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Conserved domains on  [gi|1985390546|ref|XP_039403478|]
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DNA replication ATP-dependent helicase/nuclease DNA2 isoform X2 [Mauremys reevesii]

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 ...
540-743 1.11e-120

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: 366.18  E-value: 1.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQK 619
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 620 VHPDIRKFTEEEIckSKSIKSITHLEELYNNQPVVATTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVL 699
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1985390546 700 VGDHQQLPPLVHNTEARDLGMSESLFKRLEQNK-NAVVQLTVQYR 743
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
41-280 4.78e-107

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: 331.40  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  41 SGTTVSNSIRCMRKAVLSEKFRTCESSSRQMLIGTILHETFQQGVPNN-FAHEKLQELAFRTVHGPKYLKEMYYLNLKQE 119
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNiFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 120 EIMQEIEEYLPSISKWAEDFMHKPSqanhNKMQLKLPSEGKiedlsCNIEVTEFLDIEENIWSPRFGLKGKIDVTVGVKI 199
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDGN-----SKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 200 HRKSGTQYKIMPLELKTGKESNSIEHRSQVVLYTLLNQERR-VDPEAGFLLYLKTGNMYPVSGNRMDRRELLKLRNQLAF 278
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 1985390546 279 YL 280
Cdd:cd22318   232 YL 233
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
387-930 1.06e-72

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: 252.81  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 387 EREKAGDCIGNMirveHVEEASE--GQYLHYFQRKNGTmpGTNLLVGDRVVVSGEKTLLGLSAGYVKEVNVTKISCLLDR 464
Cdd:TIGR00376  21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAI--ATEISVGDIVLVSRGNPLQSDLTGVVTRVGKRFITVALEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 465 NLSKLPKDTIfRLDHEEGISGIDAPLRNLSKLMENSSaseKLRNLIIDFHKPQfiqhlssvlPPEAKETVANILKGLNKP 544
Cdd:TIGR00376  95 SVPQWSLKRV-RIDLYANDVTFKRMKEALRALTENHS---RLLEFLLGREAPS---------KASEIHDFQFFDPNLNES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 545 QKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQKV---- 620
Cdd:TIGR00376 162 QKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLlksn 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 621 -----------HP------DIRK----------------------FTEEEICK------------SKSIKS-----ITH- 643
Cdd:TIGR00376 242 kqhsldylienHPkyqivaDIREkidelieernkktkpspqkrrgLSDIKILRkalkkreargieSLKIASmaewiETNk 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 644 -----LEELYNNQPVVA--------TTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVLVGDHQQLPPLV 710
Cdd:TIGR00376 322 sidrlLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTI 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 711 HNTEARDLgmSESLFKRLEQNKNAVVQ-LTVQYRMNSKIMSLSNKLVYEGKLECGSEKVSKATVILPNLknlklelelfa 789
Cdd:TIGR00376 402 LSHDAEEL--SLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKV----------- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 790 dsSETWLKETLEPNNPVCFLNTEKVPAPEQAEKGGVS--NVTEAKLVLFLTTFFIKAGCKASDIGIVSPYRHQLKIITDL 867
Cdd:TIGR00376 469 --EATESEDDLETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQL 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985390546 868 MTSSCIStVEVNTVDKYQGRDKSIIIVSFVRNNNDGNLGtLLMDWRRLNVAITRAKHKLIMVG 930
Cdd:TIGR00376 547 LEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIG 607
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
540-743 1.11e-120

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: 366.18  E-value: 1.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQK 619
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 620 VHPDIRKFTEEEIckSKSIKSITHLEELYNNQPVVATTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVL 699
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1985390546 700 VGDHQQLPPLVHNTEARDLGMSESLFKRLEQNK-NAVVQLTVQYR 743
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
41-280 4.78e-107

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: 331.40  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  41 SGTTVSNSIRCMRKAVLSEKFRTCESSSRQMLIGTILHETFQQGVPNN-FAHEKLQELAFRTVHGPKYLKEMYYLNLKQE 119
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNiFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 120 EIMQEIEEYLPSISKWAEDFMHKPSqanhNKMQLKLPSEGKiedlsCNIEVTEFLDIEENIWSPRFGLKGKIDVTVGVKI 199
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDGN-----SKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 200 HRKSGTQYKIMPLELKTGKESNSIEHRSQVVLYTLLNQERR-VDPEAGFLLYLKTGNMYPVSGNRMDRRELLKLRNQLAF 278
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 1985390546 279 YL 280
Cdd:cd22318   232 YL 233
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
387-930 1.06e-72

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: 252.81  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 387 EREKAGDCIGNMirveHVEEASE--GQYLHYFQRKNGTmpGTNLLVGDRVVVSGEKTLLGLSAGYVKEVNVTKISCLLDR 464
Cdd:TIGR00376  21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAI--ATEISVGDIVLVSRGNPLQSDLTGVVTRVGKRFITVALEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 465 NLSKLPKDTIfRLDHEEGISGIDAPLRNLSKLMENSSaseKLRNLIIDFHKPQfiqhlssvlPPEAKETVANILKGLNKP 544
Cdd:TIGR00376  95 SVPQWSLKRV-RIDLYANDVTFKRMKEALRALTENHS---RLLEFLLGREAPS---------KASEIHDFQFFDPNLNES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 545 QKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQKV---- 620
Cdd:TIGR00376 162 QKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLlksn 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 621 -----------HP------DIRK----------------------FTEEEICK------------SKSIKS-----ITH- 643
Cdd:TIGR00376 242 kqhsldylienHPkyqivaDIREkidelieernkktkpspqkrrgLSDIKILRkalkkreargieSLKIASmaewiETNk 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 644 -----LEELYNNQPVVA--------TTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVLVGDHQQLPPLV 710
Cdd:TIGR00376 322 sidrlLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTI 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 711 HNTEARDLgmSESLFKRLEQNKNAVVQ-LTVQYRMNSKIMSLSNKLVYEGKLECGSEKVSKATVILPNLknlklelelfa 789
Cdd:TIGR00376 402 LSHDAEEL--SLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKV----------- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 790 dsSETWLKETLEPNNPVCFLNTEKVPAPEQAEKGGVS--NVTEAKLVLFLTTFFIKAGCKASDIGIVSPYRHQLKIITDL 867
Cdd:TIGR00376 469 --EATESEDDLETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQL 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985390546 868 MTSSCIStVEVNTVDKYQGRDKSIIIVSFVRNNNDGNLGtLLMDWRRLNVAITRAKHKLIMVG 930
Cdd:TIGR00376 547 LEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIG 607
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
2-197 4.22e-72

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: 236.69  E-value: 4.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546   2 YSVPVVPGDIIHLEGDCHSGTWIINRDSGYLILYPDLLLSGTTVSNSIRCMRKAVLSEKFRTCESSSRQMLIGTILHETF 81
Cdd:pfam08696  17 VETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSGESSKPMLIGTILHELF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  82 QQGVPNN-FAHEKLQELAFRTVHgpKYLKEMYYLNLKQEEIMQEIEEYLPSISKWAEDFMHKPSQANHNKMQLKlpsegk 160
Cdd:pfam08696  97 QEALTANdWDLEFLEELLDELLE--KYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSPKPNAVVEDGN------ 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1985390546 161 ieDLSCNIEVTEFLDIEENIWSPRFGLKGKIDVTVGV 197
Cdd:pfam08696 169 --GKKVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
720-932 4.68e-67

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: 222.81  E-value: 4.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 720 MSESLFKRL-EQNKNAVVQLTVQYRMNSKIMSLSNKLVYEGKLECGSEKVSKATVILPNlknlklelelfadssetwlke 798
Cdd:pfam13087   1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFH--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 799 TLEPNNPVCFLNTEKVPAPEQAEKGGVSNVTEAKLVLFLTTFFIKAGCKA-SDIGIVSPYRHQLKIITDLMTSSC--IST 875
Cdd:pfam13087  60 LPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggKLE 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985390546 876 VEVNTVDKYQGRDKSIIIVSFVRNNNDGNLGtLLMDWRRLNVAITRAKHKLIMVGCV 932
Cdd:pfam13087 140 IEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
613-948 3.54e-66

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 238.49  E-value: 3.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 613 RLGRAQKVHPDIRKFTEEEICKSKSIKSIThLEELYNNQPVVATTCMGVNHPIFARK-LFDFCIVDEASQISQPICLGPL 691
Cdd:COG1112   498 KLIAELREAARLRRALRRELKKRRELRKLL-WDALLELAPVVGMTPASVARLLPLGEgSFDLVIIDEASQATLAEALGAL 576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 692 FYSHKFVLVGDHQQLPPLV---HNTEARDLGMSESLFKRL-EQNKNAVVQLTVQYRMNSKIMSLSNKLVYEGKLECGSEK 767
Cdd:COG1112   577 ARAKRVVLVGDPKQLPPVVfgeEAEEVAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSP 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 768 VSkatvilpnlknlklelelfadssetwlKETLEPNNPVCFLNtekVPAPEQAEKGGVSNVTEAKLVLFLTTFFIKAGCK 847
Cdd:COG1112   657 KA---------------------------RRLADPDSPLVFID---VDGVYERRGGSRTNPEEAEAVVELVRELLEDGPD 706
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 848 ASDIGIVSPYRHQLKIITDLMTSSCIST---VEVNTVDKYQGRDKSIIIVSFVRNNND---GNLGTLLMDWRRLNVAITR 921
Cdd:COG1112   707 GESIGVITPYRAQVALIRELLREALGDGlepVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNGGPRRLNVAVSR 786
                         330       340
                  ....*....|....*....|....*..
gi 1985390546 922 AKHKLIMVGCvPSLCRYPPLEKLLCHL 948
Cdd:COG1112   787 ARRKLIVVGS-RELLDSDPSTPALKRL 812
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
744-948 2.45e-53

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 183.97  E-value: 2.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 744 MNSKIMSLSNKLVYEGKLECGSEKVSKatvilpnlknlklelelfadsseTWLKETLEPNNPVCFLNTEKvpaPEQAEKG 823
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAAR-----------------------LNPPPLPGPSKPLVFVDVSG---GEEREES 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 824 GVS--NVTEAKLVLFLTTFFIKAGCKASDIGIVSPYRHQLKIITDLMTSSC--ISTVEVNTVDKYQGRDKSIIIVSFVRN 899
Cdd:cd18808    55 GTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRS 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1985390546 900 NNDGNLGTLLMDWRRLNVAITRAKHKLIMVGCVPSLCRYPPLEKLLCHL 948
Cdd:cd18808   135 NESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
544-711 4.68e-29

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: 116.67  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 544 PQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFS-------VLLTSFTHTAVDNILLKLAR----FKVGFL 612
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLRkgqkYGPKIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 613 RLGRAQKVHPDIRKFT-----------------------------------EEEICKSKSIKSITHL------------- 644
Cdd:pfam13086  81 RIGHPAAISEAVLPVSldylvesklnneedaqivkdiskeleklakalrafEKEIIVEKLLKSRNKDkskleqerrklrs 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 645 -----------------EELYNNQPVVATTCMGVNHPIFAR-KLFDFCIVDEASQISQPICLGPLFY-SHKFVLVGDHQQ 705
Cdd:pfam13086 161 erkelrkelrrreqsleREILDEAQIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240

                  ....*.
gi 1985390546 706 LPPLVH 711
Cdd:pfam13086 241 LPPTVI 246
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
517-755 5.09e-13

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: 72.70  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 517 QFIQHLS--SVLPPEAKETVANILKG----LNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLT 590
Cdd:COG0507    95 RRLRRLArpALDEADVEAALAALEPRagitLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 591 SFTHTAVDNILLKLARfkvgflrlgRAQKVH------PDIRKFTEEEicksksiksithleelynnqpvvattcmgvNHP 664
Cdd:COG0507   175 APTGKAAKRLSESTGI---------EARTIHrllglrPDSGRFRHNR------------------------------DNP 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 665 IFARKLFdfcIVDEASQISQpiclgPLFYS---------HKFVLVGDHQQLPPlVhntEA----RDLgmseslfkrLEQN 731
Cdd:COG0507   216 LTPADLL---VVDEASMVDT-----RLMAAllealpragARLILVGDPDQLPS-V---GAgavlRDL---------IESG 274
                         250       260
                  ....*....|....*....|....*.
gi 1985390546 732 KNAVVQLTVQYRM--NSKIMSLSNKL 755
Cdd:COG0507   275 TVPVVELTEVYRQadDSRIIELAHAI 300
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
180-313 4.77e-12

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: 65.75  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 180 IWSPRFGLKGKIDVtvgvkIHRKSGTQYkimPLELKTGKESNSIEHRSQVVLYTL-LNQERRVDPEAGFLLYLKTGNMYP 258
Cdd:COG1468    61 LDSERLGLTGKIDL-----VEFEDGELV---PVEYKKSKPKPWEADRMQLCAYALlLEEMLGIPVPKGYLYYPEERKREE 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1985390546 259 VSGNRMDRRELLKLRNQLafylfHSMCKSAlgnkqthlaSLPPVIDDSRACKYCS 313
Cdd:COG1468   133 VELTEELREEVEEAIEEI-----REILESE---------KPPPPTKSKKKCKKCS 173
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
176-313 5.54e-09

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


Pssm-ID: 273040 [Multi-domain]  Cd Length: 178  Bit Score: 56.65  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 176 IEENIW--SPRFGLKGKIDVtvgVKIHRKsgtqyKIMPLELKTGKESNSIEHRSQVVLYTLLNQERRVDPEAGFLLYLKT 253
Cdd:TIGR00372  54 EEKEVPlkSKKYGLKGVIDI---VLEEDG-----ELVPVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILYINA 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 254 GNMYPVSGNRMDRRELLKLrnqlaFYLFHSMCKSALgnkqthlasLPPVIDDSRACKYCS 313
Cdd:TIGR00372 126 GKKLEVEISEELRKKAVKL-----IEKIRELLEGGK---------PPSPPKSGPKCKFCP 171
DEXDc smart00487
DEAD-like helicases superfamily;
541-679 2.98e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 40.17  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  541 LNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTIC--ALVRILYACGFSVLLTSFTHTAVDNILLKLARFkVGFLRLGRAQ 618
Cdd:smart00487   9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALlpALEALKRGKGGRVLVLVPTRELAEQWAEELKKL-GPSLGLKVVG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985390546  619 KVHPDIRKFTEEEIcksksIKSITHLeelynnqpVVATTCMGVNHPIFARKL---FDFCIVDEA 679
Cdd:smart00487  88 LYGGDSKREQLRKL-----ESGKTDI--------LVTTPGRLLDLLENDKLSlsnVDLVILDEA 138
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
498-589 5.04e-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: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 498 ENSSASEKLRNLIIDFHKpqfiqhlSSVLPPEAKETVANILKGLNKPQkqamkqVLLskdytlIVGMPGTGKTTTICALV 577
Cdd:TIGR00064  38 KKVKDAEKLKEILKEYLK-------EILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
                          90
                  ....*....|..
gi 1985390546 578 RILYACGFSVLL 589
Cdd:TIGR00064  99 NKLKKQGKSVLL 110
 
Name Accession Description Interval E-value
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
540-743 1.11e-120

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: 366.18  E-value: 1.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQK 619
Cdd:cd18041     1 GLNKDQRQAIKKVLNAKDYALILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 620 VHPDIRKFTEEEIckSKSIKSITHLEELYNNQPVVATTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVL 699
Cdd:cd18041    81 IHPDVQEFTLEAI--LKSCKSVEELESKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1985390546 700 VGDHQQLPPLVHNTEARDLGMSESLFKRLEQNK-NAVVQLTVQYR 743
Cdd:cd18041   159 VGDHYQLPPLVKSREARELGMDESLFKRLSEAHpDAVVQLTIQYR 203
DNA2_N-like cd22318
Nuclease domain of the nuclease/helicase DNA2 and related nucleases; The eukaryotic nuclease ...
41-280 4.78e-107

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: 331.40  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  41 SGTTVSNSIRCMRKAVLSEKFRTCESSSRQMLIGTILHETFQQGVPNN-FAHEKLQELAFRTVHGPKYLKEMYYLNLKQE 119
Cdd:cd22318     1 SGTSVAGSLFCMRKAVLSERFRGIDPGNKAMLIGTILHELFQKALKNNiFSREKLEKLAEKLLQSPKYLEDLYALGLTEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 120 EIMQEIEEYLPSISKWAEDFMHKPSqanhNKMQLKLPSEGKiedlsCNIEVTEFLDIEENIWSPRFGLKGKIDVTVGVKI 199
Cdd:cd22318    81 EALEELEEYIPSIQEWAEKYVRSNS----PKGQVKLPSDGN-----SKGAISKILDIEENIWSPRFGLKGKIDATVEVKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 200 HRKSGTQYKIMPLELKTGKESNSIEHRSQVVLYTLLNQERR-VDPEAGFLLYLKTGNMYPVSGNRMDRRELLKLRNQLAF 278
Cdd:cd22318   152 HDKGKSKTKIMPLELKTGRASFSIEHRGQVILYTLMMSDRYdVDVDSGLLLYLKEGEMKEVPAGRNEKRGLIILRNELAH 231

                  ..
gi 1985390546 279 YL 280
Cdd:cd22318   232 YL 233
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
387-930 1.06e-72

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: 252.81  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 387 EREKAGDCIGNMirveHVEEASE--GQYLHYFQRKNGTmpGTNLLVGDRVVVSGEKTLLGLSAGYVKEVNVTKISCLLDR 464
Cdd:TIGR00376  21 QRERRGRAILNL----QGKIRGGllGFLLVRFGRRKAI--ATEISVGDIVLVSRGNPLQSDLTGVVTRVGKRFITVALEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 465 NLSKLPKDTIfRLDHEEGISGIDAPLRNLSKLMENSSaseKLRNLIIDFHKPQfiqhlssvlPPEAKETVANILKGLNKP 544
Cdd:TIGR00376  95 SVPQWSLKRV-RIDLYANDVTFKRMKEALRALTENHS---RLLEFLLGREAPS---------KASEIHDFQFFDPNLNES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 545 QKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQKV---- 620
Cdd:TIGR00376 162 QKEAVLFALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLlksn 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 621 -----------HP------DIRK----------------------FTEEEICK------------SKSIKS-----ITH- 643
Cdd:TIGR00376 242 kqhsldylienHPkyqivaDIREkidelieernkktkpspqkrrgLSDIKILRkalkkreargieSLKIASmaewiETNk 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 644 -----LEELYNNQPVVA--------TTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFYSHKFVLVGDHQQLPPLV 710
Cdd:TIGR00376 322 sidrlLKLLPESEERIMneilaesdATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTI 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 711 HNTEARDLgmSESLFKRLEQNKNAVVQ-LTVQYRMNSKIMSLSNKLVYEGKLECGSEKVSKATVILPNLknlklelelfa 789
Cdd:TIGR00376 402 LSHDAEEL--SLTLFERLIKEYPERSRtLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLPKV----------- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 790 dsSETWLKETLEPNNPVCFLNTEKVPAPEQAEKGGVS--NVTEAKLVLFLTTFFIKAGCKASDIGIVSPYRHQLKIITDL 867
Cdd:TIGR00376 469 --EATESEDDLETGIPLLFIDTSGCELFELKEADSTSkyNPGEAELVSEIIQALVKMGVPANDIGVITPYDAQVDLLRQL 546
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985390546 868 MTSSCIStVEVNTVDKYQGRDKSIIIVSFVRNNNDGNLGtLLMDWRRLNVAITRAKHKLIMVG 930
Cdd:TIGR00376 547 LEHRHID-IEVSSVDGFQGREKEVIIISFVRSNRKGEVG-FLKDLRRLNVALTRARRKLIVIG 607
Dna2 pfam08696
DNA replication factor Dna2; Dna2 is a DNA replication factor with single-stranded ...
2-197 4.22e-72

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: 236.69  E-value: 4.22e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546   2 YSVPVVPGDIIHLEGDCHSGTWIINRDSGYLILYPDLLLSGTTVSNSIRCMRKAVLSEKFRTCESSSRQMLIGTILHETF 81
Cdd:pfam08696  17 VETPVEPGDIIHIIGEFESGQCIIDNDSNLLILHPDILISATSVAGSFFCLRRAVLQERFKGSGESSKPMLIGTILHELF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  82 QQGVPNN-FAHEKLQELAFRTVHgpKYLKEMYYLNLKQEEIMQEIEEYLPSISKWAEDFMHKPSQANHNKMQLKlpsegk 160
Cdd:pfam08696  97 QEALTANdWDLEFLEELLDELLE--KYLEELYALGETEEEAKEELMEYLPNIQEWAQKYVKKSPKPNAVVEDGN------ 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1985390546 161 ieDLSCNIEVTEFLDIEENIWSPRFGLKGKIDVTVGV 197
Cdd:pfam08696 169 --GKKVKLSISKLLDIEENIWSPMYGLKGKIDATVEV 203
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
720-932 4.68e-67

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: 222.81  E-value: 4.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 720 MSESLFKRL-EQNKNAVVQLTVQYRMNSKIMSLSNKLVYEGKLECGSEKVSKATVILPNlknlklelelfadssetwlke 798
Cdd:pfam13087   1 LDRSLFERLqELGPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFH--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 799 TLEPNNPVCFLNTEKVPAPEQAEKGGVSNVTEAKLVLFLTTFFIKAGCKA-SDIGIVSPYRHQLKIITDLMTSSC--IST 875
Cdd:pfam13087  60 LPDPLGPLVFIDVDGSEEEESDGGTSYSNEAEAELVVQLVEKLIKSGPEEpSDIGVITPYRAQVRLIRKLLKRKLggKLE 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985390546 876 VEVNTVDKYQGRDKSIIIVSFVRNNNDGNLGtLLMDWRRLNVAITRAKHKLIMVGCV 932
Cdd:pfam13087 140 IEVNTVDGFQGREKDVIIFSCVRSNEKGGIG-FLSDPRRLNVALTRAKRGLIIVGNA 195
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
613-948 3.54e-66

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 238.49  E-value: 3.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 613 RLGRAQKVHPDIRKFTEEEICKSKSIKSIThLEELYNNQPVVATTCMGVNHPIFARK-LFDFCIVDEASQISQPICLGPL 691
Cdd:COG1112   498 KLIAELREAARLRRALRRELKKRRELRKLL-WDALLELAPVVGMTPASVARLLPLGEgSFDLVIIDEASQATLAEALGAL 576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 692 FYSHKFVLVGDHQQLPPLV---HNTEARDLGMSESLFKRL-EQNKNAVVQLTVQYRMNSKIMSLSNKLVYEGKLECGSEK 767
Cdd:COG1112   577 ARAKRVVLVGDPKQLPPVVfgeEAEEVAEEGLDESLLDRLlARLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSP 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 768 VSkatvilpnlknlklelelfadssetwlKETLEPNNPVCFLNtekVPAPEQAEKGGVSNVTEAKLVLFLTTFFIKAGCK 847
Cdd:COG1112   657 KA---------------------------RRLADPDSPLVFID---VDGVYERRGGSRTNPEEAEAVVELVRELLEDGPD 706
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 848 ASDIGIVSPYRHQLKIITDLMTSSCIST---VEVNTVDKYQGRDKSIIIVSFVRNNND---GNLGTLLMDWRRLNVAITR 921
Cdd:COG1112   707 GESIGVITPYRAQVALIRELLREALGDGlepVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNGGPRRLNVAVSR 786
                         330       340
                  ....*....|....*....|....*..
gi 1985390546 922 AKHKLIMVGCvPSLCRYPPLEKLLCHL 948
Cdd:COG1112   787 ARRKLIVVGS-RELLDSDPSTPALKRL 812
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
744-948 2.45e-53

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 183.97  E-value: 2.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 744 MNSKIMSLSNKLVYEGKLECGSEKVSKatvilpnlknlklelelfadsseTWLKETLEPNNPVCFLNTEKvpaPEQAEKG 823
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVAAR-----------------------LNPPPLPGPSKPLVFVDVSG---GEEREES 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 824 GVS--NVTEAKLVLFLTTFFIKAGCKASDIGIVSPYRHQLKIITDLMTSSC--ISTVEVNTVDKYQGRDKSIIIVSFVRN 899
Cdd:cd18808    55 GTSksNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRS 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1985390546 900 NNDGNLGTLLMDWRRLNVAITRAKHKLIMVGCVPSLCRYPPLEKLLCHL 948
Cdd:cd18808   135 NESGGSIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
541-743 1.36e-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: 153.53  E-value: 1.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 541 LNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRAQKV 620
Cdd:cd18044     2 LNDSQKEAVKFALSQKDVALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPARL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 621 HPDIRKFTEEEICKSKsiksithleelynnqpVVATTCMGVNHPIFARK-LFDFCIVDEASQISQPICLGPLFYSHKFVL 699
Cdd:cd18044    82 LESVLDHSLDALVAAQ----------------VVLATNTGAGSRQLLPNeLFDVVVIDEAAQALEASCWIPLLKARRCIL 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1985390546 700 VGDHQQLPPLVHNTEARDLGMSESLFKRLEQNKN--AVVQLTVQYR 743
Cdd:cd18044   146 AGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGesVVRMLTVQYR 191
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
541-743 3.23e-37

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: 139.69  E-value: 3.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 541 LNKPQKQAMKQVLlSKDYTLIVGMPGTGKTTTICALV-RILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRL---GR 616
Cdd:cd18039     2 LNHSQVDAVKTAL-QRPLSLIQGPPGTGKTVTSATIVyHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLcakSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 617 AQ--------KVHPDIRKFTE--------------EEICKS---KSIKSITHLE-ELYNNQPVVATTCMGVNHPIFARKL 670
Cdd:cd18039    81 EAvespvsflALHNQVRNLDSaeklellkllkletGELSSAdekRYRKLKRKAErELLRNADVICCTCVGAGDPRLSKMK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985390546 671 FDFCIVDEASQISQPICLGPLFY-SHKFVLVGDHQQLPPLVHNTEARDLGMSESLFKRLEQNKNAVVQLTVQYR 743
Cdd:cd18039   161 FRTVLIDEATQATEPECLIPLVHgAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
541-743 6.72e-36

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: 135.42  E-value: 6.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 541 LNKPQKQAMKQVLL-SKDYTLIVGMPGTGKTTTICALVRILYA-------------------------CGFSVLLTSFTH 594
Cdd:cd18042     1 LNESQLEAIASALQnSPGITLIQGPPGTGKTKTIVGILSVLLAgkyrkyyekvkkklrklqrnlnnkkKKNRILVCAPSN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 595 TAVDNILLKLARfkvGFLRLGRAQKVHPDIRKFTEEEICKSksiksithleeLYNNQPVVATTCMGVNHPIFAR--KLFD 672
Cdd:cd18042    81 AAVDEIVLRLLS---EGFLDGDGRSYKPNVVRVGRQELRAS-----------ILNEADIVCTTLSSSGSDLLESlpRGFD 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985390546 673 FCIVDEASQISQPICLGPL-FYSHKFVLVGDHQQLPPLVHNTEARDLGMSESLFKRLEQNKNAVVQLTVQYR 743
Cdd:cd18042   147 TVIIDEAAQAVELSTLIPLrLGCKRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
558-743 7.52e-32

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: 120.42  E-value: 7.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 558 YTLIVGMPGTGKTTTICALVRIL--YACGFSVLLTSFTHTAVDNIllklarfkvgflrlgraqkvhpdirkfteeeicks 635
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLlkGLRGKRVLVTAQSNVAVDNV----------------------------------- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 636 ksiksithleelynnqpvvattcmgvnhpifarklfDFCIVDEASQISQPICLGPLFYSHKFVLVGDHQQLPPLVHNTEA 715
Cdd:cd17934    46 ------------------------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQEDHA 89
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1985390546 716 RDLG----MSESLFKRLEQNKNAVVQLTVQYR 743
Cdd:cd17934    90 ALLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
544-711 4.68e-29

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: 116.67  E-value: 4.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 544 PQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFS-------VLLTSFTHTAVDNILLKLAR----FKVGFL 612
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPGTGKTTTIVELIRQLLSYPATsaaagprILVCAPSNAAVDNILERLLRkgqkYGPKIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 613 RLGRAQKVHPDIRKFT-----------------------------------EEEICKSKSIKSITHL------------- 644
Cdd:pfam13086  81 RIGHPAAISEAVLPVSldylvesklnneedaqivkdiskeleklakalrafEKEIIVEKLLKSRNKDkskleqerrklrs 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 645 -----------------EELYNNQPVVATTCMGVNHPIFAR-KLFDFCIVDEASQISQPICLGPLFY-SHKFVLVGDHQQ 705
Cdd:pfam13086 161 erkelrkelrrreqsleREILDEAQIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRgPKKVVLVGDPKQ 240

                  ....*.
gi 1985390546 706 LPPLVH 711
Cdd:pfam13086 241 LPPTVI 246
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
541-743 7.42e-27

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: 109.63  E-value: 7.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 541 LNKPQKQAMKQVLLSKD----YtLIVGMPGTGKTTTI--CAL-VRILYaCGFSVLLTSFTHTAVDNILLKLARFKVG--- 610
Cdd:cd18038     2 LNDEQKLAVRNIVTGTSrpppY-IIFGPPGTGKTVTLveAILqVLRQP-PEARILVCAPSNSAADLLAERLLNALVTkre 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 611 FLRL---GRAQK-VHPDIRKFTeeeICKSKSIKSITHLEELYNnQPVVATTCMGVNHPI---FARKLFDFCIVDEASQIS 683
Cdd:cd18038    80 ILRLnapSRDRAsVPPELLPYC---NSKAEGTFRLPSLEELKK-YRIVVCTLMTAGRLVqagVPNGHFTHIFIDEAGQAT 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985390546 684 QPICLGPLFYSHKF----VLVGDHQQLPPLVHNTEARDLGMSESLFKRL----------EQNKNAVVQLTVQYR 743
Cdd:cd18038   156 EPEALIPLSELASKntqiVLAGDPKQLGPVVRSPLARKYGLGKSLLERLmerplyykdgEYNPSYITKLLKNYR 229
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
559-753 7.99e-16

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: 77.08  E-value: 7.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 559 TLIVGMPGTGKTTTICALVRILYACGFS--VLLTSFTHTAVDNILLKLAR---FKVGFLRLGRAQKVhpdirkfteeeic 633
Cdd:cd17935    23 TMVVGPPGTGKTDVAVQIISNLYHNFPNqrTLIVTHSNQALNQLFEKIMAldiDERHLLRLGHGAKI------------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 634 ksksiksithleelynnqpvVATTCmgvNHPIFARKLF---DFC----IVDEASQISQPICLGPLFYSH---------KF 697
Cdd:cd17935    90 --------------------IAMTC---THAALKRGELvelGFKydniLMEEAAQILEIETFIPLLLQNpedgpnrlkRL 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985390546 698 VLVGDHQQLPPLVHNTEARDLG-MSESLFKRLEQNKNAVVQLTVQYRMNSKIMSLSN 753
Cdd:cd17935   147 IMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRLVRLGVPTVDLDAQGRARASISSLYN 203
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
542-711 8.69e-16

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: 74.54  E-value: 8.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 542 NKPQKQAMKQVLLSKDyTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLklarfkvgflrlgraqkvh 621
Cdd:cd18043     1 DSSQEAAIISARNGKN-VVIQGPPGTGKSQTIANIIANALARGKRVLFVSEKKAALDVVRF------------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 622 pdirkfteeeicksksiksithleelynnqPVVATTCMGVNHPI-FARKLFDFCIVDEASQISQPICLGPLFYSHKFVLV 700
Cdd:cd18043    61 ------------------------------PCWIMSPLSVSQYLpLNRNLFDLVIFDEASQIPIEEALPALFRGKQVVVV 110
                         170
                  ....*....|.
gi 1985390546 701 GDHQQLPPLVH 711
Cdd:cd18043   111 GDDKQLPPSIL 121
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
540-743 2.55e-15

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


Pssm-ID: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 77.18  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLlSKDYTLIVGMPGTGKTTTICALV--------RILYACGFS-----VLLTSFTHTAVD---NILLK 603
Cdd:cd18040     1 KLNPSQNHAVRTAL-TKPFTLIQGPPGTGKTVTGVHIAywfakqnrEIQSVSGEGdggpcVLYCGPSNKSVDvvaELLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 604 LARFKV------------------------GFLRLGRAQKVHPDI----------------------------RKFTEEE 631
Cdd:cd18040    80 VPGLKIlrvyseqietteypipneprhpnkKSERESKPNSELSSItlhhrirqpsnphsqqikafearfertqEKITEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 632 ICKSKSIKSITHLEELyNNQPVVATTCMGVNHPIFARKL-FDFCIVDEASQISQPICLGPLFYSH---KFVLVGDHQQLP 707
Cdd:cd18040   160 IKTYKILIWEARFEEL-ETVDVILCTCSEAASQKMRTHAnVKQCIVDECGMCTEPESLIPIVSAPraeQVVLIGDHKQLR 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1985390546 708 PLVHNTEARDLGMSESLFKRLEQnknAVVQLTVQYR 743
Cdd:cd18040   239 PVVQNKEAQKLGLGRSLFERYAE---KACMLDTQYR 271
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
540-742 1.14e-14

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


Pssm-ID: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 72.96  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLlSKDYTLIVGMPGTGKTTTICALVRILY-----ACGFSVLLTSFTHTAVDNILLKLARFKVG-FLR 613
Cdd:cd17936     1 TLDPSQLEALKHAL-TSELALIQGPPGTGKTFLGVKLVRALLqnqdlSITGPILVVCYTNHALDQFLEGLLDFGPTkIVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 614 LGraqkvhpdirkfteeeicksKSIKSIThleelynnqpvvaTTCMGVNHPIFARKLFDFCIVDEASQI--SQPI-CLGP 690
Cdd:cd17936    80 LG--------------------ARVIGMT-------------TTGAAKYRELLQALGPKVVIVEEAAEVleAHILaALTP 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985390546 691 LFySHkFVLVGDHQQLPPLV--HNTEARDLGMSESLFKRLEQNKNAVVQLTVQY 742
Cdd:cd17936   127 ST-EH-LILIGDHKQLRPKVnvYELTAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
525-731 2.26e-14

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: 73.56  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 525 VLPPEAKETVANILKGLNKPqkqaMKQVLLskdytlivGMPGTGKTTTIC-ALVRILYACGFS-VLLTSFTHTAVDNILL 602
Cdd:cd18078     1 DLNELQKEAVKRILGGECRP----LPYILF--------GPPGTGKTVTIIeAILQVVYNLPRSrILVCAPSNSAADLVTS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 603 KL---ARFKVG-FLRL---GRAQKVHPDIRKFTEEEICKSKsiKSITHleelynnqPVVATTC--------MG--VNHpi 665
Cdd:cd18078    69 RLhesKVLKPGdMVRLnavNRFESTVIDARKLYCRLGEDLS--KASRH--------RIVISTCstagllyqMGlpVGH-- 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 666 farklFDFCIVDEASQISQPICLGPLFYSHK----FVLVGDHQQLPPLVHNTEARDLGMSESLFKRLEQN 731
Cdd:cd18078   137 -----FTHVFVDEAGQATEPESLIPLGLISSrdgqIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNR 201
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
517-755 5.09e-13

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: 72.70  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 517 QFIQHLS--SVLPPEAKETVANILKG----LNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLT 590
Cdd:COG0507    95 RRLRRLArpALDEADVEAALAALEPRagitLSDEQREAVALALTTRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 591 SFTHTAVDNILLKLARfkvgflrlgRAQKVH------PDIRKFTEEEicksksiksithleelynnqpvvattcmgvNHP 664
Cdd:COG0507   175 APTGKAAKRLSESTGI---------EARTIHrllglrPDSGRFRHNR------------------------------DNP 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 665 IFARKLFdfcIVDEASQISQpiclgPLFYS---------HKFVLVGDHQQLPPlVhntEA----RDLgmseslfkrLEQN 731
Cdd:COG0507   216 LTPADLL---VVDEASMVDT-----RLMAAllealpragARLILVGDPDQLPS-V---GAgavlRDL---------IESG 274
                         250       260
                  ....*....|....*....|....*.
gi 1985390546 732 KNAVVQLTVQYRM--NSKIMSLSNKL 755
Cdd:COG0507   275 TVPVVELTEVYRQadDSRIIELAHAI 300
Cas4 COG1468
CRISPR/Cas system-associated exonuclease Cas4, RecB family [Defense mechanisms]; CRISPR/Cas ...
180-313 4.77e-12

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: 65.75  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 180 IWSPRFGLKGKIDVtvgvkIHRKSGTQYkimPLELKTGKESNSIEHRSQVVLYTL-LNQERRVDPEAGFLLYLKTGNMYP 258
Cdd:COG1468    61 LDSERLGLTGKIDL-----VEFEDGELV---PVEYKKSKPKPWEADRMQLCAYALlLEEMLGIPVPKGYLYYPEERKREE 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1985390546 259 VSGNRMDRRELLKLRNQLafylfHSMCKSAlgnkqthlaSLPPVIDDSRACKYCS 313
Cdd:COG1468   133 VELTEELREEVEEAIEEI-----REILESE---------KPPPPTKSKKKCKKCS 173
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
850-930 7.40e-12

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: 62.07  E-value: 7.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 850 DIGIVSPYRHQLKIITDLMTSSCIST-----VEVNTVDKYQGRDKSIIIVSFVRNNNDgnlgtllmDWRRLNVAITRAKH 924
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLQGLSLDEfdlqlVGAITIDSSQGLTFDVVTLYLPTANSL--------TPRRLYVALTRARK 83

                  ....*.
gi 1985390546 925 KLIMVG 930
Cdd:cd18786    84 RLVIYD 89
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
545-708 2.97e-11

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: 62.57  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 545 QKQAMKQVLLSKdYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDnillklarfkvgflRLGRAQKVHpdi 624
Cdd:cd17933     2 QKAAVRLVLRNR-VSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPTGKAAK--------------RLSESTGIE--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 625 rkfteeeickSKSIKSitHLEELYNNQPVvattcMGVNHPIFARKLFdfcIVDEASQISQpiclgPLFYS--------HK 696
Cdd:cd17933    64 ----------ASTIHR--LLGINPGGGGF-----YYNEENPLDADLL---IVDEASMVDT-----RLMAAllsaipagAR 118
                         170
                  ....*....|..
gi 1985390546 697 FVLVGDHQQLPP 708
Cdd:cd17933   119 LILVGDPDQLPS 130
AAA_19 pfam13245
AAA domain;
545-708 1.41e-09

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 57.23  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 545 QKQAMKQVLLSKdYTLIVGMPGTGKTTTICALVRILYACG---FSVLLTSFTHTAVDNILLKLarfkvgflrLGRAQKVH 621
Cdd:pfam13245   1 QREAVRTALPSK-VVLLTGGPGTGKTTTIRHIVALLVALGgvsFPILLAAPTGRAAKRLSERT---------GLPASTIH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 622 pdirkfteeeicksksiksithleELYNNQPVVATTCMGVNHPIFARKLFdfcIVDEASQISQPIC---LGPLFYSHKFV 698
Cdd:pfam13245  71 ------------------------RLLGFDDLEAGGFLRDEEEPLDGDLL---IVDEFSMVDLPLAyrlLKALPDGAQLL 123
                         170
                  ....*....|
gi 1985390546 699 LVGDHQQLPP 708
Cdd:pfam13245 124 LVGDPDQLPS 133
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
541-728 2.30e-09

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: 58.65  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 541 LNKPQKQAMKQVLLSKDYT----LIVGMPGTGKTTTICALVR-ILYACGFSVLLTSFTHTAVD--------------NIL 601
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQlppvLLIGPFGTGKTFTLAQAVKhILQQPETRILICTHSNSAADlyikeylhpyvetgNPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 602 LKLARFkvgFLRLGRAQKVHPDIRKFTeeeICKSKSIKSITHLEELYNNQPVVAT--TCMGVNHPIFARKLFDFCIVDEA 679
Cdd:cd18077    82 ARPLRV---YYRNRWVKTVHPVVQKYC---LIDEHGTFRMPTREDVMRHRVVVVTlsTSQYLCQLDLEPGFFTHILLDEA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1985390546 680 SQISQPICLGPLFY---SHKFVLVGDHQQLPPLVHNTEARDLGMSESLFKRL 728
Cdd:cd18077   156 AQAMECEAIMPLALatkSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
cas4 TIGR00372
CRISPR-associated protein Cas4; This model represents a family of proteins associated with ...
176-313 5.54e-09

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


Pssm-ID: 273040 [Multi-domain]  Cd Length: 178  Bit Score: 56.65  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 176 IEENIW--SPRFGLKGKIDVtvgVKIHRKsgtqyKIMPLELKTGKESNSIEHRSQVVLYTLLNQERRVDPEAGFLLYLKT 253
Cdd:TIGR00372  54 EEKEVPlkSKKYGLKGVIDI---VLEEDG-----ELVPVEVKSGKPSPREAHKYQLLAYAYLLEEMYGEIVRGYILYINA 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 254 GNMYPVSGNRMDRRELLKLrnqlaFYLFHSMCKSALgnkqthlasLPPVIDDSRACKYCS 313
Cdd:TIGR00372 126 GKKLEVEISEELRKKAVKL-----IEKIRELLEGGK---------PPSPPKSGPKCKFCP 171
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
540-708 1.60e-08

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


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 55.65  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLLSKD-YTLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDnillklarfkvgflRLGraq 618
Cdd:pfam13604   1 TLNAEQAAAVRALLTSGDrVAVLVGPAGTGKTTALKALREAWEAAGYRVIGLAPTGRAAK--------------VLG--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 619 kvhpdirkfteeeicKSKSIKSIThleelynnqpvVA--TTCMGVNHPIFARKLFdfcIVDEASQISQPIcLGPLF---- 692
Cdd:pfam13604  64 ---------------EELGIPADT-----------IAklLHRLGGRAGLDPGTLL---IVDEAGMVGTRQ-MARLLklae 113
                         170
                  ....*....|....*..
gi 1985390546 693 -YSHKFVLVGDHQQLPP 708
Cdd:pfam13604 114 dAGARVILVGDPRQLPS 130
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
559-742 1.64e-07

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


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 50.95  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 559 TLIVGMPGTGKTTT----ICALVRILYACGFSVLLTSFTHTAVDNillklarfkvgflrlgraqkvhpdirkfteeeick 634
Cdd:cd17914     2 SLIQGPPGTGKTRVlvkiVAALMQNKNGEPGRILLVTPTNKAAAQ----------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 635 sksiksithleelynnqpvvattcmgvnhpifarklFDFCIVDEASQISQPIC--LGPLFYSHKFV-LVGDHQQLPPLVH 711
Cdd:cd17914    47 ------------------------------------LDNILVDEAAQILEPETsrLIDLALDQGRViLVGDHDQLGPVWR 90
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1985390546 712 NTEARDLGMSESLFKRLEQNKNAVVQLTVQY 742
Cdd:cd17914    91 GAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
Cas4_I-A_I-B_I-C_I-D_II-B cd09637
CRISPR/Cas system-associated protein Cas4; CRISPR (Clustered Regularly Interspaced Short ...
176-313 1.37e-06

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


Pssm-ID: 187768 [Multi-domain]  Cd Length: 178  Bit Score: 49.74  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 176 IEENIW--SPRFGLKGKIDvtvgvkIHRKSGTQYkiMPLELKTGKESNSIE-HRSQVVLYTLLNQERRVDPEA-GFLLYL 251
Cdd:cd09637    54 EEKEVPlkSKKYGLKGVID------IVLKEDGEL--VPVEVKSGRAGSPREaHKLQLVAYAYLLEEMYGKRVArGYIVYL 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985390546 252 KTGNMYPVSGNRMDRRELLKLRNQLAFYLFHSmcksalgnkqthlasLPPVIDDSRACKYCS 313
Cdd:cd09637   126 EGGKRLEVEISEELRKKAEKLLEEIRKLLEGE---------------LPPPVKSSPKCKFCP 172
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
540-624 1.29e-04

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: 43.29  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 540 GLNKPQKQAMKQVLLSKDY--TLIVGMPGTGKTTTICALVRILYACGFSVLLTSFTHTAVDNILLKLARFKVGFLRLGRA 617
Cdd:cd00009     1 VGQEEAIEALREALELPPPknLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELA 80

                  ....*..
gi 1985390546 618 QKVHPDI 624
Cdd:cd00009    81 EKAKPGV 87
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
560-708 3.02e-04

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: 43.34  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 560 LIVGMPGTGKTTTIC-ALVRILYACGFSVLLTSFT------------HTAVDNILLKLARFKVGFLRLGRAQkVHPDirk 626
Cdd:cd18076    27 LIYGPFGTGKTFTLAmAALEVIREPGTKVLICTHTnsaadiyireyfHPYVDKGHPEARPLRIKATDRPNAI-TDPD--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 627 fTEEEICKSKSIKSITH-LEELYNNQPVVATTCMGVNHPIFARKLFDFCIVDEASQISQPICLGPLFY-SHK--FVLVGD 702
Cdd:cd18076   103 -TITYCCLTKDRQCFRLpTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLECEALIPLSYaGPKtrVVLAGD 181

                  ....*.
gi 1985390546 703 HQQLPP 708
Cdd:cd18076   182 HMQMTP 187
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
559-592 1.48e-03

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


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 39.90  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1985390546 559 TLIVGMPGTGKTTTICALVRILYACGFSVLLTSF 592
Cdd:cd01127     2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVIITDP 35
DEXDc smart00487
DEAD-like helicases superfamily;
541-679 2.98e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 40.17  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  541 LNKPQKQAMKQVLLSKDYTLIVGMPGTGKTTTIC--ALVRILYACGFSVLLTSFTHTAVDNILLKLARFkVGFLRLGRAQ 618
Cdd:smart00487   9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALlpALEALKRGKGGRVLVLVPTRELAEQWAEELKKL-GPSLGLKVVG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985390546  619 KVHPDIRKFTEEEIcksksIKSITHLeelynnqpVVATTCMGVNHPIFARKL---FDFCIVDEA 679
Cdd:smart00487  88 LYGGDSKREQLRKL-----ESGKTDI--------LVTTPGRLLDLLENDKLSlsnVDLVILDEA 138
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
498-589 5.04e-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: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546 498 ENSSASEKLRNLIIDFHKpqfiqhlSSVLPPEAKETVANILKGLNKPQkqamkqVLLskdytlIVGMPGTGKTTTICALV 577
Cdd:TIGR00064  38 KKVKDAEKLKEILKEYLK-------EILKEDLLKNTDLELIVEENKPN------VIL------FVGVNGVGKTTTIAKLA 98
                          90
                  ....*....|..
gi 1985390546 578 RILYACGFSVLL 589
Cdd:TIGR00064  99 NKLKKQGKSVLL 110
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
559-676 6.84e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390546  559 TLIVGMPGTGKTTTICALVRILYACGFSVLLTS-----------FTHTAVDNILLKLARFKVGFLRLGRAQKVHPDI--- 624
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedileevldqLLLIIVGGKKASGSGELRLRLALALARKLKPDVlil 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985390546  625 -------RKFTEEEICKSKSIKSITHLEELYNNQPVVATTCMGVNHPIFARKLFDFCIV 676
Cdd:smart00382  85 deitsllDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
 
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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