKLRVQSAVGG-TSRRAELNRlrrgrPDILVATPGRLIDHLENPGVAKAFTDLDYLVLDEAdRL 158
|
170
....*....|....*..
gi 24647182 1469 LgeDRG--PVIEVIVSR 1483
Cdd:cd17964 159 L--DMGfrPDLEQILRH 173
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
1354-1470 |
6.55e-03 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 39.71 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNqNPKcKVVYIAPLKALVKERiadwEQRFQRSSLGLKVVELTGDVTPDIQAirESQ 1433
Cdd:cd17918 38 DRLLSGDVGSGKTLVALGAALLAYK-NGK-QVAILVPTEILAHQH----YEEARKFLPFINVELVTGGTKAQILS--GIS 109
|
90 100 110
....*....|....*....|....*....|....*..
gi 24647182 1434 LIVttpekwdGISRSWQTREYVQHVSLIVIDEIHLLG 1470
Cdd:cd17918 110 LLV-------GTHALLHLDVKFKNLDLVIVDEQHRFG 139
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
1354-1400 |
7.73e-03 |
|
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.
Pssm-ID: 350670 [Multi-domain] Cd Length: 81 Bit Score: 37.50 E-value: 7.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFrALNQNPKcKVVYIAPLKALVKERIA 1400
Cdd:cd17912 1 NILHLGPTGSGKTLVAIQKIA-SAMSSGK-SVLVVTPTKLLAHEILI 45
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
1354-1466 |
9.40e-03 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It belongs 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: 350683 [Multi-domain] Cd Length: 143 Bit Score: 38.82 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647182 1354 NVLLGAPTGSGKTIVAEIAIFRALNQNpkCKVVYIAPLKALVKEriadWEQRFQRSSLGLKVVELTGDvtpDIQAIRESQ 1433
Cdd:cd17925 18 DLLVWAVTGAGKTEMLFPAIAQALRQG--GRVAIASPRIDVCLE----LAPRLKAAFPGAAIVLLHGG---SEDQYQRSP 88
|
90 100 110
....*....|....*....|....*....|...
gi 24647182 1434 LIVTTpekwdgisrSWQTREYVQHVSLIVIDEI 1466
Cdd:cd17925 89 LVIAT---------THQLLRFYRAFDLLIIDEV 112
|
|
| |
