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Conserved domains on  [gi|1207115187|ref|XP_021336509|]
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DNA replication ATP-dependent helicase/nuclease DNA2 isoform X1 [Danio rerio]

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 ...
943-1145 6.02e-116

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: 361.17  E-value: 6.02e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQK 1022
Cdd:cd18041      1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1023 VHHEILPFTEEAcRAKGIQTLEELEQLYSRELIVATTCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLV 1102
Cdd:cd18041     81 IHPDVQEFTLEA-ILKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207115187 1103 GDHQQLPPIVQNAEARSLGMDESLFKRL-EHHRDAVVQLNVQYR 1145
Cdd:cd18041    160 GDHYQLPPLVKSREARELGMDESLFKRLsEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
443-686 9.53e-102

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: 323.70  E-value: 9.53e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  443 SGTSIASSIRCMRRGVLGEMFKAFDGGSKQMLNGTIVHDIFQKAAMSSDFSSEKIQTFATEALRSPNYLGQMYSLKLTQA 522
Cdd:cd22318      1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  523 DMRQEVEEYLPSISEWAKQYLHtspqAGQKQLTLKLPSDGalskqdaSSSVMVTDFVDIEENIWCPRFGLKGKIDVTAGV 602
Cdd:cd22318     81 EALEELEEYIPSIQEWAEKYVR----SNSPKGQVKLPSDG-------NSKGAISKILDIEENIWSPRFGLKGKIDATVEV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  603 KIHRRGrKPMERIVPLELKTGKESNSIEHRSQVILYTLMSSARR-CDPEAGFLVYLKTGSLHPVVGNHMDRRELIKIRNS 681
Cdd:cd22318    150 KIHDKG-KSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNE 228

                   ....*
gi 1207115187  682 LAHHI 686
Cdd:cd22318    229 LAHYL 233
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
788-1354 6.69e-76

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: 265.53  E-value: 6.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  788 QQREKIGGCAGNMRlaggVSILSDGVYKH--SFERKEGEQTltGLIVGDRIVVSDQDSvLIGLSTGYVTEIAVNRVTCSL 865
Cdd:TIGR00376   20 KQRERRGRAILNLQ----GKIRGGLLGFLlvRFGRRKAIAT--EISVGDIVLVSRGNP-LQSDLTGVVTRVGKRFITVAL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  866 DKNLSKYSSNTVfRLDqdegagglsthlgnlsmLMENTPTSERLRELIVEFRppQFIDSLSSVL-----PRDAKDIVS-- 938
Cdd:TIGR00376   93 EESVPQWSLKRV-RID-----------------LYANDVTFKRMKEALRALT--ENHSRLLEFLlgreaPSKASEIHDfq 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  939 NILKGLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLG 1018
Cdd:TIGR00376  153 FFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLG 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1019 RPQKVHHEILPFT--------EEACRAKGI-QTLEELEQ------------------------------------LYSRE 1053
Cdd:TIGR00376  233 HPARLLKSNKQHSldylienhPKYQIVADIrEKIDELIEernkktkpspqkrrglsdikilrkalkkreargiesLKIAS 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1054 LIVAT------------------------------TCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLVG 1103
Cdd:TIGR00376  313 MAEWIetnksidrllkllpeseerimneilaesdaTNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1104 DHQQLPPIVQNAEARSLgmDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEKTANAVLQLPSRAQ 1182
Cdd:TIGR00376  393 DHKQLPPTILSHDAEEL--SLTLFERLiKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVEA 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1183 AEEELElyvcqpqysawvqaaLEPNSPVCFLDTSEVPAPETVEKSGIS--NHTEAVLVQGLVTLLLKAGCRACDIGVIAP 1260
Cdd:TIGR00376  471 TESEDD---------------LETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITP 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1261 YRQQLKVISSLLQGDAFKaLEVNTVDKYQGRDKSVIIVSFVRSNAEGNLGeLLQDWRRLNVAITRAKHKLLMLGSAPTLR 1340
Cdd:TIGR00376  536 YDAQVDLLRQLLEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLS 613
                          650
                   ....*....|....
gi 1207115187 1341 RYAPLEKLLCHLQQ 1354
Cdd:TIGR00376  614 NHKFYKRLIEWCKQ 627
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
943-1145 6.02e-116

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: 361.17  E-value: 6.02e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQK 1022
Cdd:cd18041      1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1023 VHHEILPFTEEAcRAKGIQTLEELEQLYSRELIVATTCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLV 1102
Cdd:cd18041     81 IHPDVQEFTLEA-ILKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207115187 1103 GDHQQLPPIVQNAEARSLGMDESLFKRL-EHHRDAVVQLNVQYR 1145
Cdd:cd18041    160 GDHYQLPPLVKSREARELGMDESLFKRLsEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
443-686 9.53e-102

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: 323.70  E-value: 9.53e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  443 SGTSIASSIRCMRRGVLGEMFKAFDGGSKQMLNGTIVHDIFQKAAMSSDFSSEKIQTFATEALRSPNYLGQMYSLKLTQA 522
Cdd:cd22318      1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  523 DMRQEVEEYLPSISEWAKQYLHtspqAGQKQLTLKLPSDGalskqdaSSSVMVTDFVDIEENIWCPRFGLKGKIDVTAGV 602
Cdd:cd22318     81 EALEELEEYIPSIQEWAEKYVR----SNSPKGQVKLPSDG-------NSKGAISKILDIEENIWSPRFGLKGKIDATVEV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  603 KIHRRGrKPMERIVPLELKTGKESNSIEHRSQVILYTLMSSARR-CDPEAGFLVYLKTGSLHPVVGNHMDRRELIKIRNS 681
Cdd:cd22318    150 KIHDKG-KSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNE 228

                   ....*
gi 1207115187  682 LAHHI 686
Cdd:cd22318    229 LAHYL 233
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
388-602 2.33e-82

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: 268.28  E-value: 2.33e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  388 SKTSQATETCILKDGWESTLVTVGDIIHLEGKCVSGLWTIDRDSAFLILLPDLLISGTSIASSIRCMRRGVLGEMFKAFD 467
Cdd:pfam08696    1 SDKSGETRTVILRDDWVETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  468 GGSKQMLNGTIVHDIFQKAAMSSDFSSEKIQTFATEALRSpnYLGQMYSLKLTQADMRQEVEEYLPSISEWAKQYLHTSP 547
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALTANDWDLEFLEELLDELLEK--YLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSP 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  548 QAGQKQLtlklpsDGALSKQDASssvmVTDFVDIEENIWCPRFGLKGKIDVTAGV 602
Cdd:pfam08696  159 KPNAVVE------DGNGKKVKLS----ISKLLDIEENIWSPMYGLKGKIDATVEV 203
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
788-1354 6.69e-76

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: 265.53  E-value: 6.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  788 QQREKIGGCAGNMRlaggVSILSDGVYKH--SFERKEGEQTltGLIVGDRIVVSDQDSvLIGLSTGYVTEIAVNRVTCSL 865
Cdd:TIGR00376   20 KQRERRGRAILNLQ----GKIRGGLLGFLlvRFGRRKAIAT--EISVGDIVLVSRGNP-LQSDLTGVVTRVGKRFITVAL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  866 DKNLSKYSSNTVfRLDqdegagglsthlgnlsmLMENTPTSERLRELIVEFRppQFIDSLSSVL-----PRDAKDIVS-- 938
Cdd:TIGR00376   93 EESVPQWSLKRV-RID-----------------LYANDVTFKRMKEALRALT--ENHSRLLEFLlgreaPSKASEIHDfq 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  939 NILKGLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLG 1018
Cdd:TIGR00376  153 FFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLG 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1019 RPQKVHHEILPFT--------EEACRAKGI-QTLEELEQ------------------------------------LYSRE 1053
Cdd:TIGR00376  233 HPARLLKSNKQHSldylienhPKYQIVADIrEKIDELIEernkktkpspqkrrglsdikilrkalkkreargiesLKIAS 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1054 LIVAT------------------------------TCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLVG 1103
Cdd:TIGR00376  313 MAEWIetnksidrllkllpeseerimneilaesdaTNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1104 DHQQLPPIVQNAEARSLgmDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEKTANAVLQLPSRAQ 1182
Cdd:TIGR00376  393 DHKQLPPTILSHDAEEL--SLTLFERLiKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVEA 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1183 AEEELElyvcqpqysawvqaaLEPNSPVCFLDTSEVPAPETVEKSGIS--NHTEAVLVQGLVTLLLKAGCRACDIGVIAP 1260
Cdd:TIGR00376  471 TESEDD---------------LETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITP 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1261 YRQQLKVISSLLQGDAFKaLEVNTVDKYQGRDKSVIIVSFVRSNAEGNLGeLLQDWRRLNVAITRAKHKLLMLGSAPTLR 1340
Cdd:TIGR00376  536 YDAQVDLLRQLLEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLS 613
                          650
                   ....*....|....
gi 1207115187 1341 RYAPLEKLLCHLQQ 1354
Cdd:TIGR00376  614 NHKFYKRLIEWCKQ 627
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1037-1355 4.33e-70

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 252.74  E-value: 4.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1037 AKGIQTLEELEQLYSREL-----IVATTCMGVKHPI-FSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLVGDHQQLPP 1110
Cdd:COG1112    514 RRELKKRRELRKLLWDALlelapVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPP 593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1111 IVQNAEA---RSLGMDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEKTAnavlqlpsraqaeee 1186
Cdd:COG1112    594 VVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA--------------- 658
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1187 lelyvcqpqysawvQAALEPNSPVCFLDTSEVPAPETvekSGISNHTEAVLVQGLVTLLLKAGCRACDIGVIAPYRQQLK 1266
Cdd:COG1112    659 --------------RRLADPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVA 721
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1267 VISSLLQ---GDAFKALEVNTVDKYQGRDKSVIIVSFVRSNAE---GNLGELLQDWRRLNVAITRAKHKLLMLGSAPTL- 1339
Cdd:COG1112    722 LIRELLRealGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNGGPRRLNVAVSRARRKLIVVGSRELLd 801
                          330
                   ....*....|....*...
gi 1207115187 1340 --RRYAPLEKLLCHLQQE 1355
Cdd:COG1112    802 sdPSTPALKRLLEYLERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1122-1336 8.64e-70

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: 232.44  E-value: 8.64e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1122 MDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEktanavlqLPSRAQaeeelelyvcqPQYSAWv 1200
Cdd:pfam13087    1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS--------VAERPL-----------PDDFHL- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1201 qaaLEPNSPVCFLDTSEVPAPETVEKSGISNHTEAVLVQGLVTLLLKAGCRA-CDIGVIAPYRQQLKVISSLLQGDAFKA 1279
Cdd:pfam13087   61 ---PDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLGGK 137
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207115187 1280 --LEVNTVDKYQGRDKSVIIVSFVRSNAEGNLGeLLQDWRRLNVAITRAKHKLLMLGSA 1336
Cdd:pfam13087  138 leIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1146-1353 5.91e-55

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: 189.37  E-value: 5.91e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1146 MNSAIMSLSNALMYEGRLECGSEKTANAvlqlpsraqaeeelelyvcqpqysaWVQAALEPNSPVCFLDTSEVPAPETVE 1225
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARL-------------------------NPPPLPGPSKPLVFVDVSGGEEREESG 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1226 KSgISNHTEAVLVQGLVTLLLKAGCRACDIGVIAPYRQQLKVISSLLQ--GDAFKALEVNTVDKYQGRDKSVIIVSFVRS 1303
Cdd:cd18808     56 TS-KSNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRkrGGLLEDVEVGTVDNFQGREKDVIILSLVRS 134
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1304 NAEGNLGELLQDWRRLNVAITRAKHKLLMLGSAPTLRRYAPLEKLLCHLQ 1353
Cdd:cd18808    135 NESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
947-1112 1.08e-28

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: 116.29  E-value: 1.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  947 PQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFS-------VLLTSYTHSAVDNILLKLKR----FKIGFL 1015
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLRkgqkYGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1016 RLGRPQKVHHEILPFT------------------------------------EEACRAKGIQTLEELEQLYSREL----- 1054
Cdd:pfam13086   81 RIGHPAAISEAVLPVSldylvesklnneedaqivkdiskeleklakalrafeKEIIVEKLLKSRNKDKSKLEQERrklrs 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1055 -------------------------IVATTCMGVKHPIFSRR-RFDFCIVDEASQISQPVCIGPLFYAQ-RFVLVGDHQQ 1107
Cdd:pfam13086  161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGPkKVVLVGDPKQ 240

                   ....*
gi 1207115187 1108 LPPIV 1112
Cdd:pfam13086  241 LPPTV 245
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
944-1341 1.70e-16

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: 84.26  E-value: 1.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNIllklkrfkigflrlgrpqkv 1023
Cdd:COG0507    125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1024 hheilpftEEACRAKGiQTLEELEQLYSRELIVATtcmGVKHPIFSRRRFdfcIVDEASQISQpvcigPLFYA------- 1096
Cdd:COG0507    185 --------SESTGIEA-RTIHRLLGLRPDSGRFRH---NRDNPLTPADLL---VVDEASMVDT-----RLMAAllealpr 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1097 --QRFVLVGDHQQLPPIVQNAEARSLgmdeslfkrLEHHRDAVVQLNVQYRM--NSAIMSLSNALMyEGRLECGSEKTAN 1172
Cdd:COG0507    245 agARLILVGDPDQLPSVGAGAVLRDL---------IESGTVPVVELTEVYRQadDSRIIELAHAIR-EGDAPEALNARYA 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1173 AV--LQLPSRAQAEEEL-ELYVCQP-----------------QYSAWVQAALEPNSPVcfldtsevpapetveKSGISNH 1232
Cdd:COG0507    315 DVvfVEAEDAEEAAEAIvELYADRPaggediqvlaptnagvdALNQAIREALNPAGEL---------------ERELAED 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1233 TEAVLVQG---LVT-----LLLKAGcracDIGVIAPYRQQLKVISSLLQGDAFKALEVN-----------TVDKYQGR-- 1291
Cdd:COG0507    380 GELELYVGdrvMFTrndydLGVFNG----DIGTVLSIDEDEGRLTVRFDGREIVTYDPSeldqlelayaiTVHKSQGStf 455
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1292 DKSVIIVSFVRSNAEgnlgellqDWRRLNVAITRAKHKLLMLGSAPTLRR 1341
Cdd:COG0507    456 DRVILVLPSEHSPLL--------SRELLYTALTRARELLTLVGDRDALAR 497
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
579-721 6.20e-08

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: 53.95  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  579 VDIEENIWC--PRFGLKGKIDVtagVKIHRRgrkpmeRIVPLELKTGKESNSIEHRSQVILYTLMSSARRCDPEAGFLVY 656
Cdd:TIGR00372   52 VREEKEVPLksKKYGLKGVIDI---VLEEDG------ELVPVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILY 122
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  657 LKTGSLHPVVGNHMDRRELIKIrnslahhignnLIKVDGKSQMAQLPAIVSDQQTCKYCPQKRNC 721
Cdd:TIGR00372  123 INAGKKLEVEISEELRKKAVKL-----------IEKIRELLEGGKPPSPPKSGPKCKFCPYREIC 176
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
585-716 8.63e-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: 50.73  E-value: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  585 IWCPRFGLKGKIDVtagVKIHRRgrkpmeRIVPLELKTGKESNSIEHRSQVILYTLM-SSARRCDPEAGFLVYLKTGSLH 663
Cdd:COG1468     61 LDSERLGLTGKIDL---VEFEDG------ELVPVEYKKSKPKPWEADRMQLCAYALLlEEMLGIPVPKGYLYYPEERKRE 131
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207115187  664 PVVGNHMDRRELIKIRNSLAHHIgnnlikvdgksQMAQLPAIVSDQQTCKYCP 716
Cdd:COG1468    132 EVELTEELREEVEEAIEEIREIL-----------ESEKPPPPTKSKKKCKKCS 173
DEXDc smart00487
DEAD-like helicases superfamily;
944-1081 1.35e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 47.49  E-value: 1.35e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187   944 LNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILHACGFSVLLTSYTHSAVDNILLKLKRFkiGFLRLGRPQ 1021
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL--GPSLGLKVV 86
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  1022 KVHHeilpfteeacrakGIQTLEELEQLYSRE--LIVATTCMGVKHPI---FSRRRFDFCIVDEA 1081
Cdd:smart00487   87 GLYG-------------GDSKREQLRKLESGKtdILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
963-992 7.38e-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: 39.93  E-value: 7.38e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207115187  963 LIVGMPGTGKTTTICTLVRILHACGFSVLL 992
Cdd:TIGR00064   81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLL 110
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
934-992 8.92e-03

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 40.08  E-value: 8.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207115187  934 KDIVSNILKGLNKPQKQAMKK--VLLskdytlIVGMPGTGKTTTICTLVRILHACGFSVLL 992
Cdd:PRK10416    93 KEELAEILEPVEKPLNIEEKKpfVIL------VVGVNGVGKTTTIGKLAHKYKAQGKKVLL 147
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
943-1145 6.02e-116

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: 361.17  E-value: 6.02e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQK 1022
Cdd:cd18041      1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1023 VHHEILPFTEEAcRAKGIQTLEELEQLYSRELIVATTCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLV 1102
Cdd:cd18041     81 IHPDVQEFTLEA-ILKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLV 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1207115187 1103 GDHQQLPPIVQNAEARSLGMDESLFKRL-EHHRDAVVQLNVQYR 1145
Cdd:cd18041    160 GDHYQLPPLVKSREARELGMDESLFKRLsEAHPDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
443-686 9.53e-102

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: 323.70  E-value: 9.53e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  443 SGTSIASSIRCMRRGVLGEMFKAFDGGSKQMLNGTIVHDIFQKAAMSSDFSSEKIQTFATEALRSPNYLGQMYSLKLTQA 522
Cdd:cd22318      1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNIFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  523 DMRQEVEEYLPSISEWAKQYLHtspqAGQKQLTLKLPSDGalskqdaSSSVMVTDFVDIEENIWCPRFGLKGKIDVTAGV 602
Cdd:cd22318     81 EALEELEEYIPSIQEWAEKYVR----SNSPKGQVKLPSDG-------NSKGAISKILDIEENIWSPRFGLKGKIDATVEV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  603 KIHRRGrKPMERIVPLELKTGKESNSIEHRSQVILYTLMSSARR-CDPEAGFLVYLKTGSLHPVVGNHMDRRELIKIRNS 681
Cdd:cd22318    150 KIHDKG-KSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNE 228

                   ....*
gi 1207115187  682 LAHHI 686
Cdd:cd22318    229 LAHYL 233
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
388-602 2.33e-82

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: 268.28  E-value: 2.33e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  388 SKTSQATETCILKDGWESTLVTVGDIIHLEGKCVSGLWTIDRDSAFLILLPDLLISGTSIASSIRCMRRGVLGEMFKAFD 467
Cdd:pfam08696    1 SDKSGETRTVILRDDWVETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  468 GGSKQMLNGTIVHDIFQKAAMSSDFSSEKIQTFATEALRSpnYLGQMYSLKLTQADMRQEVEEYLPSISEWAKQYLHTSP 547
Cdd:pfam08696   81 ESSKPMLIGTILHELFQEALTANDWDLEFLEELLDELLEK--YLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSP 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  548 QAGQKQLtlklpsDGALSKQDASssvmVTDFVDIEENIWCPRFGLKGKIDVTAGV 602
Cdd:pfam08696  159 KPNAVVE------DGNGKKVKLS----ISKLLDIEENIWSPMYGLKGKIDATVEV 203
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
788-1354 6.69e-76

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: 265.53  E-value: 6.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  788 QQREKIGGCAGNMRlaggVSILSDGVYKH--SFERKEGEQTltGLIVGDRIVVSDQDSvLIGLSTGYVTEIAVNRVTCSL 865
Cdd:TIGR00376   20 KQRERRGRAILNLQ----GKIRGGLLGFLlvRFGRRKAIAT--EISVGDIVLVSRGNP-LQSDLTGVVTRVGKRFITVAL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  866 DKNLSKYSSNTVfRLDqdegagglsthlgnlsmLMENTPTSERLRELIVEFRppQFIDSLSSVL-----PRDAKDIVS-- 938
Cdd:TIGR00376   93 EESVPQWSLKRV-RID-----------------LYANDVTFKRMKEALRALT--ENHSRLLEFLlgreaPSKASEIHDfq 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  939 NILKGLNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLG 1018
Cdd:TIGR00376  153 FFDPNLNESQKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLG 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1019 RPQKVHHEILPFT--------EEACRAKGI-QTLEELEQ------------------------------------LYSRE 1053
Cdd:TIGR00376  233 HPARLLKSNKQHSldylienhPKYQIVADIrEKIDELIEernkktkpspqkrrglsdikilrkalkkreargiesLKIAS 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1054 LIVAT------------------------------TCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLVG 1103
Cdd:TIGR00376  313 MAEWIetnksidrllkllpeseerimneilaesdaTNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1104 DHQQLPPIVQNAEARSLgmDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEKTANAVLQLPSRAQ 1182
Cdd:TIGR00376  393 DHKQLPPTILSHDAEEL--SLTLFERLiKEYPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKVEA 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1183 AEEELElyvcqpqysawvqaaLEPNSPVCFLDTSEVPAPETVEKSGIS--NHTEAVLVQGLVTLLLKAGCRACDIGVIAP 1260
Cdd:TIGR00376  471 TESEDD---------------LETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITP 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1261 YRQQLKVISSLLQGDAFKaLEVNTVDKYQGRDKSVIIVSFVRSNAEGNLGeLLQDWRRLNVAITRAKHKLLMLGSAPTLR 1340
Cdd:TIGR00376  536 YDAQVDLLRQLLEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIGDSRTLS 613
                          650
                   ....*....|....
gi 1207115187 1341 RYAPLEKLLCHLQQ 1354
Cdd:TIGR00376  614 NHKFYKRLIEWCKQ 627
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
1037-1355 4.33e-70

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 252.74  E-value: 4.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1037 AKGIQTLEELEQLYSREL-----IVATTCMGVKHPI-FSRRRFDFCIVDEASQISQPVCIGPLFYAQRFVLVGDHQQLPP 1110
Cdd:COG1112    514 RRELKKRRELRKLLWDALlelapVVGMTPASVARLLpLGEGSFDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPP 593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1111 IVQNAEA---RSLGMDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEKTAnavlqlpsraqaeee 1186
Cdd:COG1112    594 VVFGEEAeevAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA--------------- 658
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1187 lelyvcqpqysawvQAALEPNSPVCFLDTSEVPAPETvekSGISNHTEAVLVQGLVTLLLKAGCRACDIGVIAPYRQQLK 1266
Cdd:COG1112    659 --------------RRLADPDSPLVFIDVDGVYERRG---GSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVA 721
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1267 VISSLLQ---GDAFKALEVNTVDKYQGRDKSVIIVSFVRSNAE---GNLGELLQDWRRLNVAITRAKHKLLMLGSAPTL- 1339
Cdd:COG1112    722 LIRELLRealGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNGGPRRLNVAVSRARRKLIVVGSRELLd 801
                          330
                   ....*....|....*...
gi 1207115187 1340 --RRYAPLEKLLCHLQQE 1355
Cdd:COG1112    802 sdPSTPALKRLLEYLERA 819
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
1122-1336 8.64e-70

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: 232.44  E-value: 8.64e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1122 MDESLFKRL-EHHRDAVVQLNVQYRMNSAIMSLSNALMYEGRLECGSEktanavlqLPSRAQaeeelelyvcqPQYSAWv 1200
Cdd:pfam13087    1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPS--------VAERPL-----------PDDFHL- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1201 qaaLEPNSPVCFLDTSEVPAPETVEKSGISNHTEAVLVQGLVTLLLKAGCRA-CDIGVIAPYRQQLKVISSLLQGDAFKA 1279
Cdd:pfam13087   61 ---PDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLGGK 137
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1207115187 1280 --LEVNTVDKYQGRDKSVIIVSFVRSNAEGNLGeLLQDWRRLNVAITRAKHKLLMLGSA 1336
Cdd:pfam13087  138 leIEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
1146-1353 5.91e-55

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: 189.37  E-value: 5.91e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1146 MNSAIMSLSNALMYEGRLECGSEKTANAvlqlpsraqaeeelelyvcqpqysaWVQAALEPNSPVCFLDTSEVPAPETVE 1225
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARL-------------------------NPPPLPGPSKPLVFVDVSGGEEREESG 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1226 KSgISNHTEAVLVQGLVTLLLKAGCRACDIGVIAPYRQQLKVISSLLQ--GDAFKALEVNTVDKYQGRDKSVIIVSFVRS 1303
Cdd:cd18808     56 TS-KSNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRkrGGLLEDVEVGTVDNFQGREKDVIILSLVRS 134
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1304 NAEGNLGELLQDWRRLNVAITRAKHKLLMLGSAPTLRRYAPLEKLLCHLQ 1353
Cdd:cd18808    135 NESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
944-1145 5.47e-42

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: 152.38  E-value: 5.47e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQKV 1023
Cdd:cd18044      2 LNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPARL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1024 HHEILPFTEEAcrakgiqtleeleQLYSRelIVATTCMGVKHPIFSR-RRFDFCIVDEASQISQPVCIGPLFYAQRFVLV 1102
Cdd:cd18044     82 LESVLDHSLDA-------------LVAAQ--VVLATNTGAGSRQLLPnELFDVVVIDEAAQALEASCWIPLLKARRCILA 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1207115187 1103 GDHQQLPPIVQNAEARSLGMDESLFKRLEH-HRDAVVQ-LNVQYR 1145
Cdd:cd18044    147 GDHKQLPPTILSDKAARGGLGVTLFERLVNlYGESVVRmLTVQYR 191
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
944-1145 2.89e-34

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: 131.18  E-value: 2.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLL-SKDYTLIVGMPGTGKTTTICTLVRILHA-------------------------CGFSVLLTSYTH 997
Cdd:cd18042      1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILSVLLAgkyrkyyekvkkklrklqrnlnnkkKKNRILVCAPSN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  998 SAVDNILLKL----------KRFKIGFLRLGRpQKVHHEILpfteeaCRAKgiqtleeleqlysrelIVATTCMGVKHPI 1067
Cdd:cd18042     81 AAVDEIVLRLlsegfldgdgRSYKPNVVRVGR-QELRASIL------NEAD----------------IVCTTLSSSGSDL 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1068 FSR--RRFDFCIVDEASQISQPVCIGPL-FYAQRFVLVGDHQQLPPIVQNAEARSLGMDESLFKRLEHHRDAVVQLNVQY 1144
Cdd:cd18042    138 LESlpRGFDTVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQY 217

                   .
gi 1207115187 1145 R 1145
Cdd:cd18042    218 R 218
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
961-1145 9.36e-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: 126.20  E-value: 9.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  961 YTLIVGMPGTGKTTTICTLVRILHA--CGFSVLLTSYTHSAVDNIllklkrfkigflrlgrpqkvhheilpfteeacrak 1038
Cdd:cd17934      1 ISLIQGPPGTGKTTTIAAIVLQLLKglRGKRVLVTAQSNVAVDNV----------------------------------- 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1039 giqtleeleqlysrelivattcmgvkhpifsrrrfDFCIVDEASQISQPVCIGPLFYAQRFVLVGDHQQLPPIVQNAEAR 1118
Cdd:cd17934     46 -----------------------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHAA 90
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207115187 1119 SLG----MDESLFKRLEHHRDAVVQLNVQYR 1145
Cdd:cd17934     91 LLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
944-1145 4.46e-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: 128.52  E-value: 4.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLlSKDYTLIVGMPGTGKTTTICTLV-RILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRL---GR 1019
Cdd:cd18039      2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVyHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLcakSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1020 PQ--------KVHHEILPFTEEACRAKGIQTLEELEQLYS--------------RELI-----VATTCMGVKHPIFSRRR 1072
Cdd:cd18039     81 EAvespvsflALHNQVRNLDSAEKLELLKLLKLETGELSSadekryrklkrkaeRELLrnadvICCTCVGAGDPRLSKMK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1073 FDFCIVDEASQISQPVCIGPLFY-AQRFVLVGDHQQLPPIVQNAEARSLGMDESLFKRLehhrdavVQLN-------VQY 1144
Cdd:cd18039    161 FRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL-------VQLGirpirlqVQY 233

                   .
gi 1207115187 1145 R 1145
Cdd:cd18039    234 R 234
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
947-1112 1.08e-28

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: 116.29  E-value: 1.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  947 PQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFS-------VLLTSYTHSAVDNILLKLKR----FKIGFL 1015
Cdd:pfam13086    1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLRkgqkYGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1016 RLGRPQKVHHEILPFT------------------------------------EEACRAKGIQTLEELEQLYSREL----- 1054
Cdd:pfam13086   81 RIGHPAAISEAVLPVSldylvesklnneedaqivkdiskeleklakalrafeKEIIVEKLLKSRNKDKSKLEQERrklrs 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1055 -------------------------IVATTCMGVKHPIFSRR-RFDFCIVDEASQISQPVCIGPLFYAQ-RFVLVGDHQQ 1107
Cdd:pfam13086  161 erkelrkelrrreqslereildeaqIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGPkKVVLVGDPKQ 240

                   ....*
gi 1207115187 1108 LPPIV 1112
Cdd:pfam13086  241 LPPTV 245
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
944-1145 1.01e-26

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: 110.02  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKD----YtLIVGMPGTGKTTTI--CTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIG---F 1014
Cdd:cd18038      2 LNDEQKLAVRNIVTGTSrpppY-IIFGPPGTGKTVTLveAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVTkreI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1015 LRL---GRPQK-VHHEILPFTeeACRAKGIQTLEELEQLYS-RelIVATTCMGVKHPI---FSRRRFDFCIVDEASQISQ 1086
Cdd:cd18038     81 LRLnapSRDRAsVPPELLPYC--NSKAEGTFRLPSLEELKKyR--IVVCTLMTAGRLVqagVPNGHFTHIFIDEAGQATE 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207115187 1087 PVCIGPLFYAQ----RFVLVGDHQQLPPIVQNAEARSLGMDESLFKRL----------EHHRDAVVQLNVQYR 1145
Cdd:cd18038    157 PEALIPLSELAskntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLmerplyykdgEYNPSYITKLLKNYR 229
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
943-1145 7.97e-20

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


Pssm-ID: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 91.05  E-value: 7.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLlSKDYTLIVGMPGTGKTTTICTLVRILHA-------------CGFSVLLTSYTHSAVD---NILLK 1006
Cdd:cd18040      1 KLNPSQNHAVRTAL-TKPFTLIQGPPGTGKTVTGVHIAYWFAKqnreiqsvsgegdGGPCVLYCGPSNKSVDvvaELLLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1007 LKRFKI------------------------GFLRLGRPQK------VHHEIL----PFTEE--ACRAKGIQTLEEL---E 1047
Cdd:cd18040     80 VPGLKIlrvyseqietteypipneprhpnkKSERESKPNSelssitLHHRIRqpsnPHSQQikAFEARFERTQEKIteeD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1048 QLYSRELIVAT-------------TC-------MGVKHPIFSrrrfdfCIVDEASQISQPVCIGPL---FYAQRFVLVGD 1104
Cdd:cd18040    160 IKTYKILIWEArfeeletvdvilcTCseaasqkMRTHANVKQ------CIVDECGMCTEPESLIPIvsaPRAEQVVLIGD 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1207115187 1105 HQQLPPIVQNAEARSLGMDESLFKRleHHRDAVVqLNVQYR 1145
Cdd:cd18040    234 HKQLRPVVQNKEAQKLGLGRSLFER--YAEKACM-LDTQYR 271
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
962-1155 4.60e-19

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: 87.10  E-value: 4.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  962 TLIVGMPGTGKTTTICTLVRIL-HAC-GFSVLLTSYTHSAVDNILLKLKRFKIG---FLRLGRPQKvhheilpfteeacr 1036
Cdd:cd17935     23 TMVVGPPGTGKTDVAVQIISNLyHNFpNQRTLIVTHSNQALNQLFEKIMALDIDerhLLRLGHGAK-------------- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1037 akgiqtleeleqlysrelIVATTCMgvkHPIFSRRRF---DFC----IVDEASQISQPVCIGPLFYA---------QRFV 1100
Cdd:cd17935     89 ------------------IIAMTCT---HAALKRGELvelGFKydniLMEEAAQILEIETFIPLLLQnpedgpnrlKRLI 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207115187 1101 LVGDHQQLPPIVQN-AEARSLGMDESLFKRLEHHRDAVVQLNVQYRMNSAIMSLSN 1155
Cdd:cd17935    148 MIGDHHQLPPVIKNmAFQKYSNMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
944-1341 1.70e-16

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: 84.26  E-value: 1.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNIllklkrfkigflrlgrpqkv 1023
Cdd:COG0507    125 LSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKAAKRL-------------------- 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1024 hheilpftEEACRAKGiQTLEELEQLYSRELIVATtcmGVKHPIFSRRRFdfcIVDEASQISQpvcigPLFYA------- 1096
Cdd:COG0507    185 --------SESTGIEA-RTIHRLLGLRPDSGRFRH---NRDNPLTPADLL---VVDEASMVDT-----RLMAAllealpr 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1097 --QRFVLVGDHQQLPPIVQNAEARSLgmdeslfkrLEHHRDAVVQLNVQYRM--NSAIMSLSNALMyEGRLECGSEKTAN 1172
Cdd:COG0507    245 agARLILVGDPDQLPSVGAGAVLRDL---------IESGTVPVVELTEVYRQadDSRIIELAHAIR-EGDAPEALNARYA 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1173 AV--LQLPSRAQAEEEL-ELYVCQP-----------------QYSAWVQAALEPNSPVcfldtsevpapetveKSGISNH 1232
Cdd:COG0507    315 DVvfVEAEDAEEAAEAIvELYADRPaggediqvlaptnagvdALNQAIREALNPAGEL---------------ERELAED 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1233 TEAVLVQG---LVT-----LLLKAGcracDIGVIAPYRQQLKVISSLLQGDAFKALEVN-----------TVDKYQGR-- 1291
Cdd:COG0507    380 GELELYVGdrvMFTrndydLGVFNG----DIGTVLSIDEDEGRLTVRFDGREIVTYDPSeldqlelayaiTVHKSQGStf 455
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1292 DKSVIIVSFVRSNAEgnlgellqDWRRLNVAITRAKHKLLMLGSAPTLRR 1341
Cdd:COG0507    456 DRVILVLPSEHSPLL--------SRELLYTALTRARELLTLVGDRDALAR 497
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
943-1144 3.03e-16

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 77.97  E-value: 3.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLlSKDYTLIVGMPGTGKTTTICTLVRILH-----ACGFSVLLTSYTHSAVDNILLKLKRFKIG-FLR 1016
Cdd:cd17936      1 TLDPSQLEALKHAL-TSELALIQGPPGTGKTFLGVKLVRALLqnqdlSITGPILVVCYTNHALDQFLEGLLDFGPTkIVR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1017 LGrpqkvhheilpfteeacrakgiqtleeleqlysRELIVATTCMGVKH-PIFSRRRFDFCIVDEASQISQP---VCIGP 1092
Cdd:cd17936     80 LG---------------------------------ARVIGMTTTGAAKYrELLQALGPKVVIVEEAAEVLEAhilAALTP 126
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207115187 1093 LFyaQRFVLVGDHQQLPPIVQNAE--ARSLGMDESLFKRLEHHRDAVVQLNVQY 1144
Cdd:cd17936    127 ST--EHLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
945-1110 1.03e-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: 74.93  E-value: 1.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  945 NKPQKQAMKKVLLSKDyTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNIllklkRFKIgflRLGRPQKVH 1024
Cdd:cd18043      1 DSSQEAAIISARNGKN-VVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVV-----RFPC---WIMSPLSVS 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1025 HEILPFTEEacrakgiqtleeleqlysrelivattcmgvkhpifsrrrFDFCIVDEASQISQPVCIGPLFYAQRFVLVGD 1104
Cdd:cd18043     72 QYLPLNRNL---------------------------------------FDLVIFDEASQIPIEEALPALFRGKQVVVVGD 112

                   ....*.
gi 1207115187 1105 HQQLPP 1110
Cdd:cd18043    113 DKQLPP 118
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
944-1130 1.47e-15

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: 77.41  E-value: 1.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKDYTL---IVGMPGTGKTTTIC-TLVRILHACGFS-VLLTSYTHSAVDNILLKLKRFKIgfLRLG 1018
Cdd:cd18078      2 LNELQKEAVKRILGGECRPLpyiLFGPPGTGKTVTIIeAILQVVYNLPRSrILVCAPSNSAADLVTSRLHESKV--LKPG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1019 ---RPQKVHHEILPFTEEacRAKGIQTLEELEQLySRELIVATTC--------MGVKhpifsRRRFDFCIVDEASQISQP 1087
Cdd:cd18078     80 dmvRLNAVNRFESTVIDA--RKLYCRLGEDLSKA-SRHRIVISTCstagllyqMGLP-----VGHFTHVFVDEAGQATEP 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207115187 1088 VCIGPL-FYAQR---FVLVGDHQQLPPIVQNAEARSLGMDESLFKRL 1130
Cdd:cd18078    152 ESLIPLgLISSRdgqIILAGDPMQLGPVIKSRLASAYGLGVSFLERL 198
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
948-1144 9.04e-14

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: 70.28  E-value: 9.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  948 QKQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDnillklkrfkigflRLGrpqkvhhei 1027
Cdd:cd17933      2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAK--------------RLS--------- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1028 lpfteeacRAKGI--QTLEELEQLYSRElivattcMGVKHPIFSRRRFDFCIVDEASQISQpvcigPLFYA--------Q 1097
Cdd:cd17933     58 --------ESTGIeaSTIHRLLGINPGG-------GGFYYNEENPLDADLLIVDEASMVDT-----RLMAAllsaipagA 117
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1207115187 1098 RFVLVGDHQQLPPIvqnaearslGMDESLFKRLEHHRDAVVQLNVQY 1144
Cdd:cd17933    118 RLILVGDPDQLPSV---------GAGNVLRDLIASKGVPTVELTEVF 155
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
962-1144 5.53e-12

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: 64.04  E-value: 5.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  962 TLIVGMPGTGKTTT----ICTLVRILHACGFSVLLTSYTHSAVDnillklkrfkigflrlgrpqkvhheilpfteeacra 1037
Cdd:cd17914      2 SLIQGPPGTGKTRVlvkiVAALMQNKNGEPGRILLVTPTNKAAA------------------------------------ 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1038 kgiqtleeleqlysrelivattcmgvkhpifsrrRFDFCIVDEASQISQPVCIGP---LFYAQRFVLVGDHQQLPPIVQN 1114
Cdd:cd17914     46 ----------------------------------QLDNILVDEAAQILEPETSRLidlALDQGRVILVGDHDQLGPVWRG 91
                          170       180       190
                   ....*....|....*....|....*....|
gi 1207115187 1115 AEARSLGMDESLFKRLEHHRDAVVQLNVQY 1144
Cdd:cd17914     92 AVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
943-1168 8.61e-12

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: 65.66  E-value: 8.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  943 GLNKPQKQAMKKVLLSKD-YTLIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDnillklkrfkigflRLGRpq 1021
Cdd:pfam13604    1 TLNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAK--------------VLGE-- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1022 kvhheilpftEEACRAKGIQTLeeLEQLYSRELIVATTCMgvkhpifsrrrfdfcIVDEASQISQPVCIGPLFYAQRF-- 1099
Cdd:pfam13604   65 ----------ELGIPADTIAKL--LHRLGGRAGLDPGTLL---------------IVDEAGMVGTRQMARLLKLAEDAga 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1100 --VLVGDHQQLPPIvqnaEArslGmdeSLFKRLEHHRDAVVQLNVQYRM-NSAIMSLSNAL----------MYE--GRLE 1164
Cdd:pfam13604  118 rvILVGDPRQLPSV----EA---G---GAFRDLLAAGIGTAELTEIVRQrDPWQRAASLALrdgdpaealdALAdrGRIH 187

                   ....
gi 1207115187 1165 CGSE 1168
Cdd:pfam13604  188 EGDD 191
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
1254-1334 1.76e-11

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


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 61.68  E-value: 1.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1254 DIGVIAPYRQQLKVISSLLQG-----DAFKALEVNTVDKYQGRDKSVIIVSFVRSNAEgnlgellqDWRRLNVAITRAKH 1328
Cdd:cd18786     12 KGVVLTPYHRDRAYLNQYLQGlsldeFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL--------TPRRLYVALTRARK 83

                   ....*.
gi 1207115187 1329 KLLMLG 1334
Cdd:cd18786     84 RLVIYD 89
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
944-1133 8.95e-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: 63.27  E-value: 8.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLSKDYT----LIVGMPGTGKTTTICTLVR-ILHACGFSVLLTSYTHSAVDnilLKLKRFKIGFLRLG 1018
Cdd:cd18077      2 LNAKQKEAVLAITTPLSIQlppvLLIGPFGTGKTFTLAQAVKhILQQPETRILICTHSNSAAD---LYIKEYLHPYVETG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1019 ----RPQKVHHE------ILPFTEEACRAKGIQTLE--ELEQLYSRELIVAT--TCMGVKHPIFSRRRFDFCIVDEASQI 1084
Cdd:cd18077     79 npraRPLRVYYRnrwvktVHPVVQKYCLIDEHGTFRmpTREDVMRHRVVVVTlsTSQYLCQLDLEPGFFTHILLDEAAQA 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207115187 1085 SQPVCIGPLFYAQ---RFVLVGDHQQLPPIVQNAEARSLGMDESLFKRLEHH 1133
Cdd:cd18077    159 MECEAIMPLALATkstRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEH 210
AAA_19 pfam13245
AAA domain;
948-1111 2.85e-10

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 59.54  E-value: 2.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  948 QKQAMKKVLLSKdYTLIVGMPGTGKTTTICTLVRILHACG---FSVLLTSYTHSAVDNILlklkrfkigfLRLGRPQKVH 1024
Cdd:pfam13245    1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKRLS----------ERTGLPASTI 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1025 HEILPFteeacrakgiQTLEELEQLYSRElivattcmgvkhpifSRRRFDFCIVDEASQISQPVC---IGPLFYAQRFVL 1101
Cdd:pfam13245   70 HRLLGF----------DDLEAGGFLRDEE---------------EPLDGDLLIVDEFSMVDLPLAyrlLKALPDGAQLLL 124
                          170
                   ....*....|
gi 1207115187 1102 VGDHQQLPPI 1111
Cdd:pfam13245  125 VGDPDQLPSV 134
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
579-721 6.20e-08

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: 53.95  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  579 VDIEENIWC--PRFGLKGKIDVtagVKIHRRgrkpmeRIVPLELKTGKESNSIEHRSQVILYTLMSSARRCDPEAGFLVY 656
Cdd:TIGR00372   52 VREEKEVPLksKKYGLKGVIDI---VLEEDG------ELVPVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILY 122
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  657 LKTGSLHPVVGNHMDRRELIKIrnslahhignnLIKVDGKSQMAQLPAIVSDQQTCKYCPQKRNC 721
Cdd:TIGR00372  123 INAGKKLEVEISEELRKKAVKL-----------IEKIRELLEGGKPPSPPKSGPKCKFCPYREIC 176
Cas4_I-A_I-B_I-C_I-D_II-B cd09637
CRISPR/Cas system-associated protein Cas4; CRISPR (Clustered Regularly Interspaced Short ...
588-721 1.29e-07

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: 53.21  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  588 PRFGLKGKIDVTAGVKihrrgrkpmERIVPLELKTGKESNSIE-HRSQVILYTLMSSARRCDPEA-GFLVYLKTGSLHPV 665
Cdd:cd09637     63 KKYGLKGVIDIVLKED---------GELVPVEVKSGRAGSPREaHKLQLVAYAYLLEEMYGKRVArGYIVYLEGGKRLEV 133
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207115187  666 VGNHMDRRELIKirnsLAHHIgNNLIKVDgksqmaqLPAIVSDQQTCKYCPQKRNC 721
Cdd:cd09637    134 EISEELRKKAEK----LLEEI-RKLLEGE-------LPPPVKSSPKCKFCPYREIC 177
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
585-716 8.63e-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: 50.73  E-value: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  585 IWCPRFGLKGKIDVtagVKIHRRgrkpmeRIVPLELKTGKESNSIEHRSQVILYTLM-SSARRCDPEAGFLVYLKTGSLH 663
Cdd:COG1468     61 LDSERLGLTGKIDL---VEFEDG------ELVPVEYKKSKPKPWEADRMQLCAYALLlEEMLGIPVPKGYLYYPEERKRE 131
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1207115187  664 PVVGNHMDRRELIKIRNSLAHHIgnnlikvdgksQMAQLPAIVSDQQTCKYCP 716
Cdd:COG1468    132 EVELTEELREEVEEAIEEIREIL-----------ESEKPPPPTKSKKKCKKCS 173
DEXDc smart00487
DEAD-like helicases superfamily;
944-1081 1.35e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 47.49  E-value: 1.35e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187   944 LNKPQKQAMKKVLLSKDYTLIVGMPGTGKTTTICT--LVRILHACGFSVLLTSYTHSAVDNILLKLKRFkiGFLRLGRPQ 1021
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLpaLEALKRGKGGRVLVLVPTRELAEQWAEELKKL--GPSLGLKVV 86
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207115187  1022 KVHHeilpfteeacrakGIQTLEELEQLYSRE--LIVATTCMGVKHPI---FSRRRFDFCIVDEA 1081
Cdd:smart00487   87 GLYG-------------GDSKREQLRKLESGKtdILVTTPGRLLDLLEndkLSLSNVDLVILDEA 138
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
963-1110 4.91e-05

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: 46.42  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  963 LIVGMPGTGKTTTICTLVR-ILHACGFSVLLTSYTHSAVDnilLKLKRFKIGFLRLGRPQKVHHEIL----------PFT 1031
Cdd:cd18076     27 LIYGPFGTGKTFTLAMAALeVIREPGTKVLICTHTNSAAD---IYIREYFHPYVDKGHPEARPLRIKatdrpnaitdPDT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1032 EEAC------RAKGIQTLEELEqlysRELIVATTCMGVKHPIFSRRRFDFCIVDEASQISQPVCIGPLFYA---QRFVLV 1102
Cdd:cd18076    104 ITYCcltkdrQCFRLPTRDELD----FHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLECEALIPLSYAgpkTRVVLA 179

                   ....*...
gi 1207115187 1103 GDHQQLPP 1110
Cdd:cd18076    180 GDHMQMTP 187
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
944-1081 2.85e-04

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 42.93  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  944 LNKPQKQAMKKVLLS----KDYTLIVgMP-GTGKTTTICTLVRILHAcgfsvlltsytHSAVDNILlklkrfkigFLrlg 1018
Cdd:cd18032      1 PRYYQQEAIEALEEArekgQRRALLV-MAtGTGKTYTAAFLIKRLLE-----------ANRKKRIL---------FL--- 56
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207115187 1019 rpqkVHHEILPF-TEEACRA-KGIQTLEELEQL----YSRELIVAT--TCMGVKH-PIFSRRRFDFCIVDEA 1081
Cdd:cd18032     57 ----AHREELLEqAERSFKEvLPDGSFGNLKGGkkkpDDARVVFATvqTLNKRKRlEKFPPDYFDLIIIDEA 124
betaCoV_Nsp13-helicase cd21722
helicase domain of betacoronavirus non-structural protein 13; This model represents the ...
948-1339 3.67e-04

helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.


Pssm-ID: 409655 [Multi-domain]  Cd Length: 340  Bit Score: 44.41  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  948 QKQAMKKvllskdYTLIVGMPGTGKTTTICTLVriLHACGFSVLLTSYTHSAVDniLLKLKRFKigFLRLGR-----PQK 1022
Cdd:cd21722     20 QKIGMKR------YCTVQGPPGTGKSHLAIGLA--VYYPTARVVYTACSHAAVD--ALCEKAFK--FLNINKcsriiPAK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1023 VHHEilpfteeaCrakgiqtleeleqlYSRELIVATTCMGVKHPI--FSRRRFDFCIVDEASQIS--QPVCIGPLFYAQR 1098
Cdd:cd21722     88 ARVE--------C--------------YDKFKVNDTSRQYVFSTInaLPETVTDILVVDEVSMCTnyDLSVINARVRAKH 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1099 FVLVGDHQQLPPivqnaeARSLGMDESLFKRlehHRDAVVQ----------LNVQYRMNSAIMSLSNALMYEGRLEcgse 1168
Cdd:cd21722    146 IVYIGDPAQLPA------PRTLLTKGTLEPE---YFNSVTRlmcclgpdifLGTCYRCPKEIVDTVSALVYDNKLK---- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1169 ktanavlqlpsraqaeeelelyvcqpqysawvqaALEPNSPVCFldtsevpapeTVEKSGISNHTEAVLVQ----GLVTL 1244
Cdd:cd21722    213 ----------------------------------AKKDNSGQCF----------KVYYKGSVTHDSSSAINrpqiYLVKK 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187 1245 LLKAGCRACDIGVIAPYRQQLKVISSLLqgdafkALEVNTVDKYQGRDKSVIIVSFVRSNAEGNlgellqDWRRLNVAIT 1324
Cdd:cd21722    249 FLKANPAWSKAVFISPYNSQNAVARRVL------GLQTQTVDSSQGSEYDYVIYCQTAETAHSV------NVNRFNVAIT 316
                          410
                   ....*....|....*
gi 1207115187 1325 RAKHKLLMLGSAPTL 1339
Cdd:cd21722    317 RAKKGILCVMSSMQL 331
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
963-1028 2.45e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.82  E-value: 2.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207115187  963 LIVGMPGTGKTTTICTLVRILHACGFSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQKVHHEIL 1028
Cdd:cd00009     23 LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPGVL 88
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
934-992 3.08e-03

Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 41.16  E-value: 3.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207115187  934 KDIVSNILKGLNKPQKQAMKK--VLLskdytlIVGMPGTGKTTTICTLVRILHACGFSVLL 992
Cdd:COG0552     79 KEELLEILDPVDKPLAIEEKKpfVIL------VVGVNGVGKTTTIGKLAHRLKAEGKSVLL 133
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
901-1081 5.04e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 41.16  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  901 ENTPTSERLRELIVEFRPPQFIDSLSsvlprdAKDIVSNILKGLNKPQKQAMKKVLL----SKDYTLIVGMPGTGKTTTI 976
Cdd:COG1061     44 EGTREDGRRLPEEDTERELAEAEALE------AGDEASGTSFELRPYQQEALEALLAalerGGGRGLVVAPTGTGKTVLA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115187  977 CTLVRILHACGfSVLLTSYTHSAVDNILLKLKRFKIGFLRLGRPQKVHHEILpFTeeacrakGIQTLeeleqlySRELIV 1056
Cdd:COG1061    118 LALAAELLRGK-RVLVLVPRRELLEQWAEELRRFLGDPLAGGGKKDSDAPIT-VA-------TYQSL-------ARRAHL 181
                          170       180
                   ....*....|....*....|....*
gi 1207115187 1057 ATTcmgvkhpifsRRRFDFCIVDEA 1081
Cdd:COG1061    182 DEL----------GDRFGLVIIDEA 196
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
963-992 7.38e-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: 39.93  E-value: 7.38e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1207115187  963 LIVGMPGTGKTTTICTLVRILHACGFSVLL 992
Cdd:TIGR00064   81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLL 110
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
934-992 8.92e-03

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 40.08  E-value: 8.92e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207115187  934 KDIVSNILKGLNKPQKQAMKK--VLLskdytlIVGMPGTGKTTTICTLVRILHACGFSVLL 992
Cdd:PRK10416    93 KEELAEILEPVEKPLNIEEKKpfVIL------VVGVNGVGKTTTIGKLAHKYKAQGKKVLL 147
 
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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