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Conserved domains on  [gi|1745156558|gb|KAA4718055|]
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AAA family ATPase [Bacteroides ovatus]

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 ...
 157-647 4.42e-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: 4.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 157 VQLYFDETSYRAMFEALEDTIRAKDnrlaELRDILLGTQKPG-FRELYPVRF--PWLNSTQETAVNKVLCTRDVSIVHGP 233
Cdd:TIGR00376 106 IDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSkASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 234 PGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTRVNDKMLSSTYERRFESHPAYPELWG 313
Cdd:TIGR00376 182 PGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVAD 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 314 IHKSIREM---------GSRMRRGSYSEREGMRNRMSRLRDRATELEIQIN--------------------ADLFDSARV 364
Cdd:TIGR00376 262 IREKIDELieernkktkPSPQKRRGLSDIKILRKALKKREARGIESLKIASmaewietnksidrllkllpeSEERIMNEI 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 365 IA---STLVSSNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASrgGLDHTLMEKVVQ 441
Cdd:TIGR00376 342 LAesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIK 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 442 QKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYRGILDFDT--------------PMNWIDTSEMDFHEDFVG 507
Cdd:TIGR00376 420 EYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKveateseddletgiPLLFIDTSGCELFELKEA 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 508 ESFGRINKQEANLLLQeletYIERIGKKRILDERIdfGLISPYKAQVQYLRGKIKGSsflrpfRSLITVNTVDGFQGQER 587
Cdd:TIGR00376 500 DSTSKYNPGEAELVSE----IIQALVKMGVPANDI--GVITPYDAQVDLLRQLLEHR------HIDIEVSSVDGFQGREK 567

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 588 DVIFISLVRANEDGQIGFLNDLRRMNVAITRARMKLVILGDASTLAKHPFYKRLMLFIKK 647
Cdd:TIGR00376 568 EVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQ 627
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 157-647 4.42e-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: 4.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 157 VQLYFDETSYRAMFEALEDTIRAKDnrlaELRDILLGTQKPG-FRELYPVRF--PWLNSTQETAVNKVLCTRDVSIVHGP 233
Cdd:TIGR00376 106 IDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSkASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 234 PGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTRVNDKMLSSTYERRFESHPAYPELWG 313
Cdd:TIGR00376 182 PGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVAD 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 314 IHKSIREM---------GSRMRRGSYSEREGMRNRMSRLRDRATELEIQIN--------------------ADLFDSARV 364
Cdd:TIGR00376 262 IREKIDELieernkktkPSPQKRRGLSDIKILRKALKKREARGIESLKIASmaewietnksidrllkllpeSEERIMNEI 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 365 IA---STLVSSNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASrgGLDHTLMEKVVQ 441
Cdd:TIGR00376 342 LAesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIK 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 442 QKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYRGILDFDT--------------PMNWIDTSEMDFHEDFVG 507
Cdd:TIGR00376 420 EYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKveateseddletgiPLLFIDTSGCELFELKEA 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 508 ESFGRINKQEANLLLQeletYIERIGKKRILDERIdfGLISPYKAQVQYLRGKIKGSsflrpfRSLITVNTVDGFQGQER 587
Cdd:TIGR00376 500 DSTSKYNPGEAELVSE----IIQALVKMGVPANDI--GVITPYDAQVDLLRQLLEHR------HIDIEVSSVDGFQGREK 567

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 588 DVIFISLVRANEDGQIGFLNDLRRMNVAITRARMKLVILGDASTLAKHPFYKRLMLFIKK 647
Cdd:TIGR00376 568 EVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQ 627
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 209-455 9.26e-92

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: 282.19  E-value: 9.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 209 WLNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTR 288
Cdd:cd18044     1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 289 VNDKMLSSTYERRFEshpaypelwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqinadlfdsARVIAST 368
Cdd:cd18044    81 LLESVLDHSLDALVA----------------------------------------------------------AQVVLAT 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 369 LVSSNHRLL-NGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASRGGLDHTLMEKVVQQK-PSA 446
Cdd:cd18044   103 NTGAGSRQLlPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYgESV 182


                  ....*....
gi 1745156558 447 VSLLKVQYR 455
Cdd:cd18044   183 VRMLTVQYR 191
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
123-648 3.23e-85

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 284.33  E-value: 3.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 123 DFIATVSFADEERMVVVLPGAGALAELQTDGILGVQLYFDETSYRAMFEALEDTIRAKDNRLAELRDILLGTQKPGFREL 202
Cdd:COG1112   292 ALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLL 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 203 YPVRFPWLNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWicEKLVDRGVPVLR 282
Cdd:COG1112   372 LLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAAL--LALLLLLAAALA 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 283 IGNPTRVNDKMLSSTYERRFESHPAYPELWGIHKSIREMGS------RMRRGSYSEREGMRNRMSRLRDRATELEIQINA 356
Cdd:COG1112   450 ALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEehpeelEKLIAELREAARLRRALRRELKKRRELRKLLWD 529

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 357 DLFDSARVIASTLVS-SNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEA---SRGGLD 432
Cdd:COG1112   530 ALLELAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAeevAEEGLD 609

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 433 HTLMEKVVQQKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYRGILDFDTPMNWIDTSEMdfhedFVGESFGR 512
Cdd:COG1112   610 ESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSPLVFIDVDGV-----YERRGGSR 684

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 513 INKQEANLLLQELETYIERIGKKRilderiDFGLISPYKAQVQYLRGKIKgsSFLRPFRSLITVNTVDGFQGQERDVIFI 592
Cdd:COG1112   685 TNPEEAEAVVELVRELLEDGPDGE------SIGVITPYRAQVALIRELLR--EALGDGLEPVFVGTVDRFQGDERDVIIF 756

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1745156558 593 SLVRANED---GQIGFLN-DLRRMNVAITRARMKLVILGDASTLAKHPF---YKRLMLFIKKE 648
Cdd:COG1112   757 SLVYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPStpaLKRLLEYLERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 431-630 3.99e-72

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: 231.28  E-value: 3.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 431 LDHTLMEKVVQQKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYR------GILDFDTPMNWIDTSEMdfHED 504
Cdd:pfam13087   1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfHLPDPLGPLVFIDVDGS--EEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 505 FVGESFGRINKQEANLLLQELETYIerigkKRILDERIDFGLISPYKAQVQYLRGKIKGSSFLRPfrsLITVNTVDGFQG 584
Cdd:pfam13087  79 ESDGGTSYSNEAEAELVVQLVEKLI-----KSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGKL---EIEVNTVDGFQG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1745156558 585 QERDVIFISLVRANEDGQIGFLNDLRRMNVAITRARMKLVILGDAS 630
Cdd:pfam13087 151 REKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DEXDc smart00487
DEAD-like helicases superfamily;
210-300 1.16e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 43.63  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558  210 LNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHRE--PQVLVCA-QSNTAVDWI--CEKLVD--RGVPVLR 282
Cdd:smart00487   9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGkgGRVLVLVpTRELAEQWAeeLKKLGPslGLKVVGL 88

                           90       100
                   ....*....|....*....|....*..
gi 1745156558  283 IGNPTRVNDK---------MLSSTYER 300
Cdd:smart00487  89 YGGDSKREQLrklesgktdILVTTPGR 115
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 157-647 4.42e-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: 4.42e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 157 VQLYFDETSYRAMFEALEDTIRAKDnrlaELRDILLGTQKPG-FRELYPVRF--PWLNSTQETAVNKVLCTRDVSIVHGP 233
Cdd:TIGR00376 106 IDLYANDVTFKRMKEALRALTENHS----RLLEFLLGREAPSkASEIHDFQFfdPNLNESQKEAVLFALSSKDLFLIHGP 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 234 PGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTRVNDKMLSSTYERRFESHPAYPELWG 313
Cdd:TIGR00376 182 PGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQHSLDYLIENHPKYQIVAD 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 314 IHKSIREM---------GSRMRRGSYSEREGMRNRMSRLRDRATELEIQIN--------------------ADLFDSARV 364
Cdd:TIGR00376 262 IREKIDELieernkktkPSPQKRRGLSDIKILRKALKKREARGIESLKIASmaewietnksidrllkllpeSEERIMNEI 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 365 IA---STLVSSNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASrgGLDHTLMEKVVQ 441
Cdd:TIGR00376 342 LAesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIK 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 442 QKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYRGILDFDT--------------PMNWIDTSEMDFHEDFVG 507
Cdd:TIGR00376 420 EYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKveateseddletgiPLLFIDTSGCELFELKEA 499

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 508 ESFGRINKQEANLLLQeletYIERIGKKRILDERIdfGLISPYKAQVQYLRGKIKGSsflrpfRSLITVNTVDGFQGQER 587
Cdd:TIGR00376 500 DSTSKYNPGEAELVSE----IIQALVKMGVPANDI--GVITPYDAQVDLLRQLLEHR------HIDIEVSSVDGFQGREK 567

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 588 DVIFISLVRANEDGQIGFLNDLRRMNVAITRARMKLVILGDASTLAKHPFYKRLMLFIKK 647
Cdd:TIGR00376 568 EVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQ 627
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 209-455 9.26e-92

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: 282.19  E-value: 9.26e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 209 WLNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTR 288
Cdd:cd18044     1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 289 VNDKMLSSTYERRFEshpaypelwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqinadlfdsARVIAST 368
Cdd:cd18044    81 LLESVLDHSLDALVA----------------------------------------------------------AQVVLAT 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 369 LVSSNHRLL-NGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASRGGLDHTLMEKVVQQK-PSA 446
Cdd:cd18044   103 NTGAGSRQLlPNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYgESV 182


                  ....*....
gi 1745156558 447 VSLLKVQYR 455
Cdd:cd18044   183 VRMLTVQYR 191
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
123-648 3.23e-85

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 284.33  E-value: 3.23e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 123 DFIATVSFADEERMVVVLPGAGALAELQTDGILGVQLYFDETSYRAMFEALEDTIRAKDNRLAELRDILLGTQKPGFREL 202
Cdd:COG1112   292 ALALLLLAALALLLALALAALLALLALLALLAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLL 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 203 YPVRFPWLNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWicEKLVDRGVPVLR 282
Cdd:COG1112   372 LLALEELLLLALLRLLAEGLALLLLLLLAALLRLARALLLLALLLAAAAAALAALLLLALALLAAL--LALLLLLAAALA 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 283 IGNPTRVNDKMLSSTYERRFESHPAYPELWGIHKSIREMGS------RMRRGSYSEREGMRNRMSRLRDRATELEIQINA 356
Cdd:COG1112   450 ALLALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEehpeelEKLIAELREAARLRRALRRELKKRRELRKLLWD 529

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 357 DLFDSARVIASTLVS-SNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEA---SRGGLD 432
Cdd:COG1112   530 ALLELAPVVGMTPASvARLLPLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAeevAEEGLD 609

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 433 HTLMEKVVQQKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYRGILDFDTPMNWIDTSEMdfhedFVGESFGR 512
Cdd:COG1112   610 ESLLDRLLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLADPDSPLVFIDVDGV-----YERRGGSR 684

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 513 INKQEANLLLQELETYIERIGKKRilderiDFGLISPYKAQVQYLRGKIKgsSFLRPFRSLITVNTVDGFQGQERDVIFI 592
Cdd:COG1112   685 TNPEEAEAVVELVRELLEDGPDGE------SIGVITPYRAQVALIRELLR--EALGDGLEPVFVGTVDRFQGDERDVIIF 756

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1745156558 593 SLVRANED---GQIGFLN-DLRRMNVAITRARMKLVILGDASTLAKHPF---YKRLMLFIKKE 648
Cdd:COG1112   757 SLVYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPStpaLKRLLEYLERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 431-630 3.99e-72

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: 231.28  E-value: 3.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 431 LDHTLMEKVVQQKPSAVSLLKVQYRMHEAIMQFPSDWFYHGELEAAPEVRYR------GILDFDTPMNWIDTSEMdfHED 504
Cdd:pfam13087   1 LDRSLFERLQELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERplpddfHLPDPLGPLVFIDVDGS--EEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 505 FVGESFGRINKQEANLLLQELETYIerigkKRILDERIDFGLISPYKAQVQYLRGKIKGSSFLRPfrsLITVNTVDGFQG 584
Cdd:pfam13087  79 ESDGGTSYSNEAEAELVVQLVEKLI-----KSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGKL---EIEVNTVDGFQG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1745156558 585 QERDVIFISLVRANEDGQIGFLNDLRRMNVAITRARMKLVILGDAS 630
Cdd:pfam13087 151 REKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 213-422 3.63e-57

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: 193.33  E-value: 3.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 213 TQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAI-------YETLHREPQVLVCAQSNTAVDWICEKLVDRG----VPVL 281
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIrqllsypATSAAAGPRILVCAPSNAAVDNILERLLRKGqkygPKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 282 RIGNPTRVNDKMLSSTYERRFESHPAYPELWGIHKSI-REMGSRM----------------------RRGSYSEREGMRN 338
Cdd:pfam13086  81 RIGHPAAISEAVLPVSLDYLVESKLNNEEDAQIVKDIsKELEKLAkalrafekeiivekllksrnkdKSKLEQERRKLRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 339 RMSRLRDRATELEIQINADLFDSARVIASTLVSSNHRLLNGR-RFPTLFIDEAAQALEAACWIAIRKA-DRVILAGDHCQ 416
Cdd:pfam13086 161 ERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGpKKVVLVGDPKQ 240


                  ....*.
gi 1745156558 417 LPPTIK 422
Cdd:pfam13086 241 LPPTVI 246
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 456-646 8.82e-54

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: 182.05  E-value: 8.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 456 MHEAIMQFPSDWFYHGELEAAPEVRYRG----ILDFDTPMNWIDTSEMDFHEdfvGESFGRINKQEANLLLQeletYIER 531
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAARLnpppLPGPSKPLVFVDVSGGEERE---ESGTSKSNEAEAELVVE----LVKY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 532 IGKKRILDERIdfGLISPYKAQVQYLRGKIKGSsflRPFRSLITVNTVDGFQGQERDVIFISLVRANEDG-QIGFLNDLR 610
Cdd:cd18808    74 LLKSGVKPSSI--GVITPYRAQVALIRELLRKR---GGLLEDVEVGTVDNFQGREKDVIILSLVRSNESGgSIGFLSDPR 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1745156558 611 RMNVAITRARMKLVILGDASTLAKHPFYKRLMLFIK 646
Cdd:cd18808   149 RLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 210-455 6.64e-53

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: 180.51  E-value: 6.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTRV 289
Cdd:cd18041     2 LNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 290 NDKMLSSTYERRFESHPAYPELwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqinADLFDSARVIASTL 369
Cdd:cd18041    82 HPDVQEFTLEAILKSCKSVEEL--------------------------------------------ESKYESVSVVATTC 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 370 VSSNHRLLNGRRFPTLFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASRGGLDHTLMEKVVQQKPSAVSL 449
Cdd:cd18041   118 LGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQ 197


                  ....*.
gi 1745156558 450 LKVQYR 455
Cdd:cd18041   198 LTIQYR 203
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 210-455 3.39e-50

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: 174.36  E-value: 3.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLcTRDVSIVHGPPGTGKTTTLVEAIYETLHREP-QVLVCAQSNTAVDWICEKLVDRGVPVLRIGNPTR 288
Cdd:cd18039     2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVYHLVKQGNgPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 289 vndkmlsstyerrfESHPAYPELWGIHKSIREMGSRMRR----------GSYSEREGMRNRMSRlrdRATELEIQINADl 358
Cdd:cd18039    81 --------------EAVESPVSFLALHNQVRNLDSAEKLellkllkletGELSSADEKRYRKLK---RKAERELLRNAD- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 359 fdsarVIASTLVSSNHRLLNGRRFPTLFIDEAAQALEAACWIAI-RKADRVILAGDHCQLPPTIKCIEASRGGLDHTLME 437
Cdd:cd18039   143 -----VICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLvHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFE 217

                         250       260
                  ....*....|....*....|
gi 1745156558 438 KVVQ--QKPsavSLLKVQYR 455
Cdd:cd18039   218 RLVQlgIRP---IRLQVQYR 234
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 210-444 2.51e-41

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: 149.69  E-value: 2.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVL-CTRDV--SIVHGPPGTGKTTTLVEAIYE--TLHREPQVLVCAQSNTAVDWICEKLVDRGVP---VL 281
Cdd:cd18038     2 LNDEQKLAVRNIVtGTSRPppYIIFGPPGTGKTVTLVEAILQvlRQPPEARILVCAPSNSAADLLAERLLNALVTkreIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 282 RIGNPTR------VNDKMLSSTYERRFESHPAYPELwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqin 355
Cdd:cd18038    82 RLNAPSRdrasvpPELLPYCNSKAEGTFRLPSLEEL-------------------------------------------- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 356 adlfDSARVIASTLVSSNHrlLNGRRFP-----TLFIDEAAQALEAACWIAIRKAD----RVILAGDHCQLPPTIKCIEA 426
Cdd:cd18038   118 ----KKYRIVVCTLMTAGR--LVQAGVPnghftHIFIDEAGQATEPEALIPLSELAskntQIVLAGDPKQLGPVVRSPLA 191

                         250
                  ....*....|....*...
gi 1745156558 427 SRGGLDHTLMEKVVQQKP 444
Cdd:cd18038   192 RKYGLGKSLLERLMERPL 209
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 210-455 1.19e-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: 133.88  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLCT-RDVSIVHGPPGTGKTTTLVEAIYETLHRE-------------------------PQVLVCAQSN 263
Cdd:cd18042     1 LNESQLEAIASALQNsPGITLIQGPPGTGKTKTIVGILSVLLAGKyrkyyekvkkklrklqrnlnnkkkkNRILVCAPSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 264 TAVDWICEKLVDRGVpvlrignptrVNDKMLSSTYerrfeshpaypelwgihksiremgsrmrrgsyseregmrnRMSRL 343
Cdd:cd18042    81 AAVDEIVLRLLSEGF----------LDGDGRSYKP----------------------------------------NVVRV 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 344 RDRATELEIqinadlFDSARVIASTLVSSNHRLLN--GRRFPTLFIDEAAQALEAACWIAIRK-ADRVILAGDHCQLPPT 420
Cdd:cd18042   111 GRQELRASI------LNEADIVCTTLSSSGSDLLEslPRGFDTVIIDEAAQAVELSTLIPLRLgCKRLILVGDPKQLPAT 184

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1745156558 421 IKCIEASRGGLDHTLMEKvVQQKPSAVSLLKVQYR 455
Cdd:cd18042   185 VFSKVAQKLGYDRSLFER-LQLAGYPVLMLTTQYR 218
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 210-444 4.29e-28

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: 112.85  E-value: 4.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVL---CTRDVSIVHGPPGTGKTTTLVEAIYE--TLHREPQVLVCAQSNTAVDWICEKLVDRGvpVLRIG 284
Cdd:cd18078     2 LNELQKEAVKRILggeCRPLPYILFGPPGTGKTVTIIEAILQvvYNLPRSRILVCAPSNSAADLVTSRLHESK--VLKPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 285 NPTRVNdkmlsstyerrfeshpaypelwgihksiremgsrmrrgSYSEREGMRNRMSRLRDRATEleiqinaDLFDS--A 362
Cdd:cd18078    80 DMVRLN--------------------------------------AVNRFESTVIDARKLYCRLGE-------DLSKAsrH 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 363 RVIASTLVSSNHRLLNGRR---FPTLFIDEAAQALEAACWIAI----RKADRVILAGDHCQLPPTIKCIEASRGGLDHTL 435
Cdd:cd18078   115 RIVISTCSTAGLLYQMGLPvghFTHVFVDEAGQATEPESLIPLglisSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSF 194


                  ....*....
gi 1745156558 436 MEKVVQQKP 444
Cdd:cd18078   195 LERLMNRPL 203
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 227-455 1.92e-23

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: 95.76  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 227 VSIVHGPPGTGKTTTLVEAIYETL--HREPQVLVCAQSNTAVDwiceklvdrgvpvlrignptrvndkmlsstyerrfes 304
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLkgLRGKRVLVTAQSNVAVD------------------------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 305 hpaypelwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqiNADlfdsarviastlvssnhrllngrrfpT 384
Cdd:cd17934    44 --------------------------------------------------NVD--------------------------V 47

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1745156558 385 LFIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTIKCIEASRGGLDHT---LMEKVVQQKPSAVSLLKVQYR 455
Cdd:cd17934    48 VIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAALLGLSFIlslLLLFRLLLPGSPKVMLDTQYR 121
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 210-449 4.80e-16

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: 76.43  E-value: 4.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLcTRDVSIVHGPPGTGKTTT---LVEAIYETL--HREPQVLVCAQSNTAVDWICEKLVDRGVP-VLRI 283
Cdd:cd17936     2 LDPSQLEALKHAL-TSELALIQGPPGTGKTFLgvkLVRALLQNQdlSITGPILVVCYTNHALDQFLEGLLDFGPTkIVRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 284 GnptrvndkmlsstyerrfeshpaypelwgihksiremgsrmrrgsyseregmrnrmsrlrdrateleiqinadlfdsAR 363
Cdd:cd17936    81 G-----------------------------------------------------------------------------AR 83

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 364 VIASTL--VSSNHRLLNGRRFPTLFIDEAAQALEAACwIAI--RKADRVILAGDHCQLPPTIKC--IEASRGGLDHTLME 437
Cdd:cd17936    84 VIGMTTtgAAKYRELLQALGPKVVIVEEAAEVLEAHI-LAAltPSTEHLILIGDHKQLRPKVNVyeLTAKKYNLDVSLFE 162

                         250
                  ....*....|..
gi 1745156558 438 KVVQQKPSAVSL 449
Cdd:cd17936   163 RLVKNGLPFVTL 174
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 210-455 1.14e-15

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: 77.57  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLCtRDVSIVHGPPGTGKTTTLVEAIY--ETLHRE-----------PQVLVCAQSNTAVDWICEKLVDr 276
Cdd:cd18040     2 LNPSQNHAVRTALT-KPFTLIQGPPGTGKTVTGVHIAYwfAKQNREiqsvsgegdggPCVLYCGPSNKSVDVVAELLLK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 277 gVPVLRignPTRVNDKMLSSTyERRFESHPAYPELwgihKSIREMGS-----------RMRRGS--YSER-EGMRNRMSR 342
Cdd:cd18040    80 -VPGLK---ILRVYSEQIETT-EYPIPNEPRHPNK----KSERESKPnselssitlhhRIRQPSnpHSQQiKAFEARFER 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 343 LRDRATELEIQINADLFDSAR--------VIASTL-VSSNHRLLNGRRFPTLFIDEAAQALEAACWIAI---RKADRVIL 410
Cdd:cd18040   151 TQEKITEEDIKTYKILIWEARfeeletvdVILCTCsEAASQKMRTHANVKQCIVDECGMCTEPESLIPIvsaPRAEQVVL 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1745156558 411 AGDHCQLPPTIKCIEASRGGLDHTLMEKVVQQkpsaVSLLKVQYR 455
Cdd:cd18040   231 IGDHKQLRPVVQNKEAQKLGLGRSLFERYAEK----ACMLDTQYR 271
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 210-445 9.09e-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: 70.98  E-value: 9.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLCTRDVSI----VHGPPGTGKTTTLVEAIYETLHR-EPQVLVCAQSNTAVD-WICEKL---VDRGVPV 280
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQLppvlLIGPFGTGKTFTLAQAVKHILQQpETRILICTHSNSAADlYIKEYLhpyVETGNPR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 281 LRignPTRVndkmlssTYERRFES--HPAypelwgIHK-SIREMGSRMRrgsYSEREGMRNrmsrlrdrateleiqinad 357
Cdd:cd18077    82 AR---PLRV-------YYRNRWVKtvHPV------VQKyCLIDEHGTFR---MPTREDVMR------------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 358 lfdsARVIASTLVSSNH--RLLNGRRFPT-LFIDEAAQALEAACWIAIRKAD---RVILAGDHCQLPPTIKCIEASRGGL 431
Cdd:cd18077   124 ----HRVVVVTLSTSQYlcQLDLEPGFFThILLDEAAQAMECEAIMPLALATkstRIVLAGDHMQLSPEVYSEFARERNL 199

                         250
                  ....*....|....
gi 1745156558 432 DHTLMEKVVQQKPS 445
Cdd:cd18077   200 HISLLERLYEHYPS 213
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 210-441 5.72e-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: 5.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVN----KVLCTRDVS--IVHGPPGTGKTTTLVEAIYEtLHREP--QVLVCAQSNTAVD-WICE---KLVDRG 277
Cdd:cd18076     2 GNNKQQLAFNfiagKPSEARFVPplLIYGPFGTGKTFTLAMAALE-VIREPgtKVLICTHTNSAADiYIREyfhPYVDKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 278 VPVLRignPTRVndkmlsstyerRFESHPAypelwgihkSIREMGSRMRRGSYSEREGMRNRMSRLRDRateleiqinad 357
Cdd:cd18076    81 HPEAR---PLRI-----------KATDRPN---------AITDPDTITYCCLTKDRQCFRLPTRDELDF----------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 358 lfdSARVIASTLVSSNHRLLNGRrFPTLFIDEAAQALEAACWIAIRKAD---RVILAGDHCQLPPTIKCIEASRGGlDHT 434
Cdd:cd18076   127 ---HNIVITTTAMAFNLHVLSGF-FTHIFIDEAAQMLECEALIPLSYAGpktRVVLAGDHMQMTPKLFSVADYNRA-NHT 201


                  ....*..
gi 1745156558 435 LMEKVVQ 441
Cdd:cd18076   202 LLNRLFH 208
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 542-627 1.47e-11

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: 60.91  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 542 IDFGLISPYKAQVQYLRGKIKGSSFLRPFRSLITVNTVDGFQGQERDVIFISLVRANEDgqigflnDLRRMNVAITRARM 621
Cdd:cd18786    11 YKGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL-------TPRRLYVALTRARK 83


                  ....*.
gi 1745156558 622 KLVILG 627
Cdd:cd18786    84 RLVIYD 89
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 211-421 6.68e-09

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: 54.51  E-value: 6.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 211 NSTQETAVNKVLCTRDVsIVHGPPGTGKTTTLVEAIYETLHREPQVLVCAQSNTAVDwiceklvdrgvpVLRIgnptrvn 290
Cdd:cd18043     1 DSSQEAAIISARNGKNV-VIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALD------------VVRF------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 291 dkmlsstyerrfeshPAYpelwgihksireMGSRMRRGSYseregmrnrmsrlrdrateleIQINADLFDSarVIastlv 370
Cdd:cd18043    61 ---------------PCW------------IMSPLSVSQY---------------------LPLNRNLFDL--VI----- 85

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1745156558 371 ssnhrllngrrfptlfIDEAAQALEAACWIAIRKADRVILAGDHCQLPPTI 421
Cdd:cd18043    86 ----------------FDEASQIPIEEALPALFRGKQVVVVGDDKQLPPSI 120
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 145-260 1.96e-08

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: 57.29  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 145 ALAELQTDGilgvQLYFDETSYRAMFEALEDTIRAKDNRLAElRDILLGTQKPGFRELYPVRFPWLNSTQETAVNKVLCT 224
Cdd:COG0507    65 ALAALVESG----PLVLDGRRYLTRLLEAEQRLARRLRRLAR-PALDEADVEAALAALEPRAGITLSDEQREAVALALTT 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1745156558 225 RDVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCA 260
Cdd:COG0507   140 RRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAA 175
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 210-476 2.62e-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: 54.11  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 210 LNSTQETAVNKVLCTRD-VSIVHGPPGTGKTTTLvEAIYETLHRE-PQVLVCAQSNTAVDwiceklvdrgvpvlrignpt 287
Cdd:pfam13604   2 LNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTAL-KALREAWEAAgYRVIGLAPTGRAAK-------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 288 rvndkmlsstyerrfeshpaypelwgihksiremgsrmrrgsyseregmrnrmsRLRDratELEIQinadlfdsARVIAS 367
Cdd:pfam13604  61 ------------------------------------------------------VLGE---ELGIP--------ADTIAK 75

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 368 TLVSSNHRLLNGRRfpTLFI-DEAAQA----LEAACWIAIRKADRVILAGDHCQLPPtikcIEAsrGGLDHTLMEKVVQq 442
Cdd:pfam13604  76 LLHRLGGRAGLDPG--TLLIvDEAGMVgtrqMARLLKLAEDAGARVILVGDPRQLPS----VEA--GGAFRDLLAAGIG- 146

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1745156558 443 kpsAVSLLKVqYRMHEAIMQFPSDWFYHGELEAA 476
Cdd:pfam13604 147 ---TAELTEI-VRQRDPWQRAASLALRDGDPAEA 176
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 228-469 4.01e-07

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: 51.27  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 228 SIVHGPPGTGKTTTLVEAIYETLHREP--QVLVCAQSNTAVDWICEKLVDRGVpvlrignptrvndkmlsstyerrFESH 305
Cdd:cd17935    23 TMVVGPPGTGKTDVAVQIISNLYHNFPnqRTLIVTHSNQALNQLFEKIMALDI-----------------------DERH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 306 paypelwgihksiremgsrmrrgsyseregmrnrmsRLRdrateleiqinadLFDSARVIASTLVSSN---HRLLN-GRR 381
Cdd:cd17935    80 ------------------------------------LLR-------------LGHGAKIIAMTCTHAAlkrGELVElGFK 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 382 FPTLFIDEAAQALEAACWIAIR---------KADRVILAGDHCQLPPTIKCIE-ASRGGLDHTLMEKVVQQKPSAVsLLK 451
Cdd:cd17935   111 YDNILMEEAAQILEIETFIPLLlqnpedgpnRLKRLIMIGDHHQLPPVIKNMAfQKYSNMEQSLFTRLVRLGVPTV-DLD 189

                         250
                  ....*....|....*...
gi 1745156558 452 VQYRMHEAIMQFPSdWFY 469
Cdd:cd17935   190 AQGRARASISSLYN-WRY 206
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 361-454 6.28e-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: 48.64  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 361 SARVIASTlvssNHRLlngRRFPTLFIDEAAQALEAACWI---AIRKADRVILAGDHCQLPPTIKCIEASRGGLDHTLME 437
Cdd:cd17914    33 RILLVTPT----NKAA---AQLDNILVDEAAQILEPETSRlidLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFT 105

                          90
                  ....*....|....*..
gi 1745156558 438 KVVQQKPSAVsLLKVQY 454
Cdd:cd17914   106 RLVRLGVSLI-RLQVQY 121
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 214-260 1.02e-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: 46.01  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1745156558 214 QETAVNKVLCTRdVSIVHGPPGTGKTTTLVEAIYETLHREPQVLVCA 260
Cdd:cd17933     2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAA 47
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 228-283 1.65e-05

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: 44.40  E-value: 1.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558 228 SIVHGPPGTGKTTTLVE---AIYETLHREPQ-VLVCAQSNTAVDWICEKLVDRGVPVLRI 283
Cdd:cd17914     2 SLIQGPPGTGKTRVLVKivaALMQNKNGEPGrILLVTPTNKAAAQLDNILVDEAAQILEP 61
DEXDc smart00487
DEAD-like helicases superfamily;
210-300 1.16e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 43.63  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745156558  210 LNSTQETAVNKVLCTRDVSIVHGPPGTGKTTTLVEAIYETLHRE--PQVLVCA-QSNTAVDWI--CEKLVD--RGVPVLR 282
Cdd:smart00487   9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGkgGRVLVLVpTRELAEQWAeeLKKLGPslGLKVVGL 88

                           90       100
                   ....*....|....*....|....*..
gi 1745156558  283 IGNPTRVNDK---------MLSSTYER 300
Cdd:smart00487  89 YGGDSKREQLrklesgktdILVTTPGR 115
AAA_19 pfam13245
AAA domain;
214-273 3.19e-04

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 41.05  E-value: 3.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1745156558 214 QETAVNKVLcTRDVSIVHGPPGTGKTTTLVE--AIYETLHREP-QVLVCAQSNTAVDWICEKL 273
Cdd:pfam13245   1 QREAVRTAL-PSKVVLLTGGPGTGKTTTIRHivALLVALGGVSfPILLAAPTGRAAKRLSERT 62
 
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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