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Conserved domains on  [gi|659515400|gb|KEJ91151|]
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hypothetical protein EH55_12040, partial [Synergistes jonesii]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COG0610 super family cl33974
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 2-528 2.24e-123

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


The actual alignment was detected with superfamily member COG0610:

Pssm-ID: 440375 [Multi-domain]  Cd Length: 936  Bit Score: 383.83  E-value: 2.24e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   2 QQIIEQIKT--LRTPLKLNGFI-----NGKSVSItrdnpddkEHFGKEVSLKIYDRQEIAagQSRYQIARQPKFTAKTSm 74
Cdd:COG0610   61 ERALRELTKpeSNGLLEANKGFydllrNGVKVEY--------DGEEKTKTVRLIDFKNPE--NNDFLVVNQFTVSGGNY- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  75 lpGRRGDFMLLINGMPLIHVELKKS--GIPVSQAYNQIEKYSHEgvFTGLFALVQVFVAVNPEEAVYFANpgpdgKFNSD 152
Cdd:COG0610  130 --KRRPDVVLFVNGLPLVVIELKNPltQVTIKEAFNQIQRYRRE--IPGLFAYNQLFVISDGVEARYGTN-----TAPFE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 153 FYFHWADFNNE-----PINDWKTLASTFLSIPMAHQLIGFYTVADDTDG--ILKVMRSYQYYAANKISDTVAKHkweNGN 225
Cdd:COG0610  201 FFLPWKDGDGNdlnpdGITDLDYLIEGLLSKERLLDIIRNFIVFDEDEGglIKIVARYHQYFAVRKAVERVKEA---EGD 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 226 QLGGYIWHTTGSGKTMTSFKSAQLIANSKDADK--VVFLIDRIELGTQSAGEYRGFAEatDDIQETEDTSVLIAKLKSnd 303
Cdd:COG0610  278 GKGGVIWHTQGSGKSLTMVFLAQKLARLPDLDNptVVVVTDRKDLDDQLFDTFKAFGR--ESVVQAESRADLRELLES-- 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 304 PANTLIVTSVQKMSNIKDdtegklKKADLDLITSKRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGFSGTPIQAENEkk 383
Cdd:COG0610  354 DSGGIIVTTIQKFPEALD------EIKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPIFKEDR-- 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 384 gsTTADVFGSELHRYSIADGIRDKNVLGFDPDKV---LTFKEKDIREAVAldkakakTVAEVFSDAKKQKIyyeymhnvp 460
Cdd:COG0610  426 --TTLEVFGDYIHTYTITQAIEDGATLPLLYEYRlakLKLDKEKIDEEFD-------ELTEGLDDEEKEKL--------- 487

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659515400 461 magfedangKYVKGIEDFLLENgqyrtEEHQKMVVRDIIDNWITISHNHKFH*IFATSSIPEAIQYYK 528
Cdd:COG0610  488 ---------KAKWALLEEVLGA-----PERIEQIAEDIVEHFEERTRPGKGKAMVVTSSREAAVRYYE 541
 
Name Accession Description Interval E-value
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 2-528 2.24e-123

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: 383.83  E-value: 2.24e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   2 QQIIEQIKT--LRTPLKLNGFI-----NGKSVSItrdnpddkEHFGKEVSLKIYDRQEIAagQSRYQIARQPKFTAKTSm 74
Cdd:COG0610   61 ERALRELTKpeSNGLLEANKGFydllrNGVKVEY--------DGEEKTKTVRLIDFKNPE--NNDFLVVNQFTVSGGNY- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  75 lpGRRGDFMLLINGMPLIHVELKKS--GIPVSQAYNQIEKYSHEgvFTGLFALVQVFVAVNPEEAVYFANpgpdgKFNSD 152
Cdd:COG0610  130 --KRRPDVVLFVNGLPLVVIELKNPltQVTIKEAFNQIQRYRRE--IPGLFAYNQLFVISDGVEARYGTN-----TAPFE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 153 FYFHWADFNNE-----PINDWKTLASTFLSIPMAHQLIGFYTVADDTDG--ILKVMRSYQYYAANKISDTVAKHkweNGN 225
Cdd:COG0610  201 FFLPWKDGDGNdlnpdGITDLDYLIEGLLSKERLLDIIRNFIVFDEDEGglIKIVARYHQYFAVRKAVERVKEA---EGD 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 226 QLGGYIWHTTGSGKTMTSFKSAQLIANSKDADK--VVFLIDRIELGTQSAGEYRGFAEatDDIQETEDTSVLIAKLKSnd 303
Cdd:COG0610  278 GKGGVIWHTQGSGKSLTMVFLAQKLARLPDLDNptVVVVTDRKDLDDQLFDTFKAFGR--ESVVQAESRADLRELLES-- 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 304 PANTLIVTSVQKMSNIKDdtegklKKADLDLITSKRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGFSGTPIQAENEkk 383
Cdd:COG0610  354 DSGGIIVTTIQKFPEALD------EIKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPIFKEDR-- 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 384 gsTTADVFGSELHRYSIADGIRDKNVLGFDPDKV---LTFKEKDIREAVAldkakakTVAEVFSDAKKQKIyyeymhnvp 460
Cdd:COG0610  426 --TTLEVFGDYIHTYTITQAIEDGATLPLLYEYRlakLKLDKEKIDEEFD-------ELTEGLDDEEKEKL--------- 487

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659515400 461 magfedangKYVKGIEDFLLENgqyrtEEHQKMVVRDIIDNWITISHNHKFH*IFATSSIPEAIQYYK 528
Cdd:COG0610  488 ---------KAKWALLEEVLGA-----PERIEQIAEDIVEHFEERTRPGKGKAMVVTSSREAAVRYYE 541
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
 55-528 1.83e-66

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: 227.28  E-value: 1.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   55 AGQSRYQIARQPKFTAKTSmlpgrRGDFMLLINGMPLIHVELKKSGIPVSQAYNQIEKYSHEgvFTGLFALVQVFVAVNP 134
Cdd:TIGR00348 101 ISQNIFQFANQVSFKGHNI-----RPDVTLFVNGIPLVIIELKKRSVTIREAFNQIKRYEKE--IPELFKYVQIFVISNG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  135 EEAVYFANpGPDGKFnsDFYFHWADFNNEPINDWKTLASTFLSIPMAHQLIGFYTVADDTDGIL--KVMRSYQYYAANKI 212
Cdd:TIGR00348 174 TDTRYYTG-SDEDDF--DFTFNWKESDNKLIEDLKEFDILLLKKERLLDFIRNFIIFDKDTGLVtkPYQRYMQYRAVKKI 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  213 SDTVAKHKWENgNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGFAEatDDIQETEDT 292
Cdd:TIGR00348 251 VESITRKTWGK-DERGGLIWHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQK--DCAERIESI 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  293 SVLIAKLKSNDpaNTLIVTSVQKM-SNIKDDTEGKLkkadldlITSKRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGF 371
Cdd:TIGR00348 328 AELKELLEKDD--GGIIITTIQKFdDKLKEEEEKFP-------VDRKEVVVIFDEAHRSQYGELAKNLKKALKNASFFGF 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  372 SGTPIQAENEKKGSTTADVFGSELHRYSIADGIRDKNVLGFDPDKVLTFKEKDIREAVALDKAKAKTVAEVFSDAKKQKI 451
Cdd:TIGR00348 399 TGTPIFKKDRDTSLTFAYVFGRYLHRYFITDAIRDGLTVKIDYEDRLPEDHLDKKKLDAFFDEIFELLPERIREITKESL 478

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659515400  452 yyeymhnvpmagfedanGKYVKGIEDFLLengqyrTEEHQKMVVRDIIDNWITISHNHKFH*IFATSSIPEAIQYYK 528
Cdd:TIGR00348 479 -----------------KEKLQKTKKILF------NEDRLESIAKDIAEHYAKFKELFKFKAMVVAISRYACVEEKN 532
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
 181-400 4.69e-65

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: 210.16  E-value: 4.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 181 AHQLIGFYTVADDTDG-ILKVMRSYQYYAANKISDTVAKHKWENGNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKV 259
Cdd:cd18030    1 LLDVLRNFIVFDEDDDkTKKVARYYQYYAVEAALERIKTATNKDGDKKGGYIWHTQGSGKSLTMFKAAKLLIEDPKNPKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 260 VFLIDRIELGTQSAGEYRGFAeATDDIQ--ETEDTSVLIAKLKsndpaNTLIVTSVQKMSNIKDDTEgklkkaDLDLITS 337
Cdd:cd18030   81 VFVVDRKDLDYQTSSTFSRFA-AEDVVRanSTKELKELLKNLS-----GGIIVTTIQKFNNAVKEES------KPVLIYR 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 659515400 338 KRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGFSGTPIQAENEKkgsTTADVFGSELHRYSI 400
Cdd:cd18030  149 KNIVVIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEGDK---TTEKVFGDYLHKYTI 208
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
 204-449 3.23e-62

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


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 203.05  E-value: 3.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  204 YQYYAANKISDTVAkhkwENGNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGFAEAT 283
Cdd:pfam18766   1 QQYFAVNKAVERVL----EDGDRRGGVIWHTQGSGKSLTMVFLARKLRRELKNPTVVVVTDRNDLDDQLTKTFAACGREV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  284 DdiQETEDTSVLIAKLksnDPANTLIVTSVQKMSNIKDDTEGKLKkadldliTSKRIVFIVDECHRSTFGDMMRVVKQTF 363
Cdd:pfam18766  77 P--VQAESRKDLRELL---RGSGGIIFTTIQKFGETPDEGFPVLS-------DRRNIIVLVDEAHRSQYGGLAANMRDAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  364 PKALFFGFSGTPIqaenEKKGSTTADVFGSELHRYSIADGIRDKNVLgfdpdKVL---TFKEKDIREAvALDKaKAKTVA 440
Cdd:pfam18766 145 PNAAFIGFTGTPI----LKKDKNTRAVFGDYIDTYTIQDAVEDGATV-----PILyegRLAELELDDE-ALDE-EFEEIT 213


                  ....*....
gi 659515400  441 EVFSDAKKQ 449
Cdd:pfam18766 214 EDLEDEERE 222
DEXDc smart00487
DEAD-like helicases superfamily;
199-378 9.34e-13

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 67.13  E-value: 9.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   199 KVMRSYQYYAANKISDtvakhkwengNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRG 278
Cdd:smart00487   7 EPLRPYQKEAIEALLS----------GLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   279 FAEATDD----IQETEDTSVLIAKLKSNDPAntLIVTSVQKMSNIKDdtEGKLKKADLDLItskrivfIVDECHR---ST 351
Cdd:smart00487  77 LGPSLGLkvvgLYGGDSKREQLRKLESGKTD--ILVTTPGRLLDLLE--NDKLSLSNVDLV-------ILDEAHRlldGG 145

                          170       180
                   ....*....|....*....|....*...
gi 659515400   352 FGD-MMRVVKQTFPKALFFGFSGTPIQA 378
Cdd:smart00487 146 FGDqLEKLLKLLPKNVQLLLLSATPPEE 173
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 235-349 9.67e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  235 TGSGKTMTSfksaqlIA------NSKDADKVVFLIDRIELGTQSAGEYR-----GFAEATD--DIQETEDtsvliaklKS 301
Cdd:PRK11448  442 TGTGKTRTA------IAlmyrllKAKRFRRILFLVDRSALGEQAEDAFKdtkieGDQTFASiyDIKGLED--------KF 507

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 659515400  302 NDPANTLIVTSVQKMsnIK-----DDTEGKLKKADLDLItskrivfIVDECHR 349
Cdd:PRK11448  508 PEDETKVHVATVQGM--VKrilysDDPMDKPPVDQYDCI-------IVDEAHR 551
 
Name Accession Description Interval E-value
COG0610 COG0610
Type I site-specific restriction-modification system, R (restriction) subunit and related ...
 2-528 2.24e-123

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: 383.83  E-value: 2.24e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   2 QQIIEQIKT--LRTPLKLNGFI-----NGKSVSItrdnpddkEHFGKEVSLKIYDRQEIAagQSRYQIARQPKFTAKTSm 74
Cdd:COG0610   61 ERALRELTKpeSNGLLEANKGFydllrNGVKVEY--------DGEEKTKTVRLIDFKNPE--NNDFLVVNQFTVSGGNY- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  75 lpGRRGDFMLLINGMPLIHVELKKS--GIPVSQAYNQIEKYSHEgvFTGLFALVQVFVAVNPEEAVYFANpgpdgKFNSD 152
Cdd:COG0610  130 --KRRPDVVLFVNGLPLVVIELKNPltQVTIKEAFNQIQRYRRE--IPGLFAYNQLFVISDGVEARYGTN-----TAPFE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 153 FYFHWADFNNE-----PINDWKTLASTFLSIPMAHQLIGFYTVADDTDG--ILKVMRSYQYYAANKISDTVAKHkweNGN 225
Cdd:COG0610  201 FFLPWKDGDGNdlnpdGITDLDYLIEGLLSKERLLDIIRNFIVFDEDEGglIKIVARYHQYFAVRKAVERVKEA---EGD 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 226 QLGGYIWHTTGSGKTMTSFKSAQLIANSKDADK--VVFLIDRIELGTQSAGEYRGFAEatDDIQETEDTSVLIAKLKSnd 303
Cdd:COG0610  278 GKGGVIWHTQGSGKSLTMVFLAQKLARLPDLDNptVVVVTDRKDLDDQLFDTFKAFGR--ESVVQAESRADLRELLES-- 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 304 PANTLIVTSVQKMSNIKDdtegklKKADLDLITSKRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGFSGTPIQAENEkk 383
Cdd:COG0610  354 DSGGIIVTTIQKFPEALD------EIKYPELSDRKNIIVIVDEAHRSQYGGLAKNMRDALPNASFFGFTGTPIFKEDR-- 425

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 384 gsTTADVFGSELHRYSIADGIRDKNVLGFDPDKV---LTFKEKDIREAVAldkakakTVAEVFSDAKKQKIyyeymhnvp 460
Cdd:COG0610  426 --TTLEVFGDYIHTYTITQAIEDGATLPLLYEYRlakLKLDKEKIDEEFD-------ELTEGLDDEEKEKL--------- 487

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 659515400 461 magfedangKYVKGIEDFLLENgqyrtEEHQKMVVRDIIDNWITISHNHKFH*IFATSSIPEAIQYYK 528
Cdd:COG0610  488 ---------KAKWALLEEVLGA-----PERIEQIAEDIVEHFEERTRPGKGKAMVVTSSREAAVRYYE 541
hsdR TIGR00348
type I site-specific deoxyribonuclease, HsdR family; This gene is part of the type I ...
 55-528 1.83e-66

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: 227.28  E-value: 1.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   55 AGQSRYQIARQPKFTAKTSmlpgrRGDFMLLINGMPLIHVELKKSGIPVSQAYNQIEKYSHEgvFTGLFALVQVFVAVNP 134
Cdd:TIGR00348 101 ISQNIFQFANQVSFKGHNI-----RPDVTLFVNGIPLVIIELKKRSVTIREAFNQIKRYEKE--IPELFKYVQIFVISNG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  135 EEAVYFANpGPDGKFnsDFYFHWADFNNEPINDWKTLASTFLSIPMAHQLIGFYTVADDTDGIL--KVMRSYQYYAANKI 212
Cdd:TIGR00348 174 TDTRYYTG-SDEDDF--DFTFNWKESDNKLIEDLKEFDILLLKKERLLDFIRNFIIFDKDTGLVtkPYQRYMQYRAVKKI 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  213 SDTVAKHKWENgNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGFAEatDDIQETEDT 292
Cdd:TIGR00348 251 VESITRKTWGK-DERGGLIWHTQGSGKTLTMLFAARKALELLKNPKVFFVVDRRELDYQLMKEFQSLQK--DCAERIESI 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  293 SVLIAKLKSNDpaNTLIVTSVQKM-SNIKDDTEGKLkkadldlITSKRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGF 371
Cdd:TIGR00348 328 AELKELLEKDD--GGIIITTIQKFdDKLKEEEEKFP-------VDRKEVVVIFDEAHRSQYGELAKNLKKALKNASFFGF 398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  372 SGTPIQAENEKKGSTTADVFGSELHRYSIADGIRDKNVLGFDPDKVLTFKEKDIREAVALDKAKAKTVAEVFSDAKKQKI 451
Cdd:TIGR00348 399 TGTPIFKKDRDTSLTFAYVFGRYLHRYFITDAIRDGLTVKIDYEDRLPEDHLDKKKLDAFFDEIFELLPERIREITKESL 478

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659515400  452 yyeymhnvpmagfedanGKYVKGIEDFLLengqyrTEEHQKMVVRDIIDNWITISHNHKFH*IFATSSIPEAIQYYK 528
Cdd:TIGR00348 479 -----------------KEKLQKTKKILF------NEDRLESIAKDIAEHYAKFKELFKFKAMVVAISRYACVEEKN 532
DEXHc_RE_I_HsdR cd18030
DEXH-box helicase domain of type I restriction enzyme HdsR subunit; The HdsR motor subunit of ...
 181-400 4.69e-65

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: 210.16  E-value: 4.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 181 AHQLIGFYTVADDTDG-ILKVMRSYQYYAANKISDTVAKHKWENGNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKV 259
Cdd:cd18030    1 LLDVLRNFIVFDEDDDkTKKVARYYQYYAVEAALERIKTATNKDGDKKGGYIWHTQGSGKSLTMFKAAKLLIEDPKNPKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 260 VFLIDRIELGTQSAGEYRGFAeATDDIQ--ETEDTSVLIAKLKsndpaNTLIVTSVQKMSNIKDDTEgklkkaDLDLITS 337
Cdd:cd18030   81 VFVVDRKDLDYQTSSTFSRFA-AEDVVRanSTKELKELLKNLS-----GGIIVTTIQKFNNAVKEES------KPVLIYR 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 659515400 338 KRIVFIVDECHRSTFGDMMRVVKQTFPKALFFGFSGTPIQAENEKkgsTTADVFGSELHRYSI 400
Cdd:cd18030  149 KNIVVIVDEAHRSQFGELAKALKKALPNATFIGFTGTPIFKEGDK---TTEKVFGDYLHKYTI 208
SWI2_SNF2 pfam18766
SWI2/SNF2 ATPase; A SWi2/SNF2 ATPase found in polyvalent proteins.
 204-449 3.23e-62

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


Pssm-ID: 465860 [Multi-domain]  Cd Length: 222  Bit Score: 203.05  E-value: 3.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  204 YQYYAANKISDTVAkhkwENGNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGFAEAT 283
Cdd:pfam18766   1 QQYFAVNKAVERVL----EDGDRRGGVIWHTQGSGKSLTMVFLARKLRRELKNPTVVVVTDRNDLDDQLTKTFAACGREV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  284 DdiQETEDTSVLIAKLksnDPANTLIVTSVQKMSNIKDDTEGKLKkadldliTSKRIVFIVDECHRSTFGDMMRVVKQTF 363
Cdd:pfam18766  77 P--VQAESRKDLRELL---RGSGGIIFTTIQKFGETPDEGFPVLS-------DRRNIIVLVDEAHRSQYGGLAANMRDAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  364 PKALFFGFSGTPIqaenEKKGSTTADVFGSELHRYSIADGIRDKNVLgfdpdKVL---TFKEKDIREAvALDKaKAKTVA 440
Cdd:pfam18766 145 PNAAFIGFTGTPI----LKKDKNTRAVFGDYIDTYTIQDAVEDGATV-----PILyegRLAELELDDE-ALDE-EFEEIT 213


                  ....*....
gi 659515400  441 EVFSDAKKQ 449
Cdd:pfam18766 214 EDLEDEERE 222
HsdR_N cd22332
N-terminal domain of HsdR motor subunit of type I restriction-modification enzyme EcoR124I and ...
 1-187 1.26e-60

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: 199.42  E-value: 1.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   1 MQQIIEQIKTLRTPLKLngfingksvsitrdnpdDKEHFGKEVSLKIYDRQEIAaGQSRYQIARQPKFTAKTSmlpGRRG 80
Cdd:cd22332   61 FNQLLLELGRDVTPLLT-----------------LDDDGGKEKTRVILIDFENP-ENNDFQVVNQFTVEGGKH---NRRP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  81 DFMLLINGMPLIHVELKKSGIPVSQAYNQIEKYSHEGVFTGLFALVQVFVAVNPEEAVYFANPGPDGKFNSDFYFHWADF 160
Cdd:cd22332  120 DVVLFVNGLPLVVIELKNPGVTIREAYNQIKRYYKEIFIPGLFKYNQLFVISNGTETRYGANTAPYERFNEWFTFDWADE 199

                        170       180
                 ....*....|....*....|....*..
gi 659515400 161 NNEPINDWKTLASTFLSIPMAHQLIGF 187
Cdd:cd22332  200 DNEPITDLETFIKGLLSKERLLDLIRN 226
ResIII pfam04851
Type III restriction enzyme, res subunit;
198-376 8.03e-30

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 114.69  E-value: 8.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  198 LKVMRSYQYYAANKISDTVAKhkwengNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYR 277
Cdd:pfam04851   1 KLELRPYQIEAIENLLESIKN------GQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  278 GFAEATDDIqeTEDTSVLIAKLKSNDpaNTLIVTSVQKMSNIkddtegkLKKADLDLITSKRIVFIVDECHRSTFgDMMR 357
Cdd:pfam04851  75 KFLPNYVEI--GEIISGDKKDESVDD--NKIVVTTIQSLYKA-------LELASLELLPDFFDVIIIDEAHRSGA-SSYR 142

                         170
                  ....*....|....*....
gi 659515400  358 VVKQTFPKALFFGFSGTPI 376
Cdd:pfam04851 143 NILEYFKPAFLLGLTATPE 161
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 202-375 6.96e-17

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: 77.99  E-value: 6.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 202 RSYQYYAANKISDTVAKHKWENGNQLGgyiwhtTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGFae 281
Cdd:cd18032    2 RYYQQEAIEALEEAREKGQRRALLVMA------TGTGKTYTAAFLIKRLLEANRKKRILFLAHREELLEQAERSFKEV-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 282 atddiqETEDTSVLIAKLKSNDPANTLIVTSVQKMSNIKDDTegKLKKADLDLItskrivfIVDECHRSTFGDMMRVVKQ 361
Cdd:cd18032   74 ------LPDGSFGNLKGGKKKPDDARVVFATVQTLNKRKRLE--KFPPDYFDLI-------IIDEAHHAIASSYRKILEY 138

                        170
                 ....*....|....
gi 659515400 362 tFPKALFFGFSGTP 375
Cdd:cd18032  139 -FEPAFLLGLTATP 151
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 217-375 1.37e-16

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: 76.58  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 217 AKHKW-ENGNQLGGYIWHTTGSGKTMTSFKSAQLIANskdaDKVVFLIDRIELGTQSAGEYRGFAEATDDIQETEDtsvl 295
Cdd:cd17926    8 ALEAWlAHKNNRRGILVLPTGSGKTLTALALIAYLKE----LRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGG---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 296 iaKLKSNDPANtLIVTSVQKMSNikDDTEGKLKKADLDLItskrivfIVDECHRSTfGDMMRVVKQTFPKALFFGFSGTP 375
Cdd:cd17926   80 --KKKDFDDAN-VVVATYQSLSN--LAEEEKDLFDQFGLL-------IVDEAHHLP-AKTFSEILKELNAKYRLGLTATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
187-407 3.23e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.98  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 187 FYTVADDTDGILKVMRSYQYYAANKIsdtvaKHKWENGNQLGGYIwHTTGSGKTMTSfksAQLIANSKDADKVVFLIDRI 266
Cdd:COG1061   67 ALEAGDEASGTSFELRPYQQEALEAL-----LAALERGGGRGLVV-APTGTGKTVLA---LALAAELLRGKRVLVLVPRR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 267 ELGTQSAGEyrgFAEATDDIQETEDtsvliaklkSNDPANTLIVTSVQKMSNikddtegklkKADLDLITSKRIVFIVDE 346
Cdd:COG1061  138 ELLEQWAEE---LRRFLGDPLAGGG---------KKDSDAPITVATYQSLAR----------RAHLDELGDRFGLVIIDE 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659515400 347 CHRSTfGDMMRVVKQTFPKALFFGFSGTPiqaENEKKGSTTADVFGSELHRYSIADGIRDK 407
Cdd:COG1061  196 AHHAG-APSYRRILEAFPAAYRLGLTATP---FRSDGREILLFLFDGIVYEYSLKEAIEDG 252
HSDR_N pfam04313
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 51-148 3.45e-13

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: 67.33  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   51 QEIAAGQSRYQIARQPKFTAKTsmlpGRRGDFMLLINGMPLIHVELKKSGipVSQAYNQIEKYSHE--GVFTGLFALV-- 126
Cdd:pfam04313  56 GITKTENNSFQVANQVEVKGVQ----KRRPDYVLFVNGLPLAVIELKRPG--TEEAINQIRRYEKDsfNAIPQLFRYAnv 129

                          90       100
                  ....*....|....*....|..
gi 659515400  127 QVFVAVNPEEAVYFANPGPDGK 148
Cdd:pfam04313 130 QFGILSNGRETRFYTKTAKENR 151
DEXDc smart00487
DEAD-like helicases superfamily;
199-378 9.34e-13

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 67.13  E-value: 9.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   199 KVMRSYQYYAANKISDtvakhkwengNQLGGYIWHTTGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRG 278
Cdd:smart00487   7 EPLRPYQKEAIEALLS----------GLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400   279 FAEATDD----IQETEDTSVLIAKLKSNDPAntLIVTSVQKMSNIKDdtEGKLKKADLDLItskrivfIVDECHR---ST 351
Cdd:smart00487  77 LGPSLGLkvvgLYGGDSKREQLRKLESGKTD--ILVTTPGRLLDLLE--NDKLSLSNVDLV-------ILDEAHRlldGG 145

                          170       180
                   ....*....|....*....|....*...
gi 659515400   352 FGD-MMRVVKQTFPKALFFGFSGTPIQA 378
Cdd:smart00487 146 FGDqLEKLLKLLPKNVQLLLLSATPPEE 173
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 228-374 1.96e-10

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: 58.95  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 228 GGYIWHTTGSGKTMTSFKSAQLIANSKdADKVVFLIDRIELGTQSAGEYRGFAEATDDIQE-TEDTSVLIAKLKSNDPAN 306
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLLLKK-GKKVLVLVPTKALALQTAERLRELFGPGIRVAVlVGGSSAEEREKNKLGDAD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659515400 307 tLIVTSVQKMSNikddtegkLKKADLDLITSKRIVFIVDECH------RSTFGDMMRVVKQTFPKALFFGFSGT 374
Cdd:cd00046   82 -IIIATPDMLLN--------LLLREDRLFLKDLKLIIVDEAHallidsRGALILDLAVRKAGLKNAQVILLSAT 146
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
 235-350 2.23e-10

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 63.32  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400 235 TGSGKTMTSFKSAQLIANSKDADKVVFLIDRIELGTQSAGEYRGF---AEATDDIQETEdtsvliaklKSNDPANTLIVT 311
Cdd:COG4096  187 TGTGKTRTAIALIYRLLKAGRAKRILFLADRNALVDQAKNAFKPFlpdLDAFTKLYNKS---------KDIDKSARVYFS 257

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 659515400 312 SVQKMSNIKDDTEGKLKKADL-----DLItskrivfIVDECHRS 350
Cdd:COG4096  258 TYQTMMNRIDGEEEEPGYRQFppdffDLI-------IIDECHRG 294
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 235-377 6.15e-04

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: 40.69  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  235 TGSGKTMTSFKSA-QLIANSKDADKVVFLIDRIELGTQSAGEYRGFAEATD----DIQETEDTSVLIAKLKSNDpantLI 309
Cdd:pfam00270  23 TGSGKTLAFLLPAlEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGlkvaSLLGGDSRKEQLEKLKGPD----IL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659515400  310 VTsvqkmsnikddTEGKLkkadLDLITSKRIV-----FIVDECHR---STFGD-MMRVVKQTFPKALFFGFSGTPIQ 377
Cdd:pfam00270  99 VG-----------TPGRL----LDLLQERKLLknlklLVLDEAHRlldMGFGPdLEEILRRLPKKRQILLLSATLPR 160
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 235-349 9.67e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659515400  235 TGSGKTMTSfksaqlIA------NSKDADKVVFLIDRIELGTQSAGEYR-----GFAEATD--DIQETEDtsvliaklKS 301
Cdd:PRK11448  442 TGTGKTRTA------IAlmyrllKAKRFRRILFLVDRSALGEQAEDAFKdtkieGDQTFASiyDIKGLED--------KF 507

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 659515400  302 NDPANTLIVTSVQKMsnIK-----DDTEGKLKKADLDLItskrivfIVDECHR 349
Cdd:PRK11448  508 PEDETKVHVATVQGM--VKrilysDDPMDKPPVDQYDCI-------IVDEAHR 551
 
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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