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Conserved domains on  [gi|1469545504|gb|RGR13891|]
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helicase [Parabacteroides merdae]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1007248)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to Saccharomyces cerevisiae DNA polymerase alpha-associated DNA helicase A that acts as DNA polymerase alpha-associated DNA helicase which may be involved in DNA replication

EC:  3.6.4.12
Gene Ontology:  GO:0003678|GO:0003677|GO:0016887|GO:0005524
PubMed:  16935882|1552844

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 22-632 3.67e-117

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00376:

Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 363.37  E-value: 3.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504  22 EFEYEKEMYRQQIERTGIHRRIQQGLCWYPVvPGKSYYNSLNQLVVEIERLEDKETEhnFEYGRPVCFFttngSGNPEYL 101
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNL-QGKIRGGLLGFLLVRFGRRKAIATE--ISVGDIVLVS----RGNPLQS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 102 NFSTVISYVQDDRMVVVLPSPN---ALTDIQkageigIQLYFDETSYKTMFNALSTVIQaKGNRLAYlrdVLLG-KTPVG 177
Cdd:TIGR00376  75 DLTGVVTRVGKRFITVALEESVpqwSLKRVR------IDLYANDVTFKRMKEALRALTE-NHSRLLE---FLLGrEAPSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 178 RRTFFPMRF--PWLNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDR 255
Cdd:TIGR00376 145 ASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 256 GIHVLRIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREIQSNLRKKSHGEKETARNR----------------- 318
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEERNKKTKPSPQKRRGLsdikilrkalkkrearg 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 319 ----LSRLRFRATELEVKIDTELF----DEARVVACTLVGS-------ANRVLTNRNFTTLFIDEAAQALEAACWIAIGK 383
Cdd:TIGR00376 305 ieslKIASMAEWIETNKSIDRLLKllpeSEERIMNEILAESdatnsmaGSEILNGQYFDVAVIDEASQAMEPSCLIPLLK 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 384 ADRVILAGDHHQLPPTIKCIEAArgGLDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAPEVKHRGI 463
Cdd:TIGR00376 385 ARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILL 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 464 LEFDT--------------PVVWLDTADCHFEEDRLDDSMSRINRDEATLLVstlqKYIEKIGKERVLDESIdfGLISPY 529
Cdd:TIGR00376 463 RDLPKveateseddletgiPLLFIDTSGCELFELKEADSTSKYNPGEAELVS----EIIQALVKMGVPANDI--GVITPY 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 530 KSQVQYIRGLIKRDTFfkpfrrLITAHTVDGFQGQERDVIMISLVRANDKGRIGFLGDLRRMNVAITRARMKLMILGDAP 609
Cdd:TIGR00376 537 DAQVDLLRQLLEHRHI------DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSR 610

                         650       660
                  ....*....|....*....|...
gi 1469545504 610 TLTRHAFYKELYEYIWENGQVIT 632
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEVRE 633
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 22-632 3.67e-117

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 363.37  E-value: 3.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504  22 EFEYEKEMYRQQIERTGIHRRIQQGLCWYPVvPGKSYYNSLNQLVVEIERLEDKETEhnFEYGRPVCFFttngSGNPEYL 101
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNL-QGKIRGGLLGFLLVRFGRRKAIATE--ISVGDIVLVS----RGNPLQS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 102 NFSTVISYVQDDRMVVVLPSPN---ALTDIQkageigIQLYFDETSYKTMFNALSTVIQaKGNRLAYlrdVLLG-KTPVG 177
Cdd:TIGR00376  75 DLTGVVTRVGKRFITVALEESVpqwSLKRVR------IDLYANDVTFKRMKEALRALTE-NHSRLLE---FLLGrEAPSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 178 RRTFFPMRF--PWLNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDR 255
Cdd:TIGR00376 145 ASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 256 GIHVLRIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREIQSNLRKKSHGEKETARNR----------------- 318
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEERNKKTKPSPQKRRGLsdikilrkalkkrearg 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 319 ----LSRLRFRATELEVKIDTELF----DEARVVACTLVGS-------ANRVLTNRNFTTLFIDEAAQALEAACWIAIGK 383
Cdd:TIGR00376 305 ieslKIASMAEWIETNKSIDRLLKllpeSEERIMNEILAESdatnsmaGSEILNGQYFDVAVIDEASQAMEPSCLIPLLK 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 384 ADRVILAGDHHQLPPTIKCIEAArgGLDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAPEVKHRGI 463
Cdd:TIGR00376 385 ARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILL 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 464 LEFDT--------------PVVWLDTADCHFEEDRLDDSMSRINRDEATLLVstlqKYIEKIGKERVLDESIdfGLISPY 529
Cdd:TIGR00376 463 RDLPKveateseddletgiPLLFIDTSGCELFELKEADSTSKYNPGEAELVS----EIIQALVKMGVPANDI--GVITPY 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 530 KSQVQYIRGLIKRDTFfkpfrrLITAHTVDGFQGQERDVIMISLVRANDKGRIGFLGDLRRMNVAITRARMKLMILGDAP 609
Cdd:TIGR00376 537 DAQVDLLRQLLEHRHI------DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSR 610

                         650       660
                  ....*....|....*....|...
gi 1469545504 610 TLTRHAFYKELYEYIWENGQVIT 632
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEVRE 633
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 188-434 1.88e-84

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 262.93  E-value: 1.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 188 WLNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRGIHVLRIGNPTR 267
Cdd:cd18044     1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 268 INDKMLSFTYERRFeshpdyaelwgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidtelfdEARVVACT 347
Cdd:cd18044    81 LLESVLDHSLDALV----------------------------------------------------------AAQVVLAT 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 348 LVGSANRVL-TNRNFTTLFIDEAAQALEAACWIAIGKADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKITDRKPETV 426
Cdd:cd18044   103 NTGAGSRQLlPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGESV 182


                  ....*....
gi 1469545504 427 S-LLKTQYR 434
Cdd:cd18044   183 VrMLTVQYR 191
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
221-624 2.10e-83

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 279.32  E-value: 2.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 221 LVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRGIHVLRIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREI 300
Cdd:COG1112   415 LLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 301 QSNLRKKSHGEKETARNRLSRLRFRATELEVKIDTELFDEARVVACTLVGSANRV-LTNRNFTTLFIDEAAQALEAACWI 379
Cdd:COG1112   495 ELEKLIAELREAARLRRALRRELKKRRELRKLLWDALLELAPVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALG 574

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 380 AIGKADRVILAGDHHQLPPTIKCIEAAR---GGLDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAP 456
Cdd:COG1112   575 ALARAKRVVLVGDPKQLPPVVFGEEAEEvaeEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLP 654

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 457 EVKHRGILEFDTPVVWLDTADCHFEEDRlddsmSRINRDEATLLVSTLQKYIEKIGKERvldesiDFGLISPYKSQVQYI 536
Cdd:COG1112   655 SPKARRLADPDSPLVFIDVDGVYERRGG-----SRTNPEEAEAVVELVRELLEDGPDGE------SIGVITPYRAQVALI 723

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 537 RGLIKRDtfFKPFRRLITAHTVDGFQGQERDVIMISLVRANDK---GRIGFL-GDLRRMNVAITRARMKLMILGDAPTLT 612
Cdd:COG1112   724 RELLREA--LGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLD 801

                         410
                  ....*....|....*
gi 1469545504 613 RH---AFYKELYEYI 624
Cdd:COG1112   802 SDpstPALKRLLEYL 816
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 410-608 2.07e-71

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 228.97  E-value: 2.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 410 LDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAPEVKHR------GILEFDTPVVWLDTADCHFEED 483
Cdd:pfam13087   1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfHLPDPLGPLVFIDVDGSEEEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 484 rlDDSMSRINRDEATLLVSTLQKYIEKIGKERvldesIDFGLISPYKSQVQYIRGLIKRDTFFKPfrrLITAHTVDGFQG 563
Cdd:pfam13087  81 --DGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITPYRAQVRLIRKLLKRKLGGKL---EIEVNTVDGFQG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1469545504 564 QERDVIMISLVRANDKGRIGFLGDLRRMNVAITRARMKLMILGDA 608
Cdd:pfam13087 151 REKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXDc smart00487
DEAD-like helicases superfamily;
193-250 1.27e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 43.63  E-value: 1.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545504  193 QEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQ---VMVCAQSNTAVDWISE 250
Cdd:smart00487  13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGgrvLVLVPTRELAEQWAEE 73
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 22-632 3.67e-117

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 363.37  E-value: 3.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504  22 EFEYEKEMYRQQIERTGIHRRIQQGLCWYPVvPGKSYYNSLNQLVVEIERLEDKETEhnFEYGRPVCFFttngSGNPEYL 101
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNL-QGKIRGGLLGFLLVRFGRRKAIATE--ISVGDIVLVS----RGNPLQS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 102 NFSTVISYVQDDRMVVVLPSPN---ALTDIQkageigIQLYFDETSYKTMFNALSTVIQaKGNRLAYlrdVLLG-KTPVG 177
Cdd:TIGR00376  75 DLTGVVTRVGKRFITVALEESVpqwSLKRVR------IDLYANDVTFKRMKEALRALTE-NHSRLLE---FLLGrEAPSK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 178 RRTFFPMRF--PWLNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDR 255
Cdd:TIGR00376 145 ASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALC 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 256 GIHVLRIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREIQSNLRKKSHGEKETARNR----------------- 318
Cdd:TIGR00376 225 DQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVADIREKIDELIEERNKKTKPSPQKRRGLsdikilrkalkkrearg 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 319 ----LSRLRFRATELEVKIDTELF----DEARVVACTLVGS-------ANRVLTNRNFTTLFIDEAAQALEAACWIAIGK 383
Cdd:TIGR00376 305 ieslKIASMAEWIETNKSIDRLLKllpeSEERIMNEILAESdatnsmaGSEILNGQYFDVAVIDEASQAMEPSCLIPLLK 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 384 ADRVILAGDHHQLPPTIKCIEAArgGLDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAPEVKHRGI 463
Cdd:TIGR00376 385 ARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILL 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 464 LEFDT--------------PVVWLDTADCHFEEDRLDDSMSRINRDEATLLVstlqKYIEKIGKERVLDESIdfGLISPY 529
Cdd:TIGR00376 463 RDLPKveateseddletgiPLLFIDTSGCELFELKEADSTSKYNPGEAELVS----EIIQALVKMGVPANDI--GVITPY 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 530 KSQVQYIRGLIKRDTFfkpfrrLITAHTVDGFQGQERDVIMISLVRANDKGRIGFLGDLRRMNVAITRARMKLMILGDAP 609
Cdd:TIGR00376 537 DAQVDLLRQLLEHRHI------DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSR 610

                         650       660
                  ....*....|....*....|...
gi 1469545504 610 TLTRHAFYKELYEYIWENGQVIT 632
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEVRE 633
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 188-434 1.88e-84

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 262.93  E-value: 1.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 188 WLNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRGIHVLRIGNPTR 267
Cdd:cd18044     1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 268 INDKMLSFTYERRFeshpdyaelwgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidtelfdEARVVACT 347
Cdd:cd18044    81 LLESVLDHSLDALV----------------------------------------------------------AAQVVLAT 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 348 LVGSANRVL-TNRNFTTLFIDEAAQALEAACWIAIGKADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKITDRKPETV 426
Cdd:cd18044   103 NTGAGSRQLlPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGESV 182


                  ....*....
gi 1469545504 427 S-LLKTQYR 434
Cdd:cd18044   183 VrMLTVQYR 191
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
221-624 2.10e-83

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 279.32  E-value: 2.10e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 221 LVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRGIHVLRIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREI 300
Cdd:COG1112   415 LLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPE 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 301 QSNLRKKSHGEKETARNRLSRLRFRATELEVKIDTELFDEARVVACTLVGSANRV-LTNRNFTTLFIDEAAQALEAACWI 379
Cdd:COG1112   495 ELEKLIAELREAARLRRALRRELKKRRELRKLLWDALLELAPVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALG 574

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 380 AIGKADRVILAGDHHQLPPTIKCIEAAR---GGLDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAP 456
Cdd:COG1112   575 ALARAKRVVLVGDPKQLPPVVFGEEAEEvaeEGLDESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLP 654

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 457 EVKHRGILEFDTPVVWLDTADCHFEEDRlddsmSRINRDEATLLVSTLQKYIEKIGKERvldesiDFGLISPYKSQVQYI 536
Cdd:COG1112   655 SPKARRLADPDSPLVFIDVDGVYERRGG-----SRTNPEEAEAVVELVRELLEDGPDGE------SIGVITPYRAQVALI 723

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 537 RGLIKRDtfFKPFRRLITAHTVDGFQGQERDVIMISLVRANDK---GRIGFL-GDLRRMNVAITRARMKLMILGDAPTLT 612
Cdd:COG1112   724 RELLREA--LGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLD 801

                         410
                  ....*....|....*
gi 1469545504 613 RH---AFYKELYEYI 624
Cdd:COG1112   802 SDpstPALKRLLEYL 816
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 410-608 2.07e-71

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 228.97  E-value: 2.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 410 LDHTLMQKITDRKPETVSLLKTQYRMNEDIMRFPSRWFYHDELQSAPEVKHR------GILEFDTPVVWLDTADCHFEED 483
Cdd:pfam13087   1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfHLPDPLGPLVFIDVDGSEEEES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 484 rlDDSMSRINRDEATLLVSTLQKYIEKIGKERvldesIDFGLISPYKSQVQYIRGLIKRDTFFKPfrrLITAHTVDGFQG 563
Cdd:pfam13087  81 --DGGTSYSNEAEAELVVQLVEKLIKSGPEEP-----SDIGVITPYRAQVRLIRKLLKRKLGGKL---EIEVNTVDGFQG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1469545504 564 QERDVIMISLVRANDKGRIGFLGDLRRMNVAITRARMKLMILGDA 608
Cdd:pfam13087 151 REKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 192-401 3.04e-58

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 196.03  E-value: 3.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 192 SQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAI-------YETLHRENQVMVCAQSNTAVDWISEKLVDRGIH----VL 260
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIrqllsypATSAAAGPRILVCAPSNAAVDNILERLLRKGQKygpkIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 261 RIGNPTRINDKMLSFTYERRFESHPDYAELWGIRKAIREIQSNLRK-----------------------KSHGEKETARN 317
Cdd:pfam13086  81 RIGHPAAISEAVLPVSLDYLVESKLNNEEDAQIVKDISKELEKLAKalrafekeiivekllksrnkdksKLEQERRKLRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 318 RLSRLRFRATELEVKIDTELFDEARVVACTLVGSANRVLTNR-NFTTLFIDEAAQALEAACWIAI-GKADRVILAGDHHQ 395
Cdd:pfam13086 161 ERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLlRGPKKVVLVGDPKQ 240


                  ....*.
gi 1469545504 396 LPPTIK 401
Cdd:pfam13086 241 LPPTVI 246
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 435-624 2.08e-53

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 180.89  E-value: 2.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 435 MNEDIMRFPSRWFYHDELQSAPEVKHRG----ILEFDTPVVWLDTADChfeEDRLDDSMSRINRDEATLLVSTLQKYIek 510
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLnpppLPGPSKPLVFVDVSGG---EEREESGTSKSNEAEAELVVELVKYLL-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 511 igKERVLDESIdfGLISPYKSQVQYIRGLIKRDtffKPFRRLITAHTVDGFQGQERDVIMISLVRANDKGR-IGFLGDLR 589
Cdd:cd18808    76 --KSGVKPSSI--GVITPYRAQVALIRELLRKR---GGLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPR 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1469545504 590 RMNVAITRARMKLMILGDAPTLTRHAFYKELYEYI 624
Cdd:cd18808   149 RLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 189-434 1.26e-49

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 171.65  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRGIHVLRIGNPTRI 268
Cdd:cd18041     2 LNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 269 NDKMLSFTYERRFESHPDYAELwgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidTELFDEARVVACTL 348
Cdd:cd18041    82 HPDVQEFTLEAILKSCKSVEEL--------------------------------------------ESKYESVSVVATTC 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 349 VGSANRVLTNRNFTTLFIDEAAQALEAACWIAIGKADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKITDRKPETVSL 428
Cdd:cd18041   118 LGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQ 197


                  ....*.
gi 1469545504 429 LKTQYR 434
Cdd:cd18041   198 LTIQYR 203
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 189-434 2.55e-45

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 160.88  E-value: 2.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAaKDVSIVHGPPGTGKTTTLVEAIYEtLHREN--QVMVCAQSNTAVDWISEKLVDRGIHVLRIgnpt 266
Cdd:cd18039     2 LNHSQVDAVKTALQ-RPLSLIQGPPGTGKTVTSATIVYH-LVKQGngPVLVCAPSNVAVDQLTEKIHQTGLKVVRL---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 267 rindkmLSFTYERRFESHPDYAelwgIRKAIREIQSNLRKKSHGEKETARNRLSRL---RFRAteLEVKIDTELFDEARV 343
Cdd:cd18039    76 ------CAKSREAVESPVSFLA----LHNQVRNLDSAEKLELLKLLKLETGELSSAdekRYRK--LKRKAERELLRNADV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 344 VACTLVGSANRVLTNRNFTTLFIDEAAQALEAACWIAIGK-ADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKITD-- 420
Cdd:cd18039   144 ICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQlg 223

                         250
                  ....*....|....
gi 1469545504 421 RKPetvSLLKTQYR 434
Cdd:cd18039   224 IRP---IRLQVQYR 234
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 189-424 4.67e-40

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 146.23  E-value: 4.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAAKDVS---IVHGPPGTGKTTTLVEAIYE--TLHRENQVMVCAQSNTAVDWISEKLVDrgiHVLRIG 263
Cdd:cd18038     2 LNDEQKLAVRNIVTGTSRPppyIIFGPPGTGKTVTLVEAILQvlRQPPEARILVCAPSNSAADLLAERLLN---ALVTKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 264 NPTRINDkmlsftYERRFESHPdyaelwgirkaireiqSNLRKKSHGEKETarnrlsrlRFRATELEVkidtelFDEARV 343
Cdd:cd18038    79 EILRLNA------PSRDRASVP----------------PELLPYCNSKAEG--------TFRLPSLEE------LKKYRI 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 344 VACTLVgSANRV----LTNRNFTTLFIDEAAQALEAACWIAI----GKADRVILAGDHHQLPPTIKCIEAARGGLDHTLM 415
Cdd:cd18038   123 VVCTLM-TAGRLvqagVPNGHFTHIFIDEAGQATEPEALIPLselaSKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLL 201


                  ....*....
gi 1469545504 416 QKITDRKPE 424
Cdd:cd18038   202 ERLMERPLY 210
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 189-434 2.37e-35

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 132.72  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAA-KDVSIVHGPPGTGKTTTLVEAIYETLHRE-------------------------NQVMVCAQSN 242
Cdd:cd18042     1 LNESQLEAIASALQNsPGITLIQGPPGTGKTKTIVGILSVLLAGKyrkyyekvkkklrklqrnlnnkkkkNRILVCAPSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 243 TAVDWISEKLVDRGihvLRIGNPTRINDKMlsftyerrfeshpdyaelwgIRKAIREIQsnlrkkshgeketarnrlsrl 322
Cdd:cd18042    81 AAVDEIVLRLLSEG---FLDGDGRSYKPNV--------------------VRVGRQELR--------------------- 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 323 rfratelevkidTELFDEARVVACTLVGSANRVLTN--RNFTTLFIDEAAQALEAACWIAIGK-ADRVILAGDHHQLPPT 399
Cdd:cd18042   117 ------------ASILNEADIVCTTLSSSGSDLLESlpRGFDTVIIDEAAQAVELSTLIPLRLgCKRLILVGDPKQLPAT 184

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1469545504 400 IKCIEAARGGLDHTLMQKItDRKPETVSLLKTQYR 434
Cdd:cd18042   185 VFSKVAQKLGYDRSLFERL-QLAGYPVLMLTTQYR 218
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 189-448 5.45e-24

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 100.91  E-value: 5.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLA--AKDVS-IVHGPPGTGKTTTLVEAIYE--TLHRENQVMVCAQSNTAVDWISEKLVDRGihVLRIG 263
Cdd:cd18078     2 LNELQKEAVKRILGgeCRPLPyILFGPPGTGKTVTIIEAILQvvYNLPRSRILVCAPSNSAADLVTSRLHESK--VLKPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 264 NPTRINdkmlsfTYERRFESHPDyAELWGIRKAIReiqsnlrkkshgeKETArnrlsrLRFRATelevkidtelfdearV 343
Cdd:cd18078    80 DMVRLN------AVNRFESTVID-ARKLYCRLGED-------------LSKA------SRHRIV---------------I 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 344 VACTLVGSANRV-LTNRNFTTLFIDEAAQALEAACWIAIG----KADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKI 418
Cdd:cd18078   119 STCSTAGLLYQMgLPVGHFTHVFVDEAGQATEPESLIPLGlissRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERL 198

                         250       260       270
                  ....*....|....*....|....*....|
gi 1469545504 419 TDRKPetvsllktqYRMNEDimRFPSRWFY 448
Cdd:cd18078   199 MNRPL---------YLRDPN--RFGESGGY 217
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 206-434 1.07e-21

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 90.76  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 206 VSIVHGPPGTGKTTTLVEAIYETLHREN--QVMVCAQSNTAVDwiseklvdrgihvlrignptrindkmlsftyerrfes 283
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRgkRVLVTAQSNVAVD------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 284 hpdyaelwgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidtelfdearvvactlvgsanrvltnrNFTT 363
Cdd:cd17934    44 ----------------------------------------------------------------------------NVDV 47

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469545504 364 LFIDEAAQALEAACWIAIGKADRVILAGDHHQLPPTIKCIEAARGGLDHTLMQKITDRK---PETVSLLKTQYR 434
Cdd:cd17934    48 VIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAALLGLSFILSLLLLFRLllpGSPKVMLDTQYR 121
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 189-434 3.18e-20

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 91.05  E-value: 3.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAaKDVSIVHGPPGTGKTTTLVEAIYEtLHRENQ--------------VMVCAQSNTAVDWISEKLVD 254
Cdd:cd18040     2 LNPSQNHAVRTALT-KPFTLIQGPPGTGKTVTGVHIAYW-FAKQNReiqsvsgegdggpcVLYCGPSNKSVDVVAELLLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 255 R-GIHVLRI-------------GNPTRINDKmlSFTYERRFESHPDYAELWGIRKAireiqSNLRKKSHGEKETarnRLS 320
Cdd:cd18040    80 VpGLKILRVyseqietteypipNEPRHPNKK--SERESKPNSELSSITLHHRIRQP-----SNPHSQQIKAFEA---RFE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 321 RLRFRATELEVKIDTELFDEAR--------VVACTL-VGSANRVLTNRNFTTLFIDEAAQALEAACWIAI---GKADRVI 388
Cdd:cd18040   150 RTQEKITEEDIKTYKILIWEARfeeletvdVILCTCsEAASQKMRTHANVKQCIVDECGMCTEPESLIPIvsaPRAEQVV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1469545504 389 LAGDHHQLPPTIKCIEAARGGLDHTLMQkitdRKPETVSLLKTQYR 434
Cdd:cd18040   230 LIGDHKQLRPVVQNKEAQKLGLGRSLFE----RYAEKACMLDTQYR 271
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 189-423 1.92e-14

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 72.90  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAAKDVSI----VHGPPGTGKTTTLVEAIYETLHR-ENQVMVCAQSNTAVD-WISEKLvdrGIHVlri 262
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQLppvlLIGPFGTGKTFTLAQAVKHILQQpETRILICTHSNSAADlYIKEYL---HPYV--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 263 gNPTRINDKMLSFTYERRFES--HPDyaelwgirkaireIQSNLRKKSHGeketarnrlsrlRFRateLEVKIDTElfdE 340
Cdd:cd18077    76 -ETGNPRARPLRVYYRNRWVKtvHPV-------------VQKYCLIDEHG------------TFR---MPTREDVM---R 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 341 ARVVACTLVGS---ANRVLTNRNFTTLFIDEAAQALEAACWIAIGKAD---RVILAGDHHQLPPTIKCIEAARGGLDHTL 414
Cdd:cd18077   124 HRVVVVTLSTSqylCQLDLEPGFFTHILLDEAAQAMECEAIMPLALATkstRIVLAGDHMQLSPEVYSEFARERNLHISL 203


                  ....*....
gi 1469545504 415 MQKITDRKP 423
Cdd:cd18077   204 LERLYEHYP 212
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 189-402 2.95e-14

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 71.04  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAaKDVSIVHGPPGTGKTTT---LVEAIYETL--HRENQVMVCAQSNTAVDWISEKLVDRGI-HVLRI 262
Cdd:cd17936     2 LDPSQLEALKHALT-SELALIQGPPGTGKTFLgvkLVRALLQNQdlSITGPILVVCYTNHALDQFLEGLLDFGPtKIVRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 263 GnptrindkmlsftyerrfeshpdyaelwgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidtelfdeAR 342
Cdd:cd17936    81 G-----------------------------------------------------------------------------AR 83

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469545504 343 VVACTLVGSA--NRVLTNRNFTTLFIDEAAQALEA---ACWIAigKADRVILAGDHHQLPPTIKC 402
Cdd:cd17936    84 VIGMTTTGAAkyRELLQALGPKVVIVEEAAEVLEAhilAALTP--STEHLILIGDHKQLRPKVNV 146
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 189-418 5.35e-13

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 68.76  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVL----AAKDVS--IVHGPPGTGKTTTLVEAIYETLHR-ENQVMVCAQSNTAVD-WISE---KLVDRGI 257
Cdd:cd18076     2 GNNKQQLAFNFIAgkpsEARFVPplLIYGPFGTGKTFTLAMAALEVIREpGTKVLICTHTNSAADiYIREyfhPYVDKGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 258 HVLRignPTRI--NDKMLSFTyerrfesHPDYAELWGIRKaireiqsnlrkkshgeketarnrlSRLRFRATElevkidT 335
Cdd:cd18076    82 PEAR---PLRIkaTDRPNAIT-------DPDTITYCCLTK------------------------DRQCFRLPT------R 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 336 ELFDEARVVACTLVGSANRVLTNRNFTTLFIDEAAQALEAACWIAIGKAD---RVILAGDHHQLPPTIKCIEAARGGlDH 412
Cdd:cd18076   122 DELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLECEALIPLSYAGpktRVVLAGDHMQMTPKLFSVADYNRA-NH 200


                  ....*.
gi 1469545504 413 TLMQKI 418
Cdd:cd18076   201 TLLNRL 206
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 207-448 2.12e-10

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 60.90  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 207 SIVHGPPGTGKT---TTLVEAIYETlHRENQVMVCAQSNTAVDWISEKLVDRGI---HVLRIGNPTRIndkmlsftyerr 280
Cdd:cd17935    23 TMVVGPPGTGKTdvaVQIISNLYHN-FPNQRTLIVTHSNQALNQLFEKIMALDIderHLLRLGHGAKI------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 281 feshpdYAELWgirkaireiqsnlrkkSHGEkeTARNRLSRLRFRatelevkidtelfdearvvactlvgsanrvltnrn 360
Cdd:cd17935    90 ------IAMTC----------------THAA--LKRGELVELGFK----------------------------------- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 361 FTTLFIDEAAQALEAACWIAI---------GKADRVILAGDHHQLPPTIKCIEAAR-GGLDHTLMQKITDRKPETVsLLK 430
Cdd:cd17935   111 YDNILMEEAAQILEIETFIPLllqnpedgpNRLKRLIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRLVRLGVPTV-DLD 189

                         250
                  ....*....|....*...
gi 1469545504 431 TQYRMNEDIMRFPSrWFY 448
Cdd:cd17935   190 AQGRARASISSLYN-WRY 206
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 521-606 2.70e-09

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 54.37  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 521 IDFGLISPYKSQVQYIRGLIKRDTFFKPFRRLITAHTVDGFQGQERDVIMISLVRANDKgrigflgDLRRMNVAITRARM 600
Cdd:cd18786    11 YKGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL-------TPRRLYVALTRARK 83


                  ....*.
gi 1469545504 601 KLMILG 606
Cdd:cd18786    84 RLVIYD 89
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 189-446 1.30e-08

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 55.26  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 189 LNLSQEEAVNHVLAAKD-VSIVHGPPGTGKTTTLvEAIYETLHREN-QVMVCAQSNTAVDWISEklvDRGIHVLRIGnpt 266
Cdd:pfam13604   2 LNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTAL-KALREAWEAAGyRVIGLAPTGRAAKVLGE---ELGIPADTIA--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 267 rindkmlSFTYERRFESHPDYAELWgirkaireiqsnlrkkshgeketarnrlsrlrfratelevkidteLFDEArvvac 346
Cdd:pfam13604  75 -------KLLHRLGGRAGLDPGTLL---------------------------------------------IVDEA----- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 347 TLVGSanrvltnrnfttlfiDEAAQALEAACwiaiGKADRVILAGDHHQLPPtikcIEAarGGLDHTLMQKITDrkpeTV 426
Cdd:pfam13604  98 GMVGT---------------RQMARLLKLAE----DAGARVILVGDPRQLPS----VEA--GGAFRDLLAAGIG----TA 148

                         250       260
                  ....*....|....*....|
gi 1469545504 427 SLlktqyrmnEDIMRFPSRW 446
Cdd:pfam13604 149 EL--------TEIVRQRDPW 160
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 190-246 2.29e-08

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases 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: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 52.97  E-value: 2.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469545504 190 NLSQEEAVNHVLAAKDVsIVHGPPGTGKTTTLVEAIYETLHRENQVMVCAQSNTAVD 246
Cdd:cd18043     1 DSSQEAAIISARNGKNV-VIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALD 56
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 137-258 1.68e-07

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 54.21  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 137 QLYFDETSYKT-MFNALSTVIQakgnRLAYLRDVLLGKTPVGR--RTFFPMRFPWLNLSQEEAVNHVLAAKDVSIVHGPP 213
Cdd:COG0507    74 PLVLDGRRYLTrLLEAEQRLAR----RLRRLARPALDEADVEAalAALEPRAGITLSDEQREAVALALTTRRVSVLTGGA 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1469545504 214 GTGKTTTLVEAIYETLHRENQVMVCAQSNTAVDWISEKLVDRG--IH 258
Cdd:COG0507   150 GTGKTTTLRALLAALEALGLRVALAAPTGKAAKRLSESTGIEArtIH 196
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 336-414 4.31e-07

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 49.02  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 336 ELFDEARVVACTLVGSANRVLTNrnfttLFIDEAAQALEAACWI---AIGKADRVILAGDHHQLPPTIKCIEAARGGLDH 412
Cdd:cd17914    27 KNGEPGRILLVTPTNKAAAQLDN-----ILVDEAAQILEPETSRlidLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQ 101


                  ..
gi 1469545504 413 TL 414
Cdd:cd17914   102 SL 103
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 207-262 1.64e-06

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 47.48  E-value: 1.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 207 SIVHGPPGTGKTTTLVEAIYETLHREN----QVMVCAQSNTAVDWISEKLVDRGIHVLRI 262
Cdd:cd17914     2 SLIQGPPGTGKTRVLVKIVAALMQNKNgepgRILLVTPTNKAAAQLDNILVDEAAQILEP 61
AAA_19 pfam13245
AAA domain;
193-252 2.00e-06

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 47.60  E-value: 2.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469545504 193 QEEAVNHVLAAKdVSIVHGPPGTGKTTTLVE--AIYETLHRE-NQVMVCAQSNTAVDWISEKL 252
Cdd:pfam13245   1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHivALLVALGGVsFPILLAAPTGRAAKRLSERT 62
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 193-239 1.78e-05

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 45.24  E-value: 1.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1469545504 193 QEEAVNHVLAAKdVSIVHGPPGTGKTTTLVEAIYETLHRENQVMVCA 239
Cdd:cd17933     2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA 47
DEXDc smart00487
DEAD-like helicases superfamily;
193-250 1.27e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 43.63  E-value: 1.27e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469545504  193 QEEAVNHVLAAKDVSIVHGPPGTGKTTTLVEAIYETLHRENQ---VMVCAQSNTAVDWISE 250
Cdd:smart00487  13 QKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGgrvLVLVPTRELAEQWAEE 73
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 195-279 3.98e-03

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 39.55  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469545504 195 EAVNHVLAAKDVSIVHGPPGTGKTTTLVEAiyeTLHRENQVMVCAQSNTAVDWISEKLVDRgihvLRIGNPTRINDKMLS 274
Cdd:COG2842    41 EALDEARALPGIGVVYGESGVGKTTAAREY---ANRNPNVIYVTASPSWTSKELLEELAEE----LGIPAPPGTIADLRD 113


                  ....*
gi 1469545504 275 FTYER 279
Cdd:COG2842   114 RILER 118
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 193-239 5.65e-03

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: 37.99  E-value: 5.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469545504 193 QEEAVNHVLAAKDVsIVHGPPGTGKTTTLVEAIYETLHREN---QVMVCA 239
Cdd:pfam00270   4 QAEAIPAILEGRDV-LVQAPTGSGKTLAFLLPALEALDKLDngpQALVLA 52
 
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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