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Conserved domains on  [gi|2427732186|ref|WP_270671208|]
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HsdR family type I site-specific deoxyribonuclease, partial [Aeromonas sp. QDB33]

Protein Classification

HsdR family type I site-specific deoxyribonuclease( domain architecture ID 1000693)

HsdR family type I site-specific deoxyribonuclease is involved in the endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolysed; similar to Escherichia coli type I restriction enzyme EcoR124II R protein, which recognizes 5'-GAAN(7)RTCG-3'

EC:  3.1.21.3
Gene Ontology:  GO:0009035|GO:0009307|GO:0003677|GO:0005524|GO:0016887|GO:0004386
PubMed:  15788748|24068554|32483229|12654995

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG0610 super family cl33974
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 7-388 3.24e-142

Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];


The actual alignment was detected with superfamily member COG0610:

Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 427.36  E-value: 3.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKG-EHKKRPDLVLYVNGIALGVIELKRST--VSVSEGIHQNLDNQKKdfIRNFFTTMQLVMAG 83
Cdd:COG0610   108 FKNPENNDFLVVNQFTVSGgNYKRRPDVVLFVNGLPLVVIELKNPLtqVTIKEAFNQIQRYRRE--IPGLFAYNQLFVIS 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  84 nDTQGVRYGTIETHEKYYLEWKEpadpIHSDHVDLPSANLLDQHLAQLCSKARFLELIHDFIVFDA----GTKKTCRHNQ 159
Cdd:COG0610   186 -DGVEARYGTNTAPFEFFLPWKD----GDGNDLNPDGITDLDYLIEGLLSKERLLDIIRNFIVFDEdeggLIKIVARYHQ 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 160 YFGIRAAKAYIRRRDG----GIIWHTQGSGKSLTMVWMAKWIRENVT--DSRVLIITDRTELDEQIEKVFSGVEEE-ILR 232
Cdd:COG0610   261 YFAVRKAVERVKEAEGdgkgGVIWHTQGSGKSLTMVFLAQKLARLPDldNPTVVVVTDRKDLDDQLFDTFKAFGREsVVQ 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 233 TKSGADLVTRLHAHNPWLICSLVHKFGRtpegesddeddgssddfiaDMRRSLPSDFSPKGQLFVFVDECHRTQSGKLHG 312
Cdd:COG0610   341 AESRADLRELLESDSGGIIVTTIQKFPE-------------------ALDEIKYPELSDRKNIIVIVDEAHRSQYGGLAK 401

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427732186 313 AMKSLLPEALFIGFTGTPLMKQDkKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDIDQRVKsQKKVDEWFDTK 388
Cdd:COG0610   402 NMRDALPNASFFGFTGTPIFKED-RTTLEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLD-KEKIDEEFDEL 475
 
Name Accession Description Interval E-value
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 7-388 3.24e-142

Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];


Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 427.36  E-value: 3.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKG-EHKKRPDLVLYVNGIALGVIELKRST--VSVSEGIHQNLDNQKKdfIRNFFTTMQLVMAG 83
Cdd:COG0610   108 FKNPENNDFLVVNQFTVSGgNYKRRPDVVLFVNGLPLVVIELKNPLtqVTIKEAFNQIQRYRRE--IPGLFAYNQLFVIS 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  84 nDTQGVRYGTIETHEKYYLEWKEpadpIHSDHVDLPSANLLDQHLAQLCSKARFLELIHDFIVFDA----GTKKTCRHNQ 159
Cdd:COG0610   186 -DGVEARYGTNTAPFEFFLPWKD----GDGNDLNPDGITDLDYLIEGLLSKERLLDIIRNFIVFDEdeggLIKIVARYHQ 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 160 YFGIRAAKAYIRRRDG----GIIWHTQGSGKSLTMVWMAKWIRENVT--DSRVLIITDRTELDEQIEKVFSGVEEE-ILR 232
Cdd:COG0610   261 YFAVRKAVERVKEAEGdgkgGVIWHTQGSGKSLTMVFLAQKLARLPDldNPTVVVVTDRKDLDDQLFDTFKAFGREsVVQ 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 233 TKSGADLVTRLHAHNPWLICSLVHKFGRtpegesddeddgssddfiaDMRRSLPSDFSPKGQLFVFVDECHRTQSGKLHG 312
Cdd:COG0610   341 AESRADLRELLESDSGGIIVTTIQKFPE-------------------ALDEIKYPELSDRKNIIVIVDEAHRSQYGGLAK 401

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427732186 313 AMKSLLPEALFIGFTGTPLMKQDkKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDIDQRVKsQKKVDEWFDTK 388
Cdd:COG0610   402 NMRDALPNASFFGFTGTPIFKED-RTTLEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLD-KEKIDEEFDEL 475
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
 7-386 1.31e-95

type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I restriction and modification system which is composed of three polypeptides R (restriction endonuclease), M (modification) and S (specificity). This group of enzymes recognize specific short DNA sequences and have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. They also catalyse the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.(J. Mol. Biol. 271 (3), 342-348 (1997)). Members of this family are assumed to differ from each other in DNA site specificity. [DNA metabolism, Restriction/modification]


Pssm-ID: 273028 [Multi-domain]  Cd Length: 667  Bit Score: 299.32  E-value: 1.31e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKGeHKKRPDLVLYVNGIALGVIELKRSTVSVSEGIHQNLDNQKKdfIRNFFTTMQLVMAGNDT 86
Cdd:TIGR00348  98 FRNISQNIFQFANQVSFKG-HNIRPDVTLFVNGIPLVIIELKKRSVTIREAFNQIKRYEKE--IPELFKYVQIFVISNGT 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  87 QGVRY-GTIETHEKYYLEWKEpadpihsdhVDLPSANLLDQHLAQLCSKARFLELIHDFIVFDAG----TKKTCRHNQYF 161
Cdd:TIGR00348 175 DTRYYtGSDEDDFDFTFNWKE---------SDNKLIEDLKEFDILLLKKERLLDFIRNFIIFDKDtglvTKPYQRYMQYR 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 162 GIRAAKAYIRR------RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFSGVEEEIL-RTK 234
Cdd:TIGR00348 246 AVKKIVESITRktwgkdERGGLIWHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQKDCAeRIE 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 235 SGADLVTRLHAHNPWLICSLVHKFGRTpegesddeddgssddfIADMRRSLPSDfspKGQLFVFVDECHRTQSGKLHGAM 314
Cdd:TIGR00348 326 SIAELKELLEKDDGGIIITTIQKFDDK----------------LKEEEEKFPVD---RKEVVVIFDEAHRSQYGELAKNL 386

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2427732186 315 KSLLPEALFIGFTGTPLMKQDKKKSIE---VFGPYIHTYKFNEAVSDGVVLDLRYEARdIDQRVKSQKKVDEWFD 386
Cdd:TIGR00348 387 KKALKNASFFGFTGTPIFKKDRDTSLTfayVFGRYLHRYFITDAIRDGLTVKIDYEDR-LPEDHLDKKKLDAFFD 460
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
 159-386 2.45e-86

SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 260.83  E-value: 2.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 159 QYFGIRAAKAYIRR---RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFSGVEEEIL-RTK 234
Cdd:pfam18766   2 QYFAVNKAVERVLEdgdRRGGVIWHTQGSGKSLTMVFLARKLRRELKNPTVVVVTDRNDLDDQLTKTFAACGREVPvQAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 235 SGADLVTRLHAHNPwLICSLVHKFGRTPEGESDDeddgssddfiadmrrslpsdFSPKGQLFVFVDECHRTQSGKLHGAM 314
Cdd:pfam18766  82 SRKDLRELLRGSGG-IIFTTIQKFGETPDEGFPV--------------------LSDRRNIIVLVDEAHRSQYGGLAANM 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427732186 315 KSLLPEALFIGFTGTPLMKQDkKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDIDQRVKsQKKVDEWFD 386
Cdd:pfam18766 141 RDALPNAAFIGFTGTPILKKD-KNTRAVFGDYIDTYTIQDAVEDGATVPILYEGRLAELELD-DEALDEEFE 210
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
 137-352 1.47e-79

DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. 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: 350788 [Multi-domain]  Cd Length: 208  Bit Score: 243.29  E-value: 1.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 137 FLELIHDFIVFDAG---TKKTCRHNQYFGIRAAKAYIRR-------RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRV 206
Cdd:cd18030     1 LLDVLRNFIVFDEDddkTKKVARYYQYYAVEAALERIKTatnkdgdKKGGYIWHTQGSGKSLTMFKAAKLLIEDPKNPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 207 LIITDRTELDEQIEKVFSGVE-EEILRTKSGADLVTRLHAHNPWLICSLVHKFGRtpegesddeddgssddfiaDMRRSL 285
Cdd:cd18030    81 VFVVDRKDLDYQTSSTFSRFAaEDVVRANSTKELKELLKNLSGGIIVTTIQKFNN-------------------AVKEES 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2427732186 286 PSDFSPKGQLFVFVDECHRTQSGKLHGAMKSLLPEALFIGFTGTPLMKQDKKKSIEVFGPYIHTYKF 352
Cdd:cd18030   142 KPVLIYRKNIVVIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEGDKTTEKVFGDYLHKYTI 208
DEXDc smart00487
DEAD-like helicases superfamily;
164-330 2.02e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 54.04  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  164 RAAKAYIRRRDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFS-------GVEEEILRTKSG 236
Cdd:smart00487  15 EAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKklgpslgLKVVGLYGGDSK 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  237 ADLVTRLHAHNP-WLICslvhkfgrTPEGesddeddgssddfiadMRRSLPSDFSPKGQL-FVFVDECHRT----QSGKL 310
Cdd:smart00487  95 REQLRKLESGKTdILVT--------TPGR----------------LLDLLENDKLSLSNVdLVILDEAHRLldggFGDQL 150

                          170       180
                   ....*....|....*....|
gi 2427732186  311 HGAMKSLLPEALFIGFTGTP 330
Cdd:smart00487 151 EKLLKLLPKNVQLLLLSATP 170
 
Name Accession Description Interval E-value
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 7-388 3.24e-142

Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];


Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 427.36  E-value: 3.24e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKG-EHKKRPDLVLYVNGIALGVIELKRST--VSVSEGIHQNLDNQKKdfIRNFFTTMQLVMAG 83
Cdd:COG0610   108 FKNPENNDFLVVNQFTVSGgNYKRRPDVVLFVNGLPLVVIELKNPLtqVTIKEAFNQIQRYRRE--IPGLFAYNQLFVIS 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  84 nDTQGVRYGTIETHEKYYLEWKEpadpIHSDHVDLPSANLLDQHLAQLCSKARFLELIHDFIVFDA----GTKKTCRHNQ 159
Cdd:COG0610   186 -DGVEARYGTNTAPFEFFLPWKD----GDGNDLNPDGITDLDYLIEGLLSKERLLDIIRNFIVFDEdeggLIKIVARYHQ 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 160 YFGIRAAKAYIRRRDG----GIIWHTQGSGKSLTMVWMAKWIRENVT--DSRVLIITDRTELDEQIEKVFSGVEEE-ILR 232
Cdd:COG0610   261 YFAVRKAVERVKEAEGdgkgGVIWHTQGSGKSLTMVFLAQKLARLPDldNPTVVVVTDRKDLDDQLFDTFKAFGREsVVQ 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 233 TKSGADLVTRLHAHNPWLICSLVHKFGRtpegesddeddgssddfiaDMRRSLPSDFSPKGQLFVFVDECHRTQSGKLHG 312
Cdd:COG0610   341 AESRADLRELLESDSGGIIVTTIQKFPE-------------------ALDEIKYPELSDRKNIIVIVDEAHRSQYGGLAK 401

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427732186 313 AMKSLLPEALFIGFTGTPLMKQDkKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDIDQRVKsQKKVDEWFDTK 388
Cdd:COG0610   402 NMRDALPNASFFGFTGTPIFKED-RTTLEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLD-KEKIDEEFDEL 475
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
 7-386 1.31e-95

type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I restriction and modification system which is composed of three polypeptides R (restriction endonuclease), M (modification) and S (specificity). This group of enzymes recognize specific short DNA sequences and have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine. They also catalyse the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.(J. Mol. Biol. 271 (3), 342-348 (1997)). Members of this family are assumed to differ from each other in DNA site specificity. [DNA metabolism, Restriction/modification]


Pssm-ID: 273028 [Multi-domain]  Cd Length: 667  Bit Score: 299.32  E-value: 1.31e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKGeHKKRPDLVLYVNGIALGVIELKRSTVSVSEGIHQNLDNQKKdfIRNFFTTMQLVMAGNDT 86
Cdd:TIGR00348  98 FRNISQNIFQFANQVSFKG-HNIRPDVTLFVNGIPLVIIELKKRSVTIREAFNQIKRYEKE--IPELFKYVQIFVISNGT 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  87 QGVRY-GTIETHEKYYLEWKEpadpihsdhVDLPSANLLDQHLAQLCSKARFLELIHDFIVFDAG----TKKTCRHNQYF 161
Cdd:TIGR00348 175 DTRYYtGSDEDDFDFTFNWKE---------SDNKLIEDLKEFDILLLKKERLLDFIRNFIIFDKDtglvTKPYQRYMQYR 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 162 GIRAAKAYIRR------RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFSGVEEEIL-RTK 234
Cdd:TIGR00348 246 AVKKIVESITRktwgkdERGGLIWHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQKDCAeRIE 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 235 SGADLVTRLHAHNPWLICSLVHKFGRTpegesddeddgssddfIADMRRSLPSDfspKGQLFVFVDECHRTQSGKLHGAM 314
Cdd:TIGR00348 326 SIAELKELLEKDDGGIIITTIQKFDDK----------------LKEEEEKFPVD---RKEVVVIFDEAHRSQYGELAKNL 386

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2427732186 315 KSLLPEALFIGFTGTPLMKQDKKKSIE---VFGPYIHTYKFNEAVSDGVVLDLRYEARdIDQRVKSQKKVDEWFD 386
Cdd:TIGR00348 387 KKALKNASFFGFTGTPIFKKDRDTSLTfayVFGRYLHRYFITDAIRDGLTVKIDYEDR-LPEDHLDKKKLDAFFD 460
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
 159-386 2.45e-86

SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 260.83  E-value: 2.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 159 QYFGIRAAKAYIRR---RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFSGVEEEIL-RTK 234
Cdd:pfam18766   2 QYFAVNKAVERVLEdgdRRGGVIWHTQGSGKSLTMVFLARKLRRELKNPTVVVVTDRNDLDDQLTKTFAACGREVPvQAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 235 SGADLVTRLHAHNPwLICSLVHKFGRTPEGESDDeddgssddfiadmrrslpsdFSPKGQLFVFVDECHRTQSGKLHGAM 314
Cdd:pfam18766  82 SRKDLRELLRGSGG-IIFTTIQKFGETPDEGFPV--------------------LSDRRNIIVLVDEAHRSQYGGLAANM 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427732186 315 KSLLPEALFIGFTGTPLMKQDkKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDIDQRVKsQKKVDEWFD 386
Cdd:pfam18766 141 RDALPNAAFIGFTGTPILKKD-KNTRAVFGDYIDTYTIQDAVEDGATVPILYEGRLAELELD-DEALDEEFE 210
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
 137-352 1.47e-79

DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of type I restriction-modification enzymes contains the DNA cleavage and ATP-dependent DNA translocation activities of the heteromeric complex. 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: 350788 [Multi-domain]  Cd Length: 208  Bit Score: 243.29  E-value: 1.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 137 FLELIHDFIVFDAG---TKKTCRHNQYFGIRAAKAYIRR-------RDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRV 206
Cdd:cd18030     1 LLDVLRNFIVFDEDddkTKKVARYYQYYAVEAALERIKTatnkdgdKKGGYIWHTQGSGKSLTMFKAAKLLIEDPKNPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 207 LIITDRTELDEQIEKVFSGVE-EEILRTKSGADLVTRLHAHNPWLICSLVHKFGRtpegesddeddgssddfiaDMRRSL 285
Cdd:cd18030    81 VFVVDRKDLDYQTSSTFSRFAaEDVVRANSTKELKELLKNLSGGIIVTTIQKFNN-------------------AVKEES 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2427732186 286 PSDFSPKGQLFVFVDECHRTQSGKLHGAMKSLLPEALFIGFTGTPLMKQDKKKSIEVFGPYIHTYKF 352
Cdd:cd18030   142 KPVLIYRKNIVVIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEGDKTTEKVFGDYLHKYTI 208
HsdR_N cd22332
N-terminal domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I and ...
 7-143 1.87e-36

N-terminal domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I and similar systems; The N-terminal endonuclease-like domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I belongs to a wider 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: 411736 [Multi-domain]  Cd Length: 226  Bit Score: 132.39  E-value: 1.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   7 WTNPQANDFALAEEVTVKGE-HKKRPDLVLYVNGIALGVIELKRSTVSVSEGIHQNLDNQKKDFIRNFFTTMQLVMAGND 85
Cdd:cd22332    94 FENPENNDFQVVNQFTVEGGkHNRRPDVVLFVNGLPLVVIELKNPGVTIREAYNQIKRYYKEIFIPGLFKYNQLFVISNG 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2427732186  86 TQgVRYGTIETHEKYYLEWKEpadpIHSDHVDLPSANLLDQHLAQLCSKARFLELIHD 143
Cdd:cd22332   174 TE-TRYGANTAPYERFNEWFT----FDWADEDNEPITDLETFIKGLLSKERLLDLIRN 226
HSDR_N pfam04313
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 2-99 3.73e-17

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


Pssm-ID: 427858 [Multi-domain]  Cd Length: 151  Bit Score: 77.73  E-value: 3.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186   2 GEPLHWTNPQANDFALAEEVTVKGEHKKRPDLVLYVNGIALGVIELKRStvSVSEGIHQnLDNQKKDFIRNF-----FTT 76
Cdd:pfam04313  52 GVTDGITKTENNSFQVANQVEVKGVQKRRPDYVLFVNGLPLAVIELKRP--GTEEAINQ-IRRYEKDSFNAIpqlfrYAN 128

                          90       100
                  ....*....|....*....|...
gi 2427732186  77 MQLVMAGNDTQGVRYGTIETHEK 99
Cdd:pfam04313 129 VQFGILSNGRETRFYTKTAKENR 151
ResIII pfam04851
Type III restriction enzyme, res subunit;
156-330 3.44e-13

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 66.93  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 156 RHNQYFGIRAAKAYIRRRD-GGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQ----IEKVFSGVEEEI 230
Cdd:pfam04851   5 RPYQIEAIENLLESIKNGQkRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQaleeFKKFLPNYVEIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 231 LRTKSGADLVTRLHAHnpwLICSLVHKFGRtpegesddeddgssddfiADMRRSLPsdFSPKGQLFVFVDECHRTQSGKl 310
Cdd:pfam04851  85 EIISGDKKDESVDDNK---IVVTTIQSLYK------------------ALELASLE--LLPDFFDVIIIDEAHRSGASS- 140

                         170       180
                  ....*....|....*....|
gi 2427732186 311 HGAMKSLLPEALFIGFTGTP 330
Cdd:pfam04851 141 YRNILEYFKPAFLLGLTATP 160
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
163-372 4.27e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 64.28  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 163 IRAAKAYIRRRDG-GIIWHTQGSGKSLTMvwmAKWIRENVTDSRVLIITDRTELDEQIEKVFsgveEEILRTKSGADLVT 241
Cdd:COG1061    89 LEALLAALERGGGrGLVVAPTGTGKTVLA---LALAAELLRGKRVLVLVPRRELLEQWAEEL----RRFLGDPLAGGGKK 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 242 RLHAhnPWLICSlVHKFGRtpegesddeddgssddfiADMRRSLPSDFSpkgqlFVFVDECHRTQSGKLHGAMKsLLPEA 321
Cdd:COG1061   162 DSDA--PITVAT-YQSLAR------------------RAHLDELGDRFG-----LVIIDEAHHAGAPSYRRILE-AFPAA 214

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2427732186 322 LFIGFTGTPLMKQDKKKSIEVFGPYIHTYKFNEAVSDGVVLDLRYEARDID 372
Cdd:COG1061   215 YRLGLTATPFRSDGREILLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVD 265
DEXDc smart00487
DEAD-like helicases superfamily;
164-330 2.02e-08

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 54.04  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  164 RAAKAYIRRRDGGIIWHTQGSGKSLTMVWMAKWIRENVTDSRVLIITDRTELDEQIEKVFS-------GVEEEILRTKSG 236
Cdd:smart00487  15 EAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKklgpslgLKVVGLYGGDSK 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  237 ADLVTRLHAHNP-WLICslvhkfgrTPEGesddeddgssddfiadMRRSLPSDFSPKGQL-FVFVDECHRT----QSGKL 310
Cdd:smart00487  95 REQLRKLESGKTdILVT--------TPGR----------------LLDLLENDKLSLSNVdLVILDEAHRLldggFGDQL 150

                          170       180
                   ....*....|....*....|
gi 2427732186  311 HGAMKSLLPEALFIGFTGTP 330
Cdd:smart00487 151 EKLLKLLPKNVQLLLLSATP 170
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 163-330 1.10e-07

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 50.77  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 163 IRAAKAYIRRRdGGIIWHTQGSGKSLTMVWMAKWIRENvtdsRVLIITDRTELDEQIEkvfsgveEEILRtksgadlvtr 242
Cdd:cd17926     9 LEAWLAHKNNR-RGILVLPTGSGKTLTALALIAYLKEL----RTLIVVPTDALLDQWK-------ERFED---------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 243 lhahnpWLICSLVHKFGRTPEGESDDEDDgssddFIADM----RRSLPSDFSPKGQLFVFVDECHRTqSGKLHGAMKSLL 318
Cdd:cd17926    67 ------FLGDSSIGLIGGGKKKDFDDANV-----VVATYqslsNLAEEEKDLFDQFGLLIVDEAHHL-PAKTFSEILKEL 134

                         170
                  ....*....|..
gi 2427732186 319 PEALFIGFTGTP 330
Cdd:cd17926   135 NAKYRLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 175-329 2.77e-05

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 43.55  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 175 GGIIWHTQGSGKSLTmvwMAKWIRENVTD--SRVLIITDRTELDEQIEKVFSGVEEEILRTK---SGADLVTRLHA---H 246
Cdd:cd00046     3 NVLITAPTGSGKTLA---ALLAALLLLLKkgKKVLVLVPTKALALQTAERLRELFGPGIRVAvlvGGSSAEEREKNklgD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 247 NPWLICSlVHKFGRtpegesddeddgssddfiaDMRRSLPSDFspKGQLFVFVDECHRT-QSGKLHGAM-----KSLLPE 320
Cdd:cd00046    80 ADIIIAT-PDMLLN-------------------LLLREDRLFL--KDLKLIIVDEAHALlIDSRGALILdlavrKAGLKN 137


                  ....*....
gi 2427732186 321 ALFIGFTGT 329
Cdd:cd00046   138 AQVILLSAT 146
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
 16-372 6.31e-05

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 45.22  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  16 ALAEEVTVKGehKKRPDLVLYV-NGIALGVIELKRSTVSVSEGIHQ------NLDNQ--KKDFIrnFFTTmqlvmaGNDT 86
Cdd:COG4096    40 VIGEWPTRGG--KGYADYVLFGdDGKPLAVVEAKRTSKDVSAGLQQaklyadGLEKQygQVPFI--FATN------GREI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186  87 QGVRYGTIETHEKYYLEWKEPAdpihsdhvDLpsANLLDQHLAQLcsKARFLELihdfivfDAGTKKTCRHNQYFGIRAA 166
Cdd:COG4096   110 WFWDDRDPYPREREVDGFPSPE--------EL--WELLKRRKGTA--RKRLATE-------PYNDGIALRYYQIEAIRRV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 167 -KAYIRRRDGGIIwhTQ--GSGK---SLTMVWM---AKWIRenvtdsRVLIITDRTELDEQIEKVFSGVEE------EIL 231
Cdd:COG4096   171 eEAIAKGQRRALL--VMatGTGKtrtAIALIYRllkAGRAK------RILFLADRNALVDQAKNAFKPFLPdldaftKLY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427732186 232 RTKSGADLVTRLHahnpwlIC---SLVHKFGRTPEGesddeddgssddfiaDMRRSLPSDFspkgqlF--VFVDECHRTQ 306
Cdd:COG4096   243 NKSKDIDKSARVY------FStyqTMMNRIDGEEEE---------------PGYRQFPPDF------FdlIIIDECHRGI 295

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2427732186 307 SGKlhgaMKSLLP--EALFIGFTGTPlmKQDKKKS-IEVFG--PyIHTYKFNEAVSDGVVLDlrYEARDID 372
Cdd:COG4096   296 YSK----WRAILDyfDALQIGLTATP--KDTIDRNtYEYFNgnP-VYTYSLEQAVADGFLVP--YKVIRID 357
 
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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