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Conserved domains on  [gi|222831595|ref|NP_060101|]
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probable ATP-dependent RNA helicase DDX60 isoform 1 [Homo sapiens]

Protein Classification

DEXHc_DDX60 and SF2_C_Ski2 domain-containing protein( domain architecture ID 13408691)

DEXHc_DDX60 and SF2_C_Ski2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
763-952 2.09e-120

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: 376.32  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  763 IPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNL-PSGEV 841
Cdd:cd18025     1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGVFTREYRHD-ALNCQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 920
Cdd:cd18025    81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 222831595  921 ISNPEHLTEWLQSVKWYWKQEDKIIENNTASK 952
Cdd:cd18025   161 IGNPQKFHEWLQSVQRARKAELKKIEHNHRDS 192
BRR2 super family cl34180
Replicative superfamily II helicase [Replication, recombination and repair];
768-1442 7.04e-38

Replicative superfamily II helicase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1204:

Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 150.82  E-value: 7.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKEsdDGVVVYVAPTKALVNQVAatvqNRFTKNLPSGEVLCGVF 846
Cdd:COG1204    27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKY----REFKRDFEELGIKVGVS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  847 TREYRHDAL---NCQVLITVPACFEILLLapHRQNWVKKIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---FLAL 917
Cdd:COG1204   101 TGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqIVAL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  918 SATISNPEHLTEWLqsvkwywkqEDKIIENntaskrhvgrqagfpkDYLQVKQSYKVrlvlygeryndlekhvcsIKHGD 997
Cdd:COG1204   178 SATIGNAEEIAEWL---------DAELVKS----------------DWRPVPLNEGV------------------LYDGV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  998 IHFDhfhpcaalttdhierygfppDLTLSPRESIQlydamfqiwkswpraqelcpenfihfnnKLVIKKMDarkyeeslk 1077
Cdd:COG1204   215 LRFD--------------------DGSRRSKDPTL----------------------------ALALDLLE--------- 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1078 aeltswiKNGNVeqarmvlqnlspeadlspenmitmfplLVeklrkmeklpalfflfklgavenaaesvstFLKKKQETK 1157
Cdd:COG1204   238 -------EGGQV---------------------------LV------------------------------FVSSRRDAE 253
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1158 RppkadkeahvMANKLRKVKKsiekqKIIDEKSQKKTRNVDQSLIHEAEHdnlvkcleknleipqdctyadqkavdTETl 1237
Cdd:COG1204   254 S----------LAKKLADELK-----RRLTPEEREELEELAEELLEVSEE--------------------------THT- 291
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1238 qkvfgrvkferkGEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFA----QNSVY 1313
Cdd:COG1204   292 ------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGMVP 359
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1314 LDALNYRQMSGRAGRRGQDLMGDVYFFDIPFPKIGKL----IKSNVPELRGHfpLSITLVLRLMLLASKGDDPEDAKAKV 1389
Cdd:COG1204   360 IPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALIASGFANSREEL 437
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 222831595 1390 LSVLKHSLLSFKQPrvMDMLKLYFLFSLQFLVKEGYLDQEGN---PMGFAGLVSHL 1442
Cdd:COG1204   438 LDFLENTFYAYQYD--KGDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRL 491
 
Name Accession Description Interval E-value
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
763-952 2.09e-120

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: 376.32  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  763 IPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNL-PSGEV 841
Cdd:cd18025     1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGVFTREYRHD-ALNCQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 920
Cdd:cd18025    81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 222831595  921 ISNPEHLTEWLQSVKWYWKQEDKIIENNTASK 952
Cdd:cd18025   161 IGNPQKFHEWLQSVQRARKAELKKIEHNHRDS 192
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
768-1442 7.04e-38

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 150.82  E-value: 7.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKEsdDGVVVYVAPTKALVNQVAatvqNRFTKNLPSGEVLCGVF 846
Cdd:COG1204    27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKY----REFKRDFEELGIKVGVS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  847 TREYRHDAL---NCQVLITVPACFEILLLapHRQNWVKKIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---FLAL 917
Cdd:COG1204   101 TGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqIVAL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  918 SATISNPEHLTEWLqsvkwywkqEDKIIENntaskrhvgrqagfpkDYLQVKQSYKVrlvlygeryndlekhvcsIKHGD 997
Cdd:COG1204   178 SATIGNAEEIAEWL---------DAELVKS----------------DWRPVPLNEGV------------------LYDGV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  998 IHFDhfhpcaalttdhierygfppDLTLSPRESIQlydamfqiwkswpraqelcpenfihfnnKLVIKKMDarkyeeslk 1077
Cdd:COG1204   215 LRFD--------------------DGSRRSKDPTL----------------------------ALALDLLE--------- 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1078 aeltswiKNGNVeqarmvlqnlspeadlspenmitmfplLVeklrkmeklpalfflfklgavenaaesvstFLKKKQETK 1157
Cdd:COG1204   238 -------EGGQV---------------------------LV------------------------------FVSSRRDAE 253
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1158 RppkadkeahvMANKLRKVKKsiekqKIIDEKSQKKTRNVDQSLIHEAEHdnlvkcleknleipqdctyadqkavdTETl 1237
Cdd:COG1204   254 S----------LAKKLADELK-----RRLTPEEREELEELAEELLEVSEE--------------------------THT- 291
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1238 qkvfgrvkferkGEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFA----QNSVY 1313
Cdd:COG1204   292 ------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGMVP 359
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1314 LDALNYRQMSGRAGRRGQDLMGDVYFFDIPFPKIGKL----IKSNVPELRGHfpLSITLVLRLMLLASKGDDPEDAKAKV 1389
Cdd:COG1204   360 IPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALIASGFANSREEL 437
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 222831595 1390 LSVLKHSLLSFKQPrvMDMLKLYFLFSLQFLVKEGYLDQEGN---PMGFAGLVSHL 1442
Cdd:COG1204   438 LDFLENTFYAYQYD--KGDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRL 491
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
1246-1340 1.69e-37

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: 138.45  E-value: 1.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1246 FERKGEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQNSVY-------LDALN 1318
Cdd:cd18795    51 SSRKECEKTAKDLAGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLE 130
                          90       100
                  ....*....|....*....|..
gi 222831595 1319 YRQMSGRAGRRGQDLMGDVYFF 1340
Cdd:cd18795   131 YLQMIGRAGRPGFDTRGEAIIM 152
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
768-922 1.52e-23

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: 98.85  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595   768 QRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGV-VVYVAPTKALVNQVAATVQNRFTKNLPSGEVLCGVF 846
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595   847 TREYRHDAL-NCQVLITVPacfEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 922
Cdd:pfam00270   84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
DEXDc smart00487
DEAD-like helicases superfamily;
762-931 6.54e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.78  E-value: 6.54e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595    762 FIPDTWQRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGE 840
Cdd:smart00487    7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595    841 VLCGVFTREYRHDAL---NCQVLITVPACFEILLLapHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFL 915
Cdd:smart00487   87 GLYGGDSKREQLRKLesgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknVQLL 164
                           170
                    ....*....|....*.
gi 222831595    916 ALSATISNPEHLTEWL 931
Cdd:smart00487  165 LLSATPPEEIENLLEL 180
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
768-926 5.51e-15

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: 80.65  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYAsyYC---MEKVLKESdDGVVVYVAPTKALVN-QVAATvqNRFTKNLPSGeVLC 843
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDP-GATALYLYPTKALARdQLRRL--RELAEALGLG-VRV 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  844 GVFT----REYRHDAL-NCQVLITVPacfEIL---LLaPHRQNWV---KKIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 911
Cdd:COG1205   135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
                         170       180
                  ....*....|....*....|....*..
gi 222831595  912 ----CP-------FLALSATISNP-EH 926
Cdd:COG1205   207 lrriCRhygsdpqFILASATIGNPaEH 233
PRK01172 PRK01172
ATP-dependent DNA helicase;
1251-1456 7.01e-15

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 80.31  E-value: 7.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1251 EELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQ-------NSVYLDALNYRQMS 1323
Cdd:PRK01172  278 DSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDitrygngGIRYLSNMEIKQMI 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1324 GRAGRRGQDLMGDVYFF---------------DIPFPKIGKLIKSNVPELRghfplsiTLVLRLMLLASKgddPEDakak 1388
Cdd:PRK01172  358 GRAGRPGYDQYGIGYIYaaspasydaakkylsGEPEPVISYMGSQRKVRFN-------TLAAISMGLASS---MED---- 423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1389 vLSVLKHSLLSFKQPRVmDMLKLYFLFSLQFLVKEGYLDQEG--NPMGFAGLVSHLHYHEPSNLVFVSFL 1456
Cdd:PRK01172  424 -LILFYNETLMAIQNGV-DEIDYYIESSLKFLKENGFIKGDVtlRATRLGKLTSDLYIDPESALILKSAF 491
HELICc smart00490
helicase superfamily c-terminal domain;
1254-1330 2.68e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 63.77  E-value: 2.68e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595   1254 KALAERGIGY--HHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1330
Cdd:smart00490    5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
PRK00254 PRK00254
ski2-like helicase; Provisional
777-933 8.91e-12

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 70.23  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  777 KNESAVIVAPTSSGKTYASYYCM-EKVLKESddGVVVYVAPTKALVNQ--------------VAATvqnrfTKNLPSGEV 841
Cdd:PRK00254   38 EGKNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKALAEEkyrefkdweklglrVAMT-----TGDYDSTDE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGvftreyRHDalncqVLITVPACFEILLlaPHRQNWVKKIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLAL 917
Cdd:PRK00254  111 WLG------KYD-----IIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGL 175
                         170
                  ....*....|....*.
gi 222831595  918 SATISNPEHLTEWLQS 933
Cdd:PRK00254  176 SATVGNAEELAEWLNA 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1251-1330 1.33e-07

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: 51.44  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  1251 EELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1330
Cdd:pfam00271   31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPASYIQRIGRAGRAG 109
 
Name Accession Description Interval E-value
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
763-952 2.09e-120

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: 376.32  E-value: 2.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  763 IPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNL-PSGEV 841
Cdd:cd18025     1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVYVAPTKALVNQVVAEVYARFSKKYpPSGKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGVFTREYRHD-ALNCQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIRCPFLALSAT 920
Cdd:cd18025    81 LWGVFTRDYRHNnPMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIPCPFLALSAT 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 222831595  921 ISNPEHLTEWLQSVKWYWKQEDKIIENNTASK 952
Cdd:cd18025   161 IGNPQKFHEWLQSVQRARKAELKKIEHNHRDS 192
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
765-934 7.79e-49

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: 172.06  E-value: 7.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  765 DTWQRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDdGVVVYVAPTKALVNQVAATVQNRFTknlpSGEVLC 843
Cdd:cd17921     3 NPIQREALRaLYLSGDSVLVSAPTSSGKTLIAELAILRALATSG-GKAVYIAPTRALVNQKEADLRERFG----PLGKNV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  844 GVFTREYRHDAL---NCQVLITVPACFEILLLAPHrQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFL 915
Cdd:cd17921    78 GLLTGDPSVNKLllaEADILVATPEKLDLLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinknARFV 156
                         170
                  ....*....|....*....
gi 222831595  916 ALSATISNPEHLTEWLQSV 934
Cdd:cd17921   157 GLSATLPNAEDLAEWLGVE 175
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
768-1442 7.04e-38

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 150.82  E-value: 7.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKEsdDGVVVYVAPTKALVNQVAatvqNRFTKNLPSGEVLCGVF 846
Cdd:COG1204    27 QAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKY----REFKRDFEELGIKVGVS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  847 TREYRHDAL---NCQVLITVPACFEILLLapHRQNWVKKIRYVIFDEVHCLG-GEIGAEIwEHLLVMIR--CP---FLAL 917
Cdd:COG1204   101 TGDYDSDDEwlgRYDILVATPEKLDSLLR--NGPSWLRDVDLVVVDEAHLIDdESRGPTL-EVLLARLRrlNPeaqIVAL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  918 SATISNPEHLTEWLqsvkwywkqEDKIIENntaskrhvgrqagfpkDYLQVKQSYKVrlvlygeryndlekhvcsIKHGD 997
Cdd:COG1204   178 SATIGNAEEIAEWL---------DAELVKS----------------DWRPVPLNEGV------------------LYDGV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  998 IHFDhfhpcaalttdhierygfppDLTLSPRESIQlydamfqiwkswpraqelcpenfihfnnKLVIKKMDarkyeeslk 1077
Cdd:COG1204   215 LRFD--------------------DGSRRSKDPTL----------------------------ALALDLLE--------- 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1078 aeltswiKNGNVeqarmvlqnlspeadlspenmitmfplLVeklrkmeklpalfflfklgavenaaesvstFLKKKQETK 1157
Cdd:COG1204   238 -------EGGQV---------------------------LV------------------------------FVSSRRDAE 253
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1158 RppkadkeahvMANKLRKVKKsiekqKIIDEKSQKKTRNVDQSLIHEAEHdnlvkcleknleipqdctyadqkavdTETl 1237
Cdd:COG1204   254 S----------LAKKLADELK-----RRLTPEEREELEELAEELLEVSEE--------------------------THT- 291
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1238 qkvfgrvkferkGEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFA----QNSVY 1313
Cdd:COG1204   292 ------------NEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRdtkrGGMVP 359
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1314 LDALNYRQMSGRAGRRGQDLMGDVYFFDIPFPKIGKL----IKSNVPELRGHfpLSITLVLRLMLLASKGDDPEDAKAKV 1389
Cdd:COG1204   360 IPVLEFKQMAGRAGRPGYDPYGEAILVAKSSDEADELferyILGEPEPIRSK--LANESALRTHLLALIASGFANSREEL 437
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 222831595 1390 LSVLKHSLLSFKQPrvMDMLKLYFLFSLQFLVKEGYLDQEGN---PMGFAGLVSHL 1442
Cdd:COG1204   438 LDFLENTFYAYQYD--KGDLEEVVDDALEFLLENGFIEEDGDrlrATKLGKLVSRL 491
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
1246-1340 1.69e-37

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: 138.45  E-value: 1.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1246 FERKGEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQNSVY-------LDALN 1318
Cdd:cd18795    51 SSRKECEKTAKDLAGIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYdgkgyreLSPLE 130
                          90       100
                  ....*....|....*....|..
gi 222831595 1319 YRQMSGRAGRRGQDLMGDVYFF 1340
Cdd:cd18795   131 YLQMIGRAGRPGFDTRGEAIIM 152
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
760-1404 7.63e-33

Superfamily II RNA helicase [Replication, recombination and repair];


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 138.15  E-value: 7.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  760 QDFIPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKEsdDGVVVYVAPTKALVNQVAATVQNRFtknlpsG 839
Cdd:COG4581    22 RGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALSNQKFFDLVERF------G 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  840 EVLCGVFT--REYRHDAlncQVLI-TVpacfEILL-LAPHRQNWVKKIRYVIFDEVHCLG-GEIGAeIWEhlLVMIRCP- 913
Cdd:COG4581    94 AENVGLLTgdASVNPDA---PIVVmTT----EILRnMLYREGADLEDVGVVVMDEFHYLAdPDRGW-VWE--EPIIHLPa 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  914 ---FLALSATISNPEHLTEWLQSVkwywkqedkiienntaskrhvgrqagfpkdylqvkqsykvrlvlygeryndlekhv 990
Cdd:COG4581   164 rvqLVLLSATVGNAEEFAEWLTRV-------------------------------------------------------- 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  991 csikHGdihfdhfhPCAALTTDHierygfppdltlspresiqlydamfqiwkswpRAQELcpenfihfnnklvikkmdar 1070
Cdd:COG4581   188 ----RG--------ETAVVVSEE--------------------------------RPVPL-------------------- 203
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1071 kyeeslkaeltswikngnvEQARMVLQNLSPEADLSPENMITM-FPLLVEKLRKMEKLPALFFLF-KLGAVENAAESVST 1148
Cdd:COG4581   204 -------------------EFHYLVTPRLFPLFRVNPELLRPPsRHEVIEELDRGGLLPAIVFIFsRRGCDEAAQQLLSA 264
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1149 FLkkkqetkrppkADKEahvmanklrkvkksiEKQKIIDEksqkktrnvdqslIHEAEHDnlvkcleknleipqdctyad 1228
Cdd:COG4581   265 RL-----------TTKE---------------ERAEIREA-------------IDEFAED-------------------- 285
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1229 qkavdtetLQKVFGRvkferkgeELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFA 1308
Cdd:COG4581   286 --------FSVLFGK--------TLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFT 349
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1309 QNS-------VYLDALNYRQMSGRAGRRGQDLMGDVYFFDIPFP---KIGKLIKSNVPELRGHFPLSITLVLRlmLLASK 1378
Cdd:COG4581   350 KLSkfdgerhRPLTAREFHQIAGRAGRRGIDTEGHVVVLAPEHDdpkKFARLASARPEPLRSSFRPSYNMVLN--LLARP 427
                         650       660
                  ....*....|....*....|....*.
gi 222831595 1379 GddPEDAKAkvlsVLKHSLLSFKQPR 1404
Cdd:COG4581   428 G--LERARE----LLEDSFAQFQADR 447
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
768-922 1.52e-23

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: 98.85  E-value: 1.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595   768 QRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGV-VVYVAPTKALVNQVAATVQNRFTKNLPSGEVLCGVF 846
Cdd:pfam00270    4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPqALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGD 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595   847 TREYRHDAL-NCQVLITVPacfEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFLALSATIS 922
Cdd:pfam00270   84 SRKEQLEKLkGPDILVGTP---GRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPkkRQILLLSATLP 159
DEXDc smart00487
DEAD-like helicases superfamily;
762-931 6.54e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 86.78  E-value: 6.54e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595    762 FIPDTWQRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGE 840
Cdd:smart00487    7 EPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVV 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595    841 VLCGVFTREYRHDAL---NCQVLITVPACFEILLLapHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR--CPFL 915
Cdd:smart00487   87 GLYGGDSKREQLRKLesgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPknVQLL 164
                           170
                    ....*....|....*.
gi 222831595    916 ALSATISNPEHLTEWL 931
Cdd:smart00487  165 LLSATPPEEIENLLEL 180
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
778-931 2.24e-18

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: 84.17  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  778 NESAVIVAPTSSGKTYASYYC-MEKVLKESDDGV-VVYVAPTKALVNQVAATVQ---NRFTKNLP----SGEVlcgvfTR 848
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPaLSSLADEPEKGVqVLYISPLKALINDQERRLEeplDEIDLEIPvavrHGDT-----SQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  849 EYRHDALNC--QVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCL-GGEIGAEI---WEHLLVMIRCPF--LALSAT 920
Cdd:cd17922    76 SEKAKQLKNppGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALlGSKRGVQLellLERLRKLTGRPLrrIGLSAT 155
                         170
                  ....*....|.
gi 222831595  921 ISNPEHLTEWL 931
Cdd:cd17922   156 LGNLEEAAAFL 166
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
768-931 2.04e-17

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: 81.61  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLD-VVDKNESAVIVAPTSSGKTYASYYCMEKVLkeSDDGVVVYVAPTKALVNQVaatvQNRFTKNLPSGeVLCGVF 846
Cdd:cd18028     6 QAEAVRaGLLKGENLLISIPTASGKTLIAEMAMVNTL--LEGGKALYLVPLRALASEK----YEEFKKLEEIG-LKVGIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  847 TREYRHDAL---NCQVLITVPACFEILLlaPHRQNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMIR-----CPFLALS 918
Cdd:cd18028    79 TGDYDEDDEwlgDYDIIVATYEKFDSLL--RHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARLRrlnpnTQIIGLS 156
                         170
                  ....*....|...
gi 222831595  919 ATISNPEHLTEWL 931
Cdd:cd18028   157 ATIGNPDELAEWL 169
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
768-932 1.71e-16

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: 80.09  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELL-DVVDKNESAVIVAPTSSGKTYASYYCMEKVLKES-----DDGVVVYVAPTKALVNQVAATVQNRFTknlPSGeV 841
Cdd:cd18023     6 QSEVFpDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnplpwGNRKVVYIAPIKALCSEKYDDWKEKFG---PLG-L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGVFTREYRHDAL----NCQVLITVPACFE-ILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAEIwE---------HLL 907
Cdd:cd18023    82 SCAELTGDTEMDDTfeiqDADIILTTPEKWDsMTRRWRDNGNLVQLVALVLIDEVHIIKENRGATL-EvvvsrmktlSSS 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 222831595  908 VMIRCP------FLALSATISNPEHLTEWLQ 932
Cdd:cd18023   161 SELRGStvrpmrFVAVSATIPNIEDLAEWLG 191
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
746-935 2.24e-16

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: 79.41  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  746 YLIRDERKDPDPRVQDFIPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDgvVVYVAPTKALVNQVA 825
Cdd:cd18024    15 PISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQR--VIYTSPIKALSNQKY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  826 ATVQNRFTK-NLPSGEVLCgvftreyrHDALNCQVLITvpacfEILLLAPHR-QNWVKKIRYVIFDEVHCLGGEIGAEIW 903
Cdd:cd18024    93 RELQEEFGDvGLMTGDVTI--------NPNASCLVMTT-----EILRSMLYRgSEIMREVAWVIFDEIHYMRDKERGVVW 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 222831595  904 EHLLV----MIRcpFLALSATISNPEHLTEWLQSVK 935
Cdd:cd18024   160 EETIIllpdKVR--YVFLSATIPNARQFAEWICKIH 193
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
778-936 6.00e-16

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: 77.80  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  778 NESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGEV-LCGVFTREYRhDALN 856
Cdd:cd18022    17 DNNVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKKRFEEKLGKKVVeLTGDVTPDMK-ALAD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  857 CQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGA----------EIWEHLLVMIRcpFLALSATISNPEH 926
Cdd:cd18022    96 ADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSDRGPvlevivsrmnYISSQTEKPVR--LVGLSTALANAGD 173
                         170
                  ....*....|
gi 222831595  927 LTEWLQSVKW 936
Cdd:cd18022   174 LANWLGIKKM 183
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
768-926 5.51e-15

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: 80.65  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYAsyYC---MEKVLKESdDGVVVYVAPTKALVN-QVAATvqNRFTKNLPSGeVLC 843
Cdd:COG1205    61 QAEAIEAARAGKNVVIATPTASGKSLA--YLlpvLEALLEDP-GATALYLYPTKALARdQLRRL--RELAEALGLG-VRV 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  844 GVFT----REYRHDAL-NCQVLITVPacfEIL---LLaPHRQNWV---KKIRYVIFDEVHCLGGEIGAeiweHLLVMIR- 911
Cdd:COG1205   135 ATYDgdtpPEERRWIReHPDIVLTNP---DMLhygLL-PHHTRWArffRNLRYVVIDEAHTYRGVFGS----HVANVLRr 206
                         170       180
                  ....*....|....*....|....*..
gi 222831595  912 ----CP-------FLALSATISNP-EH 926
Cdd:COG1205   207 lrriCRhygsdpqFILASATIGNPaEH 233
PRK01172 PRK01172
ATP-dependent DNA helicase;
1251-1456 7.01e-15

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 80.31  E-value: 7.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1251 EELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQ-------NSVYLDALNYRQMS 1323
Cdd:PRK01172  278 DSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDitrygngGIRYLSNMEIKQMI 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1324 GRAGRRGQDLMGDVYFF---------------DIPFPKIGKLIKSNVPELRghfplsiTLVLRLMLLASKgddPEDakak 1388
Cdd:PRK01172  358 GRAGRPGYDQYGIGYIYaaspasydaakkylsGEPEPVISYMGSQRKVRFN-------TLAAISMGLASS---MED---- 423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1389 vLSVLKHSLLSFKQPRVmDMLKLYFLFSLQFLVKEGYLDQEG--NPMGFAGLVSHLHYHEPSNLVFVSFL 1456
Cdd:PRK01172  424 -LILFYNETLMAIQNGV-DEIDYYIESSLKFLKENGFIKGDVtlRATRLGKLTSDLYIDPESALILKSAF 491
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
767-920 1.02e-14

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: 73.11  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  767 WQRELLDVVDKNES---AVIVAPTSSGKTYASYYCMEKVLKESddgvVVYVAPTKALVNQVAAtvqnRFTKNLPSGEVlc 843
Cdd:cd17926     4 YQEEALEAWLAHKNnrrGILVLPTGSGKTLTALALIAYLKELR----TLIVVPTDALLDQWKE----RFEDFLGDSSI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  844 GVFTREYRHDALNCQVLITVP----ACFEILLLAPHRQNwvkkirYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALS 918
Cdd:cd17926    74 GLIGGGKKKDFDDANVVVATYqslsNLAEEEKDLFDQFG------LLIVDEAH----HLPAKTFSEILKELNAKYrLGLT 143

                  ..
gi 222831595  919 AT 920
Cdd:cd17926   144 AT 145
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
762-935 1.34e-14

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: 73.84  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  762 FIPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDgvVVYVAPTKALVNQVAATVQNRFtknlpsGEV 841
Cdd:cd18027     7 FELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTR--TIYTSPIKALSNQKFRDFKNTF------GDV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 lcGVFTREYR-HDALNCQVLITvpacfEILLLAPHR-QNWVKKIRYVIFDEVHCLGGEIGAEIWEHLLVMI--RCPFLAL 917
Cdd:cd18027    79 --GLITGDVQlNPEASCLIMTT-----EILRSMLYNgSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLpdHVSIILL 151
                         170
                  ....*....|....*...
gi 222831595  918 SATISNPEHLTEWLQSVK 935
Cdd:cd18027   152 SATVPNTVEFADWIGRIK 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
767-920 1.85e-14

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.53  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  767 WQRELLD-----VVDKNESAVIVAPTSSGKTYASYYCMEKVLKesdDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGev 841
Cdd:COG1061    84 YQQEALEallaaLERGGGRGLVVAPTGTGKTVLALALAAELLR---GKRVLVLVPRRELLEQWAEELRRFLGDPLAGG-- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 lcgvftreyRHDALNCQVLITVPAcfeILLLAPHRQNWVKKIRYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALSAT 920
Cdd:COG1061   159 ---------GKKDSDAPITVATYQ---SLARRAHLDELGDRFGLVIIDEAH----HAGAPSYRRILEAFPAAYrLGLTAT 222
PRK02362 PRK02362
ATP-dependent DNA helicase;
1250-1447 1.86e-14

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 78.85  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1250 GEELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVV------FAQNS--VYLDALNYRQ 1321
Cdd:PRK02362  295 SKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIirdyrrYDGGAgmQPIPVLEYHQ 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1322 MSGRAGRRGQDLMG----------------DVYFFDIPFPKIGKLIKSnvPELRGHfplsitlvlrlmLLASKGDDPEDA 1385
Cdd:PRK02362  375 MAGRAGRPGLDPYGeavllaksydeldelfERYIWADPEDVRSKLATE--PALRTH------------VLSTIASGFART 440
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222831595 1386 KAKVLSVLKHSLLSFKQP------RVMDMlklyflfSLQFLVKEGYLDQEGN---PMGFAGLVSHLhYHEP 1447
Cdd:PRK02362  441 RDGLLEFLEATFYATQTDdtgrleRVVDD-------VLDFLERNGMIEEDGEtleATELGHLVSRL-YIDP 503
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
778-920 2.36e-14

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: 72.05  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  778 NESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVvYVAPTKALVNQVAATVQNRFTKNLPsgevlCGVFTRE------YR 851
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLKKGKKVL-VLVPTKALALQTAERLRELFGPGIR-----VAVLVGGssaeerEK 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222831595  852 HDALNCQVLITVPACFEILLLAPHRQnWVKKIRYVIFDEVHCLGGeIGAEIWEHLLVMIR-----CPFLALSAT 920
Cdd:cd00046    75 NKLGDADIIIATPDMLLNLLLREDRL-FLKDLKLIIVDEAHALLI-DSRGALILDLAVRKaglknAQVILLSAT 146
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
774-931 1.13e-13

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: 71.14  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  774 VVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNLP-SGEVLCGVFTREYRH 852
Cdd:cd18021    15 LYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRAKFGPLLGkKVVKLTGETSTDLKL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  853 DALNcQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGAeIWEHLLVMIR---------CPFLALSATISN 923
Cdd:cd18021    95 LAKS-DVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGENGP-VYEVVVSRMRyissqlekpIRIVGLSSSLAN 172

                  ....*...
gi 222831595  924 PEHLTEWL 931
Cdd:cd18021   173 ARDVGEWL 180
ResIII pfam04851
Type III restriction enzyme, res subunit;
767-920 4.11e-13

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 68.85  E-value: 4.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595   767 WQRELLD-----VVDKNESAVIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQvaatVQNRFTKNLPSGEV 841
Cdd:pfam04851    7 YQIEAIEnllesIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQ----ALEEFKKFLPNYVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595   842 LCGVFT-REYRHDALNCQVLI-TVPACFEILLLAPHrQNWVKKIRYVIFDEVHclggEIGAEIWEHLLVMIRCPF-LALS 918
Cdd:pfam04851   83 IGEIISgDKKDESVDDNKIVVtTIQSLYKALELASL-ELLPDFFDVIIIDEAH----RSGASSYRNILEYFKPAFlLGLT 157

                   ..
gi 222831595   919 AT 920
Cdd:pfam04851  158 AT 159
HELICc smart00490
helicase superfamily c-terminal domain;
1254-1330 2.68e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 63.77  E-value: 2.68e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595   1254 KALAERGIGY--HHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1330
Cdd:smart00490    5 ELLKELGIKVarLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAGRAG 82
PRK00254 PRK00254
ski2-like helicase; Provisional
777-933 8.91e-12

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 70.23  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  777 KNESAVIVAPTSSGKTYASYYCM-EKVLKESddGVVVYVAPTKALVNQ--------------VAATvqnrfTKNLPSGEV 841
Cdd:PRK00254   38 EGKNLVLAIPTASGKTLVAEIVMvNKLLREG--GKAVYLVPLKALAEEkyrefkdweklglrVAMT-----TGDYDSTDE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  842 LCGvftreyRHDalncqVLITVPACFEILLlaPHRQNWVKKIRYVIFDEVHCLGG-EIGAE---IWEHLLVmiRCPFLAL 917
Cdd:PRK00254  111 WLG------KYD-----IIIATAEKFDSLL--RHGSSWIKDVKLVVADEIHLIGSyDRGATlemILTHMLG--RAQILGL 175
                         170
                  ....*....|....*.
gi 222831595  918 SATISNPEHLTEWLQS 933
Cdd:PRK00254  176 SATVGNAEELAEWLNA 191
PRK00254 PRK00254
ski2-like helicase; Provisional
1251-1336 4.28e-11

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 67.92  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1251 EELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQNSVYLD-------ALNYRQMS 1323
Cdd:PRK00254  288 EKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNfgwedipVLEIQQMM 367
                          90
                  ....*....|...
gi 222831595 1324 GRAGRRGQDLMGD 1336
Cdd:PRK00254  368 GRAGRPKYDEVGE 380
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
768-926 6.57e-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: 62.99  E-value: 6.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYAsyY---CMEKVLKESdDGVVVYVAPTKALVN-QVAATvqNRFTKNLpSGEVLC 843
Cdd:cd17923     5 QAEAIEAARAGRSVVVTTGTASGKSLC--YqlpILEALLRDP-GSRALYLYPTKALAQdQLRSL--RELLEQL-GLGIRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  844 GVFT----REYRHDAL--NCQVLITVPACFEILLLAPHRQ--NWVKKIRYVIFDEVHCLGGEIGAeiweHLLVMIR---- 911
Cdd:cd17923    79 ATYDgdtpREERRAIIrnPPRILLTNPDMLHYALLPHHDRwaRFLRNLRYVVLDEAHTYRGVFGS----HVALLLRrlrr 154
                         170       180
                  ....*....|....*....|....
gi 222831595  912 -CP-------FLALSATISNP-EH 926
Cdd:cd17923   155 lCRrygadpqFILTSATIGNPaEH 178
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
756-931 3.87e-09

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 61.66  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  756 DPRVQDFIPDTW------QRELLDVVDKNESAVIVAPTSSGKTYASY------YCMEKVLKESDDGV-VVYVAPTKALVN 822
Cdd:COG1201    11 HPAVRAWFAARFgaptppQREAWPAIAAGESTLLIAPTGSGKTLAAFlpaldeLARRPRPGELPDGLrVLYISPLKALAN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  823 QVA-------------------------------ATVQNRFTKNLPsgevlcgvftreyrhdalncQVLITVPACFEILL 871
Cdd:COG1201    91 DIErnlrapleeigeaaglplpeirvgvrtgdtpASERQRQRRRPP--------------------HILITTPESLALLL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222831595  872 LAPHRQNWVKKIRYVIFDEVHCLGG-------EIGAEIWEHL----LVMIrcpflALSATISNPEHLTEWL 931
Cdd:COG1201   151 TSPDARELLRGVRTVIVDEIHALAGskrgvhlALSLERLRALaprpLQRI-----GLSATVGPLEEVARFL 216
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
778-923 2.85e-08

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: 55.90  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  778 NESAVIVAPTSSGKTYASYYCMEKVLKES---------DDGVVVYVAPTKALvnqvAATVQNRFTKNLPSgevlCGVFTR 848
Cdd:cd18020    17 NENMLICAPTGAGKTNIAMLTILHEIRQHvnqggvikkDDFKIVYIAPMKAL----AAEMVEKFSKRLAP----LGIKVK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  849 EYRHDA-------LNCQVLITVPACFEILLLAPHRQN-WVKKIRYVIFDEVHCLGGEIGAEIwEHLLV-----------M 909
Cdd:cd18020    89 ELTGDMqltkkeiAETQIIVTTPEKWDVVTRKSSGDVaLSQLVRLLIIDEVHLLHDDRGPVI-ESLVArtlrqvestqsM 167
                         170
                  ....*....|....
gi 222831595  910 IRcpFLALSATISN 923
Cdd:cd18020   168 IR--IVGLSATLPN 179
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1251-1330 1.33e-07

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: 51.44  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  1251 EELKALAERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFaQNSVYLDALNYRQMSGRAGRRG 1330
Cdd:pfam00271   31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI-NYDLPWNPASYIQRIGRAGRAG 109
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
776-925 3.98e-07

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: 52.76  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  776 DKNESAVIVAPTSSGKTYASYYCM----EKVLKES-----DDGVVVYVAPTKALVNQVAATVQNRFTK-NLPSGEvLCG- 844
Cdd:cd18019    31 ETDENLLLCAPTGAGKTNVALLTIlreiGKHRNPDgtinlDAFKIVYIAPMKALVQEMVGNFSKRLAPyGITVAE-LTGd 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  845 -VFTREYRHDAlncQVLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCLGGEIGA--------EIW--EHLLVMIRcp 913
Cdd:cd18019   110 qQLTKEQISET---QIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDDRGPvlesivarTIRqiEQTQEYVR-- 184
                         170
                  ....*....|..
gi 222831595  914 FLALSATISNPE 925
Cdd:cd18019   185 LVGLSATLPNYE 196
PRK13767 PRK13767
ATP-dependent helicase; Provisional
768-931 5.83e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.51  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYASY-------YCMEKVlKESDDGV-VVYVAPTKALVNQVaatvqnrfTKNL--P 837
Cdd:PRK13767   37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFlaiidelFRLGRE-GELEDKVyCLYVSPLRALNNDI--------HRNLeeP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  838 SGEV-----LCGVFTREYRH-----DALNCQ----------VLITVPACFEILLLAPHRQNWVKKIRYVIFDEVHCL-GG 896
Cdd:PRK13767  108 LTEIreiakERGEELPEIRVairtgDTSSYEkqkmlkkpphILITTPESLAILLNSPKFREKLRTVKWVIVDEIHSLaEN 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 222831595  897 EIGAeiweHLLV-------MIRCPF--LALSATISNPEHLTEWL 931
Cdd:PRK13767  188 KRGV----HLSLslerleeLAGGEFvrIGLSATIEPLEEVAKFL 227
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
1247-1331 1.25e-06

C-terminal helicase domain of LHR family helicases; 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. LHR family 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: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 49.96  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1247 ERKGEELKALAERG-----IGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNM-PCKSVVfaQNSVYLDALNYR 1320
Cdd:cd18796    52 ERLAQRLRELCPDRvppdfIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIgDVDLVI--QIGSPKSVARLL 129
                          90
                  ....*....|.
gi 222831595 1321 QMSGRAGRRGQ 1331
Cdd:cd18796   130 QRLGRSGHRPG 140
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
1263-1338 2.47e-06

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 52.59  E-value: 2.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595 1263 YHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQNSVYLDALN---YRQMSGRAGRRGQDLMGDVY 1338
Cdd:COG1202   453 PYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSvqeFHQMLGRAGRPDYHDRGKVY 531
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
768-892 2.62e-06

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: 49.44  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLkESDDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGEVLCGVFT 847
Cdd:cd18035     6 YQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRL-TKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKP 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 222831595  848 REYRHDALNCQVLITVPACFEILLLApHRQNwVKKIRYVIFDEVH 892
Cdd:cd18035    85 EERAERWDASKIIVATPQVIENDLLA-GRIT-LDDVSLLIFDEAH 127
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
762-923 3.87e-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: 49.57  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  762 FIPDTWQRELLDVVdKNESAVIVAPTSSGKTYASyyCM------EKVLKESDDG-VVVYVAPTKALVNQVAATVQNRFT- 833
Cdd:cd18034     1 FTPRSYQLELFEAA-LKRNTIVVLPTGSGKTLIA--VMlikemgELNRKEKNPKkRAVFLVPTVPLVAQQAEAIRSHTDl 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  834 KNLP-SGEVLCGVFTREYRHDAL-NCQVLITVPACFEILLlaphRQNWVK--KIRYVIFDEVH-CLGGEIGAEI---WEH 905
Cdd:cd18034    78 KVGEySGEMGVDKWTKERWKEELeKYDVLVMTAQILLDAL----RHGFLSlsDINLLIFDECHhATGDHPYARImkeFYH 153
                         170
                  ....*....|....*....
gi 222831595  906 LLVMIRCP-FLALSATISN 923
Cdd:cd18034   154 LEGRTSRPrILGLTASPVN 172
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
767-920 5.82e-06

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: 50.85  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  767 WQRELLDVVDKNESA-----VIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNL----- 836
Cdd:COG1203   131 LQNEALELALEAAEEepglfILTAPTGGGKTEAALLFALRLAAKHGGRRIIYALPFTSIINQTYDRLRDLFGEDVllhhs 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  837 ---PSGEVLCGVFTREYRHDALNCQVL---ITVpaC-----FEILLLAPHRQ-----NWVKKIryVIFDEVHClggeIGA 900
Cdd:COG1203   211 ladLDLLEEEEEYESEARWLKLLKELWdapVVV--TtidqlFESLFSNRKGQerrlhNLANSV--IILDEVQA----YPP 282
                         170       180
                  ....*....|....*....|....*.
gi 222831595  901 EIWEHLLVMIR------CPFLALSAT 920
Cdd:COG1203   283 YMLALLLRLLEwlknlgGSVILMTAT 308
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
762-892 1.03e-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: 48.24  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  762 FIPDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLKE----SDDGVVVYVAPTKALVNQVAATVQNRFTK--- 834
Cdd:cd18036     1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrsaGEKGRVVVLVNKVPLVEQQLEKFFKYFRKgyk 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222831595  835 -NLPSGEVLCGVFTREYrhdALNCQVLITVPACFEILLLAPhRQN---WVKKIRYVIFDEVH 892
Cdd:cd18036    81 vTGLSGDSSHKVSFGQI---VKASDVIICTPQILINNLLSG-REEervYLSDFSLLIFDECH 138
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
764-934 1.50e-05

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: 47.81  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  764 PDTWQRELLDVVDKNESAVIVAPTSSGKTYASYYCMEKVLK---ESDDGVVVYVAPTKALVNQVAATVQNRFtkNLP--- 837
Cdd:cd17927     3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKkfpAGRKGKVVFLANKVPLVEQQKEVFRKHF--ERPgyk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  838 ----SGEVLCGVFTREYrhdALNCQVLITVPACFEILLLA---PHRQNwvkkIRYVIFDEVHCLGGE-IGAEIWEHLL-- 907
Cdd:cd17927    81 vtglSGDTSENVSVEQI---VESSDVIIVTPQILVNDLKSgtiVSLSD----FSLLVFDECHNTTKNhPYNEIMFRYLdq 153
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 222831595  908 ---VMIRCP-FLALSATI-----SNPEHLTEWLQSV 934
Cdd:cd17927   154 klgSSGPLPqILGLTASPgvggaKNTEEALEHICKL 189
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
782-920 2.89e-05

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: 46.52  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  782 VIVAPTSSGKTYASYYCMEKVLKESDDGVVVYVAPTKALVNQVAATVQNRFTKNLPSGEVL------------------- 842
Cdd:cd17930     5 ILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKVLllhskaalellesdeepdd 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  843 ---CGVFTREYRHDALNCQVLI-TVPACFEILLLAPHRqnwVKKI-----RYVIFDEVHCLGGEIGAEIWEHLLVMIR-- 911
Cdd:cd17930    85 dpvEAVDWALLLKRSWLAPIVVtTIDQLLESLLKYKHF---ERRLhglanSVVVLDEVQAYDPEYMALLLKALLELLGel 161
                         170
                  ....*....|
gi 222831595  912 -CPFLALSAT 920
Cdd:cd17930   162 gGPVVLMTAT 171
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
777-892 6.98e-05

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 47.80  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  777 KNESAVIVAPTSSGKTYASYYCMEKVLKEsDDGVVVYVAPTKALVNQVAATvqnrFTKNLPSGEVLCGVFTREYRHD--- 853
Cdd:COG1111    16 LRKNTLVVLPTGLGKTAVALLVIAERLHK-KGGKVLFLAPTKPLVEQHAEF----FKEALNIPEDEIVVFTGEVSPEkrk 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 222831595  854 AL--NCQVLITVPACFEILLLAphrqNWV--KKIRYVIFDEVH 892
Cdd:COG1111    91 ELweKARIIVATPQVIENDLIA----GRIdlDDVSLLIFDEAH 129
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
1240-1332 4.47e-04

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: 45.21  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1240 VFGRvkfERKGEEL------KALAERGIGY----HHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCksvvfaq 1309
Cdd:COG1205   293 VFTR---SRRGAELlaryarRALREPDLADrvaaYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGG------- 362
                          90       100       110
                  ....*....|....*....|....*....|...
gi 222831595 1310 nsvyLDA----------LNYRQMSGRAGRRGQD 1332
Cdd:COG1205   363 ----LDAvvlagypgtrASFWQQAGRAGRRGQD 391
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
779-924 7.57e-04

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 42.63  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  779 ESAVIVAPTSSGKTyASYYCMEKVLKESDDGVVVYVAPTKALV-NQVAAtvqnrftknLP---SGEVLCGVFTREYRHDA 854
Cdd:cd18018    28 RSTLVVLPTGAGKS-LCYQLPALLLRRRGPGLTLVVSPLIALMkDQVDA---------LPraiKAAALNSSLTREERRRI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  855 LN------CQVLITVPacfEILLLAPHRQNW--VKKIRYVIFDEVHCLggeigAEiWEH--------LLVMIR-----CP 913
Cdd:cd18018    98 LEklrageVKILYVSP---ERLVNESFRELLrqTPPISLLVVDEAHCI-----SE-WSHnfrpdylrLCRVLRellgaPP 168
                         170
                  ....*....|.
gi 222831595  914 FLALSATISNP 924
Cdd:cd18018   169 VLALTATATKR 179
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
766-829 8.53e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 42.31  E-value: 8.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222831595  766 TWQRELLdvvdKNESAVIVAPTSSGKT-----YASYYcmekvlkESDDGVVVYVAPTKALVNQVAATVQ 829
Cdd:cd17924    24 TWAKRLL----RGKSFAIIAPTGVGKTtfglaTSLYL-------ASKGKRSYLIFPTKSLVKQAYERLS 81
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
1254-1331 3.23e-03

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 39.50  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1254 KALAERGI--GYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPckSVVF-AQNSVYLDALNYRQMSGRAGRRG 1330
Cdd:cd18794    48 ARLQSKGIsaAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKP--DVRFvIHYSLPKSMESYYQESGRAGRDG 125

                  .
gi 222831595 1331 Q 1331
Cdd:cd18794   126 L 126
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
1271-1340 4.75e-03

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 41.40  E-value: 4.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222831595 1271 KEKqlVEIlFRKGYLRVVTATGTLALGVNMPCKSV--VFAQNSVY-LDALnyRQMSGRAGRRGQDLMGDVYFF 1340
Cdd:COG4098   359 KEK--VQA-FRDGEIPILVTTTILERGVTFPNVDVavLGADHPVFtEAAL--VQIAGRVGRSADYPTGEVIFF 426
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
768-891 6.38e-03

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: 39.73  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  768 QRELLDVVDKNESAVIVAPTSSGKTYAsyYCM---EKVLKESDDG-----VVVyVAPTKALVNQVAATVQnRFTKNLP-- 837
Cdd:cd00268    17 QAQAIPLILSGRDVIGQAQTGSGKTLA--FLLpilEKLLPEPKKKgrgpqALV-LAPTRELAMQIAEVAR-KLGKGTGlk 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 222831595  838 SGEVLCGV-FTREYRHDALNCQVLITVPACFeILLLAPHRQNwVKKIRYVIFDEV 891
Cdd:cd00268    93 VAAIYGGApIKKQIEALKKGPDIVVGTPGRL-LDLIERGKLD-LSNVKYLVLDEA 145
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
1251-1328 6.48e-03

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: 39.25  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595 1251 EELKAL--AERGIGYHHSAMSFKEKQLVEILFRKGYLRVVTATGTLALGVNMPCKSVVFAQNSVYLDALNYRQMSGRAGR 1328
Cdd:cd18811    52 EYLKERfrPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGR 131
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
783-930 9.15e-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: 39.54  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  783 IVAPTSSGKTYAsyYCMEKVLKESDDGV----VVYVAPTKALVNQVAATVQnRFTKNLPSGEVLCG---VFTRE------ 849
Cdd:cd17956    41 VSAPTGSGKTLA--YVLPIVQALSKRVVprlrALIVVPTKELVQQVYKVFE-SLCKGTGLKVVSLSgqkSFKKEqklllv 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  850 YRHDALNC--QVLITVPAcfeilLLAPHRQNW----VKKIRYVIFDE----------------VHCLGGEI-----GAEI 902
Cdd:cd17956   118 DTSGRYLSrvDILVATPG-----RLVDHLNSTpgftLKHLRFLVIDEadrllnqsfqdwletvMKALGRPTapdlgSFGD 192
                         170       180       190
                  ....*....|....*....|....*....|
gi 222831595  903 WEHLLVM-IRCPFLALSATIS-NPEHLTEW 930
Cdd:cd17956   193 ANLLERSvRPLQKLLFSATLTrDPEKLSSL 222
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
1280-1332 9.19e-03

C-terminal helicase domain of HrQ family helicases; 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. HrQ family 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: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 38.39  E-value: 9.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222831595 1280 FRKGYLRVVTATGTLALGVNMPCksvvfaqnsvyLDAL----------NYRQMSGRAGRRGQD 1332
Cdd:cd18797    88 LFNGELLGVVATNALELGIDIGG-----------LDAVvlagypgslaSLWQQAGRAGRRGKD 139
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
777-890 9.75e-03

DEAD-box helicase domain of DEAD box protein 55; DDX55 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: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 39.10  E-value: 9.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222831595  777 KNESAVIVAPTSSGKTYAsyY---CMEKVLK----ESDDGVV-VYVAPTKALVNQVAATVQNRFTKNLP--SGEVLCG-- 844
Cdd:cd17960    26 SNKDVVVEAVTGSGKTLA--FlipVLEILLKrkanLKKGQVGaLIISPTRELATQIYEVLQSFLEHHLPklKCQLLIGgt 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 222831595  845 -VFTREYRHDALNCQVLITVPACFEILLLAPHRQNWVKKIRYVIFDE 890
Cdd:cd17960   104 nVEEDVKKFKRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDE 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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