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Conserved domains on  [gi|429241027|ref|NP_596499|]
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DNA replication endonuclease-helicase Dna2 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
931-1132 6.43e-93

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: 298.00  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  931 CLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHK 1010
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1011 IHPLVKEFCLTEG-TTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVG 1089
Cdd:cd18041    81 IHPDVQEFTLEAIlKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 429241027 1090 DHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYR 1132
Cdd:cd18041   161 DHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
440-663 6.37e-79

Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease/helicase DNA2 processes double-strand breaks in DNA that have single-stranded ends/overhangs, as well as Okazaki fragments and stalled replication forks; it is therefore crucial for maintaining the integrity of the genome. The nuclease domain modeled here belongs to a superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


:

Pssm-ID: 411722 [Multi-domain]  Cd Length: 234  Bit Score: 260.14  E-value: 6.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  440 SATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVD--INLETSIKTYISDIYFADLSLD 517
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEklAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  518 EIREELDARLPLLKSIVERYLIS-------KKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPeSSST 590
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSnspkgqvKLPSDGNSKGAISKILDIEENIWSPRFGLKGKIDATVEVKIHDKG-KSKT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  591 LTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQH 663
Cdd:cd22318   160 KIMPLELKTGRASFSIEHRGQVILYTLMMSDRYDVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAHY 232
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1040-1334 1.33e-64

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


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 236.56  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1040 QIVACSSLGVYHSI-FNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLF---KL 1115
Cdd:COG1112   536 PVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAEEVAEEGLDEsllDR 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1116 LSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQkklilpkahlsdglpdsssslhwvnKLINPSHSVIF 1195
Cdd:COG1112   616 LLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKAR-------------------------RLADPDSPLVF 670
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1196 FNTDdilGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKS-----FTEIEINTVDRYQ 1270
Cdd:COG1112   671 IDVD---GVYERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREalgdgLEPVFVGTVDRFQ 747
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429241027 1271 GRDKDIILISFVRSNSKNLVGE---LLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLE 1334
Cdd:COG1112   748 GDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKLIVVGSRELLDSDPSTPALKRLLE 814
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
931-1132 6.43e-93

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: 298.00  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  931 CLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHK 1010
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1011 IHPLVKEFCLTEG-TTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVG 1089
Cdd:cd18041    81 IHPDVQEFTLEAIlKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 429241027 1090 DHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYR 1132
Cdd:cd18041   161 DHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
440-663 6.37e-79

Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease/helicase DNA2 processes double-strand breaks in DNA that have single-stranded ends/overhangs, as well as Okazaki fragments and stalled replication forks; it is therefore crucial for maintaining the integrity of the genome. The nuclease domain modeled here belongs to a superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411722 [Multi-domain]  Cd Length: 234  Bit Score: 260.14  E-value: 6.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  440 SATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVD--INLETSIKTYISDIYFADLSLD 517
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEklAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  518 EIREELDARLPLLKSIVERYLIS-------KKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPeSSST 590
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSnspkgqvKLPSDGNSKGAISKILDIEENIWSPRFGLKGKIDATVEVKIHDKG-KSKT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  591 LTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQH 663
Cdd:cd22318   160 KIMPLELKTGRASFSIEHRGQVILYTLMMSDRYDVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAHY 232
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
385-579 1.50e-70

DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, ( 5'-flap endonuclease) and helicase activities. It is required for Okazaki fragment processing and is involved in DNA repair pathways.


Pssm-ID: 462565  Cd Length: 203  Bit Score: 234.76  E-value: 1.50e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   385 EANDILHQLFLRGDWTETSIFVGDSIRVEATFDkDNTAIVDNDKGLIIIHPKILMSATAVASSFPCLRKAVISDRVGIYG 464
Cdd:pfam08696    2 DKSGETRTVILRDDWVETPVEPGDIIHIIGEFE-SGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   465 PPTKAMVTGNILHDFFQHALYRGIDALENVDINLETSIKTYISDIYFADLSLDEIREELDARLPLLKSIVERYLISKKND 544
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALTANDWDLEFLEELLDELLEKYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSPKP 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 429241027   545 NNN--------ESIHISRLLDIEESIWSPRFGLKGNIDATVEV 579
Cdd:pfam08696  161 NAVvedgngkkVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1040-1334 1.33e-64

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 236.56  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1040 QIVACSSLGVYHSI-FNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLF---KL 1115
Cdd:COG1112   536 PVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAEEVAEEGLDEsllDR 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1116 LSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQkklilpkahlsdglpdsssslhwvnKLINPSHSVIF 1195
Cdd:COG1112   616 LLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKAR-------------------------RLADPDSPLVF 670
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1196 FNTDdilGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKS-----FTEIEINTVDRYQ 1270
Cdd:COG1112   671 IDVD---GVYERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREalgdgLEPVFVGTVDRFQ 747
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429241027 1271 GRDKDIILISFVRSNSKNLVGE---LLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLE 1334
Cdd:COG1112   748 GDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKLIVVGSRELLDSDPSTPALKRLLE 814
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1118-1316 1.23e-60

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: 206.25  E-value: 1.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1118 EKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQkklilpkahlsdglpdsssSLHWVNKLINPSHSVIFFN 1197
Cdd:pfam13087   11 ELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAER-------------------PLPDDFHLPDPLGPLVFID 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1198 TDDILGVESKTNNILENHTEAFLIEQAVSSFLERGVKQ-SSIGIISIYKSQVELLSKNLKS----FTEIEINTVDRYQGR 1272
Cdd:pfam13087   72 VDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRklggKLEIEVNTVDGFQGR 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 429241027  1273 DKDIILISFVRSNSKNLVGeLLRDWHRLNVALSRAKVKCIMFGS 1316
Cdd:pfam13087  152 EKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGN 194
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
802-1344 1.40e-57

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: 211.60  E-value: 1.40e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   802 SVGERVFISDEHGHWSLAKGHIVHIQDSCIEVRTRHRLHIPWLKMPNFDFKKNQVFFGNYEDSKLSFigsnhTRYRidkd 881
Cdd:TIGR00376   59 SVGDIVLVSRGNPLQSDLTGVVTRVGKRFITVALEESVPQWSLKRVRIDLYANDVTFKRMKEALRAL-----TENH---- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   882 efSSGIASIRGTLMSSVLPDapliirdmIIRLKPpkfcnsalidpeFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKT 961
Cdd:TIGR00376  130 --SRLLEFLLGREAPSKASE--------IHDFQF------------FDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKT 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   962 TTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHKI---------------HP------------- 1013
Cdd:TIGR00376  188 RTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLlksnkqhsldylienHPkyqivadirekid 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1014 -------------------------LVKEFCLTEGTTFDDLAS----------------LKHFYEDPQIVACSSLGVYHS 1052
Cdd:TIGR00376  268 elieernkktkpspqkrrglsdikiLRKALKKREARGIESLKIasmaewietnksidrlLKLLPESEERIMNEILAESDA 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1053 --------IFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSkdGLSLSLFKLLSEKHPEAV 1124
Cdd:TIGR00376  348 tnsmagseILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEYPERS 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1125 TTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQKKLILPKAHlsdglPDSSsslhwVNKLINPShSVIFFNTDDILGV 1204
Cdd:TIGR00376  426 RTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVE-----ATES-----EDDLETGI-PLLFIDTSGCELF 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1205 ESKTNNILE--NHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLK-SFTEIEINTVDRYQGRDKDIILISF 1281
Cdd:TIGR00376  495 ELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLEhRHIDIEVSSVDGFQGREKEVIIISF 574
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  1282 VRSNSKNLVGeLLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLEKNKWIFTLNE 1344
Cdd:TIGR00376  575 VRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAFK 636
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1133-1334 7.24e-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: 183.59  E-value: 7.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1133 MNEDINSLSSELIYGGNLVCGsktisqkklilpkahlsdglpDSSSSLHWVNKLINPSHSVIFFNTDDILGVESKTNNIL 1212
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAG---------------------VSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKS 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1213 eNHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKS----FTEIEINTVDRYQGRDKDIILISFVRSNSKN 1288
Cdd:cd18808    60 -NEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKrgglLEDVEVGTVDNFQGREKDVIILSLVRSNESG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 429241027 1289 LVGELLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLE 1334
Cdd:cd18808   139 GSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
935-1099 7.74e-22

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: 96.26  E-value: 7.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   935 DQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHL-------AVDNILIKLKGCDST----IV 1003
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGPRILvcapsnaAVDNILERLLRKGQKygpkIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1004 RLGSPHKIHPLVKEFCL----------------------------------------------------TEGTTFDDLAS 1031
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLdylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdksKLEQERRKLRS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1032 LK----------------HFYEDPQIVACSSLGVYHSIFNKR-KFDYCIIDEASQIPLPICLGPLQLA-EKFVLVGDHYQ 1093
Cdd:pfam13086  161 ERkelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGpKKVVLVGDPKQ 240

                   ....*.
gi 429241027  1094 LPPLVK 1099
Cdd:pfam13086  241 LPPTVI 246
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
559-689 1.80e-07

CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas system-associated exonuclease Cas4, RecB family is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 441077 [Multi-domain]  Cd Length: 184  Bit Score: 52.65  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  559 EESIWSPRFGLKGNIDatveVVLTEKPEssstlTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENS 638
Cdd:COG1468    58 EVPLDSERLGLTGKID----LVEFEDGE-----LVPVEYKKSKPKPWEADRMQLCAYALLLEEMLGIPVPKGYLYYPEER 128
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 429241027  639 TIKNlVASNSQLRGLImtRNSLAQ-HNFRRS--LPEMISNRKICDHCSLVSECL 689
Cdd:COG1468   129 KREE-VELTEELREEV--EEAIEEiREILESekPPPPTKSKKKCKKCSYREFCL 179
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
906-1096 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  906 IRDMIIRLKPPKFCNSAL------IDPEFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKIL 979
Cdd:COG0507    93 LARRLRRLARPALDEADVeaalaaLEPRAGITLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  980 LTSFTHLAVDNIliklkgcdstivrlgsphkihplvKEFCLTEGTTfddLASLkhFYEDPQivacSSLGVYHSIFNKRKF 1059
Cdd:COG0507   173 LAAPTGKAAKRL------------------------SESTGIEART---IHRL--LGLRPD----SGRFRHNRDNPLTPA 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 429241027 1060 DYCIIDEASQIPLPI--CLgpLQLAE----KFVLVGDHYQLPP 1096
Cdd:COG0507   220 DLLVVDEASMVDTRLmaAL--LEALPragaRLILVGDPDQLPS 260
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
938-1149 1.79e-05

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 48.99  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   938 TALKKChaaehYSLILGMPGTGKTTTISSLIRSLLAKKKKILL-----TSFT-----HLA--VDNILIKLKGCDSTIVRL 1005
Cdd:TIGR01447  155 LALKSN-----FSLITGGPGTGKTTTVARLLLALVKQSPKQGKlrialAAPTgkaaaRLAesLRKAVKNLAAAEALIAAL 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1006 GSP-HKIHPLVKefcltegttfdDLASLKHFYEDPQivacsslgvyhsifNKRKFDYCIIDEASQIPLPICLGPLQL--- 1081
Cdd:TIGR01447  230 PSEaVTIHRLLG-----------IKPDTKRFRHHER--------------NPLPLDVLVVDEASMVDLPLMAKLLKAlpp 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1082 AEKFVLVGDHYQLPP------LVKNSRTSKDGLSLSLFKLLSEKHPEA------VTTLRLQYRMNED--INSLsSELIYG 1147
Cdd:TIGR01447  285 NTKLILLGDKNQLPSveagavLGDLCELASIGKSILYALCKKINSKTRnplsdnVCFLKTSHRFGKDsgIGQL-AKAINS 363

                   ..
gi 429241027  1148 GN 1149
Cdd:TIGR01447  364 GD 365
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
931-1132 6.43e-93

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: 298.00  E-value: 6.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  931 CLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHK 1010
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1011 IHPLVKEFCLTEG-TTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVG 1089
Cdd:cd18041    81 IHPDVQEFTLEAIlKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 429241027 1090 DHYQLPPLVKNSRTSKDGLSLSLFKLLSEKHPEAVTTLRLQYR 1132
Cdd:cd18041   161 DHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
440-663 6.37e-79

Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease/helicase DNA2 processes double-strand breaks in DNA that have single-stranded ends/overhangs, as well as Okazaki fragments and stalled replication forks; it is therefore crucial for maintaining the integrity of the genome. The nuclease domain modeled here belongs to a superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.


Pssm-ID: 411722 [Multi-domain]  Cd Length: 234  Bit Score: 260.14  E-value: 6.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  440 SATAVASSFPCLRKAVISDRVGIYGPPTKAMVTGNILHDFFQHALYRGIDALENVD--INLETSIKTYISDIYFADLSLD 517
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEklAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  518 EIREELDARLPLLKSIVERYLIS-------KKNDNNNESIHISRLLDIEESIWSPRFGLKGNIDATVEVVLTEKPeSSST 590
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSnspkgqvKLPSDGNSKGAISKILDIEENIWSPRFGLKGKIDATVEVKIHDKG-KSKT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  591 LTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENSTIKNLVASNSQLRGLIMTRNSLAQH 663
Cdd:cd22318   160 KIMPLELKTGRASFSIEHRGQVILYTLMMSDRYDVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAHY 232
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
385-579 1.50e-70

DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded DNA-dependent ATPase, ATP-dependent nuclease, ( 5'-flap endonuclease) and helicase activities. It is required for Okazaki fragment processing and is involved in DNA repair pathways.


Pssm-ID: 462565  Cd Length: 203  Bit Score: 234.76  E-value: 1.50e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   385 EANDILHQLFLRGDWTETSIFVGDSIRVEATFDkDNTAIVDNDKGLIIIHPKILMSATAVASSFPCLRKAVISDRVGIYG 464
Cdd:pfam08696    2 DKSGETRTVILRDDWVETPVEPGDIIHIIGEFE-SGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   465 PPTKAMVTGNILHDFFQHALYRGIDALENVDINLETSIKTYISDIYFADLSLDEIREELDARLPLLKSIVERYLISKKND 544
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALTANDWDLEFLEELLDELLEKYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSPKP 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 429241027   545 NNN--------ESIHISRLLDIEESIWSPRFGLKGNIDATVEV 579
Cdd:pfam08696  161 NAVvedgngkkVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1040-1334 1.33e-64

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 236.56  E-value: 1.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1040 QIVACSSLGVYHSI-FNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKDGLSLSLF---KL 1115
Cdd:COG1112   536 PVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFGEEAEEVAEEGLDEsllDR 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1116 LSEKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQkklilpkahlsdglpdsssslhwvnKLINPSHSVIF 1195
Cdd:COG1112   616 LLARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKAR-------------------------RLADPDSPLVF 670
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1196 FNTDdilGVESKTNNILENHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKS-----FTEIEINTVDRYQ 1270
Cdd:COG1112   671 IDVD---GVYERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREalgdgLEPVFVGTVDRFQ 747
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429241027 1271 GRDKDIILISFVRSNSKNLVGE---LLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLE 1334
Cdd:COG1112   748 GDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKLIVVGSRELLDSDPSTPALKRLLE 814
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1118-1316 1.23e-60

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: 206.25  E-value: 1.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1118 EKHPEAVTTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQkklilpkahlsdglpdsssSLHWVNKLINPSHSVIFFN 1197
Cdd:pfam13087   11 ELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAER-------------------PLPDDFHLPDPLGPLVFID 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1198 TDDILGVESKTNNILENHTEAFLIEQAVSSFLERGVKQ-SSIGIISIYKSQVELLSKNLKS----FTEIEINTVDRYQGR 1272
Cdd:pfam13087   72 VDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRklggKLEIEVNTVDGFQGR 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 429241027  1273 DKDIILISFVRSNSKNLVGeLLRDWHRLNVALSRAKVKCIMFGS 1316
Cdd:pfam13087  152 EKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGN 194
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
802-1344 1.40e-57

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: 211.60  E-value: 1.40e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   802 SVGERVFISDEHGHWSLAKGHIVHIQDSCIEVRTRHRLHIPWLKMPNFDFKKNQVFFGNYEDSKLSFigsnhTRYRidkd 881
Cdd:TIGR00376   59 SVGDIVLVSRGNPLQSDLTGVVTRVGKRFITVALEESVPQWSLKRVRIDLYANDVTFKRMKEALRAL-----TENH---- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   882 efSSGIASIRGTLMSSVLPDapliirdmIIRLKPpkfcnsalidpeFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKT 961
Cdd:TIGR00376  130 --SRLLEFLLGREAPSKASE--------IHDFQF------------FDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKT 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   962 TTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHKI---------------HP------------- 1013
Cdd:TIGR00376  188 RTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLlksnkqhsldylienHPkyqivadirekid 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1014 -------------------------LVKEFCLTEGTTFDDLAS----------------LKHFYEDPQIVACSSLGVYHS 1052
Cdd:TIGR00376  268 elieernkktkpspqkrrglsdikiLRKALKKREARGIESLKIasmaewietnksidrlLKLLPESEERIMNEILAESDA 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1053 --------IFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSkdGLSLSLFKLLSEKHPEAV 1124
Cdd:TIGR00376  348 tnsmagseILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEYPERS 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1125 TTLRLQYRMNEDINSLSSELIYGGNLVCGSKTISQKKLILPKAHlsdglPDSSsslhwVNKLINPShSVIFFNTDDILGV 1204
Cdd:TIGR00376  426 RTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVE-----ATES-----EDDLETGI-PLLFIDTSGCELF 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1205 ESKTNNILE--NHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLK-SFTEIEINTVDRYQGRDKDIILISF 1281
Cdd:TIGR00376  495 ELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQLLEhRHIDIEVSSVDGFQGREKEVIIISF 574
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  1282 VRSNSKNLVGeLLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLEKNKWIFTLNE 1344
Cdd:TIGR00376  575 VRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEVREAFK 636
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1133-1334 7.24e-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: 183.59  E-value: 7.24e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1133 MNEDINSLSSELIYGGNLVCGsktisqkklilpkahlsdglpDSSSSLHWVNKLINPSHSVIFFNTDDILGVESKTNNIL 1212
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAG---------------------VSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKS 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1213 eNHTEAFLIEQAVSSFLERGVKQSSIGIISIYKSQVELLSKNLKS----FTEIEINTVDRYQGRDKDIILISFVRSNSKN 1288
Cdd:cd18808    60 -NEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKrgglLEDVEVGTVDNFQGREKDVIILSLVRSNESG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 429241027 1289 LVGELLRDWHRLNVALSRAKVKCIMFGSLSTLSSSNIVSHLLKLLE 1334
Cdd:cd18808   139 GSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
931-1132 6.51e-31

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: 120.79  E-value: 6.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  931 CLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKLKGCDSTIVRLGSPHK 1010
Cdd:cd18044     1 NLNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1011 IHPLVKEFCLtegttfDDLASlkhfyedPQIVACSSLGVYHSIF-NKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVG 1089
Cdd:cd18044    81 LLESVLDHSL------DALVA-------AQVVLATNTGAGSRQLlPNELFDVVVIDEAAQALEASCWIPLLKARRCILAG 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 429241027 1090 DHYQLPPLVKNSRTSKDGLSLSLFKLLSEKH-PEAVTTLRLQYR 1132
Cdd:cd18044   148 DHKQLPPTILSDKAARGGLGVTLFERLVNLYgESVVRMLTVQYR 191
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
949-1132 8.44e-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: 94.99  E-value: 8.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  949 YSLILGMPGTGKTTTISSLIRSLLAKKKKIL--LTSFTHLAVDNIliklkgcdstivrlgsphkihplvkefcltegttf 1026
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKRvlVTAQSNVAVDNV----------------------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1027 ddlaslkhfyedpqivacsslgvyhsifnkrkfDYCIIDEASQIPLPICLGPLQLAEKFVLVGDHYQLPPLVKNSRTSKD 1106
Cdd:cd17934    46 ---------------------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAALL 92
                         170       180
                  ....*....|....*....|....*....
gi 429241027 1107 GLSLSLFKLLSEKH---PEAVTTLRLQYR 1132
Cdd:cd17934    93 GLSFILSLLLLFRLllpGSPKVMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
935-1099 7.74e-22

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: 96.26  E-value: 7.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   935 DQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHL-------AVDNILIKLKGCDST----IV 1003
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATSAAAGPRILvcapsnaAVDNILERLLRKGQKygpkIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1004 RLGSPHKIHPLVKEFCL----------------------------------------------------TEGTTFDDLAS 1031
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLdylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdksKLEQERRKLRS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1032 LK----------------HFYEDPQIVACSSLGVYHSIFNKR-KFDYCIIDEASQIPLPICLGPLQLA-EKFVLVGDHYQ 1093
Cdd:pfam13086  161 ERkelrkelrrreqslerEILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGpKKVVLVGDPKQ 240

                   ....*.
gi 429241027  1094 LPPLVK 1099
Cdd:pfam13086  241 LPPTVI 246
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
932-1105 3.02e-19

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: 88.04  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  932 LNEDQITALKKC-HAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHL------------------------ 986
Cdd:cd18042     1 LNESQLEAIASAlQNSPGITLIQGPPGTGKTKTIVGILSVLLAGKYRKYYEKVKKKlrklqrnlnnkkkknrilvcapsn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  987 -AVDNILIKL----------KGCDSTIVRLGSphkihplvKEFCltegttfddlaslKHFYEDPQIVACSSLGVYHSIFN 1055
Cdd:cd18042    81 aAVDEIVLRLlsegfldgdgRSYKPNVVRVGR--------QELR-------------ASILNEADIVCTTLSSSGSDLLE 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 429241027 1056 K--RKFDYCIIDEASQIPLPICLGPLQL-AEKFVLVGDHYQLPPLVKNSRTSK 1105
Cdd:cd18042   140 SlpRGFDTVIIDEAAQAVELSTLIPLRLgCKRLILVGDPKQLPATVFSKVAQK 192
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
932-1107 1.03e-15

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: 78.06  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  932 LNEDQITALKkcHAAEH-YSLILGMPGTGKTTTISSLIRSLLAKKKKILL-TSFTHLAVDNILIKLKGCDSTIVRLGSPH 1009
Cdd:cd18039     2 LNHSQVDAVK--TALQRpLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLvCAPSNVAVDQLTEKIHQTGLKVVRLCAKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1010 K-----------IHPLVKEFCLTEGTTFDDL----------ASLKHFY-----------EDPQIVACSSLGVYHSIFNKR 1057
Cdd:cd18039    80 ReavespvsflaLHNQVRNLDSAEKLELLKLlkletgelssADEKRYRklkrkaerellRNADVICCTCVGAGDPRLSKM 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 429241027 1058 KFDYCIIDEASQIPLPICLGPLQL-AEKFVLVGDHYQLPPLVKNSRTSKDG 1107
Cdd:cd18039   160 KFRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAG 210
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
933-1098 2.09e-12

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: 65.30  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  933 NEDQITALKKchAAEHYSLIL-GMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDNILIKlkgcdstiVRLGSPHKI 1011
Cdd:cd18043     1 DSSQEAAIIS--ARNGKNVVIqGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVRFP--------CWIMSPLSV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1012 HPLVKefcltegttfddlaslkhfyedpqivacsslgvyhsiFNKRKFDYCIIDEASQIPLPICLGPLQLAEKFVLVGDH 1091
Cdd:cd18043    71 SQYLP-------------------------------------LNRNLFDLVIFDEASQIPIEEALPALFRGKQVVVVGDD 113

                  ....*..
gi 429241027 1092 YQLPPLV 1098
Cdd:cd18043   114 KQLPPSI 120
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
932-1102 4.60e-10

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: 61.48  E-value: 4.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  932 LNEDQITALKkcHAAEHYS-----LILGMPGTGKTTTISSLIRSLLAKKKKIL--LTSFTHLAVDNI---LIKLKGCDST 1001
Cdd:cd18038     2 LNDEQKLAVR--NIVTGTSrpppyIIFGPPGTGKTVTLVEAILQVLRQPPEARilVCAPSNSAADLLaerLLNALVTKRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1002 IVRLGSPHK----IHPLVKEFCLTEGTTFDDLASLKHFYEDPQIVA-CSSLGVYHSIFNKRK-FDYCIIDEASQIPLPIC 1075
Cdd:cd18038    80 ILRLNAPSRdrasVPPELLPYCNSKAEGTFRLPSLEELKKYRIVVCtLMTAGRLVQAGVPNGhFTHIFIDEAGQATEPEA 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 429241027 1076 LGPL-QLAEK---FVLVGDHYQLPPLVKNSR 1102
Cdd:cd18038   160 LIPLsELASKntqIVLAGDPKQLGPVVRSPL 190
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
1238-1315 1.32e-08

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: 53.60  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1238 IGIISIYKSQVE-------LLSKNLKSFTEIEINTVDRYQGRDKDIILISFVRSNSknlvgellRDWHRLNVALSRAKVK 1310
Cdd:cd18786    13 GVVLTPYHRDRAylnqylqGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANS--------LTPRRLYVALTRARKR 84

                  ....*
gi 429241027 1311 CIMFG 1315
Cdd:cd18786    85 LVIYD 89
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
935-1096 1.70e-08

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: 54.87  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  935 DQITALKKChAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKILLTSFTHLAVDniliklkgcdstivRLGsphkihpl 1014
Cdd:cd17933     1 EQKAAVRLV-LRNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAK--------------RLS-------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1015 vkEFCLTEGTTfddLASLKHFYEDPQivacsslGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAE---KFVLVGDH 1091
Cdd:cd17933    58 --ESTGIEAST---IHRLLGINPGGG-------GFYYNEENPLDADLLIVDEASMVDTRLMAALLSAIPagaRLILVGDP 125

                  ....*
gi 429241027 1092 YQLPP 1096
Cdd:cd17933   126 DQLPS 130
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
932-1100 6.39e-08

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: 54.09  E-value: 6.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  932 LNEDQITALKkcHAAEH-YSLILGMPGTGKTTTISSLIRSLLAKKKKILLT-----SFTHLAVDNILIKLKGCDST-IVR 1004
Cdd:cd17936     2 LDPSQLEALK--HALTSeLALIQGPPGTGKTFLGVKLVRALLQNQDLSITGpilvvCYTNHALDQFLEGLLDFGPTkIVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1005 LGSphkihplvkefcltegttfddlaslkhfyedpQIVACSSLGV--YHSIFNKRKFDYCIIDEASQIPLP---ICLGPl 1079
Cdd:cd17936    80 LGA--------------------------------RVIGMTTTGAakYRELLQALGPKVVIVEEAAEVLEAhilAALTP- 126
                         170       180
                  ....*....|....*....|.
gi 429241027 1080 qLAEKFVLVGDHYQLPPLVKN 1100
Cdd:cd17936   127 -STEHLILIGDHKQLRPKVNV 146
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
931-1104 1.03e-07

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: 54.30  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  931 CLNEDQITALKKCHAAEHYSL---ILGMPGTGKTTTIsslIRSLLAKKKKILLTSF-----THLAVDNILIKLKgcDSTI 1002
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLpyiLFGPPGTGKTVTI---IEAILQVVYNLPRSRIlvcapSNSAADLVTSRLH--ESKV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1003 VRLGSPHKihplVKEFCLTEGTTFDDLASLKHFYEDPQ--------IVACSSLGVYHSI-FNKRKFDYCIIDEASQIPLP 1073
Cdd:cd18078    76 LKPGDMVR----LNAVNRFESTVIDARKLYCRLGEDLSkasrhrivISTCSTAGLLYQMgLPVGHFTHVFVDEAGQATEP 151
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 429241027 1074 ICLGPLQLAEK----FVLVGDHYQLPPLVKnSRTS 1104
Cdd:cd18078   152 ESLIPLGLISSrdgqIILAGDPMQLGPVIK-SRLA 185
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
559-689 1.80e-07

CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas system-associated exonuclease Cas4, RecB family is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 441077 [Multi-domain]  Cd Length: 184  Bit Score: 52.65  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  559 EESIWSPRFGLKGNIDatveVVLTEKPEssstlTLPLELKTGRYVDNISHFAQSLLYTLLISDRYGINTNQALLCYLENS 638
Cdd:COG1468    58 EVPLDSERLGLTGKID----LVEFEDGE-----LVPVEYKKSKPKPWEADRMQLCAYALLLEEMLGIPVPKGYLYYPEER 128
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 429241027  639 TIKNlVASNSQLRGLImtRNSLAQ-HNFRRS--LPEMISNRKICDHCSLVSECL 689
Cdd:COG1468   129 KREE-VELTEELREEV--EEAIEEiREILESekPPPPTKSKKKCKKCSYREFCL 179
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
906-1096 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  906 IRDMIIRLKPPKFCNSAL------IDPEFLKCLNEDQITALKKCHAAEHYSLILGMPGTGKTTTISSLIRSLLAKKKKIL 979
Cdd:COG0507    93 LARRLRRLARPALDEADVeaalaaLEPRAGITLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  980 LTSFTHLAVDNIliklkgcdstivrlgsphkihplvKEFCLTEGTTfddLASLkhFYEDPQivacSSLGVYHSIFNKRKF 1059
Cdd:COG0507   173 LAAPTGKAAKRL------------------------SESTGIEART---IHRL--LGLRPD----SGRFRHNRDNPLTPA 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 429241027 1060 DYCIIDEASQIPLPI--CLgpLQLAE----KFVLVGDHYQLPP 1096
Cdd:COG0507   220 DLLVVDEASMVDTRLmaAL--LEALPragaRLILVGDPDQLPS 260
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
1062-1132 5.57e-07

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: 52.91  E-value: 5.57e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429241027 1062 CIIDEASQIPLPICLGPL---QLAEKFVLVGDHYQLPPLVKNSRTSKDGlslsLFKLLSEKHPEAVTTLRLQYR 1132
Cdd:cd18040   202 CIVDECGMCTEPESLIPIvsaPRAEQVVLIGDHKQLRPVVQNKEAQKLG----LGRSLFERYAEKACMLDTQYR 271
Cas4_I-A_I-B_I-C_I-D_II-B cd09637
CRISPR/Cas system-associated protein Cas4; CRISPR (Clustered Regularly Interspaced Short ...
558-689 9.70e-06

CRISPR/Cas system-associated protein Cas4; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas4 is RecB-like nuclease with three-cysteine C-terminal cluster


Pssm-ID: 187768 [Multi-domain]  Cd Length: 178  Bit Score: 47.43  E-value: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  558 IEESIW--SPRFGLKGNIDATVEVVLTEkpessstltLPLELKTGRYVDNISHF-AQSLLYTLLISDRYGINTNQALLCY 634
Cdd:cd09637    54 EEKEVPlkSKKYGLKGVIDIVLKEDGEL---------VPVEVKSGRAGSPREAHkLQLVAYAYLLEEMYGKRVARGYIVY 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 429241027  635 LENSTIKNLVASNSQLRGLIMTR---NSLAQHNFrrsLPEMISNRKiCDHCSLVSECL 689
Cdd:cd09637   125 LEGGKRLEVEISEELRKKAEKLLeeiRKLLEGEL---PPPVKSSPK-CKFCPYREICL 178
AAA_19 pfam13245
AAA domain;
950-1096 1.40e-05

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 46.06  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   950 SLILGMPGTGKTTTISSLIRSLLAKKKKILLT---SFTHLAVDNILIKLKGCDSTIvrlgsphkiHPLVkefcltegtTF 1026
Cdd:pfam13245   14 VLLTGGPGTGKTTTIRHIVALLVALGGVSFPIllaAPTGRAAKRLSERTGLPASTI---------HRLL---------GF 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429241027  1027 DDLASLKhFYEDPQivacsslgvyhsifNKRKFDYCIIDEASQIPLPIC---LGPLQLAEKFVLVGDHYQLPP 1096
Cdd:pfam13245   76 DDLEAGG-FLRDEE--------------EPLDGDLLIVDEFSMVDLPLAyrlLKALPDGAQLLLVGDPDQLPS 133
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
938-1149 1.79e-05

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 48.99  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027   938 TALKKChaaehYSLILGMPGTGKTTTISSLIRSLLAKKKKILL-----TSFT-----HLA--VDNILIKLKGCDSTIVRL 1005
Cdd:TIGR01447  155 LALKSN-----FSLITGGPGTGKTTTVARLLLALVKQSPKQGKlrialAAPTgkaaaRLAesLRKAVKNLAAAEALIAAL 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1006 GSP-HKIHPLVKefcltegttfdDLASLKHFYEDPQivacsslgvyhsifNKRKFDYCIIDEASQIPLPICLGPLQL--- 1081
Cdd:TIGR01447  230 PSEaVTIHRLLG-----------IKPDTKRFRHHER--------------NPLPLDVLVVDEASMVDLPLMAKLLKAlpp 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  1082 AEKFVLVGDHYQLPP------LVKNSRTSKDGLSLSLFKLLSEKHPEA------VTTLRLQYRMNED--INSLsSELIYG 1147
Cdd:TIGR01447  285 NTKLILLGDKNQLPSveagavLGDLCELASIGKSILYALCKKINSKTRnplsdnVCFLKTSHRFGKDsgIGQL-AKAINS 363

                   ..
gi 429241027  1148 GN 1149
Cdd:TIGR01447  364 GD 365
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
1023-1107 3.57e-04

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: 41.70  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1023 GTTFDDLASLKHFYEDPQIVACSSLGVYHSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEKF---VLVGDHYQLPPLVK 1099
Cdd:cd17914    11 GKTRVLVKIVAALMQNKNGEPGRILLVTPTNKAAAQLDNILVDEAAQILEPETSRLIDLALDQgrvILVGDHDQLGPVWR 90

                  ....*...
gi 429241027 1100 NSRTSKDG 1107
Cdd:cd17914    91 GAVLAKIC 98
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
1058-1100 5.91e-04

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: 42.80  E-value: 5.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 429241027 1058 KFDYCIIDEASQI-------PLPICL---GPLQLaEKFVLVGDHYQLPPLVKN 1100
Cdd:cd17935   110 KYDNILMEEAAQIleietfiPLLLQNpedGPNRL-KRLIMIGDHHQLPPVIKN 161
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
951-1098 9.97e-03

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: 39.39  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027  951 LILGMPGTGKTTTISS-------------LIRSLLAKKKKILLTSFTHLAVDNILIKLKGCdSTIVRLGSPHKIHPLVKE 1017
Cdd:cd18077    25 LLIGPFGTGKTFTLAQavkhilqqpetriLICTHSNSAADLYIKEYLHPYVETGNPRARPL-RVYYRNRWVKTVHPVVQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429241027 1018 FCLT-EGTTFDDLASlkhfyEDPQ----IVACSSLGVY--HSIFNKRKFDYCIIDEASQIPLPICLGPLQLAEK---FVL 1087
Cdd:cd18077   104 YCLIdEHGTFRMPTR-----EDVMrhrvVVVTLSTSQYlcQLDLEPGFFTHILLDEAAQAMECEAIMPLALATKstrIVL 178
                         170
                  ....*....|.
gi 429241027 1088 VGDHYQLPPLV 1098
Cdd:cd18077   179 AGDHMQLSPEV 189
 
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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