|
Name |
Accession |
Description |
Interval |
E-value |
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
12-1087 |
0e+00 |
|
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: 801.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 12 EYSAKIPALTLLTSLGWTFLSPKqimDYRGYKQDEVVLRPVLREELSKRSfmaggktCQLSEKALANLISQVCSPALNeG 91
Cdd:COG0610 6 EAALEQAIIELLQELGYEYLSGP---DIAPEDESEVLLEDNLRAALERLN-------PGLSDDEIERALRELTKPESN-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 92 LLKANERMYNHLLYGIAVTefVDGKKVNPTIALIDWEHPENNQFHFTEEFTVlrSGGVETRRPDIVCFVNGIPLAVIEAK 171
Cdd:COG0610 75 LLEANKGFYDLLRNGVKVE--YDGEEKTKTVRLIDFKNPENNDFLVVNQFTV--SGGNYKRRPDVVLFVNGLPLVVIELK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 172 SPAghgkKGPTIDEGISQSIRNQfnDEIPQLFVYSQLLLSINGHDGRYGTCHTPMKFWAAWREEDitdpqmyalrNHPLS 251
Cdd:COG0610 151 NPL----TQVTIKEAFNQIQRYR--REIPGLFAYNQLFVISDGVEARYGTNTAPFEFFLPWKDGD----------GNDLN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 252 TEQIHALfdhrpsvdlkwyqqlidggelavsgqDKLLISLLSPERLLEMTRFFTLFDKKTG---KIVARYQQVFGIKRLL 328
Cdd:COG0610 215 PDGITDL--------------------------DYLIEGLLSKERLLDIIRNFIVFDEDEGgliKIVARYHQYFAVRKAV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 329 ERIstRRPDGGREGGVIWHTTGSGKSYTMVFLSKALILHDSLKQCRIVVVTDRVDLEGQLSGTFVSGGElagkddKAKAM 408
Cdd:COG0610 269 ERV--KEAEGDGKGGVIWHTQGSGKSLTMVFLAQKLARLPDLDNPTVVVVTDRKDLDDQLFDTFKAFGR------ESVVQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 409 ATSGQKLAQQIGSGKERIIFTLIQKFNSATK--LPECVNTSPDIIVLIDEGHRSQGGENHVRMKLALPNAAFVAFTGTPL 486
Cdd:COG0610 341 AESRADLRELLESDSGGIIVTTIQKFPEALDeiKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPI 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 487 LKEDKTT-NKFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFDRITDGLSEAQKADLKRKYARKGEVYSA 565
Cdd:COG0610 421 FKEDRTTlEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLDKEKIDEEFDELTEGLDDEEKEKLKAKWALLEEVLGA 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 566 DDRIRLIALDIATHFSKNIDEG-LKGQLACDSKISAIKYKKYLDEAG------LFESAVVISPPDTREGntevdesklPE 638
Cdd:COG0610 501 PERIEQIAEDIVEHFEERTRPGkGKAMVVTSSREAAVRYYEAFDKLRpewgykPLKIAVVFSGSANDDP---------EE 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 639 VTKWwkdnvgtqDESVYTRNIISRF-DTDEKLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNLIQAIARVNRLHPLKKF 717
Cdd:COG0610 572 LKEH--------GNKEYEKDLAKRFkDPDDPLKLLIVVDMLLTGFDAPSLHTLYVDKPLKGHNLMQAISRVNRVFPGKPY 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 718 GLLIDYRGILAELDTTIGKYqdlASRTQGGYDIKDIDglysamsSEYKRLPHLYNQLWAIFA-GVKNKNDTEQLRAVLVP 796
Cdd:COG0610 644 GLIVDYRGIFENLKKALALY---SEEDGKEDVLTDPE-------EALEELKEALDELRALFPeGVDFSAFDPTEKLEALD 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 797 KMEERdgemVDIHQKTRDDFFEALTAFAGCLKVALQsatfftDKSFTEQDRNLYKETVKQMSSLRQWaMQVSGEQVNYDD 876
Cdd:COG0610 714 EAVER----FLGDEEARKEFKKLFKELSRLYNLLSP------DDEFGDLELEKYRDDVSFYLALRAK-LRKLGEKLDLKE 782
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 877 YAEQVKKLLDKHVtgvevrepdgvyevgkmgKSEKpeewdnnktrnetdiiktrvtKMIEQELRDDPYAQEAFSKLLRMA 956
Cdd:COG0610 783 YEEKIRQLLDEAI------------------DLER---------------------KEIKPRIKQNPVQYRKFSELLEEI 823
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 957 IEEAEKLFDHPLKQYLLFREFEEQVEARKLSDIPDALvvNKHAQAYYGVFKKELPEvfavndvqvqDKWTKLAFEVDNII 1036
Cdd:COG0610 824 IEEYNNGALDADEVLEELEELAKEVKEEEERAEEEGL--NEEELAFYDALAENLGD----------EKLKELAKELDDLL 891
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 749548701 1037 VKAVAENSLNPQDIEKVVKTSLLPLLFTacreigAGMNQVNRIVETIIQIL 1087
Cdd:COG0610 892 KKNVTVDWRKRESVRAKLRDAIKRLLRK------YGYPKQDEAVEEVYEQA 936
|
|
| hsdR |
TIGR00348 |
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ... |
92-739 |
3.18e-129 |
|
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: 408.71 E-value: 3.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 92 LLKANERMYNHLLYGIAVTEFVDGKKVNpTIALIDWEHPENNQFHFTEEFTVLRSGGvetrRPDIVCFVNGIPLAVIEAK 171
Cdd:TIGR00348 64 LYETNKIFYDYIKNGVKIKESQKGEKKR-IVKLIDFRNISQNIFQFANQVSFKGHNI----RPDVTLFVNGIPLVIIELK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 172 spaghgKKGPTIDEGISQSIRNQfnDEIPQLFVYSQLLLSINGHDGRYGTCH--TPMKFWAAWREEDITDPqmyalrnhp 249
Cdd:TIGR00348 139 ------KRSVTIREAFNQIKRYE--KEIPELFKYVQIFVISNGTDTRYYTGSdeDDFDFTFNWKESDNKLI--------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 250 lsteqihalfdhrpsvdlKWYQQLIdggelavsgqdkllISLLSPERLLEMTRFFTLFDKKTG---KIVARYQQVFGIKR 326
Cdd:TIGR00348 202 ------------------EDLKEFD--------------ILLLKKERLLDFIRNFIIFDKDTGlvtKPYQRYMQYRAVKK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 327 LLERISTRRPDGGREGGVIWHTTGSGKSYTMVFLskALILHDSLKQCRIVVVTDRVDLEGQLSGTFVSGGelagKDDKAK 406
Cdd:TIGR00348 250 IVESITRKTWGKDERGGLIWHTQGSGKTLTMLFA--ARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQ----KDCAER 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 407 AmaTSGQKLAQQIGSGKERIIFTLIQKFNSatKLPECVNTSP----DIIVLIDEGHRSQGGENHVRMKLALPNAAFVAFT 482
Cdd:TIGR00348 324 I--ESIAELKELLEKDDGGIIITTIQKFDD--KLKEEEEKFPvdrkEVVVIFDEAHRSQYGELAKNLKKALKNASFFGFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 483 GTPLLKEDKTTN-----KFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFD----RITDGLSEAQKADLK 553
Cdd:TIGR00348 400 GTPIFKKDRDTSltfayVFGRYLHRYFITDAIRDGLTVKIDYEDRLPEDHLDKKKLDAFFDeifeLLPERIREITKESLK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 554 RKYARKGEVYSADDRIRLIALDIATHFSKNID-EGLKGQLACDSKISAIKYKKYLDE---AGLFESAVVISppdtregNT 629
Cdd:TIGR00348 480 EKLQKTKKILFNEDRLESIAKDIAEHYAKFKElFKFKAMVVAISRYACVEEKNALDEelnEKFEASAIVMT-------GK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 630 EVDESKLPEVTKWWKDNVGTQDESVYTRNIISRFDTDEKLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNLIQAIARVN 709
Cdd:TIGR00348 553 ESDDAEIRDYNKHIRTKFDKSDGFEIYYKDLERFKKNENPKLLIVVDMLLTGFDAPILNTLYLDKPLKYHGLLQAIARTN 632
|
650 660 670
....*....|....*....|....*....|.
gi 749548701 710 RLH-PLKKFGLLIDYRGILAELDTTIGKYQD 739
Cdd:TIGR00348 633 RIDgKDKTFGLIVDYRGLEKSLIDALSLYGN 663
|
|
| SWI2_SNF2 |
pfam18766 |
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins. |
319-550 |
3.51e-105 |
|
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
Pssm-ID: 465860 [Multi-domain] Cd Length: 222 Bit Score: 328.62 E-value: 3.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 319 QQVFGIKRLLERISTrrpDGGREGGVIWHTTGSGKSYTMVFLSKALILHdsLKQCRIVVVTDRVDLEGQLSGTFVSGGEl 398
Cdd:pfam18766 1 QQYFAVNKAVERVLE---DGDRRGGVIWHTQGSGKSLTMVFLARKLRRE--LKNPTVVVVTDRNDLDDQLTKTFAACGR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 399 agkddKAKAMATSGQKLAQQIGsGKERIIFTLIQKFNSA-TKLPECVNTSPDIIVLIDEGHRSQGGENHVRMKLALPNAA 477
Cdd:pfam18766 75 -----EVPVQAESRKDLRELLR-GSGGIIFTTIQKFGETpDEGFPVLSDRRNIIVLVDEAHRSQYGGLAANMRDALPNAA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749548701 478 FVAFTGTPLLKEDKTT-NKFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFDRITDGLSEAQKA 550
Cdd:pfam18766 149 FIGFTGTPILKKDKNTrAVFGDYIDTYTIQDAVEDGATVPILYEGRLAELELDDEALDEEFEEITEDLEDEERE 222
|
|
| DEXHc_RE_I_HsdR |
cd18030 |
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ... |
297-505 |
1.38e-68 |
|
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: 228.65 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 297 LLEMTRFFTLFD--KKTGKIVARYQQVFGIKRLLERIST-RRPDGGREGGVIWHTTGSGKSYTMVFLSKALILHdsLKQC 373
Cdd:cd18030 1 LLDVLRNFIVFDedDDKTKKVARYYQYYAVEAALERIKTaTNKDGDKKGGYIWHTQGSGKSLTMFKAAKLLIED--PKNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 374 RIVVVTDRVDLEGQLSGTFVSGGelagkdDKAKAMATSGQKLAQQIGSGKERIIFTLIQKFNSATK--LPECVNTSPDII 451
Cdd:cd18030 79 KVVFVVDRKDLDYQTSSTFSRFA------AEDVVRANSTKELKELLKNLSGGIIVTTIQKFNNAVKeeSKPVLIYRKNIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749548701 452 VLIDEGHRSQGGENHVRMKLALPNAAFVAFTGTPLLKE-DKTTNK-FGPIVHAYTM 505
Cdd:cd18030 153 VIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEgDKTTEKvFGDYLHKYTI 208
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
309-497 |
1.26e-10 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 62.12 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 309 KKTGKIVARYQQVFGIKRLLEristrrpdgGREGGVIWHTTGSGKSYTMVFLskALILHDSLKQCRIVVVTDRVDLEGQL 388
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLS---------GLRDVILAAPTGSGKTLAALLP--ALEALKRGKGGRVLVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 389 SGTFVsggELAGKDDKAKAMATSG---QKLAQQIGSGKERIIFTLIQKFNSATKLPECVNTSPDIIVlIDEGHRSQGGEN 465
Cdd:smart00487 71 AEELK---KLGPSLGLKVVGLYGGdskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVI-LDEAHRLLDGGF 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 749548701 466 HVRM----KLALPNAAFVAFTGTPLLKEDKTTNKFG 497
Cdd:smart00487 147 GDQLekllKLLPKNVQLLLLSATPPEEIENLLELFL 182
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
12-1087 |
0e+00 |
|
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: 801.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 12 EYSAKIPALTLLTSLGWTFLSPKqimDYRGYKQDEVVLRPVLREELSKRSfmaggktCQLSEKALANLISQVCSPALNeG 91
Cdd:COG0610 6 EAALEQAIIELLQELGYEYLSGP---DIAPEDESEVLLEDNLRAALERLN-------PGLSDDEIERALRELTKPESN-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 92 LLKANERMYNHLLYGIAVTefVDGKKVNPTIALIDWEHPENNQFHFTEEFTVlrSGGVETRRPDIVCFVNGIPLAVIEAK 171
Cdd:COG0610 75 LLEANKGFYDLLRNGVKVE--YDGEEKTKTVRLIDFKNPENNDFLVVNQFTV--SGGNYKRRPDVVLFVNGLPLVVIELK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 172 SPAghgkKGPTIDEGISQSIRNQfnDEIPQLFVYSQLLLSINGHDGRYGTCHTPMKFWAAWREEDitdpqmyalrNHPLS 251
Cdd:COG0610 151 NPL----TQVTIKEAFNQIQRYR--REIPGLFAYNQLFVISDGVEARYGTNTAPFEFFLPWKDGD----------GNDLN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 252 TEQIHALfdhrpsvdlkwyqqlidggelavsgqDKLLISLLSPERLLEMTRFFTLFDKKTG---KIVARYQQVFGIKRLL 328
Cdd:COG0610 215 PDGITDL--------------------------DYLIEGLLSKERLLDIIRNFIVFDEDEGgliKIVARYHQYFAVRKAV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 329 ERIstRRPDGGREGGVIWHTTGSGKSYTMVFLSKALILHDSLKQCRIVVVTDRVDLEGQLSGTFVSGGElagkddKAKAM 408
Cdd:COG0610 269 ERV--KEAEGDGKGGVIWHTQGSGKSLTMVFLAQKLARLPDLDNPTVVVVTDRKDLDDQLFDTFKAFGR------ESVVQ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 409 ATSGQKLAQQIGSGKERIIFTLIQKFNSATK--LPECVNTSPDIIVLIDEGHRSQGGENHVRMKLALPNAAFVAFTGTPL 486
Cdd:COG0610 341 AESRADLRELLESDSGGIIVTTIQKFPEALDeiKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPI 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 487 LKEDKTT-NKFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFDRITDGLSEAQKADLKRKYARKGEVYSA 565
Cdd:COG0610 421 FKEDRTTlEVFGDYIHTYTITQAIEDGATLPLLYEYRLAKLKLDKEKIDEEFDELTEGLDDEEKEKLKAKWALLEEVLGA 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 566 DDRIRLIALDIATHFSKNIDEG-LKGQLACDSKISAIKYKKYLDEAG------LFESAVVISPPDTREGntevdesklPE 638
Cdd:COG0610 501 PERIEQIAEDIVEHFEERTRPGkGKAMVVTSSREAAVRYYEAFDKLRpewgykPLKIAVVFSGSANDDP---------EE 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 639 VTKWwkdnvgtqDESVYTRNIISRF-DTDEKLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNLIQAIARVNRLHPLKKF 717
Cdd:COG0610 572 LKEH--------GNKEYEKDLAKRFkDPDDPLKLLIVVDMLLTGFDAPSLHTLYVDKPLKGHNLMQAISRVNRVFPGKPY 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 718 GLLIDYRGILAELDTTIGKYqdlASRTQGGYDIKDIDglysamsSEYKRLPHLYNQLWAIFA-GVKNKNDTEQLRAVLVP 796
Cdd:COG0610 644 GLIVDYRGIFENLKKALALY---SEEDGKEDVLTDPE-------EALEELKEALDELRALFPeGVDFSAFDPTEKLEALD 713
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 797 KMEERdgemVDIHQKTRDDFFEALTAFAGCLKVALQsatfftDKSFTEQDRNLYKETVKQMSSLRQWaMQVSGEQVNYDD 876
Cdd:COG0610 714 EAVER----FLGDEEARKEFKKLFKELSRLYNLLSP------DDEFGDLELEKYRDDVSFYLALRAK-LRKLGEKLDLKE 782
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 877 YAEQVKKLLDKHVtgvevrepdgvyevgkmgKSEKpeewdnnktrnetdiiktrvtKMIEQELRDDPYAQEAFSKLLRMA 956
Cdd:COG0610 783 YEEKIRQLLDEAI------------------DLER---------------------KEIKPRIKQNPVQYRKFSELLEEI 823
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 957 IEEAEKLFDHPLKQYLLFREFEEQVEARKLSDIPDALvvNKHAQAYYGVFKKELPEvfavndvqvqDKWTKLAFEVDNII 1036
Cdd:COG0610 824 IEEYNNGALDADEVLEELEELAKEVKEEEERAEEEGL--NEEELAFYDALAENLGD----------EKLKELAKELDDLL 891
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 749548701 1037 VKAVAENSLNPQDIEKVVKTSLLPLLFTacreigAGMNQVNRIVETIIQIL 1087
Cdd:COG0610 892 KKNVTVDWRKRESVRAKLRDAIKRLLRK------YGYPKQDEAVEEVYEQA 936
|
|
| hsdR |
TIGR00348 |
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ... |
92-739 |
3.18e-129 |
|
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: 408.71 E-value: 3.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 92 LLKANERMYNHLLYGIAVTEFVDGKKVNpTIALIDWEHPENNQFHFTEEFTVLRSGGvetrRPDIVCFVNGIPLAVIEAK 171
Cdd:TIGR00348 64 LYETNKIFYDYIKNGVKIKESQKGEKKR-IVKLIDFRNISQNIFQFANQVSFKGHNI----RPDVTLFVNGIPLVIIELK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 172 spaghgKKGPTIDEGISQSIRNQfnDEIPQLFVYSQLLLSINGHDGRYGTCH--TPMKFWAAWREEDITDPqmyalrnhp 249
Cdd:TIGR00348 139 ------KRSVTIREAFNQIKRYE--KEIPELFKYVQIFVISNGTDTRYYTGSdeDDFDFTFNWKESDNKLI--------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 250 lsteqihalfdhrpsvdlKWYQQLIdggelavsgqdkllISLLSPERLLEMTRFFTLFDKKTG---KIVARYQQVFGIKR 326
Cdd:TIGR00348 202 ------------------EDLKEFD--------------ILLLKKERLLDFIRNFIIFDKDTGlvtKPYQRYMQYRAVKK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 327 LLERISTRRPDGGREGGVIWHTTGSGKSYTMVFLskALILHDSLKQCRIVVVTDRVDLEGQLSGTFVSGGelagKDDKAK 406
Cdd:TIGR00348 250 IVESITRKTWGKDERGGLIWHTQGSGKTLTMLFA--ARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQ----KDCAER 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 407 AmaTSGQKLAQQIGSGKERIIFTLIQKFNSatKLPECVNTSP----DIIVLIDEGHRSQGGENHVRMKLALPNAAFVAFT 482
Cdd:TIGR00348 324 I--ESIAELKELLEKDDGGIIITTIQKFDD--KLKEEEEKFPvdrkEVVVIFDEAHRSQYGELAKNLKKALKNASFFGFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 483 GTPLLKEDKTTN-----KFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFD----RITDGLSEAQKADLK 553
Cdd:TIGR00348 400 GTPIFKKDRDTSltfayVFGRYLHRYFITDAIRDGLTVKIDYEDRLPEDHLDKKKLDAFFDeifeLLPERIREITKESLK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 554 RKYARKGEVYSADDRIRLIALDIATHFSKNID-EGLKGQLACDSKISAIKYKKYLDE---AGLFESAVVISppdtregNT 629
Cdd:TIGR00348 480 EKLQKTKKILFNEDRLESIAKDIAEHYAKFKElFKFKAMVVAISRYACVEEKNALDEelnEKFEASAIVMT-------GK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 630 EVDESKLPEVTKWWKDNVGTQDESVYTRNIISRFDTDEKLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNLIQAIARVN 709
Cdd:TIGR00348 553 ESDDAEIRDYNKHIRTKFDKSDGFEIYYKDLERFKKNENPKLLIVVDMLLTGFDAPILNTLYLDKPLKYHGLLQAIARTN 632
|
650 660 670
....*....|....*....|....*....|.
gi 749548701 710 RLH-PLKKFGLLIDYRGILAELDTTIGKYQD 739
Cdd:TIGR00348 633 RIDgKDKTFGLIVDYRGLEKSLIDALSLYGN 663
|
|
| SWI2_SNF2 |
pfam18766 |
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins. |
319-550 |
3.51e-105 |
|
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
Pssm-ID: 465860 [Multi-domain] Cd Length: 222 Bit Score: 328.62 E-value: 3.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 319 QQVFGIKRLLERISTrrpDGGREGGVIWHTTGSGKSYTMVFLSKALILHdsLKQCRIVVVTDRVDLEGQLSGTFVSGGEl 398
Cdd:pfam18766 1 QQYFAVNKAVERVLE---DGDRRGGVIWHTQGSGKSLTMVFLARKLRRE--LKNPTVVVVTDRNDLDDQLTKTFAACGR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 399 agkddKAKAMATSGQKLAQQIGsGKERIIFTLIQKFNSA-TKLPECVNTSPDIIVLIDEGHRSQGGENHVRMKLALPNAA 477
Cdd:pfam18766 75 -----EVPVQAESRKDLRELLR-GSGGIIFTTIQKFGETpDEGFPVLSDRRNIIVLVDEAHRSQYGGLAANMRDALPNAA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749548701 478 FVAFTGTPLLKEDKTT-NKFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAIDAWFDRITDGLSEAQKA 550
Cdd:pfam18766 149 FIGFTGTPILKKDKNTrAVFGDYIDTYTIQDAVEDGATVPILYEGRLAELELDDEALDEEFEEITEDLEDEERE 222
|
|
| DEXHc_RE_I_HsdR |
cd18030 |
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ... |
297-505 |
1.38e-68 |
|
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: 228.65 E-value: 1.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 297 LLEMTRFFTLFD--KKTGKIVARYQQVFGIKRLLERIST-RRPDGGREGGVIWHTTGSGKSYTMVFLSKALILHdsLKQC 373
Cdd:cd18030 1 LLDVLRNFIVFDedDDKTKKVARYYQYYAVEAALERIKTaTNKDGDKKGGYIWHTQGSGKSLTMFKAAKLLIED--PKNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 374 RIVVVTDRVDLEGQLSGTFVSGGelagkdDKAKAMATSGQKLAQQIGSGKERIIFTLIQKFNSATK--LPECVNTSPDII 451
Cdd:cd18030 79 KVVFVVDRKDLDYQTSSTFSRFA------AEDVVRANSTKELKELLKNLSGGIIVTTIQKFNNAVKeeSKPVLIYRKNIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749548701 452 VLIDEGHRSQGGENHVRMKLALPNAAFVAFTGTPLLKE-DKTTNK-FGPIVHAYTM 505
Cdd:cd18030 153 VIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEgDKTTEKvFGDYLHKYTI 208
|
|
| HsdR_N |
cd22332 |
N-terminal domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I and ... |
18-303 |
7.86e-39 |
|
N-terminal domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I and similar systems; The N-terminal endonuclease-like domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I belongs to a wider superfamily of PDDEXK nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411736 [Multi-domain] Cd Length: 226 Bit Score: 144.33 E-value: 7.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 18 PALTLLTSLGWTFLSPKQIMDYRgykqDEVVLRPVLREELSKRSFMAGGKTcQLSEKALANLISQvcspalnegllkane 97
Cdd:cd22332 8 ALIELLQELGYEYLPGPELERDK----TEVLLEDNLREALERLNPDIPSGV-PLTDNEFNQLLLE--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 98 rmYNHLLYGIAVTEFVDGKKVNPTIaLIDWEHPENNQFHFTEEFTVlrSGGVETRRPDIVCFVNGIPLAVIEAKSPaghg 177
Cdd:cd22332 68 --LGRDVTPLLTLDDDGGKEKTRVI-LIDFENPENNDFQVVNQFTV--EGGKHNRRPDVVLFVNGLPLVVIELKNP---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 178 kkGPTIDEGISQSIRNQFNDEIPQLFVYSQLLLSINGHDGRYGTCHTPMKFWAAWREEDitdpqmyalrnhplsteqiha 257
Cdd:cd22332 139 --GVTIREAYNQIKRYYKEIFIPGLFKYNQLFVISNGTETRYGANTAPYERFNEWFTFD--------------------- 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 749548701 258 lfdhrpsvdlkWYqqliDGGELAVSGQDKLLISLLSPERLLEMTRF 303
Cdd:cd22332 196 -----------WA----DEDNEPITDLETFIKGLLSKERLLDLIRN 226
|
|
| SF2_C_EcoR124I-like |
cd18800 |
C-terminal helicase domain of EcoR124I HsdR-like restriction enzyme family helicases; This ... |
654-724 |
5.10e-26 |
|
C-terminal helicase domain of EcoR124I 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 EcoR124I R protein. EcoR124I recognizes the sequence, 5'-GAAN(6)RTCG-3', and cleaves at random sites. 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: 350187 [Multi-domain] Cd Length: 82 Bit Score: 102.26 E-value: 5.10e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749548701 654 VYTRNIISRFDTDEKLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNLIQAIARVNRLHP-LKKFGLLIDYR 724
Cdd:cd18800 11 VVTSSRRAAVRYYKALDLLIVVDMLLTGFDAPSLNTLYVDKPLKYHGLIQAIARVNRVYKdEKEFGLIVDYR 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
318-753 |
9.79e-22 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 100.87 E-value: 9.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 318 YQQvfgikRLLERISTRRPDGGREGGVIwHTTGSGKSYTMVFLSKALilhdsLKQCRIVVVTDRVDLEGQLSGTFvsgge 397
Cdd:COG1061 84 YQQ-----EALEALLAALERGGGRGLVV-APTGTGKTVLALALAAEL-----LRGKRVLVLVPRRELLEQWAEEL----- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 398 lagKDDKAKAMATSGQKlaqqigSGKERIIFTLIQKFNSATKLPECVNTsPDIIVlIDEGHRSqGGENHVRMKLALPNAA 477
Cdd:COG1061 148 ---RRFLGDPLAGGGKK------DSDAPITVATYQSLARRAHLDELGDR-FGLVI-IDEAHHA-GAPSYRRILEAFPAAY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 478 FVAFTGTPLLKEDKT--TNKFGPIVHAYTMQRAVEDKAVTPLLYEERIPDLEVNDRAidawFDRITDGLSEAQKADLKRK 555
Cdd:COG1061 216 RLGLTATPFRSDGREilLFLFDGIVYEYSLKEAIEDGYLAPPEYYGIRVDLTDERAE----YDALSERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 556 YARKGEVYSAD-DRIRLIALdiathfsknideglkgqlaCDSKISAIKYKKYLDEAGLfeSAVVISppdtreGNTEVDEs 634
Cdd:COG1061 292 DKILRELLREHpDDRKTLVF-------------------CSSVDHAEALAELLNEAGI--RAAVVT------GDTPKKE- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 635 klpevtkwwkdnvgtqdesvyTRNIISRFDTDEkLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNL-IQAIARVNRLHP 713
Cdd:COG1061 344 ---------------------REEILEAFRDGE-LRILVTVDVLNEGVDVPRLDVAILLRPTGSPREfIQRLGRGLRPAP 401
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 749548701 714 LKKFGLLIDYRGILAELDTTIgkYQDLASRTQGGYDIKDI 753
Cdd:COG1061 402 GKEDALVYDFVGNDVPVLEEL--AKDLRDLAGYRVEFLDE 439
|
|
| HSDR_N |
pfam04313 |
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ... |
8-225 |
5.12e-21 |
|
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: 90.83 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 8 KFQEEYSAKIPALTLLTSLGWTFLSPKqimdyRGYKQDEVVLRpvlreelskrsfmaggktcqlsekalanlisqvcspa 87
Cdd:pfam04313 1 ILSEEEVEQKLILPLLKALGYDVLNEV-----RGIKAEVILEK------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 88 lneglLKANERMYNHLLYGIAvtefvDGKKVNptialidwehpENNQFHFTEEFTVLrsgGVETRRPDIVCFVNGIPLAV 167
Cdd:pfam04313 39 -----LDGNEAFYRLLKYGVT-----DGITKT-----------ENNSFQVANQVEVK---GVQKRRPDYVLFVNGLPLAV 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749548701 168 IEAKSPAGhgkkgptiDEGISQsIRNQFNDE---IPQLFVYS--QLLLSINGHDGRYGTCHTP 225
Cdd:pfam04313 95 IELKRPGT--------EEAINQ-IRRYEKDSfnaIPQLFRYAnvQFGILSNGRETRFYTKTAK 148
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
313-485 |
3.09e-19 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 85.80 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 313 KIVARYQQVFGIKRLLERISTrrpdgGREGGVIWHTTGSGKSYTMVFLSKALILHDSLKqcRIVVVTDRVDLEGQLSGTF 392
Cdd:pfam04851 1 KLELRPYQIEAIENLLESIKN-----GQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK--KVLFLVPRKDLLEQALEEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 393 ---VSGGELAGKDdkakamaTSGQKLAQQigSGKERIIFTLIQKFNSATKLP--ECVNTSPDIIVlIDEGHRSqGGENHV 467
Cdd:pfam04851 74 kkfLPNYVEIGEI-------ISGDKKDES--VDDNKIVVTTIQSLYKALELAslELLPDFFDVII-IDEAHRS-GASSYR 142
|
170
....*....|....*...
gi 749548701 468 RMKLALPNAAFVAFTGTP 485
Cdd:pfam04851 143 NILEYFKPAFLLGLTATP 160
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
309-497 |
1.26e-10 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 62.12 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 309 KKTGKIVARYQQVFGIKRLLEristrrpdgGREGGVIWHTTGSGKSYTMVFLskALILHDSLKQCRIVVVTDRVDLEGQL 388
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLS---------GLRDVILAAPTGSGKTLAALLP--ALEALKRGKGGRVLVLVPTRELAEQW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 389 SGTFVsggELAGKDDKAKAMATSG---QKLAQQIGSGKERIIFTLIQKFNSATKLPECVNTSPDIIVlIDEGHRSQGGEN 465
Cdd:smart00487 71 AEELK---KLGPSLGLKVVGLYGGdskREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVI-LDEAHRLLDGGF 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 749548701 466 HVRM----KLALPNAAFVAFTGTPLLKEDKTTNKFG 497
Cdd:smart00487 147 GDQLekllKLLPKNVQLLLLSATPPEEIENLLELFL 182
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
341-484 |
4.54e-09 |
|
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: 56.26 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 341 EGGVIWHTTGSGKSytmVFLSKALILHDSLKQCRIVVVTDRVDLEGQlsgTFVSGGELAGKDDKAkAMATSGQKLAQQ-- 418
Cdd:cd00046 2 ENVLITAPTGSGKT---LAALLAALLLLLKKGKKVLVLVPTKALALQ---TAERLRELFGPGIRV-AVLVGGSSAEERek 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749548701 419 IGSGKERIIFTLIQKFNSAtKLPECVNTSPDIIVLI-DEGHRSQGGE-NHVRM-----KLALPNAAFVAFTGT 484
Cdd:cd00046 75 NKLGDADIIIATPDMLLNL-LLREDRLFLKDLKLIIvDEAHALLIDSrGALILdlavrKAGLKNAQVILLSAT 146
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
317-485 |
1.08e-07 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 52.31 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 317 RYQQVFGIKRLLERISTRRpdggregGVIWHTTGSGKSYTMVflskALILHdsLKQCRIVVVTDRVDLEGQLsgtfvsgg 396
Cdd:cd17926 2 RPYQEEALEAWLAHKNNRR-------GILVLPTGSGKTLTAL----ALIAY--LKELRTLIVVPTDALLDQW-------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 397 elagkddKAKAMATSGQKLAQQIGSGKER------IIFTLIQKFNSATKLPECVNTSPDIIVlIDEGHRSqGGENHVRMK 470
Cdd:cd17926 61 -------KERFEDFLGDSSIGLIGGGKKKdfddanVVVATYQSLSNLAEEEKDLFDQFGLLI-VDEAHHL-PAKTFSEIL 131
|
170
....*....|....*
gi 749548701 471 LALPNAAFVAFTGTP 485
Cdd:cd17926 132 KELNAKYRLGLTATP 146
|
|
| HsdR |
COG4096 |
Type I site-specific restriction endonuclease, part of a restriction-modification system ... |
150-579 |
1.98e-07 |
|
Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];
Pssm-ID: 443272 [Multi-domain] Cd Length: 806 Bit Score: 55.23 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 150 ETRRPDIVCFV-NGIPLAVIEAKspaghgKKGPTIDEGISQSIR--NQFNDEIPQL-FVYSQlllsiNGHdgrygtchtP 225
Cdd:COG4096 49 GKGYADYVLFGdDGKPLAVVEAK------RTSKDVSAGLQQAKLyaDGLEKQYGQVpFIFAT-----NGR---------E 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 226 MKFWaawreeDITDPqmyalrnHPLSTEqihaLFD-HRPSVDLKWYQQLIDGGElavsgqdkllisllspERLLEMTrff 304
Cdd:COG4096 109 IWFW------DDRDP-------YPRERE----VDGfPSPEELWELLKRRKGTAR----------------KRLATEP--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 305 tlFDkktGKIVARYQQVFGIKRLLERISTRRPdggreggviwHT-----TGSGKSYTMVFLSKALILHDSLKqcRIVVVT 379
Cdd:COG4096 153 --YN---DGIALRYYQIEAIRRVEEAIAKGQR----------RAllvmaTGTGKTRTAIALIYRLLKAGRAK--RILFLA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 380 DRVDLEGQLSGTFvsggelagkddkaKAMATSGQKLAQQIGSGKE-----RIIFTLIQKFNSATKLPECVNT----SP-- 448
Cdd:COG4096 216 DRNALVDQAKNAF-------------KPFLPDLDAFTKLYNKSKDidksaRVYFSTYQTMMNRIDGEEEEPGyrqfPPdf 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 449 -DIIVlIDEGHRsqGGENHVRMKLALPNAAFVAFTGTPLLKEDKTTNKF--GPIVHAYTMQRAVEDKAVTPllYEERIPD 525
Cdd:COG4096 283 fDLII-IDECHR--GIYSKWRAILDYFDALQIGLTATPKDTIDRNTYEYfnGNPVYTYSLEQAVADGFLVP--YKVIRID 357
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410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749548701 526 LEVNDRAIdawfdRITDG--LSEAQKADLKRKYARKGEVYSA---------DDRIRLIALDIATH 579
Cdd:COG4096 358 TKFDREGI-----RYDAGedLSDEEGEEIELEELEEDREYEAkdfnrkvvnEDTTRKVLEELMEY 417
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| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
317-460 |
5.08e-07 |
|
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: 50.64 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 317 RYQQVFGIKRLLERIStrrpDGGREGGVIwHTTGSGKSYTMVFLSKALILHDSLKqcRIVVVTDRVDLEGQLSGTF---- 392
Cdd:cd18032 2 RYYQQEAIEALEEARE----KGQRRALLV-MATGTGKTYTAAFLIKRLLEANRKK--RILFLAHREELLEQAERSFkevl 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749548701 393 --VSGGELAGKDDKakamatsgqklaqqigSGKERIIFTLIQKFNSATKLPEcvnTSPD----IIvlIDEGHRS 460
Cdd:cd18032 75 pdGSFGNLKGGKKK----------------PDDARVVFATVQTLNKRKRLEK---FPPDyfdlII--IDEAHHA 127
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
656-723 |
7.37e-05 |
|
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: 43.32 E-value: 7.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749548701 656 TRNIISRFDTDE-KLKLLIVVDKLLTGFDEPKNTVLYIDKPLKSHNL-IQAIARVNRLHPLKKFGLLIDY 723
Cdd:cd18799 46 GDEALILLFFGElKPPILVTVDLLTTGVDIPEVDNVVFLRPTESRTLfLQMLGRGLRLHEGKDFFTILDF 115
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