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Conserved domains on  [gi|578819047|ref|XP_006717743|]
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DNA replication ATP-dependent helicase/nuclease DNA2 isoform X1 [Homo sapiens]

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 ...
655-858 3.89e-121

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: 370.03  E-value: 3.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  655 GLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQK 734
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  735 VHPAIQQFTEQEIcrSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVL 814
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578819047  815 VGDHQQLPPLVLNREARALGMSESLFKRLEQNK-SAVVQLTVQYR 858
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
156-395 2.38e-110

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: 342.58  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  156 SGTSIASSIRCMRRAVLSETFRSSDPATRQMLIGTVLHEVFQKAI-NNSFAPEKLQELAFQTIQEIRHLKEMYRLNLSQD 234
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALkNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  235 EIKQEVEDYLPSFCKWAGDFMHKNTstdfPQMQLSLPSDNskdnsTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGVKI 314
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDG-----NSKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  315 HRGYKTKYKIMPLELKTGKESNSIEHRSQVVLYTLLSQERR-ADPEAGLLLYLKTGQMYPVPANHLDKRELLKLRNQMAF 393
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 578819047  394 SL 395
Cdd:cd22318   232 YL 233
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
501-1062 2.06e-70

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: 247.81  E-value: 2.06e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   501 EMEKSGSCIGNLirmeHVKIVCD--GQYLHNFQCKHG---AIPVtnlmaGDRVIVSgEERSLFALSRGYVKEINMTTVTC 575
Cdd:TIGR00376   21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAiatEISV-----GDIVLVS-RGNPLQSDLTGVVTRVGKRFITV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   576 LLDrnlSVLPESTL--FRLDQEEKNCDIDTPLGNLSKLMENtfvSKKLRDLIIDFREPQFISYLSSVLPHDakdtvacil 653
Cdd:TIGR00376   91 ALE---ESVPQWSLkrVRIDLYANDVTFKRMKEALRALTEN---HSRLLEFLLGREAPSKASEIHDFQFFD--------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   654 KGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQ 733
Cdd:TIGR00376  156 PNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   734 KVHPAIQQFT-------------------------------------------EQEICR------------SKSIKSLA- 757
Cdd:TIGR00376  236 RLLKSNKQHSldylienhpkyqivadirekidelieernkktkpspqkrrglsDIKILRkalkkreargieSLKIASMAe 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   758 ----------LLEELYNSQLIVA--------TTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQ 819
Cdd:TIGR00376  316 wietnksidrLLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   820 QLPPLVLNREARalGMSESLFKRLEQNKSAVVQ-LTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLrhfkdVKL 898
Cdd:TIGR00376  396 QLPPTILSHDAE--ELSLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDL-----PKV 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   899 ELEFYADYSDNPwlmgvfepnNPVCFLNTDKVPAPEQVEKGGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQ 976
Cdd:TIGR00376  469 EATESEDDLETG---------IPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQ 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   977 LKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPL 1056
Cdd:TIGR00376  540 VDLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFY 618

                   ....*.
gi 578819047  1057 EKLLNH 1062
Cdd:TIGR00376  619 KRLIEW 624
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
655-858 3.89e-121

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: 370.03  E-value: 3.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  655 GLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQK 734
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  735 VHPAIQQFTEQEIcrSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVL 814
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578819047  815 VGDHQQLPPLVLNREARALGMSESLFKRLEQNK-SAVVQLTVQYR 858
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
156-395 2.38e-110

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: 342.58  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  156 SGTSIASSIRCMRRAVLSETFRSSDPATRQMLIGTVLHEVFQKAI-NNSFAPEKLQELAFQTIQEIRHLKEMYRLNLSQD 234
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALkNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  235 EIKQEVEDYLPSFCKWAGDFMHKNTstdfPQMQLSLPSDNskdnsTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGVKI 314
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDG-----NSKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  315 HRGYKTKYKIMPLELKTGKESNSIEHRSQVVLYTLLSQERR-ADPEAGLLLYLKTGQMYPVPANHLDKRELLKLRNQMAF 393
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 578819047  394 SL 395
Cdd:cd22318   232 YL 233
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
101-312 4.16e-84

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: 270.97  E-value: 4.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   101 SQSLENKELCILRNDWCSVPVEPGDIIHLEGDCTSDTWIIDKDFGYLILYPDMLISGTSIASSIRCMRRAVLSETFRSSD 180
Cdd:pfam08696    1 SDKSGETRTVILRDDWVETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   181 PATRQMLIGTVLHEVFQKAI-NNSFAPEKLQELAFQTIQeiRHLKEMYRLNLSQDEIKQEVEDYLPSFCKWAGDFMHKNT 259
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALtANDWDLEFLEELLDELLE--KYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSP 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578819047   260 STDFPQMQLSlpsdnskdNSTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGV 312
Cdd:pfam08696  159 KPNAVVEDGN--------GKKVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
501-1062 2.06e-70

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: 247.81  E-value: 2.06e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   501 EMEKSGSCIGNLirmeHVKIVCD--GQYLHNFQCKHG---AIPVtnlmaGDRVIVSgEERSLFALSRGYVKEINMTTVTC 575
Cdd:TIGR00376   21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAiatEISV-----GDIVLVS-RGNPLQSDLTGVVTRVGKRFITV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   576 LLDrnlSVLPESTL--FRLDQEEKNCDIDTPLGNLSKLMENtfvSKKLRDLIIDFREPQFISYLSSVLPHDakdtvacil 653
Cdd:TIGR00376   91 ALE---ESVPQWSLkrVRIDLYANDVTFKRMKEALRALTEN---HSRLLEFLLGREAPSKASEIHDFQFFD--------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   654 KGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQ 733
Cdd:TIGR00376  156 PNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   734 KVHPAIQQFT-------------------------------------------EQEICR------------SKSIKSLA- 757
Cdd:TIGR00376  236 RLLKSNKQHSldylienhpkyqivadirekidelieernkktkpspqkrrglsDIKILRkalkkreargieSLKIASMAe 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   758 ----------LLEELYNSQLIVA--------TTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQ 819
Cdd:TIGR00376  316 wietnksidrLLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   820 QLPPLVLNREARalGMSESLFKRLEQNKSAVVQ-LTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLrhfkdVKL 898
Cdd:TIGR00376  396 QLPPTILSHDAE--ELSLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDL-----PKV 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   899 ELEFYADYSDNPwlmgvfepnNPVCFLNTDKVPAPEQVEKGGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQ 976
Cdd:TIGR00376  469 EATESEDDLETG---------IPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQ 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   977 LKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPL 1056
Cdd:TIGR00376  540 VDLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFY 618

                   ....*.
gi 578819047  1057 EKLLNH 1062
Cdd:TIGR00376  619 KRLIEW 624
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
835-1047 1.21e-69

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: 230.90  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   835 MSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDkvanaVINLRhfkdvklelefyadysdNPWLM 913
Cdd:pfam13087    1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS-----VAERP-----------------LPDDF 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   914 GVFEPNNPVCFLNTDKVPAPEQVEKGGVSNVTEAKLIVFLTSIFVKAGCSP-SDIGIIAPYRQQLKIINDLLARS---IG 989
Cdd:pfam13087   59 HLPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKlggKL 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578819047   990 MVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCV 1047
Cdd:pfam13087  139 EIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
734-1066 5.21e-65

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 236.18  E-value: 5.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  734 KVHPAIQQFTEQEICRSKSIKSLALlEELYNSQLIVATTCMGI-NHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRF 812
Cdd:COG1112   504 REAARLRRALRRELKKRRELRKLLW-DALLELAPVVGMTPASVaRLLPLGEGSFDLVIIDEASQATLAEALGALARAKRV 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  813 VLVGDHQQLPPLVLNREA---RALGMSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLecgsdkvanavI 888
Cdd:COG1112   583 VLVGDPKQLPPVVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKL-----------V 651
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  889 NLRHFKDVKLElefyadysdnpwlmgvfEPNNPVCFLNTDKVPAPEQvekGGVSNVTEAKLIVFLTSIFVKAGCSPSDIG 968
Cdd:COG1112   652 PLPSPKARRLA-----------------DPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIG 711
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  969 IIAPYRQQLKIINDLLARSIGM----VEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGE---LLKDWRRLNVAITRAKHKL 1041
Cdd:COG1112   712 VITPYRAQVALIRELLREALGDglepVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKL 791
                         330       340
                  ....*....|....*....|....*...
gi 578819047 1042 ILLGCVP---SLNCYPPLEKLLNHLNSE 1066
Cdd:COG1112   792 IVVGSRElldSDPSTPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
859-1063 5.86e-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: 186.29  E-value: 5.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  859 MNSKIMSLSNKLTYEGKLECGSDKvanavinlrhfkdvklelefyadySDNPWLMGVFEPNNPVCFLNTDKvpaPEQVEK 938
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSV------------------------AARLNPPPLPGPSKPLVFVDVSG---GEEREE 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  939 GGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLARSIGM---VEVNTVDKYQGRDKSIVLVSFVR 1013
Cdd:cd18808    54 SGTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGGLledVEVGTVDNFQGREKDVIILSLVR 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578819047 1014 SNKDGTVGELLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPLEKLLNHL 1063
Cdd:cd18808   134 SNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
659-828 8.57e-27

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: 110.51  E-value: 8.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   659 PQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFS-------VLLTSYTHSAVDNILLKLA----KFKIGFL 727
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLrkgqKYGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   728 RLGQIQKVHPAIQQFTEQEICRSKS-------------------IKSLALLEELYNSQL--------------------- 767
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLDYLVESKLnneedaqivkdiskeleklAKALRAFEKEIIVEKllksrnkdkskleqerrklrs 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   768 -------------------------IVATTCMGINHPIFSR-KIFDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQ 820
Cdd:pfam13086  161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240

                   ....*...
gi 578819047   821 LPPLVLNR 828
Cdd:pfam13086  241 LPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
656-870 2.42e-11

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: 67.69  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkv 735
Cdd:COG0507   125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  736 hpaiqqftEQEICR-SKSIKSlaLLEELYNSQLIVAttcmGINHPIFSRKIFdfcIVDEASQISQPIclgplfFSR---- 810
Cdd:COG0507   185 --------SESTGIeARTIHR--LLGLRPDSGRFRH----NRDNPLTPADLL---VVDEASMVDTRL------MAAllea 241
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578819047  811 ------RFVLVGDHQQLPPlVlnrEA-RALGMseslfkRLEQNKSAVVQLTVQYRM--NSKIMSLSNKL 870
Cdd:COG0507   242 lpragaRLILVGDPDQLPS-V---GAgAVLRD------LIESGTVPVVELTEVYRQadDSRIIELAHAI 300
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
291-427 2.70e-09

CRISPR-associated protein Cas4; This model represents a family of proteins associated with CRISPR repeats in a wide set of prokaryotic genomes. This scope of this model has been broadened since it was first built to describe an archaeal subset only. The function of the protein is undefined. Distantly related proteins, excluded from this model, include ORFs from Mycobacteriophage D29 and Sulfolobus islandicus filamentous virus and a region of the Schizosaccharomyces pombe DNA replication helicase Dna2p.


Pssm-ID: 273040 [Multi-domain]  Cd Length: 178  Bit Score: 57.80  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   291 IEESIW--SPRFGLKGKIDVtvgVKIHRGYKTkykimPLELKTGKESNSIEHRSQVVLYTLLSQERRADPEAGLLLYLKT 368
Cdd:TIGR00372   54 EEKEVPlkSKKYGLKGVIDI---VLEEDGELV-----PVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILYINA 125
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578819047   369 GQMYPVPANHLDKRELLKLRNQMafslfhrisksatRQKTQLASLPQIIEEEKTCKYCS 427
Cdd:TIGR00372  126 GKKLEVEISEELRKKAVKLIEKI-------------RELLEGGKPPSPPKSGPKCKFCP 171
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
292-427 3.99e-09

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: 57.28  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  292 EESIWSPRFGLKGKIDVtvgVKIHRGyktkyKIMPLELKTGKESNSIEHRSQVVLYTL-LSQERRADPEAGLLLYLKTGQ 370
Cdd:COG1468    58 EVPLDSERLGLTGKIDL---VEFEDG-----ELVPVEYKKSKPKPWEADRMQLCAYALlLEEMLGIPVPKGYLYYPEERK 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578819047  371 MYPVPANHLDKRELLKLRNQMafslfHRISKSATrqktqlasLPQIIEEEKTCKYCS 427
Cdd:COG1468   130 REEVELTEELREEVEEAIEEI-----REILESEK--------PPPPTKSKKKCKKCS 173
DEXDc smart00487
DEAD-like helicases superfamily;
656-794 7.30e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 42.09  E-value: 7.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047    656 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILYACGFSVLLTSYTHSAVDNILLKLAKFkigflrlgqiq 733
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL----------- 77
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578819047    734 kvhpaIQQFTEQEICRSKSIKSLALLEELYNS--QLIVATTCMGINHPI---FSRKIFDFCIVDEA 794
Cdd:smart00487   78 -----GPSLGLKVVGLYGGDSKREQLRKLESGktDILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
613-704 7.50e-03

signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 39.55  E-value: 7.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   613 ENTFVSKKLRDLIIDfrepqfiSYLSSVLPHDAKDTVACILKGLNKPQrqamkkVLLskdytlIVGMPGTGKTTTICTLV 692
Cdd:TIGR00064   38 KKVKDAEKLKEILKE-------YLKEILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
                           90
                   ....*....|..
gi 578819047   693 RILYACGFSVLL 704
Cdd:TIGR00064   99 NKLKKQGKSVLL 110
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
655-858 3.89e-121

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: 370.03  E-value: 3.89e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  655 GLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQK 734
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  735 VHPAIQQFTEQEIcrSKSIKSLALLEELYNSQLIVATTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVL 814
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578819047  815 VGDHQQLPPLVLNREARALGMSESLFKRLEQNK-SAVVQLTVQYR 858
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
156-395 2.38e-110

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: 342.58  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  156 SGTSIASSIRCMRRAVLSETFRSSDPATRQMLIGTVLHEVFQKAI-NNSFAPEKLQELAFQTIQEIRHLKEMYRLNLSQD 234
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALkNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  235 EIKQEVEDYLPSFCKWAGDFMHKNTstdfPQMQLSLPSDNskdnsTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGVKI 314
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDG-----NSKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  315 HRGYKTKYKIMPLELKTGKESNSIEHRSQVVLYTLLSQERR-ADPEAGLLLYLKTGQMYPVPANHLDKRELLKLRNQMAF 393
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 578819047  394 SL 395
Cdd:cd22318   232 YL 233
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
101-312 4.16e-84

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: 270.97  E-value: 4.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   101 SQSLENKELCILRNDWCSVPVEPGDIIHLEGDCTSDTWIIDKDFGYLILYPDMLISGTSIASSIRCMRRAVLSETFRSSD 180
Cdd:pfam08696    1 SDKSGETRTVILRDDWVETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   181 PATRQMLIGTVLHEVFQKAI-NNSFAPEKLQELAFQTIQeiRHLKEMYRLNLSQDEIKQEVEDYLPSFCKWAGDFMHKNT 259
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALtANDWDLEFLEELLDELLE--KYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSP 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578819047   260 STDFPQMQLSlpsdnskdNSTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGV 312
Cdd:pfam08696  159 KPNAVVEDGN--------GKKVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
501-1062 2.06e-70

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: 247.81  E-value: 2.06e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   501 EMEKSGSCIGNLirmeHVKIVCD--GQYLHNFQCKHG---AIPVtnlmaGDRVIVSgEERSLFALSRGYVKEINMTTVTC 575
Cdd:TIGR00376   21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAiatEISV-----GDIVLVS-RGNPLQSDLTGVVTRVGKRFITV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   576 LLDrnlSVLPESTL--FRLDQEEKNCDIDTPLGNLSKLMENtfvSKKLRDLIIDFREPQFISYLSSVLPHDakdtvacil 653
Cdd:TIGR00376   91 ALE---ESVPQWSLkrVRIDLYANDVTFKRMKEALRALTEN---HSRLLEFLLGREAPSKASEIHDFQFFD--------- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   654 KGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQ 733
Cdd:TIGR00376  156 PNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   734 KVHPAIQQFT-------------------------------------------EQEICR------------SKSIKSLA- 757
Cdd:TIGR00376  236 RLLKSNKQHSldylienhpkyqivadirekidelieernkktkpspqkrrglsDIKILRkalkkreargieSLKIASMAe 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   758 ----------LLEELYNSQLIVA--------TTCMGINHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQ 819
Cdd:TIGR00376  316 wietnksidrLLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   820 QLPPLVLNREARalGMSESLFKRLEQNKSAVVQ-LTVQYRMNSKIMSLSNKLTYEGKLECGSDKVANAVINLrhfkdVKL 898
Cdd:TIGR00376  396 QLPPTILSHDAE--ELSLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDL-----PKV 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   899 ELEFYADYSDNPwlmgvfepnNPVCFLNTDKVPAPEQVEKGGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQ 976
Cdd:TIGR00376  469 EATESEDDLETG---------IPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQ 539
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   977 LKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPL 1056
Cdd:TIGR00376  540 VDLLRQLLEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFY 618

                   ....*.
gi 578819047  1057 EKLLNH 1062
Cdd:TIGR00376  619 KRLIEW 624
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
835-1047 1.21e-69

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: 230.90  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   835 MSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLECGSDkvanaVINLRhfkdvklelefyadysdNPWLM 913
Cdd:pfam13087    1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS-----VAERP-----------------LPDDF 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   914 GVFEPNNPVCFLNTDKVPAPEQVEKGGVSNVTEAKLIVFLTSIFVKAGCSP-SDIGIIAPYRQQLKIINDLLARS---IG 989
Cdd:pfam13087   59 HLPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKlggKL 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578819047   990 MVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGeLLKDWRRLNVAITRAKHKLILLGCV 1047
Cdd:pfam13087  139 EIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
734-1066 5.21e-65

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 236.18  E-value: 5.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  734 KVHPAIQQFTEQEICRSKSIKSLALlEELYNSQLIVATTCMGI-NHPIFSRKIFDFCIVDEASQISQPICLGPLFFSRRF 812
Cdd:COG1112   504 REAARLRRALRRELKKRRELRKLLW-DALLELAPVVGMTPASVaRLLPLGEGSFDLVIIDEASQATLAEALGALARAKRV 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  813 VLVGDHQQLPPLVLNREA---RALGMSESLFKRL-EQNKSAVVQLTVQYRMNSKIMSLSNKLTYEGKLecgsdkvanavI 888
Cdd:COG1112   583 VLVGDPKQLPPVVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKL-----------V 651
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  889 NLRHFKDVKLElefyadysdnpwlmgvfEPNNPVCFLNTDKVPAPEQvekGGVSNVTEAKLIVFLTSIFVKAGCSPSDIG 968
Cdd:COG1112   652 PLPSPKARRLA-----------------DPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIG 711
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  969 IIAPYRQQLKIINDLLARSIGM----VEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGE---LLKDWRRLNVAITRAKHKL 1041
Cdd:COG1112   712 VITPYRAQVALIRELLREALGDglepVFVGTVDRFQGDERDVIIFSLVYSNDEDVPRNfgfLNGGPRRLNVAVSRARRKL 791
                         330       340
                  ....*....|....*....|....*...
gi 578819047 1042 ILLGCVP---SLNCYPPLEKLLNHLNSE 1066
Cdd:COG1112   792 IVVGSRElldSDPSTPALKRLLEYLERA 819
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
859-1063 5.86e-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: 186.29  E-value: 5.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  859 MNSKIMSLSNKLTYEGKLECGSDKvanavinlrhfkdvklelefyadySDNPWLMGVFEPNNPVCFLNTDKvpaPEQVEK 938
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSV------------------------AARLNPPPLPGPSKPLVFVDVSG---GEEREE 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  939 GGVS--NVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLARSIGM---VEVNTVDKYQGRDKSIVLVSFVR 1013
Cdd:cd18808    54 SGTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGGLledVEVGTVDNFQGREKDVIILSLVR 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578819047 1014 SNKDGTVGELLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPLEKLLNHL 1063
Cdd:cd18808   134 SNESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
656-858 1.94e-44

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: 159.31  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRLGQIQKV 735
Cdd:cd18044     2 LNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPARL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  736 HPAIQQFTeqeicrsksikslalLEELYNSQlIVATTCMGINHPIFSRKI-FDFCIVDEASQISQPICLGPLFFSRRFVL 814
Cdd:cd18044    82 LESVLDHS---------------LDALVAAQ-VVLATNTGAGSRQLLPNElFDVVVIDEAAQALEASCWIPLLKARRCIL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578819047  815 VGDHQQLPPLVLNREARALGMSESLFKRLEQ--NKSAVVQLTVQYR 858
Cdd:cd18044   146 AGDHKQLPPTILSDKAARGGLGVTLFERLVNlyGESVVRMLTVQYR 191
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
656-858 2.02e-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: 134.26  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLL-SKDYTLIVGMPGTGKTTTICTLVRILYA-------------------------CGFSVLLTSYTH 709
Cdd:cd18042     1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILSVLLAgkyrkyyekvkkklrklqrnlnnkkKKNRILVCAPSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  710 SAVDNILLKLAKfkiGFLRLGQIQKVHPAIQQFTEQEICRSksikslalleeLYNSQLIVATTCMGINHPIFSRKI--FD 787
Cdd:cd18042    81 AAVDEIVLRLLS---EGFLDGDGRSYKPNVVRVGRQELRAS-----------ILNEADIVCTTLSSSGSDLLESLPrgFD 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578819047  788 FCIVDEASQISQPICLGPL-FFSRRFVLVGDHQQLPPLVLNREARALGMSESLFKRLEQNKSAVVQLTVQYR 858
Cdd:cd18042   147 TVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
673-858 1.96e-34

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: 127.74  E-value: 1.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  673 YTLIVGMPGTGKTTTICTLVRIL--YACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkvhpaiqqfteqeicrs 750
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLlkGLRGKRVLVTAQSNVAVDNV----------------------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  751 ksikslalleelynsqlivattcmginhpifsrkifDFCIVDEASQISQPICLGPLFFSRRFVLVGDHQQLPPLVLNREA 830
Cdd:cd17934    46 ------------------------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHA 89
                         170       180       190
                  ....*....|....*....|....*....|..
gi 578819047  831 RALG----MSESLFKRLEQNKSAVVQLTVQYR 858
Cdd:cd17934    90 ALLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
656-858 2.44e-33

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: 128.90  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLV-RILYACGFSVLLTSYTHSAVDNILLKLAKFKIGFLRL----- 729
Cdd:cd18039     2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVyHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLcaksr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  730 -------------------GQIQKVHPAIQQFTEQ-EICRSKSIKSLALLEELYNSQL----IVATTCMGINHPIFSRKI 785
Cdd:cd18039    81 eavespvsflalhnqvrnlDSAEKLELLKLLKLETgELSSADEKRYRKLKRKAERELLrnadVICCTCVGAGDPRLSKMK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578819047  786 FDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQLPPLVLNREARALGMSESLFKRLEQNKSAVVQLTVQYR 858
Cdd:cd18039   161 FRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
659-828 8.57e-27

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: 110.51  E-value: 8.57e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   659 PQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFS-------VLLTSYTHSAVDNILLKLA----KFKIGFL 727
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLrkgqKYGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   728 RLGQIQKVHPAIQQFTEQEICRSKS-------------------IKSLALLEELYNSQL--------------------- 767
Cdd:pfam13086   81 RIGHPAAISEAVLPVSLDYLVESKLnneedaqivkdiskeleklAKALRAFEKEIIVEKllksrnkdkskleqerrklrs 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   768 -------------------------IVATTCMGINHPIFSR-KIFDFCIVDEASQISQPICLGPLFF-SRRFVLVGDHQQ 820
Cdd:pfam13086  161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240

                   ....*...
gi 578819047   821 LPPLVLNR 828
Cdd:pfam13086  241 LPPTVISK 248
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
656-858 2.54e-24

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: 102.70  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKD----YtLIVGMPGTGKTTTI--CTL-VRILYaCGFSVLLTSYTHSAVDNILLKLAKFKIG--- 725
Cdd:cd18038     2 LNDEQKLAVRNIVTGTSrpppY-IIFGPPGTGKTVTLveAILqVLRQP-PEARILVCAPSNSAADLLAERLLNALVTkre 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  726 FLRLG----QIQKVHPAIQQFTeqeICRSKSIKSLALLEELYNSQlIVATTCMGINHPI---FSRKIFDFCIVDEASQIS 798
Cdd:cd18038    80 ILRLNapsrDRASVPPELLPYC---NSKAEGTFRLPSLEELKKYR-IVVCTLMTAGRLVqagVPNGHFTHIFIDEAGQAT 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578819047  799 QPICLGPLFFSR----RFVLVGDHQQLPPLVLNREARALGMSESLFKRL----------EQNKSAVVQLTVQYR 858
Cdd:cd18038   156 EPEALIPLSELAskntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLmerplyykdgEYNPSYITKLLKNYR 229
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
656-846 1.91e-18

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: 85.50  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKDYTL---IVGMPGTGKTTTIC-TLVRILYACGFS-VLLTSYTHSAVDNILLKLAKFKIgfLRLG 730
Cdd:cd18078     2 LNELQKEAVKRILGGECRPLpyiLFGPPGTGKTVTIIeAILQVVYNLPRSrILVCAPSNSAADLVTSRLHESKV--LKPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  731 QIQKVhPAIQQFTEQEI------CRSKSIKSLALLEElynsqlIVATTC--MGINHPI-FSRKIFDFCIVDEASQISQPI 801
Cdd:cd18078    80 DMVRL-NAVNRFESTVIdarklyCRLGEDLSKASRHR------IVISTCstAGLLYQMgLPVGHFTHVFVDEAGQATEPE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578819047  802 CLGPL-FFSRR---FVLVGDHQQLPPLVLNREARALGMSESLFKRLEQN 846
Cdd:cd18078   153 SLIPLgLISSRdgqIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNR 201
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
674-868 2.55e-17

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: 81.70  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  674 TLIVGMPGTGKTTTICTLVRILYACGFS--VLLTSYTHSAVDNILLKLAKFKIG---FLRLGQIQKvhpaiqqfteqeic 748
Cdd:cd17935    23 TMVVGPPGTGKTDVAVQIISNLYHNFPNqrTLIVTHSNQALNQLFEKIMALDIDerhLLRLGHGAK-------------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  749 rsksikslalleelynsqlIVATTCmgiNHPIFSRKIF---DFC----IVDEASQISQPICLGPLFFSR---------RF 812
Cdd:cd17935    89 -------------------IIAMTC---THAALKRGELvelGFKydniLMEEAAQILEIETFIPLLLQNpedgpnrlkRL 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578819047  813 VLVGDHQQLPPLVLNREARALG-MSESLFKRLEQNKSAVVQLTVQYRMNSKIMSLSN 868
Cdd:cd17935   147 IMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
655-857 1.45e-15

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: 75.66  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  655 GLNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLVRILY-----ACGFSVLLTSYTHSAVDNILLKLAKFKIG-FLR 728
Cdd:cd17936     1 TLDPSQLEALKHAL-TSELALIQGPPGTGKTFLGVKLVRALLqnqdlSITGPILVVCYTNHALDQFLEGLLDFGPTkIVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  729 LGqiqkvhpaiqqfteqeicrsKSIkslalleelynsqLIVATTCMGINHPIFSRKIFDFCIVDEASQI--SQPI-CLGP 805
Cdd:cd17936    80 LG--------------------ARV-------------IGMTTTGAAKYRELLQALGPKVVIVEEAAEVleAHILaALTP 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578819047  806 LFfsRRFVLVGDHQQLPPLVLNRE--ARALGMSESLFKRLEQNKSAVVQLTVQY 857
Cdd:cd17936   127 ST--EHLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
657-829 2.31e-15

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: 73.77  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  657 NKPQRQAMKKVLLSKDyTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNILLklakfkigflrlgqiqkvh 736
Cdd:cd18043     1 DSSQEAAIISARNGKN-VVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVRF------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  737 PAIqqfteqeicrsksIKSLALLEELYNsqlivattcmginhpiFSRKIFDFCIVDEASQISQPICLGPLFFSRRFVLVG 816
Cdd:cd18043    61 PCW-------------IMSPLSVSQYLP----------------LNRNLFDLVIFDEASQIPIEEALPALFRGKQVVVVG 111
                         170
                  ....*....|...
gi 578819047  817 DHQQLPPLVLNRE 829
Cdd:cd18043   112 DDKQLPPSILLRE 124
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
655-858 1.27e-14

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: 75.25  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  655 GLNKPQRQAMKKVLlSKDYTLIVGMPGTGKTTTICTLV--------RILYACGFS-----VLLTSYTHSAVD---NILLK 718
Cdd:cd18040     1 KLNPSQNHAVRTAL-TKPFTLIQGPPGTGKTVTGVHIAywfakqnrEIQSVSGEGdggpcVLYCGPSNKSVDvvaELLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  719 LAKFKIgfLRL--GQIQK------------------------------VHPAIQQ----------------------FTE 744
Cdd:cd18040    80 VPGLKI--LRVysEQIETteypipneprhpnkksereskpnselssitLHHRIRQpsnphsqqikafearfertqekITE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  745 QEICRSKSIKSLALLEELYNSQLIVATtCMGINHPIFSRKI-FDFCIVDEASQISQPICLGPL---FFSRRFVLVGDHQQ 820
Cdd:cd18040   158 EDIKTYKILIWEARFEELETVDVILCT-CSEAASQKMRTHAnVKQCIVDECGMCTEPESLIPIvsaPRAEQVVLIGDHKQ 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 578819047  821 LPPLVLNREARALGMSESLFKRLEQnksAVVQLTVQYR 858
Cdd:cd18040   237 LRPVVQNKEAQKLGLGRSLFERYAE---KACMLDTQYR 271
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
660-823 2.44e-12

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: 65.65  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  660 QRQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAvdnillklAKfkigflRLGQIQKVHpai 739
Cdd:cd17933     2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKA--------AK------RLSESTGIE--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  740 qqfteqeicrSKSIKSlaLLEELYNSQLivattcMGINHP-IFSRKIFdfcIVDEASQISQPIclgplfFSR-------- 810
Cdd:cd17933    64 ----------ASTIHR--LLGINPGGGG------FYYNEEnPLDADLL---IVDEASMVDTRL------MAAllsaipag 116
                         170
                  ....*....|....
gi 578819047  811 -RFVLVGDHQQLPP 823
Cdd:cd17933   117 aRLILVGDPDQLPS 130
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
656-843 2.19e-11

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: 64.81  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKDYT----LIVGMPGTGKTTTICTLVR-ILYACGFSVLLTSYTHSAVD--------------NIL 716
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQlppvLLIGPFGTGKTFTLAQAVKhILQQPETRILICTHSNSAADlyikeylhpyvetgNPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  717 LKLAKFkigFLRLGQIQKVHPAIQQFTeqeICRSKSIKSLALLEELYNSQLIVAT--TCMGINHPIFSRKIFDFCIVDEA 794
Cdd:cd18077    82 ARPLRV---YYRNRWVKTVHPVVQKYC---LIDEHGTFRMPTREDVMRHRVVVVTlsTSQYLCQLDLEPGFFTHILLDEA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578819047  795 SQISQPICLGPLFF---SRRFVLVGDHQQLPPLVLNREARALGMSESLFKRL 843
Cdd:cd18077   156 AQAMECEAIMPLALatkSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
656-870 2.42e-11

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: 67.69  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  656 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDNIllklakfkigflrlgqiqkv 735
Cdd:COG0507   125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  736 hpaiqqftEQEICR-SKSIKSlaLLEELYNSQLIVAttcmGINHPIFSRKIFdfcIVDEASQISQPIclgplfFSR---- 810
Cdd:COG0507   185 --------SESTGIeARTIHR--LLGLRPDSGRFRH----NRDNPLTPADLL---VVDEASMVDTRL------MAAllea 241
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578819047  811 ------RFVLVGDHQQLPPlVlnrEA-RALGMseslfkRLEQNKSAVVQLTVQYRM--NSKIMSLSNKL 870
Cdd:COG0507   242 lpragaRLILVGDPDQLPS-V---GAgAVLRD------LIESGTVPVVELTEVYRQadDSRIIELAHAI 300
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
966-1045 1.17e-10

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: 58.99  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  966 DIGIIAPYRQQLKIINDLLARS------IGMVEVNTVDKYQGRDKSIVLVSFVRSNKDgtvgellkDWRRLNVAITRAKH 1039
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLQGLsldefdLQLVGAITIDSSQGLTFDVVTLYLPTANSL--------TPRRLYVALTRARK 83

                  ....*.
gi 578819047 1040 KLILLG 1045
Cdd:cd18786    84 RLVIYD 89
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
291-427 2.70e-09

CRISPR-associated protein Cas4; This model represents a family of proteins associated with CRISPR repeats in a wide set of prokaryotic genomes. This scope of this model has been broadened since it was first built to describe an archaeal subset only. The function of the protein is undefined. Distantly related proteins, excluded from this model, include ORFs from Mycobacteriophage D29 and Sulfolobus islandicus filamentous virus and a region of the Schizosaccharomyces pombe DNA replication helicase Dna2p.


Pssm-ID: 273040 [Multi-domain]  Cd Length: 178  Bit Score: 57.80  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   291 IEESIW--SPRFGLKGKIDVtvgVKIHRGYKTkykimPLELKTGKESNSIEHRSQVVLYTLLSQERRADPEAGLLLYLKT 368
Cdd:TIGR00372   54 EEKEVPlkSKKYGLKGVIDI---VLEEDGELV-----PVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILYINA 125
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578819047   369 GQMYPVPANHLDKRELLKLRNQMafslfhrisksatRQKTQLASLPQIIEEEKTCKYCS 427
Cdd:TIGR00372  126 GKKLEVEISEELRKKAVKLIEKI-------------RELLEGGKPPSPPKSGPKCKFCP 171
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
292-427 3.99e-09

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: 57.28  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  292 EESIWSPRFGLKGKIDVtvgVKIHRGyktkyKIMPLELKTGKESNSIEHRSQVVLYTL-LSQERRADPEAGLLLYLKTGQ 370
Cdd:COG1468    58 EVPLDSERLGLTGKIDL---VEFEDG-----ELVPVEYKKSKPKPWEADRMQLCAYALlLEEMLGIPVPKGYLYYPEERK 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578819047  371 MYPVPANHLDKRELLKLRNQMafslfHRISKSATrqktqlasLPQIIEEEKTCKYCS 427
Cdd:COG1468   130 REEVELTEELREEVEEAIEEI-----REILESEK--------PPPPTKSKKKCKKCS 173
Cas4_I-A_I-B_I-C_I-D_II-B cd09637
CRISPR/Cas system-associated protein Cas4; CRISPR (Clustered Regularly Interspaced Short ...
291-427 2.21e-08

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: 55.13  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  291 IEESIW--SPRFGLKGKIDVtvgVKIHRGYKTkykimPLELKTGKESNSIE-HRSQVVLYTLLSQERRADPEA-GLLLYL 366
Cdd:cd09637    54 EEKEVPlkSKKYGLKGVIDI---VLKEDGELV-----PVEVKSGRAGSPREaHKLQLVAYAYLLEEMYGKRVArGYIVYL 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578819047  367 KTGQMYPVPANHLDKRELLKLRNQMafslfhrisksatrQKTQLASLPQIIEEEKTCKYCS 427
Cdd:cd09637   126 EGGKRLEVEISEELRKKAEKLLEEI--------------RKLLEGELPPPVKSSPKCKFCP 172
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
655-823 1.02e-07

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: 53.34  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   655 GLNKPQRQAMKKVLLSKD-YTLIVGMPGTGKTTTICTLVRILYACGFSVLLTSYTHSAVDnillKLAKfkigflRLGqiq 733
Cdd:pfam13604    1 TLNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAK----VLGE------ELG--- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   734 kvHPA--IQQFTeqeicrsksiKSLALLEELYNSQLIvattcmginhpifsrkifdfcIVDEASQISQPICLGplFFSR- 810
Cdd:pfam13604   68 --IPAdtIAKLL----------HRLGGRAGLDPGTLL---------------------IVDEAGMVGTRQMAR--LLKLa 112
                          170
                   ....*....|....*...
gi 578819047   811 -----RFVLVGDHQQLPP 823
Cdd:pfam13604  113 edagaRVILVGDPRQLPS 130
AAA_19 pfam13245
AAA domain;
660-823 5.00e-07

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 49.91  E-value: 5.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   660 QRQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILYACG---FSVLLTSYTHSAVDNillkLAKfkigflRLGQ-IQKV 735
Cdd:pfam13245    1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKR----LSE------RTGLpASTI 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   736 HpAIQQFteqeicrsKSIKSLALL--EELYNSQLIVattcmginhpifsrkifdfcIVDEASQISQPIC---LGPLFFSR 810
Cdd:pfam13245   70 H-RLLGF--------DDLEAGGFLrdEEEPLDGDLL--------------------IVDEFSMVDLPLAyrlLKALPDGA 120
                          170
                   ....*....|...
gi 578819047   811 RFVLVGDHQQLPP 823
Cdd:pfam13245  121 QLLLVGDPDQLPS 133
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
674-857 1.65e-06

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 48.25  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  674 TLIVGMPGTGKTTTICTLVRILYACG----FSVLLTSYTHSAVDNillklakfkigflrlgqiqkvhpaiqqfteqeicr 749
Cdd:cd17914     2 SLIQGPPGTGKTRVLVKIVAALMQNKngepGRILLVTPTNKAAAQ----------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  750 sksikslalleelynsqlivattcmginhpifsrkiFDFCIVDEASQISQPICLGP-LFFSR--RFVLVGDHQQLPPLVL 826
Cdd:cd17914    47 ------------------------------------LDNILVDEAAQILEPETSRLiDLALDqgRVILVGDHDQLGPVWR 90
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578819047  827 NREARALGMSESLFKRLEQNKSAVVQLTVQY 857
Cdd:cd17914    91 GAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
DEXDc smart00487
DEAD-like helicases superfamily;
656-794 7.30e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 42.09  E-value: 7.30e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047    656 LNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILYACGFSVLLTSYTHSAVDNILLKLAKFkigflrlgqiq 733
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL----------- 77
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578819047    734 kvhpaIQQFTEQEICRSKSIKSLALLEELYNS--QLIVATTCMGINHPI---FSRKIFDFCIVDEA 794
Cdd:smart00487   78 -----GPSLGLKVVGLYGGDSKREQLRKLESGktDILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
675-843 1.07e-03

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: 41.80  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  675 LIVGMPGTGKTTTICTLVR-ILYACGFSVLLTSYTHSA------------VDNILLKLAKFKIGFLRLGqIQKVHPAIQQ 741
Cdd:cd18076    27 LIYGPFGTGKTFTLAMAALeVIREPGTKVLICTHTNSAadiyireyfhpyVDKGHPEARPLRIKATDRP-NAITDPDTIT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  742 FTeqeiCRSKSIKSLAL--LEELYNSQLIVATTCMGINHPIFSrKIFDFCIVDEASQISQPICLGPLF---FSRRFVLVG 816
Cdd:cd18076   106 YC----CLTKDRQCFRLptRDELDFHNIVITTTAMAFNLHVLS-GFFTHIFIDEAAQMLECEALIPLSyagPKTRVVLAG 180
                         170       180
                  ....*....|....*....|....*..
gi 578819047  817 DHQQLPPLVLNrEARALGMSESLFKRL 843
Cdd:cd18076   181 DHMQMTPKLFS-VADYNRANHTLLNRL 206
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
921-1045 3.59e-03

C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases 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: 350194 [Multi-domain]  Cd Length: 150  Bit Score: 39.14  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047  921 PVCFLNTDKVPAPEQVEKGGVSnvtEAKLIVF-LTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLarsigMVEVNTVDKY 999
Cdd:cd18807    23 PLKAGNKSGGPVELLLAKDEAD---EAKAIADeIKRLIESGPVQYSDIAILVRTNRQARVIEEAL-----RVTLMTIHAS 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578819047 1000 QGRDKSIVLVSFVR---------SNKDGTVGELLKDWRRL-NVAITRAKHKLILLG 1045
Cdd:cd18807    95 KGLEFPVVFIVGLGegfipsdasYHAAKEDEERLEEERRLlYVALTRAKKELYLVG 150
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
674-706 4.47e-03

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 38.74  E-value: 4.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 578819047  674 TLIVGMPGTGKTTTICTLVRILYACGFSVLLTS 706
Cdd:cd01127     2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVIITD 34
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
613-704 7.50e-03

signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 39.55  E-value: 7.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819047   613 ENTFVSKKLRDLIIDfrepqfiSYLSSVLPHDAKDTVACILKGLNKPQrqamkkVLLskdytlIVGMPGTGKTTTICTLV 692
Cdd:TIGR00064   38 KKVKDAEKLKEILKE-------YLKEILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
                           90
                   ....*....|..
gi 578819047   693 RILYACGFSVLL 704
Cdd:TIGR00064   99 NKLKKQGKSVLL 110
 
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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