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Conserved domains on  [gi|447184992|ref|WP_001262248|]
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MULTISPECIES: DEAD/DEAH box helicase family protein [Escherichia]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HsdR super family cl34711
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
6-624 4.05e-126

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


The actual alignment was detected with superfamily member COG4096:

Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 398.45  E-value: 4.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   6 EAQARIK-INKLLESAGWRFFDDakgkanVALElnVKLSQTQINELGENFEATKNGFIDFLLLDEKNHPLVVLEAKSEDK 84
Cdd:COG4096    4 EAETRKKlIDPALKEAGWDVDDQ------ILRE--VRPTAGRNVVIGEWPTRGGKGYADYVLFGDDGKPLAVVEAKRTSK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  85 NPLVGKEQARKYAKSLD-----CRFVILSNGNLHYFWDLQQGNPHIIAV--FPTPDSLksyqkfepdQRRlitevvgrdy 157
Cdd:COG4096   76 DVSAGLQQAKLYADGLEkqygqVPFIFATNGREIWFWDDRDPYPREREVdgFPSPEEL---------WEL---------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 158 ivqtqlpgYEKEAGWLNENERSAFIAKNKLrfLREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTG 237
Cdd:COG4096  137 --------LKRRKGTARKRLATEPYNDGIA--LRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALIYRLLKAG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 238 NSHRVLFLVDRLELEEQAAKAFKDYL-KNDYVTVIYKERRDDWRKADIVVTTVQSL---LFNN---KYKRLFSPTDFDLV 310
Cdd:COG4096  207 RAKRILFLADRNALVDQAKNAFKPFLpDLDAFTKLYNKSKDIDKSARVYFSTYQTMmnrIDGEeeePGYRQFPPDFFDLI 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 311 ISDEAHRSIGGNARAVFEYFVGYKLGLTATPRDylksfdaskpttrdprEQERrlllDTYRTFGcesGQPTFRYSLLDGV 390
Cdd:COG4096  287 IIDECHRGIYSKWRAILDYFDALQIGLTATPKD----------------TIDR----NTYEYFN---GNPVYTYSLEQAV 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 391 KDGFLINPMVVDARTDITtkllsEQGYTVMApvGE---DGLQEHIFVF----------KDFEKKFFSKATNELFCQTFIK 457
Cdd:COG4096  344 ADGFLVPYKVIRIDTKFD-----REGIRYDA--GEdlsDEEGEEIELEeleedreyeaKDFNRKVVNEDTTRKVLEELME 416
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 458 NGLRdPVTGEFGKGLVFAVSQNHAARLTQILNELAdilwpGKYQSDFAVQVTSSVSDAQQYTINFTNNnllgsanfnaly 537
Cdd:COG4096  417 YLDK-PGGDRLGKTIIFAKNDDHADRIVQALRELY-----PELGGDFVKKITGDDDYGKSLIDNFKNP------------ 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 538 ktSKA-RVCVTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRkhnfleqlLDDNLKplinePEKSRFKFFDFFA 616
Cdd:COG4096  479 --EKYpRIAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTR--------LCPDLF-----PGKTHFTIFDFVG 543

                 ....*...
gi 447184992 617 NCEYFEEK 624
Cdd:COG4096  544 NTELFADP 551
 
Name Accession Description Interval E-value
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
6-624 4.05e-126

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 398.45  E-value: 4.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   6 EAQARIK-INKLLESAGWRFFDDakgkanVALElnVKLSQTQINELGENFEATKNGFIDFLLLDEKNHPLVVLEAKSEDK 84
Cdd:COG4096    4 EAETRKKlIDPALKEAGWDVDDQ------ILRE--VRPTAGRNVVIGEWPTRGGKGYADYVLFGDDGKPLAVVEAKRTSK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  85 NPLVGKEQARKYAKSLD-----CRFVILSNGNLHYFWDLQQGNPHIIAV--FPTPDSLksyqkfepdQRRlitevvgrdy 157
Cdd:COG4096   76 DVSAGLQQAKLYADGLEkqygqVPFIFATNGREIWFWDDRDPYPREREVdgFPSPEEL---------WEL---------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 158 ivqtqlpgYEKEAGWLNENERSAFIAKNKLrfLREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTG 237
Cdd:COG4096  137 --------LKRRKGTARKRLATEPYNDGIA--LRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALIYRLLKAG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 238 NSHRVLFLVDRLELEEQAAKAFKDYL-KNDYVTVIYKERRDDWRKADIVVTTVQSL---LFNN---KYKRLFSPTDFDLV 310
Cdd:COG4096  207 RAKRILFLADRNALVDQAKNAFKPFLpDLDAFTKLYNKSKDIDKSARVYFSTYQTMmnrIDGEeeePGYRQFPPDFFDLI 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 311 ISDEAHRSIGGNARAVFEYFVGYKLGLTATPRDylksfdaskpttrdprEQERrlllDTYRTFGcesGQPTFRYSLLDGV 390
Cdd:COG4096  287 IIDECHRGIYSKWRAILDYFDALQIGLTATPKD----------------TIDR----NTYEYFN---GNPVYTYSLEQAV 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 391 KDGFLINPMVVDARTDITtkllsEQGYTVMApvGE---DGLQEHIFVF----------KDFEKKFFSKATNELFCQTFIK 457
Cdd:COG4096  344 ADGFLVPYKVIRIDTKFD-----REGIRYDA--GEdlsDEEGEEIELEeleedreyeaKDFNRKVVNEDTTRKVLEELME 416
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 458 NGLRdPVTGEFGKGLVFAVSQNHAARLTQILNELAdilwpGKYQSDFAVQVTSSVSDAQQYTINFTNNnllgsanfnaly 537
Cdd:COG4096  417 YLDK-PGGDRLGKTIIFAKNDDHADRIVQALRELY-----PELGGDFVKKITGDDDYGKSLIDNFKNP------------ 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 538 ktSKA-RVCVTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRkhnfleqlLDDNLKplinePEKSRFKFFDFFA 616
Cdd:COG4096  479 --EKYpRIAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTR--------LCPDLF-----PGKTHFTIFDFVG 543

                 ....*...
gi 447184992 617 NCEYFEEK 624
Cdd:COG4096  544 NTELFADP 551
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
190-344 8.07e-49

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 170.05  E-value: 8.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLkNDYVT 269
Cdd:cd18032    1 PRYYQQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVL-PDGSF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447184992 270 VIYKERRDDWRKADIVVTTVQSlLFNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYFVG-YKLGLTATPRDY 344
Cdd:cd18032   80 GNLKGGKKKPDDARVVFATVQT-LNKRKRLEKFPPDYFDLIIIDEAHHAIASSYRKILEYFEPaFLLGLTATPERT 154
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
6-613 2.46e-46

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 179.76  E-value: 2.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992    6 EAQARIKINKLLESAGW-------RFFDDA---KGKaNVAlelnvklsqtqINElgenFEATKNGFIDF-LLLDEKnhPL 74
Cdd:PRK11448  233 EEETRILIDQQLRKAGWeadsktlRFSKGArpeKGR-NLA-----------IAE----WPTGKTGRADYaLFIGLK--PV 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   75 VVLEAKSEDKNPLVGKEQARKYAKSLDCR---------------------FVILSNGNLH----------YFWDLQQ--G 121
Cdd:PRK11448  295 GVVEAKRKNKDVASKLNQAKRYSKGFDVAeevpeyggpwqdtsggrykvpFVFSTNGRPYlkqlktksgiWFRDVRKptN 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  122 NPHIIAVFPTPDSLKsyQKFEPDQrrlitevvgrdyivqtqlpgyEKEAGWLNENERSAFIAknklrfLREYQKKAINAI 201
Cdd:PRK11448  375 HPRALQGWHTPEGLL--DLLESDI---------------------EAANQWLADEPFDYGLG------LRYYQEDAIQAV 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  202 QDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTV--IY--KERRD 277
Cdd:PRK11448  426 EKAIVEGQREILLAMATGTGKTRTAIALMYRLLKAKRFRRILFLVDRSALGEQAEDAFKDTKIEGDQTFasIYdiKGLED 505
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  278 dwRKAD----IVVTTVQSLLfnnkyKRLF---------SPTDFDLVISDEAHRsigGNA--------------------- 323
Cdd:PRK11448  506 --KFPEdetkVHVATVQGMV-----KRILysddpmdkpPVDQYDCIIVDEAHR---GYTldkemsegelqfrdqldyvsk 575
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  324 -RAVFEYFVGYKLGLTATPRdylksfdaskpttrdpreqerrllLDTYRTFgcesGQPTFRYSLLDGVKDGFLIN---PM 399
Cdd:PRK11448  576 yRRVLDYFDAVKIGLTATPA------------------------LHTTEIF----GEPVYTYSYREAVIDGYLIDhepPI 627
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  400 VvdartdITTKlLSEQGYT--------VMAPVGEDGLQEHI-----FVFKDFEKKFFSKATNELFCQTFIKNglRDPvTG 466
Cdd:PRK11448  628 R------IETR-LSQEGIHfekgeeveVINTQTGEIDLATLedevdFEVEDFNRRVITESFNRVVCEELAKY--LDP-TG 697
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  467 EfGKGLVFAVSQNHAARLTQILNE-LADILwpGKYQSDFAVQVTSSVSDAQQYTINFTNNNLlgsanfnalyktskARVC 545
Cdd:PRK11448  698 E-GKTLIFAATDAHADMVVRLLKEaFKKKY--GQVEDDAVIKITGSIDKPDQLIRRFKNERL--------------PNIV 760
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447184992  546 VTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRkhnfleqllddnlkpLINEPEKSRFKFFD 613
Cdd:PRK11448  761 VTVDLLTTGIDVPSICNLVFLRRVRSRILYEQMLGRATR---------------LCPEIGKTHFRIFD 813
ResIII pfam04851
Type III restriction enzyme, res subunit;
190-343 1.30e-42

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 152.44  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  190 LREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDY-- 267
Cdd:pfam04851   4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVei 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447184992  268 VTVIYKERRDDWRK-ADIVVTTVQSLL-FNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYF-VGYKLGLTATPRD 343
Cdd:pfam04851  84 GEIISGDKKDESVDdNKIVVTTIQSLYkALELASLELLPDFFDVIIIDEAHRSGASSYRNILEYFkPAFLLGLTATPER 162
DEXDc smart00487
DEAD-like helicases superfamily;
182-348 9.48e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.57  E-value: 9.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   182 IAKNKLRFLREYQKKAINAIqdmvADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKD 261
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL----LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   262 YLKNDYVTVIY-------KERRDDWRK--ADIVVTTVQSLLfNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYFV- 331
Cdd:smart00487  77 LGPSLGLKVVGlyggdskREQLRKLESgkTDILVTTPGRLL-DLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLk 155
                          170       180
                   ....*....|....*....|..
gi 447184992   332 -----GYKLGLTATPRDYLKSF 348
Cdd:smart00487 156 llpknVQLLLLSATPPEEIENL 177
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
73-407 1.74e-13

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: 74.36  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   73 PLVVLEAKSEDKNPLVGKEQARKYAKSLD-----CRFVILSNGNLHYFWdlqQGNPHIIAVFPTP----DSLKSYQKFEP 143
Cdd:TIGR00348 131 PLVIIELKKRSVTIREAFNQIKRYEKEIPelfkyVQIFVISNGTDTRYY---TGSDEDDFDFTFNwkesDNKLIEDLKEF 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  144 D----QRRLITEVVgRDYIVqtqlpgYEKEAGwlnenersaFIAKNKLRFLreyQKKAINAIQDMVADGSTRF-----LF 214
Cdd:TIGR00348 208 DilllKKERLLDFI-RNFII------FDKDTG---------LVTKPYQRYM---QYRAVKKIVESITRKTWGKderggLI 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  215 EMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTViykERRDDWR------KADIVVTT 288
Cdd:TIGR00348 269 WHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQKDCAERI---ESIAELKellekdDGGIIITT 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  289 VQSllFNNKYKRLFSPTDFD----LVISDEAHRS-IGGNARAVFEYFVGYK-LGLTATPRDYlksfdaskpttrdpreQE 362
Cdd:TIGR00348 346 IQK--FDDKLKEEEEKFPVDrkevVVIFDEAHRSqYGELAKNLKKALKNASfFGFTGTPIFK----------------KD 407
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 447184992  363 RrlllDTYRTFGCESGQPTFRYSLLDGVKDGFLInPMVVDARTDI 407
Cdd:TIGR00348 408 R----DTSLTFAYVFGRYLHRYFITDAIRDGLTV-KIDYEDRLPE 447
 
Name Accession Description Interval E-value
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
6-624 4.05e-126

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 398.45  E-value: 4.05e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   6 EAQARIK-INKLLESAGWRFFDDakgkanVALElnVKLSQTQINELGENFEATKNGFIDFLLLDEKNHPLVVLEAKSEDK 84
Cdd:COG4096    4 EAETRKKlIDPALKEAGWDVDDQ------ILRE--VRPTAGRNVVIGEWPTRGGKGYADYVLFGDDGKPLAVVEAKRTSK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  85 NPLVGKEQARKYAKSLD-----CRFVILSNGNLHYFWDLQQGNPHIIAV--FPTPDSLksyqkfepdQRRlitevvgrdy 157
Cdd:COG4096   76 DVSAGLQQAKLYADGLEkqygqVPFIFATNGREIWFWDDRDPYPREREVdgFPSPEEL---------WEL---------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 158 ivqtqlpgYEKEAGWLNENERSAFIAKNKLrfLREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTG 237
Cdd:COG4096  137 --------LKRRKGTARKRLATEPYNDGIA--LRYYQIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAIALIYRLLKAG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 238 NSHRVLFLVDRLELEEQAAKAFKDYL-KNDYVTVIYKERRDDWRKADIVVTTVQSL---LFNN---KYKRLFSPTDFDLV 310
Cdd:COG4096  207 RAKRILFLADRNALVDQAKNAFKPFLpDLDAFTKLYNKSKDIDKSARVYFSTYQTMmnrIDGEeeePGYRQFPPDFFDLI 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 311 ISDEAHRSIGGNARAVFEYFVGYKLGLTATPRDylksfdaskpttrdprEQERrlllDTYRTFGcesGQPTFRYSLLDGV 390
Cdd:COG4096  287 IIDECHRGIYSKWRAILDYFDALQIGLTATPKD----------------TIDR----NTYEYFN---GNPVYTYSLEQAV 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 391 KDGFLINPMVVDARTDITtkllsEQGYTVMApvGE---DGLQEHIFVF----------KDFEKKFFSKATNELFCQTFIK 457
Cdd:COG4096  344 ADGFLVPYKVIRIDTKFD-----REGIRYDA--GEdlsDEEGEEIELEeleedreyeaKDFNRKVVNEDTTRKVLEELME 416
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 458 NGLRdPVTGEFGKGLVFAVSQNHAARLTQILNELAdilwpGKYQSDFAVQVTSSVSDAQQYTINFTNNnllgsanfnaly 537
Cdd:COG4096  417 YLDK-PGGDRLGKTIIFAKNDDHADRIVQALRELY-----PELGGDFVKKITGDDDYGKSLIDNFKNP------------ 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 538 ktSKA-RVCVTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRkhnfleqlLDDNLKplinePEKSRFKFFDFFA 616
Cdd:COG4096  479 --EKYpRIAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTR--------LCPDLF-----PGKTHFTIFDFVG 543

                 ....*...
gi 447184992 617 NCEYFEEK 624
Cdd:COG4096  544 NTELFADP 551
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
167-617 1.21e-49

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 184.46  E-value: 1.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 167 EKEAGWLNENERSAFIAKNKLRF----LREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKlflRTGNSHRV 242
Cdd:COG1061   54 PEEDTERELAEAEALEAGDEASGtsfeLRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAA---ELLRGKRV 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 243 LFLVDRLELEEQAAKAFKDYLKNDYVTVIYKERRddwrkADIVVTTVQSLLFNNKYKRLFSptDFDLVISDEAHRSIGGN 322
Cdd:COG1061  131 LVLVPRRELLEQWAEELRRFLGDPLAGGGKKDSD-----APITVATYQSLARRAHLDELGD--RFGLVIIDEAHHAGAPS 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 323 ARAVFEYFVG-YKLGLTATPrdylksfdaskpttrdPREQERRLLLDTYrtfgcesGQPTFRYSLLDGVKDGFLINPMVV 401
Cdd:COG1061  204 YRRILEAFPAaYRLGLTATP----------------FRSDGREILLFLF-------DGIVYEYSLKEAIEDGYLAPPEYY 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 402 DARTDITTKL-----LSEQGYTVMAPVGEDGLQehifVFKDFEKKFfskatnelfcqtfiknglrdpvtGEFGKGLVFAV 476
Cdd:COG1061  261 GIRVDLTDERaeydaLSERLREALAADAERKDK----ILRELLREH-----------------------PDDRKTLVFCS 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 477 SQNHAARLTQILNEladilwpgkyQSDFAVQVTSSVSDAQQytinftnnnllgSANFNALyKTSKARVCVTVGMMTTGYD 556
Cdd:COG1061  314 SVDHAEALAELLNE----------AGIRAAVVTGDTPKKER------------EEILEAF-RDGELRILVTVDVLNEGVD 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447184992 557 CPDILNLALMRPVYSPSDFVQIKGRGTRKHnfleqllddnlkplinePEKSRFKFFDFFAN 617
Cdd:COG1061  371 VPRLDVAILLRPTGSPREFIQRLGRGLRPA-----------------PGKEDALVYDFVGN 414
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
190-344 8.07e-49

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 170.05  E-value: 8.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLkNDYVT 269
Cdd:cd18032    1 PRYYQQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEVL-PDGSF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447184992 270 VIYKERRDDWRKADIVVTTVQSlLFNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYFVG-YKLGLTATPRDY 344
Cdd:cd18032   80 GNLKGGKKKPDDARVVFATVQT-LNKRKRLEKFPPDYFDLIIIDEAHHAIASSYRKILEYFEPaFLLGLTATPERT 154
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
6-613 2.46e-46

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 179.76  E-value: 2.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992    6 EAQARIKINKLLESAGW-------RFFDDA---KGKaNVAlelnvklsqtqINElgenFEATKNGFIDF-LLLDEKnhPL 74
Cdd:PRK11448  233 EEETRILIDQQLRKAGWeadsktlRFSKGArpeKGR-NLA-----------IAE----WPTGKTGRADYaLFIGLK--PV 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   75 VVLEAKSEDKNPLVGKEQARKYAKSLDCR---------------------FVILSNGNLH----------YFWDLQQ--G 121
Cdd:PRK11448  295 GVVEAKRKNKDVASKLNQAKRYSKGFDVAeevpeyggpwqdtsggrykvpFVFSTNGRPYlkqlktksgiWFRDVRKptN 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  122 NPHIIAVFPTPDSLKsyQKFEPDQrrlitevvgrdyivqtqlpgyEKEAGWLNENERSAFIAknklrfLREYQKKAINAI 201
Cdd:PRK11448  375 HPRALQGWHTPEGLL--DLLESDI---------------------EAANQWLADEPFDYGLG------LRYYQEDAIQAV 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  202 QDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTV--IY--KERRD 277
Cdd:PRK11448  426 EKAIVEGQREILLAMATGTGKTRTAIALMYRLLKAKRFRRILFLVDRSALGEQAEDAFKDTKIEGDQTFasIYdiKGLED 505
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  278 dwRKAD----IVVTTVQSLLfnnkyKRLF---------SPTDFDLVISDEAHRsigGNA--------------------- 323
Cdd:PRK11448  506 --KFPEdetkVHVATVQGMV-----KRILysddpmdkpPVDQYDCIIVDEAHR---GYTldkemsegelqfrdqldyvsk 575
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  324 -RAVFEYFVGYKLGLTATPRdylksfdaskpttrdpreqerrllLDTYRTFgcesGQPTFRYSLLDGVKDGFLIN---PM 399
Cdd:PRK11448  576 yRRVLDYFDAVKIGLTATPA------------------------LHTTEIF----GEPVYTYSYREAVIDGYLIDhepPI 627
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  400 VvdartdITTKlLSEQGYT--------VMAPVGEDGLQEHI-----FVFKDFEKKFFSKATNELFCQTFIKNglRDPvTG 466
Cdd:PRK11448  628 R------IETR-LSQEGIHfekgeeveVINTQTGEIDLATLedevdFEVEDFNRRVITESFNRVVCEELAKY--LDP-TG 697
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  467 EfGKGLVFAVSQNHAARLTQILNE-LADILwpGKYQSDFAVQVTSSVSDAQQYTINFTNNNLlgsanfnalyktskARVC 545
Cdd:PRK11448  698 E-GKTLIFAATDAHADMVVRLLKEaFKKKY--GQVEDDAVIKITGSIDKPDQLIRRFKNERL--------------PNIV 760
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447184992  546 VTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRkhnfleqllddnlkpLINEPEKSRFKFFD 613
Cdd:PRK11448  761 VTVDLLTTGIDVPSICNLVFLRRVRSRILYEQMLGRATR---------------LCPEIGKTHFRIFD 813
ResIII pfam04851
Type III restriction enzyme, res subunit;
190-343 1.30e-42

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 152.44  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  190 LREYQKKAINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDY-- 267
Cdd:pfam04851   4 LRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVei 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447184992  268 VTVIYKERRDDWRK-ADIVVTTVQSLL-FNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYF-VGYKLGLTATPRD 343
Cdd:pfam04851  84 GEIISGDKKDESVDdNKIVVTTIQSLYkALELASLELLPDFFDVIIIDEAHRSGASSYRNILEYFkPAFLLGLTATPER 162
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
190-341 6.10e-34

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: 127.04  E-value: 6.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGstRFLFEMATGTGKTLTSAAVIKLFLRtgnsHRVLFLVDRLELEEQAAKAFKDYLKNDYVT 269
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNR--RGILVLPTGSGKTLTALALIAYLKE----LRTLIVVPTDALLDQWKERFEDFLGDSSIG 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447184992 270 VIYKERRDDWRKADIVVTTVQSLLFNNKYKRLFSPtDFDLVISDEAHRSIGGNARAVFEYF-VGYKLGLTATP 341
Cdd:cd17926   75 LIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFD-QFGLLIVDEAHHLPAKTFSEILKELnAKYRLGLTATP 146
DEXDc smart00487
DEAD-like helicases superfamily;
182-348 9.48e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 102.57  E-value: 9.48e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   182 IAKNKLRFLREYQKKAINAIqdmvADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKD 261
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL----LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   262 YLKNDYVTVIY-------KERRDDWRK--ADIVVTTVQSLLfNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYFV- 331
Cdd:smart00487  77 LGPSLGLKVVGlyggdskREQLRKLESgkTDILVTTPGRLL-DLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLk 155
                          170       180
                   ....*....|....*....|..
gi 447184992   332 -----GYKLGLTATPRDYLKSF 348
Cdd:smart00487 156 llpknVQLLLLSATPPEEIENL 177
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
470-614 3.64e-20

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 86.46  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 470 KGLVFAVSQNHAARLTQILNElADILWPGKYqSDFAVQVTSSVSDAQQYTINFtnnnllgsanfnalyktsKARVCVTVG 549
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNE-AGIDAVALN-SDYSDRERGDEALILLFFGEL------------------KPPILVTVD 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447184992 550 MMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRKHnfleqllddnlkplinePEKSRFKFFDF 614
Cdd:cd18799   68 LLTTGVDIPEVDNVVFLRPTESRTLFLQMLGRGLRLH-----------------EGKDFFTILDF 115
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
190-344 9.91e-18

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: 82.66  E-value: 9.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGSTRFLFEM------ATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYL 263
Cdd:cd18030   22 ARYYQYYAVEAALERIKTATNKDGDKKggyiwhTQGSGKSLTMFKAAKLLIEDPKNPKVVFVVDRKDLDYQTSSTFSRFA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 264 KNDYVTVIYKE-----RRDDwrKADIVVTTVQSllFNNKYKRLFSPTDFD----LVISDEAHRS-IGGNARAVFEYFV-G 332
Cdd:cd18030  102 AEDVVRANSTKelkelLKNL--SGGIIVTTIQK--FNNAVKEESKPVLIYrkniVVIVDEAHRSqFGELAKALKKALPnA 177
                        170
                 ....*....|..
gi 447184992 333 YKLGLTATPRDY 344
Cdd:cd18030  178 TFIGFTGTPIFK 189
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
212-340 1.69e-17

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: 80.14  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 212 FLFEMATGTGKTLTSAAVIKLFLRTGNShRVLFLVDRLELEEQAAKAFKDYLKNDYVTVIY------KERRD-DWRKADI 284
Cdd:cd00046    4 VLITAPTGSGKTLAALLAALLLLLKKGK-KVLVLVPTKALALQTAERLRELFGPGIRVAVLvggssaEEREKnKLGDADI 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447184992 285 VVTTVQSLLFNNKYKRLFSPTDFDLVISDEAHRSIGGNARAVFEYFVGYKL--------GLTAT 340
Cdd:cd00046   83 IIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAglknaqviLLSAT 146
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
73-405 8.61e-16

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: 82.22  E-value: 8.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  73 PLVVLEAKSEDKNPLV--GKEQARKYAKSLD-----CRFVILSNG-NLHY--------FWdlqqgnphiiAVFPTPDSLK 136
Cdd:COG0610  143 PLVVIELKNPLTQVTIkeAFNQIQRYRREIPglfayNQLFVISDGvEARYgtntapfeFF----------LPWKDGDGND 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 137 SYQKFEPDQRRLITEV--------VGRDYIVqtqlpgYEKEAGwlnenersafiaKNKLRFLREYQKKAINAIQDMVADG 208
Cdd:COG0610  213 LNPDGITDLDYLIEGLlskerlldIIRNFIV------FDEDEG------------GLIKIVARYHQYFAVRKAVERVKEA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 209 ST---RFLFEMATGTGKTLTSAAVIKLFLR--TGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTViykERRDDWRKA- 282
Cdd:COG0610  275 EGdgkGGVIWHTQGSGKSLTMVFLAQKLARlpDLDNPTVVVVTDRKDLDDQLFDTFKAFGRESVVQA---ESRADLRELl 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 283 -----DIVVTTVQSllFNNKYKRLFSPTDFD----LVISDEAHRS-IGGNARAVFEYFVGY-KLGLTATPRDylksfdas 351
Cdd:COG0610  352 esdsgGIIVTTIQK--FPEALDEIKYPELSDrkniIVIVDEAHRSqYGGLAKNMRDALPNAsFFGFTGTPIF-------- 421
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 447184992 352 kpttrdprEQERrlllDTYRTFgcesGQPTFRYSLLDGVKDGFlINPMVVDART 405
Cdd:COG0610  422 --------KEDR----TTLEVF----GDYIHTYTITQAIEDGA-TLPLLYEYRL 458
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
191-341 1.79e-15

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 74.97  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  191 REYQKKAINAI---QDMVAdgstrflfEMATGTGKTLTSA-AVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKND 266
Cdd:pfam00270   1 TPIQAEAIPAIlegRDVLV--------QAPTGSGKTLAFLlPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  267 YVTVI-------YKERRDDWRKADIVVTTVQSLLFNNKYKRLFSptDFDLVISDEAHRSIGGNARAVFEYFVGY------ 333
Cdd:pfam00270  73 GLKVAsllggdsRKEQLEKLKGPDILVGTPGRLLDLLQERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEILRRlpkkrq 150

                  ....*...
gi 447184992  334 KLGLTATP 341
Cdd:pfam00270 151 ILLLSATL 158
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
216-341 6.53e-14

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 71.14  E-value: 6.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 216 MATGTGKTLTSAAVIK----LFLRTGNSH-RVLFLVDRLELEEQAAKAFKDYLkNDYVTVIYKERRDDW----------R 280
Cdd:cd18034   23 LPTGSGKTLIAVMLIKemgeLNRKEKNPKkRAVFLVPTVPLVAQQAEAIRSHT-DLKVGEYSGEMGVDKwtkerwkeelE 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447184992 281 KADIVVTTVQSLLfNNKYKRLFSPTDFDLVISDEAHRSIGGN--ARAVFEYfvgYK----------LGLTATP 341
Cdd:cd18034  102 KYDVLVMTAQILL-DALRHGFLSLSDINLLIFDECHHATGDHpyARIMKEF---YHlegrtsrpriLGLTASP 170
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
73-407 1.74e-13

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: 74.36  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   73 PLVVLEAKSEDKNPLVGKEQARKYAKSLD-----CRFVILSNGNLHYFWdlqQGNPHIIAVFPTP----DSLKSYQKFEP 143
Cdd:TIGR00348 131 PLVIIELKKRSVTIREAFNQIKRYEKEIPelfkyVQIFVISNGTDTRYY---TGSDEDDFDFTFNwkesDNKLIEDLKEF 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  144 D----QRRLITEVVgRDYIVqtqlpgYEKEAGwlnenersaFIAKNKLRFLreyQKKAINAIQDMVADGSTRF-----LF 214
Cdd:TIGR00348 208 DilllKKERLLDFI-RNFII------FDKDTG---------LVTKPYQRYM---QYRAVKKIVESITRKTWGKderggLI 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  215 EMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTViykERRDDWR------KADIVVTT 288
Cdd:TIGR00348 269 WHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQKDCAERI---ESIAELKellekdDGGIIITT 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  289 VQSllFNNKYKRLFSPTDFD----LVISDEAHRS-IGGNARAVFEYFVGYK-LGLTATPRDYlksfdaskpttrdpreQE 362
Cdd:TIGR00348 346 IQK--FDDKLKEEEEKFPVDrkevVVIFDEAHRSqYGELAKNLKKALKNASfFGFTGTPIFK----------------KD 407
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 447184992  363 RrlllDTYRTFGCESGQPTFRYSLLDGVKDGFLInPMVVDARTDI 407
Cdd:TIGR00348 408 R----DTSLTFAYVFGRYLHRYFITDAIRDGLTV-KIDYEDRLPE 447
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
191-341 3.64e-12

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 70.14  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 191 REYQKK-AINAIqdmvaDGSTrfLFEMATGTGKTLTSAAVIKLFLRTGNShRVLFLVDRLELEEQAAKAFKDYLK--NDY 267
Cdd:COG1111    5 RLYQLNlAASAL-----RKNT--LVVLPTGLGKTAVALLVIAERLHKKGG-KVLFLAPTKPLVEQHAEFFKEALNipEDE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 268 VTVIY-----KERRDDWRKADIVVTTVQsLLFNNKYKRLFSPTDFDLVISDEAHRSIGGNARA-VFEYFVGYK-----LG 336
Cdd:COG1111   77 IVVFTgevspEKRKELWEKARIIVATPQ-VIENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVyIAERYHEDAkdpliLG 155

                 ....*
gi 447184992 337 LTATP 341
Cdd:COG1111  156 MTASP 160
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
218-393 6.69e-12

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


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 65.92  E-value: 6.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  218 TGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTViykERRDDWRK-----ADIVVTTVQSl 292
Cdd:pfam18766  28 QGSGKSLTMVFLARKLRRELKNPTVVVVTDRNDLDDQLTKTFAACGREVPVQA---ESRKDLREllrgsGGIIFTTIQK- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  293 lFNNKYKRLFSPTDFD---LVISDEAHRS-IGGNARAVFEYFVGY-KLGLTATPRDylksfdaskpttrdprEQERrlll 367
Cdd:pfam18766 104 -FGETPDEGFPVLSDRrniIVLVDEAHRSqYGGLAANMRDALPNAaFIGFTGTPIL----------------KKDK---- 162
                         170       180
                  ....*....|....*....|....*...
gi 447184992  368 DTYRTFGcesgqpTF--RYSLLDGVKDG 393
Cdd:pfam18766 163 NTRAVFG------DYidTYTIQDAVEDG 184
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
190-341 8.39e-11

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is 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: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 62.31  E-value: 8.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQkkaINAIQDMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLV-DRL------ELEEQAAKAFkDY 262
Cdd:cd18011    1 PLPHQ---IDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCpASLveqwqdELQDKFGLPF-LI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 263 LKNDYVTVIYKERRDDWRKADIVVTTVQSLLFNNKYKRLFSPTDFDLVISDEAHR-SIGGNARAVFEYFVG--------Y 333
Cdd:cd18011   77 LDRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLLLSEEWDLVVVDEAHKlRNSGGGKETKRYKLGrllakrarH 156

                 ....*...
gi 447184992 334 KLGLTATP 341
Cdd:cd18011  157 VLLLTATP 164
uvsW PHA02558
UvsW helicase; Provisional
191-357 2.47e-10

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 63.88  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 191 REYQKKAI-NAIQDmvadgsTRFLFEMATGTGKTLTSAAVIKLFLRTgNSHRVLFLVDRLELEEQAAKAFKDY--LKNDY 267
Cdd:PHA02558 116 HWYQYDAVyEGLKN------NRRLLNLPTSAGKSLIQYLLSRYYLEN-YEGKVLIIVPTTSLVTQMIDDFVDYrlFPREA 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 268 VTVIYkERRDDWRKADIVVTTVQSLLfnNKYKRLFSptDFDLVISDEAHRSIG----------GNARavfeyfvgYKLGL 337
Cdd:PHA02558 189 MHKIY-SGTAKDTDAPIVVSTWQSAV--KQPKEWFD--QFGMVIVDECHLFTGksltsiitklDNCK--------FKFGL 255
                        170       180
                 ....*....|....*....|....*...
gi 447184992 338 TATPRD-------YLKSF-DASKPTTRD 357
Cdd:PHA02558 256 TGSLRDgkanilqYVGLFgDIFKPVTTS 283
PRK13766 PRK13766
Hef nuclease; Provisional
191-341 2.87e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 64.12  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 191 REYQKKainaIQDMVADGSTrfLFEMATGTGKTLTSAAVIKLFLRTGNShRVLFLVDRLELEEQAAKAFKDYLK--NDYV 268
Cdd:PRK13766  17 RLYQQL----LAATALKKNT--LVVLPTGLGKTAIALLVIAERLHKKGG-KVLILAPTKPLVEQHAEFFRKFLNipEEKI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 269 TVIY-----KERRDDWRKADIVVTT---VQSLLFNNKYkrlfSPTDFDLVISDEAHRSIGGNARaVF---EYFVGYK--- 334
Cdd:PRK13766  90 VVFTgevspEKRAELWEKAKVIVATpqvIENDLIAGRI----SLEDVSLLIFDEAHRAVGNYAY-VYiaeRYHEDAKnpl 164

                 ....*...
gi 447184992 335 -LGLTATP 341
Cdd:PRK13766 165 vLGLTASP 172
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
190-341 1.51e-09

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 61.78  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGsTRFLF--EMatGTGKTLTSAAVIKLFLRTGNSHRVLFLVD---RLELEEQAAKaFKDYLK 264
Cdd:COG0553  242 LRPYQLEGAAWLLFLRRLG-LGGLLadDM--GLGKTIQALALLLELKERGLARPVLIVAPtslVGNWQRELAK-FAPGLR 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 265 ndyVTVIYKERR-----DDWRKADIVVTTVQSLLfnnKYKRLFSPTDFDLVISDEAHR---SIGGNARAVFEYFVGYKLG 336
Cdd:COG0553  318 ---VLVLDGTRErakgaNPFEDADLVITSYGLLR---RDIELLAAVDWDLVILDEAQHiknPATKRAKAVRALKARHRLA 391

                 ....*
gi 447184992 337 LTATP 341
Cdd:COG0553  392 LTGTP 396
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
218-341 2.22e-09

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 58.21  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 218 TGTGKTLTSAAVIKLFL---RTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTVI------------YKErrddWRKA 282
Cdd:cd17927   26 TGSGKTFVAVLICEHHLkkfPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTglsgdtsenvsvEQI----VESS 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 283 DIVVTTVQSLLFNNKYKRLFSPTDFDLVISDEAHRSIGGNA--RAVFEYFVGYK---------LGLTATP 341
Cdd:cd17927  102 DVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNHPynEIMFRYLDQKLgssgplpqiLGLTASP 171
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
216-341 2.24e-09

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 57.52  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 216 MATGTGKTLTSAAVIKLFLrTGNSHRVLFLVDRLELEEQAAKAFKDYLK-NDYVTVIY-----KERRDDWRKADIVVTTV 289
Cdd:cd18035   23 LPTGLGKTIIAILVAADRL-TKKGGKVLILAPSRPLVEQHAENLKRVLNiPDKITSLTgevkpEERAERWDASKIIVATP 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447184992 290 QSL---LFNNKYkrlfSPTDFDLVISDEAHRSIGGNARAvfeyFVGYK----------LGLTATP 341
Cdd:cd18035  102 QVIendLLAGRI----TLDDVSLLIFDEAHHAVGNYAYV----YIAHRykreannpliLGLTASP 158
DEXHc_priA cd17929
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ...
194-318 3.00e-09

DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain]  Cd Length: 178  Bit Score: 57.22  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 194 QKKAINAIQDMVADGSTrFLFEMATGTGKTLTSAAVIKLFLRTGNShrVLFLVDRLELEEQAAKAFKDYLKNDyVTVIY- 272
Cdd:cd17929    1 QRKAYEAIVSSLGGFKT-FLLHGVTGSGKTEVYIELIEKVLAKGKQ--VLVLVPEISLTPQLIKRFKKRFGDK-VAVLHs 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447184992 273 ----KERRDDWRKA-----DIVVTTVQSllfnnkykrLFSPT-DFDLVISDEAHRS 318
Cdd:cd17929   77 klsdKERADEWRKIkrgeaKVVIGARSA---------LFAPFkNLGLIIVDEEHDS 123
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
190-341 1.65e-08

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 54.88  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGSTRFLF-EMatGTGKTLTSAAVIK-LFLRTGNSHRVLFLV--DRLELEEQAAKAFKDYLKn 265
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILAdEM--GLGKTLQAIAFLAyLLKEGKERGPVLVVCplSVLENWEREFEKWTPDLR- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 266 dyVTVIYKERRD--------DWRKADIVVTTVQSLLfnnKYKRLFSPTDFDLVISDEAHRSIGGN---ARAVFEYFVGYK 334
Cdd:cd17919   78 --VVVYHGSQREraqirakeKLDKFDVVLTTYETLR---RDKASLRKFRWDLVVVDEAHRLKNPKsqlSKALKALRAKRR 152

                 ....*..
gi 447184992 335 LGLTATP 341
Cdd:cd17919  153 LLLTGTP 159
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
194-317 1.33e-07

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 52.42  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 194 QKKAINAI-QDMVADGSTRFLFEMATGTGKTLtsAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTVIY 272
Cdd:cd17918   20 QAQAIKDIeKDLHSPEPMDRLLSGDVGSGKTL--VALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINVELVT 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447184992 273 KERR-DDWRKADIVVTTVQSLLFNNKYKrlfsptDFDLVISDEAHR 317
Cdd:cd17918   98 GGTKaQILSGISLLVGTHALLHLDVKFK------NLDLVIVDEQHR 137
COG4889 COG4889
Predicted helicase [General function prediction only];
190-344 2.53e-07

Predicted helicase [General function prediction only];


Pssm-ID: 443917 [Multi-domain]  Cd Length: 1571  Bit Score: 54.58  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  190 LREYQKKAINAIQD--MVADgstRFLFEMATGTGKTLTSaaviklfLR-----TGNSHRVLFLVDRLELEEQA------- 255
Cdd:COG4889   170 LRPHQQEAIEAVLAgfKTHD---RGKLIMACGTGKTFTS-------LRiaeelAGKGGRVLFLVPSISLLSQTlrewtae 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  256 -------------AKAFKDYLKNDYVTVIYK----------------ERRDDWRKADIVVTTVQSLLFNNKYKRLFSPtD 306
Cdd:COG4889   240 sevplrsfavcsdSKVGKRRKKDDEDTSAHDlaypattdaeklaaaaQKRHDADRMTVVFSTYQSIDVVADAQKLGLP-E 318
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 447184992  307 FDLVISDEAHRSIG-----GNARAvfeyFV---------GYK-LGLTATPRDY 344
Cdd:COG4889   319 FDLIICDEAHRTTGatlagEDESA----FVrvhdndyikAKKrLYMTATPRIY 367
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
190-341 6.19e-07

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 50.40  E-value: 6.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQkkainaiQDMVADGstrfLFE-----MATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDY-- 262
Cdd:cd18033    3 LRDYQ-------FTIVQKA----LFQntlvaLPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYKItg 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 263 LKNDYVTVIYKE-----RRDDWRKADIVVTTVQSLLfNNKYKRLFSPTDFDLVISDEAHRSIGGNA-----RAVFEYFVG 332
Cdd:cd18033   72 IPSSQTAELTGSvpptkRAELWASKRVFFLTPQTLE-NDLKEGDCDPKSIVCLVIDEAHRATGNYAycqvvRELMRYNSH 150
                        170
                 ....*....|
gi 447184992 333 YK-LGLTATP 341
Cdd:cd18033  151 FRiLALTATP 160
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
190-340 8.29e-07

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 49.99  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAiqdMVADGSTRF-LFEMATGTGKTL---TSAAVIKlflrtgnsHRVLFLVDRLELEEQAAKAFKDY--L 263
Cdd:cd18029    9 LRPYQEKALSK---MFGNGRARSgVIVLPCGAGKTLvgiTAACTIK--------KSTLVLCTSAVSVEQWRRQFLDWttI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 264 KNDYVTVIYKERRDDWRKADIVVTTVQSLLFNN-------KYKRLFSPTDFDLVISDEAHRSiggnARAVFEYFVGY--- 333
Cdd:cd18029   78 DDEQIGRFTSDKKEIFPEAGVTVSTYSMLANTRkrspeseKFMEFITEREWGLIILDEVHVV----PAPMFRRVLTLqka 153

                 ....*....
gi 447184992 334 --KLGLTAT 340
Cdd:cd18029  154 hcKLGLTAT 162
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
181-324 1.09e-06

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 52.20  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 181 FIAKNKLRFLREYQKKAINAIqdmVADGsTRFLFEMATGTGKTL-TSAAVIKLFLRTGnshRVLFLVDRLELEEQAAKAF 259
Cdd:COG1204   14 FLKERGIEELYPPQAEALEAG---LLEG-KNLVVSAPTASGKTLiAELAILKALLNGG---KALYIVPLRALASEKYREF 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447184992 260 KDYLKNDYVTVI-----YKERRDDWRKADIVVTT---VQSLLfNNKYKRLfspTDFDLVISDEAHrSIGGNAR 324
Cdd:COG1204   87 KRDFEELGIKVGvstgdYDSDDEWLGRYDILVATpekLDSLL-RNGPSWL---RDVDLVVVDEAH-LIDDESR 154
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
218-326 1.73e-06

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 49.18  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 218 TGTGKTLTS-AAVIKLFLRTGNshRVLFLVDRLELEEQAAKAFKDYLKNDYVTVI-----YKERRDDWRKADIVVTT--- 288
Cdd:cd17921   26 TSSGKTLIAeLAILRALATSGG--KAVYIAPTRALVNQKEADLRERFGPLGKNVGlltgdPSVNKLLLAEADILVATpek 103
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447184992 289 VQSLLFNNKYKRLFsptDFDLVISDEAHrSIGGNARAV 326
Cdd:cd17921  104 LDLLLRNGGERLIQ---DVRLVVVDEAH-LIGDGERGV 137
ResIII COG3421
Type III restriction endonuclease [Defense mechanisms];
183-317 4.09e-06

Type III restriction endonuclease [Defense mechanisms];


Pssm-ID: 442647 [Multi-domain]  Cd Length: 883  Bit Score: 50.78  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 183 AKNKLRFLREYQKKAINA------IQDMVADGSTRFLFEMATGTGKTLTSAAVIkLFLRTGNSHRVLFLVDRLELEEQAA 256
Cdd:COG3421   37 LNLNENIRKRLYEEEAFYlknyieNEPFIKNKPKHLLFNMATGSGKTLIMAGLI-LYLYKKGYRNFLFFVNTNNIIYKTR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 257 KAFKDYLKNDYV---------TVIYKERRDDWRKAD-----IVVTTVQSLLFNNKYKRLFSPT--DFD----LVISDEAH 316
Cdd:COG3421  116 ENFLNPQSPKYLfnekieidgENVAIKEVDNFPEADendinIKFTSIQKLHNDLNTPRENSLTyeDFEdkklVLISDEAH 195

                 .
gi 447184992 317 R 317
Cdd:COG3421  196 H 196
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
193-347 1.81e-05

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 47.95  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 193 YQKKAINAIQDMVADGSTRFLFEmATGTGKTLTSAAVIKLFLRTGNshRVLFLVDR----LELEEQAAKAFKDYlkndYV 268
Cdd:COG4098  114 AQQKASDELLEAIKKKEEHLVWA-VCGAGKTEMLFPAIAEALKQGG--RVCIATPRvdvvLELAPRLQQAFPGV----DI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 269 TVIYKERRDDWRKADIVVTTVQSLLfnnKYKRlfsptDFDLVISDEA---------------HRSIGGNARAVFeyfvgy 333
Cdd:COG4098  187 AALYGGSEEKYRYAQLVIATTHQLL---RFYQ-----AFDLLIIDEVdafpysgdpmlqyavKRARKPDGKLIY------ 252
                        170
                 ....*....|....
gi 447184992 334 klgLTATPRDYLKS 347
Cdd:COG4098  253 ---LTATPSKALQR 263
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
190-341 2.37e-05

DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 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: 350833 [Multi-domain]  Cd Length: 200  Bit Score: 46.00  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAInaiqdMVADGSTRFLFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQ-AAKAFKDYLKNDYV 268
Cdd:cd18075    3 LHGYQWEVV-----APALRGKNSIIWLPTGAGKTRAAVYVARRHLETKRGAKVAVLVNKVHLVDQhLEKEFHVLLDKYTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 269 TVIY--KERRDDW----RKADIVVTTVQSL---LFNNKYKRLFSPTDFDLVISDEAHRSiggNARAVF----EYFVGYK- 334
Cdd:cd18075   78 TAISgdSSHKCFFgqlaRGSDVVICTAQILqnaLLSGEEEAHVELTDFSLLVIDECHHT---HKEAVYnkimLSYLEKKl 154
                        170
                 ....*....|....*.
gi 447184992 335 ---------LGLTATP 341
Cdd:cd18075  155 srqgdlpqiLGLTASP 170
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
190-341 4.54e-05

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 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: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 45.63  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAIN---AIQDM-----VADgstrflfEMatGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLEL---EEQAAKa 258
Cdd:cd18012    5 LRPYQKEGFNwlsFLRHYglggiLAD-------DM--GLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIynwEEEAAK- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 259 FKDYLKndyVTVIY---KERRDDWR--KADIVVTTVQSLLfnnKYKRLFSPTDFDLVISDEA-----HRSIggNARAVFE 328
Cdd:cd18012   75 FAPELK---VLVIHgtkRKREKLRAleDYDLVITSYGLLR---RDIELLKEVKFHYLVLDEAqniknPQTK--TAKAVKA 146
                        170
                 ....*....|...
gi 447184992 329 YFVGYKLGLTATP 341
Cdd:cd18012  147 LKADHRLALTGTP 159
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
218-320 6.07e-05

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 44.81  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 218 TGTGKTLTSAAVIKLFLR---TGNSHRVLFLVDRLELEEQAAKAFKDYLK--NDYVTVIYKERRDDW------RKADIVV 286
Cdd:cd18073   26 TGCGKTFVSLLICEHHLKkfpQGQKGKVVFFATKVPVYEQQKSVFSKYFErhGYRVTGISGATAENVpveqiiENNDIII 105
                         90       100       110
                 ....*....|....*....|....*....|....
gi 447184992 287 TTVQSLLFNNKYKRLFSPTDFDLVISDEAHRSIG 320
Cdd:cd18073  106 LTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSG 139
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
218-341 6.55e-05

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 44.77  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 218 TGTGKTLTSAAVIKLFLR----TGNSHRVLFLVDRLELEEQAAKAFKDYLKNDY-VTVIYKERRDDW------RKADIVV 286
Cdd:cd18036   26 TGSGKTRVAVYICRHHLEkrrsAGEKGRVVVLVNKVPLVEQQLEKFFKYFRKGYkVTGLSGDSSHKVsfgqivKASDVII 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447184992 287 TTVQSL---LFNNKYKRLFSPTDFDLVISDEAHRSIGGNA-----RAVFEYFVGYK------LGLTATP 341
Cdd:cd18036  106 CTPQILinnLLSGREEERVYLSDFSLLIFDECHHTQKEHPynkimRMYLDKKLSSQgplpqiLGLTASP 174
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
200-316 2.40e-04

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 42.71  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 200 AIQDMVADGStRFLFEMATGTGKTLTS-AAVIKLFLRTGnshRVLFLVDRLELEEQAAKAFKDYLK---------NDYvt 269
Cdd:cd18028    9 AVRAGLLKGE-NLLISIPTASGKTLIAeMAMVNTLLEGG---KALYLVPLRALASEKYEEFKKLEEiglkvgistGDY-- 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 447184992 270 viykERRDDW-RKADIVVTT---VQSLLFNnkykrlfSPT---DFDLVISDEAH 316
Cdd:cd18028   83 ----DEDDEWlGDYDIIVATyekFDSLLRH-------SPSwlrDVGVVVVDEIH 125
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
190-317 3.93e-04

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They 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: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 43.04  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDMVADGSTRFLF------EMatGTGKTLTSAAVIKLFLRTG-----NSHRVLF-----LVDRLELEe 253
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGGGgailadEM--GLGKTLQAIALVWTLLKQGpygkpTAKKALIvcpssLVGNWKAE- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447184992 254 qaakaFKDYLKNDYVTVIYKERRDDWRKADIVVTTVQSL---------LFNNKYKRLFSPTDFDLVISDEAHR 317
Cdd:cd18004   78 -----FDKWLGLRRIKVVTADGNAKDVKASLDFFSSASTypvliisyeTLRRHAEKLSKKISIDLLICDEGHR 145
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
2-110 3.96e-04

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 43.43  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992   2 ANAKEAQARIK-INKLLESAGWrffdDAKGKANVALElnvklsqtqinelgenfEATKNGFIDFLLLDEkNHPLVVLEAK 80
Cdd:COG2810   24 RSANEAATRQEfIDPLLEALGW----DIDNPEEVIPE-----------------ERVEGGRPDYALRLN-GKRKLFVEAK 81
                         90       100       110
                 ....*....|....*....|....*....|.
gi 447184992  81 SEDKNPLVG-KEQARKYAKSLDCRFVILSNG 110
Cdd:COG2810   82 KPGVNLKDKpARQARSYAWSSGVRWAILTNG 112
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
213-316 5.52e-04

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 40.88  E-value: 5.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 213 LFEMATGTGKTLTSAAVIKLFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLKNDYVTVIYKERRDdwrkADIVVTTVQsL 292
Cdd:cd17915    5 ALESPTGSGKTLSLLCSALSYQREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIRALALSSRD----ADIVVLPYP-Y 79
                         90       100
                 ....*....|....*....|....*...
gi 447184992 293 LFNNKYKRLfspTDFDL----VISDEAH 316
Cdd:cd17915   80 LLDARIREF---IGIDLreqvVIIDEAH 104
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
187-341 5.58e-04

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 42.67  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  187 LRFLRE-YQKKAINAIqdmVADgstrflfEMatGTGKTLTSAAVIK-LFLRTGNSHRVLFLVDRLELEEQAAKAFKDYLK 264
Cdd:pfam00176   6 VNWMLSlENNLGRGGI---LAD-------EM--GLGKTLQTISLLLyLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992  265 NDYVTV-IYKER---RDDW-------RKADIVVTTVQSLLfnnKYKRLFSPTDFDLVISDEAHRSIGGNARAVF---EYF 330
Cdd:pfam00176  74 PPALRVvVLHGNkrpQERWkndpnflADFDVVITTYETLR---KHKELLKKVHWHRIVLDEGHRLKNSKSKLSKalkSLK 150
                         170
                  ....*....|.
gi 447184992  331 VGYKLGLTATP 341
Cdd:pfam00176 151 TRNRWILTGTP 161
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
57-123 7.37e-04

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: 433331 [Multi-domain]  Cd Length: 110  Bit Score: 39.88  E-value: 7.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447184992   57 TKNGFIDFLLLDEKNHPLVVLEAKSED-KNPLVGKEQARKYAKSLDCRFVILSNGNLHYFWDLQQGNP 123
Cdd:pfam13588  34 SKKKRADIVVYNKDGKPYILVECKAPSiKISQKVFDQLARYNSVLGAPFLVVTNGLQHICFKVDYDKQ 101
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
190-341 8.86e-04

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family 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: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 41.57  E-value: 8.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 190 LREYQKKAINAIQDmvADGSTRFLfEMatGTGKTLTSAAVIKLFLRTGNSHRVLFL----VDRLELEEQAAKAfkDYLKN 265
Cdd:cd18013    1 PHPYQKVAINFIIE--HPYCGLFL-DM--GLGKTVTTLTALSDLQLDDFTRRVLVIaplrVARSTWPDEVEKW--NHLRN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 266 DYVTVIY---KERRDDWRK-ADIVVTTVQSL-LFNNKYKRLFsptDFDLVISDE-----AHRSIGGNARAVFEYFVGYKL 335
Cdd:cd18013   74 LTVSVAVgteRQRSKAANTpADLYVINRENLkWLVNKSGDPW---PFDMVVIDElssfkSPRSKRFKALRKVRPVIKRLI 150

                 ....*.
gi 447184992 336 GLTATP 341
Cdd:cd18013  151 GLTGTP 156
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
218-315 1.16e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 40.77  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 218 TGTGKTlTSAAVIKLFLRTGNShRVLFLVDRLELEEQAAKAFKDYLKNDYVTV--------IYKERRDDWRKA------D 283
Cdd:cd17924   41 TGVGKT-TFGLATSLYLASKGK-RSYLIFPTKSLVKQAYERLSKYAEKAGVEVkilvyhsrLKKKEKEELLEKiekgdfD 118
                         90       100       110
                 ....*....|....*....|....*....|..
gi 447184992 284 IVVTTVQsllFNNKYKRLFSPTDFDLVISDEA 315
Cdd:cd17924  119 ILVTTNQ---FLSKNFDLLSNKKFDFVFVDDV 147
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
169-316 1.84e-03

Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 42.03  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 169 EAGWLNENER--------SAFIAKNKLRfLREYQKKAINAIQDMvADGSTRFLFEMATGTGKT---LtsaAVIKLFLRTG 237
Cdd:COG1198  168 KKGLLEIEERevdrdpfaPDVPAEPPPT-LNEEQQAAVEAIRAA-AGGFSVFLLHGVTGSGKTevyL---QAIAEVLAQG 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992 238 NShrVLFLVDRLELEEQAAKAFKDYLKNDyvTVIY------KERRDDWRK-----ADIVVTTvqsllfnnkykR--LFSP 304
Cdd:COG1198  243 KQ--ALVLVPEIALTPQTVERFRARFGAR--VAVLhsglsdGERLDEWRRarrgeARIVIGT-----------RsaLFAP 307
                        170
                 ....*....|....*
gi 447184992 305 tdFD---LVISDEAH 316
Cdd:COG1198  308 --FPnlgLIIVDEEH 320
HSDR_N pfam04313
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
6-118 2.98e-03

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: 39.21  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447184992    6 EAQARIKINKLLESAGWRFFDDAKGKANVALELNVKLSQTQINELGENFEAT-----KNGF---------------IDFL 65
Cdd:pfam04313   5 EEVEQKLILPLLKALGYDVLNEVRGIKAEVILEKLDGNEAFYRLLKYGVTDGitkteNNSFqvanqvevkgvqkrrPDYV 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447184992   66 LLDeKNHPLVVLEAKSE------------DKNPLVGKEQARKYAkslDCRFVILSNGNLHYFWDL 118
Cdd:pfam04313  85 LFV-NGLPLAVIELKRPgteeainqirryEKDSFNAIPQLFRYA---NVQFGILSNGRETRFYTK 145
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
546-588 7.86e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 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: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.14  E-value: 7.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 447184992 546 VTVGMMTTGYDCPDILNLALMRPVYSPSDFVQIKGRGTRKHNF 588
Cdd:cd18785   27 VATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
 
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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