|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
8-362 |
9.25e-180 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 518.93 E-value: 9.25e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 8 RHSSLDTVLRERFGLTDFRPGQREVLDALLGPNAAaLAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALAR 87
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDA-LVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 88 QGIRAARLDASLSVDDSREVTQALRDGSLKLLYVAPERFNNERFTALLRELRISLFAVDEAHCVSEWGHNFRPDYLKLAK 167
Cdd:COG0514 80 AGIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 168 AARDLSAERILALTATATPSVVRDICQGFGIPEENAVVTGFYRQNLTLETTPVHAEARDAFLLGRLGSRAPGPTIVYVTQ 247
Cdd:COG0514 160 LRERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 248 QKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIG 327
Cdd:COG0514 240 RKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIG 319
|
330 340 350
....*....|....*....|....*....|....*
gi 2111050890 328 RAGRDGAPSVVELFACPDDVPSLENFALGDTPTRE 362
Cdd:COG0514 320 RAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEE 354
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
14-353 |
4.45e-127 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 387.89 E-value: 4.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 14 TVLRERFGLTDFRPGQREVLDALLGPNAAaLAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRAA 93
Cdd:TIGR01389 3 QVLKRTFGYDDFRPGQEEIISHVLDGRDV-LVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 94 RLDASLSVDDSREVTQALRDGSLKLLYVAPERFNNERFTALLRELRISLFAVDEAHCVSEWGHNFRPDYLKLAKAARDLS 173
Cdd:TIGR01389 82 YLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 174 AERILALTATATPSVVRDICQGFGIPEENAVVTGFYRQNLTLetTPVHAEARDAFLLGRLGSRAPGPTIVYVTQQKTAER 253
Cdd:TIGR01389 162 QVPRIALTATADAETRQDIRELLRLADANEFITSFDRPNLRF--SVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 254 VAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDG 333
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340
....*....|....*....|
gi 2111050890 334 APSVVELFACPDDVPSLENF 353
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRR 339
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
14-352 |
1.10e-115 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 354.46 E-value: 1.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 14 TVLRERFGLTDFRPGQREVLDA-LLGPNAaaLAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRA 92
Cdd:TIGR00614 1 KILKKYFGLSSFRPVQLEVINAvLLGRDC--FVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 93 ARLDASLSVDDSREVTQALRDGSLKLLYVAPERF--NNERFTALLRELRISLFAVDEAHCVSEWGHNFRPDYLKLAKAAR 170
Cdd:TIGR00614 79 TFLNSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsaSNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 171 DLSAERILALTATATPSVVRDICQGFGIPEENAVVTGFYRQNLTLET---TPVHAEARDAFLLGRLgsraPGPT-IVYVT 246
Cdd:TIGR00614 159 KFPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVrrkTPKILEDLLRFIRKEF----EGKSgIIYCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 247 QQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEI 326
Cdd:TIGR00614 235 SRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQES 314
|
330 340
....*....|....*....|....*.
gi 2111050890 327 GRAGRDGAPSVVELFACPDDVPSLEN 352
Cdd:TIGR00614 315 GRAGRDGLPSECHLFYAPADMNRLRR 340
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
13-347 |
3.88e-99 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 315.88 E-value: 3.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 13 DTVLRERFGLTDFRPGQREVLDALLGpNAAALAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRA 92
Cdd:PRK11057 14 KQVLQETFGYQQFRPGQQEIIDAVLS-GRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 93 ARLDASLSVDDSREVTQALRDGSLKLLYVAPERFNNERFTALLRELRISLFAVDEAHCVSEWGHNFRPDYLKLAKAARDL 172
Cdd:PRK11057 93 ACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQRF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 173 SAERILALTATATPSVVRDICQGFGIPEENAVVTGFYRQNL--TL--ETTPVHAEARdaFLLGRLGSRApgptIVYVTQQ 248
Cdd:PRK11057 173 PTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIryTLveKFKPLDQLMR--YVQEQRGKSG----IIYCNSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 249 KTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGR 328
Cdd:PRK11057 247 AKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGR 326
|
330
....*....|....*....
gi 2111050890 329 AGRDGAPSVVELFACPDDV 347
Cdd:PRK11057 327 AGRDGLPAEAMLFYDPADM 345
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
14-208 |
2.06e-86 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 268.63 E-value: 2.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 14 TVLRERFGLTDFRPGQREVLDALL-GPNAaaLAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRA 92
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLaGRDV--LVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 93 ARLDASLSVDDSREVTQALRDGSLKLLYVAPERFNNERFTALLREL----RISLFAVDEAHCVSEWGHNFRPDYLKLAKA 168
Cdd:cd17920 80 AALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLperkRLALIVVDEAHCVSQWGHDFRPDYLRLGRL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2111050890 169 ARDLSAERILALTATATPSVVRDICQGFGIPEENAVVTGF 208
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLGLRNPVIFRASF 199
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
15-209 |
1.24e-82 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 258.73 E-value: 1.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 15 VLRERFGLTDFRPGQREVLDALLGpNAAALAVFPTGGGKSLCYQLPALLLE----GITVVVSPLIALMKDQIDALARQgI 90
Cdd:cd18018 3 LLRRVFGHPSFRPGQEEAIARLLS-GRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDALPRA-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 91 RAARLDASLSVDDSREVTQALRDGSLKLLYVAPERFNNERFTALLREL-RISLFAVDEAHCVSEWGHNFRPDYLKLAKAA 169
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2111050890 170 RDLS-AERILALTATATPSVVRDICQGFGIPEENAVVTGFY 209
Cdd:cd18018 161 RELLgAPPVLALTATATKRVVEDIASHLGIPESGVVRGPLY 201
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
20-341 |
6.79e-71 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 249.81 E-value: 6.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 20 FGLTDFRPGQREVLDALLGpNAAALAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRAARLDASL 99
Cdd:PLN03137 456 FGNHSFRPNQREIINATMS-GYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 100 SVDDSREVTQAL--RDGSLKLLYVAPERFnnERFTALLRELRI-------SLFAVDEAHCVSEWGHNFRPDYLKLAKAAR 170
Cdd:PLN03137 535 EWAEQLEILQELssEYSKYKLLYVTPEKV--AKSDSLLRHLENlnsrgllARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 171 DLSAERILALTATATPSVVRDICQGFGIPeeNAVV--TGFYRQNLTLETTPVHA---EARDAFL----LGRLGsrapgpt 241
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLV--NCVVfrQSFNRPNLWYSVVPKTKkclEDIDKFIkenhFDECG------- 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 242 IVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLES 321
Cdd:PLN03137 684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
|
330 340
....*....|....*....|
gi 2111050890 322 YSQEIGRAGRDGAPSVVELF 341
Cdd:PLN03137 764 YHQECGRAGRDGQRSSCVLY 783
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
9-200 |
3.53e-63 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350773 [Multi-domain] Cd Length: 209 Bit Score: 207.99 E-value: 3.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 9 HSSLDTVLRERFGLTDFRPGQREVLDALLGpNAAALAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQ 88
Cdd:cd18015 3 SGKVKDTLKNVFKLEKFRPLQLETINATMA-GRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 89 GIRAARLDASLSVDDSREVTQALRDGS--LKLLYVAPERFN-NERFTALLREL----RISLFAVDEAHCVSEWGHNFRPD 161
Cdd:cd18015 82 GISATMLNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAkSKRFMSKLEKAynagRLARIAIDEVHCCSQWGHDFRPD 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2111050890 162 YLKLAKAARDLSAERILALTATATPSVVRDICQGFGIPE 200
Cdd:cd18015 162 YKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQK 200
|
|
| DpdF |
NF041063 |
protein DpdF; |
13-348 |
7.24e-55 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 200.52 E-value: 7.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 13 DTVLRERFGLTDFR-PGQREVLDALL--GPNAAALAVFPTGGGKSLCYQLPALLL---EGITVVVSPLIALMKDQ----I 82
Cdd:NF041063 128 DPFLAEALGFTHYRsPGQREAVRAALlaPPGSTLIVNLPTGSGKSLVAQAPALLAsrqGGLTLVVVPTVALAIDQerraR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 83 DALARQGIRAARLDA---SLSVDDSREVTQALRDGSLKLLYVAPERFnnerFTALLREL-------RISLFAVDEAHCVS 152
Cdd:NF041063 208 ELLRRAGPDLGGPLAwhgGLSAEERAAIRQRIRDGTQRILFTSPESL----TGSLRPALfdaaeagLLRYLVVDEAHLVD 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 153 EWGHNFRPDYLKLAKAARDL-------SAERILALTATATPSVVRDICQGFGIPEENAVVTG-FYRQ----NLTLETTPv 220
Cdd:NF041063 284 QWGDGFRPEFQLLAGLRRSLlrlapsgRPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAvQLRPepayWVAKCDSE- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 221 haEARDAFLLGRLgSRAPGPTIVYVTQQKTAERVAAFLATEGLP-ASAYHAGLEPEVRERVQESWmaSANG--IVVATIA 297
Cdd:NF041063 363 --EERRERVLEAL-RHLPRPLILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQW--RENEldIVVATSA 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2111050890 298 FGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELFACPDDVP 348
Cdd:NF041063 438 FGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLD 488
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
14-192 |
3.03e-53 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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: 350772 [Multi-domain] Cd Length: 205 Bit Score: 181.52 E-value: 3.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 14 TVLRERFGLTDFR-PGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRA 92
Cdd:cd18014 2 STLKKVFGHSDFKsPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 93 ARLDASLSVDDSREVTQALRDGS--LKLLYVAPERFNNERFTALLREL----RISLFAVDEAHCVSEWGHNFRPDYLKLA 166
Cdd:cd18014 82 DSLNSKLSAQERKRIIADLESEKpqTKFLYITPEMAATSSFQPLLSSLvsrnLLSYLVVDEAHCVSQWGHDFRPDYLRLG 161
|
170 180
....*....|....*....|....*.
gi 2111050890 167 KAARDLSAERILALTATATPSVVRDI 192
Cdd:cd18014 162 ALRSRYGHVPWVALTATATPQVQEDI 187
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
15-192 |
3.35e-51 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 176.17 E-value: 3.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 15 VLRERFGLTDFRPGQREVLDA-LLGPNAAALavFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRAA 93
Cdd:cd18016 8 IFHKKFGLHQFRTNQLEAINAaLLGEDCFVL--MPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 94 RLDASLSVDDSREVTQAL--RDGSLKLLYVAPE------RFNNERFTALLRELrISLFAVDEAHCVSEWGHNFRPDYLKL 165
Cdd:cd18016 86 YLTGDKTDAEATKIYLQLskKDPIIKLLYVTPEkisasnRLISTLENLYERKL-LARFVIDEAHCVSQWGHDFRPDYKRL 164
|
170 180
....*....|....*....|....*..
gi 2111050890 166 AKAARDLSAERILALTATATPSVVRDI 192
Cdd:cd18016 165 NMLRQKFPSVPMMALTATATPRVQKDI 191
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
14-208 |
8.14e-51 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 174.58 E-value: 8.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 14 TVLRERFGLTDFRPGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPALLLEGITVVVSPLIALMKDQIDALARQGIRAA 93
Cdd:cd18017 2 NALNEYFGHSSFRPVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 94 RLDASlsvdDSREVTQALRDGSLKLLYVAPERFnnERFTALLREL--RISLFAVDEAHCVSEWGHNFRPDYLKLAKAARD 171
Cdd:cd18017 82 FLGSA----QSQNVLDDIKMGKIRVIYVTPEFV--SKGLELLQQLrnGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNR 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2111050890 172 LSAERILALTATATPSVVRDICQGFGIPEENAVVTGF 208
Cdd:cd18017 156 LPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
210-341 |
5.02e-47 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 161.99 E-value: 5.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 210 RQNLTLETTPVHAEARDAFLLGRLGSRAP-GPTIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASA 288
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLgGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2111050890 289 NGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELF 341
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
26-192 |
1.84e-22 |
|
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: 94.62 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 26 RPGQREVLDALL-GPNAAALAvfPTGGGKSLCYQLPAL-----LLEGI-TVVVSPLIALMKDQIDALARQGI-RAARLDA 97
Cdd:pfam00270 1 TPIQAEAIPAILeGRDVLVQA--PTGSGKTLAFLLPALealdkLDNGPqALVLAPTRELAEQIYEELKKLGKgLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 98 SLSVDDSREVTQALRDgsLKLLYVAPERFNNerFTALLRELR-ISLFAVDEAHCVSEWGhnFRPDYLKLAKAARdlSAER 176
Cdd:pfam00270 79 LLGGDSRKEQLEKLKG--PDILVGTPGRLLD--LLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEILRRLP--KKRQ 150
|
170
....*....|....*.
gi 2111050890 177 ILALTATAtPSVVRDI 192
Cdd:pfam00270 151 ILLLSATL-PRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
18-192 |
9.40e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 90.63 E-value: 9.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 18 ERFGLTDFRPGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPALLL-----EGITVVVSPLIALMKDQIDALARQGIRA 92
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 93 ARLDASLSVDDS-REVTQALRDGSLKLLYVAPERFNNERFTALLRELRISLFAVDEAHCVSEWGhnFRPDYLKLAKAARd 171
Cdd:smart00487 82 GLKVVGLYGGDSkREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLKLLP- 158
|
170 180
....*....|....*....|.
gi 2111050890 172 lSAERILALTATATPSVVRDI 192
Cdd:smart00487 159 -KNVQLLLLSATPPEEIENLL 178
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
252-333 |
7.96e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 81.10 E-value: 7.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 252 ERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGR 331
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2111050890 332 DG 333
Cdd:smart00490 81 AG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
224-333 |
1.65e-16 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 75.71 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 224 ARDAFLLGRLGSRAPGPTIVYVTQQKTAErVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGID 303
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 2111050890 304 KADVRAVYHYNLPKGLESYSQEIGRAGRDG 333
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
220-331 |
8.20e-16 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise 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. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain] Cd Length: 131 Bit Score: 74.47 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 220 VHAEARDAFLLGRLGSRA-PGPTIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAF 298
Cdd:cd18787 8 VEEEEKKLLLLLLLLEKLkPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVA 87
|
90 100 110
....*....|....*....|....*....|...
gi 2111050890 299 GMGIDKADVRAVYHYNLPKGLESYSQEIGRAGR 331
Cdd:cd18787 88 ARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGR 120
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
29-338 |
1.72e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 80.26 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 29 QREVLDALL-GPNAAALAvfPTGGGKSLCYQLPAL--LLEGIT---VVVSPLIALMKDQIDALAR------QGIRAARLD 96
Cdd:COG1205 61 QAEAIEAARaGKNVVIAT--PTASGKSLAYLLPVLeaLLEDPGataLYLYPTKALARDQLRRLRElaealgLGVRVATYD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 97 AslsvDDSREVTQALRDGS-----------LKLLYvaperfNNERFTALLRELRisLFAVDEAHC---V--SEWGHNFRp 160
Cdd:COG1205 139 G----DTPPEERRWIREHPdivltnpdmlhYGLLP------HHTRWARFFRNLR--YVVIDEAHTyrgVfgSHVANVLR- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 161 dylKLAKAARDLSAE-RILALTATAtpsvvrdicqgfGIPEENA---------VVTG-----------FYRQNLTLETT- 218
Cdd:COG1205 206 ---RLRRICRHYGSDpQFILASATI------------GNPAEHAerltgrpvtVVDEdgsprgertfvLWNPPLVDDGIr 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 219 -PVHAEARDafLLGRL---GSRapgpTIVYVTQQKTAERVAAF----LATEGLPA--SAYHAGLEPEVRERVQEswmASA 288
Cdd:COG1205 271 rSALAEAAR--LLADLvreGLR----TLVFTRSRRGAELLARYarraLREPDLADrvAAYRAGYLPEERREIER---GLR 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2111050890 289 NG---IVVATIAFGMGIDKADVRAV--YHYnlPKGLESYSQEIGRAGRDGAPSVV 338
Cdd:COG1205 342 SGellGVVSTNALELGIDIGGLDAVvlAGY--PGTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
44-183 |
3.12e-14 |
|
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: 70.12 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 44 LAVFPTGGGKSLCYQLPALLL----EGITVVVSPLIALMKDQIDALARQGIRAARLDASLSVDDSREVTqALRDGSLKLL 119
Cdd:cd00046 5 LITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAEERE-KNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2111050890 120 YVAPERF-NNERFTALLRELRISLFAVDEAHCVSEWGHNFRPDYLKLAKAARDLSaeRILALTAT 183
Cdd:cd00046 84 IATPDMLlNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA--QVILLSAT 146
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
219-367 |
1.46e-13 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 72.87 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 219 PVHAEARDAFLLGRLGSRAPGPTIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVqeswMAS-ANG---IVVA 294
Cdd:COG0513 222 LVDKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERA----LDAfRNGkirVLVA 297
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111050890 295 T-IAfGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELFACPDDVPSLENF--ALGDTPTREAIQSL 367
Cdd:COG0513 298 TdVA-ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIekLIGQKIEEEELPGF 372
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
49-379 |
1.41e-12 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 70.57 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 49 TGGGKSLCYQLPA--------LLLEG---ITVVVSPLIALMkDQIDALARQGIRAARLDASLSVDD--SREVTQALRDGs 115
Cdd:PTZ00110 176 TGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELA-EQIREQCNKFGASSKIRNTVAYGGvpKRGQIYALRRG- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 116 LKLLYVAPER---FNNERFTALLRelrISLFAVDEAHCVSEWG---------HNFRPDYLKL----------AKAARDLS 173
Cdd:PTZ00110 254 VEILIACPGRlidFLESNVTNLRR---VTYLVLDEADRMLDMGfepqirkivSQIRPDRQTLmwsatwpkevQSLARDLC 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 174 AERIL-----ALTATATpsvvRDICQGFGIPEENAvvtgfYRQNLTLettpvhaeardafLLGRLGSRAPgPTIVYVTQQ 248
Cdd:PTZ00110 331 KEEPVhvnvgSLDLTAC----HNIKQEVFVVEEHE-----KRGKLKM-------------LLQRIMRDGD-KILIFVETK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 249 KTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGR 328
Cdd:PTZ00110 388 KGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGR 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2111050890 329 AGRDGAPSVVELFACPDDVPSLENFAlgdTPTREAIQSLVTELLGLGPELS 379
Cdd:PTZ00110 468 TGRAGAKGASYTFLTPDKYRLARDLV---KVLREAKQPVPPELEKLSNERS 515
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
241-338 |
1.17e-11 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 63.04 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 241 TIVYVTQQKTAERVAAFLATEGLPA-------SAYHAGLEPEVRERVqESWMASAN--GiVVATIAFGMGIDKADVRAVY 311
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREI-EAELFNGEllG-VVATNALELGIDIGGLDAVV 115
|
90 100
....*....|....*....|....*..
gi 2111050890 312 HYNLPKGLESYSQEIGRAGRDGAPSVV 338
Cdd:cd18797 116 LAGYPGSLASLWQQAGRAGRRGKDSLV 142
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
26-331 |
2.26e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 53.88 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 26 RPGQREVLDALLG----PNAAALAVFPTGGGKSL----CYQlpALLLEGITVVVSPLIALMKDQIDALARqgIRAARLDA 97
Cdd:COG1061 82 RPYQQEALEALLAalerGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRR--FLGDPLAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 98 SLSVDDSREVT----QALRdgslkllyvaperfNNERFTALLRelRISLFAVDEAHcvsewgHNFRPDYLKLAKAardLS 173
Cdd:COG1061 158 GGKKDSDAPITvatyQSLA--------------RRAHLDELGD--RFGLVIIDEAH------HAGAPSYRRILEA---FP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 174 AERILALTATATPSVVRDICQG------FGIPEENAVVTGF--------YRQNLTLETTP------------VHAEARDA 227
Cdd:COG1061 213 AAYRLGLTATPFRSDGREILLFlfdgivYEYSLKEAIEDGYlappeyygIRVDLTDERAEydalserlrealAADAERKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 228 FLLGRLGSRAPG--PTIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGID-- 303
Cdd:COG1061 293 KILRELLREHPDdrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDvp 372
|
330 340
....*....|....*....|....*...
gi 2111050890 304 KADVrAVYHYnlpkGLESYSQEIGRAGR 331
Cdd:COG1061 373 RLDV-AILLR----PTGSPREFIQRLGR 395
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
242-352 |
3.61e-07 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 52.91 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 242 IVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLES 321
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90 100 110
....*....|....*....|....*....|.
gi 2111050890 322 YSQEIGRAGRDGAPSVVELFACPDDVPSLEN 352
Cdd:PTZ00424 351 YIHRIGRSGRFGRKGVAINFVTPDDIEQLKE 381
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
140-341 |
4.95e-07 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 52.87 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 140 ISLFAVDEAHCVSEWGhnFRPDYLKLAKAardLSAERILALTATATPSVVRdicQGFGIPEENAVVT--GFYRQNLTLET 217
Cdd:PLN00206 271 VSVLVLDEVDCMLERG--FRDQVMQIFQA---LSQPQVLLFSATVSPEVEK---FASSLAKDIILISigNPNRPNKAVKQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 218 TPVHAEARDA----FLLGRLGSRAPGPTIVYVTQQKTAERVA-AFLATEGLPASAYHAglEPEVRER--VQESWMASANG 290
Cdd:PLN00206 343 LAIWVETKQKkqklFDILKSKQHFKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHG--EKSMKERreVMKSFLVGEVP 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2111050890 291 IVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELF 341
Cdd:PLN00206 421 VIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVF 471
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
18-183 |
5.38e-07 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 52.59 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 18 ERFGLTDFRPGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPAL--LLEGITVV-VSPLIAL----MKDQIDALARQGI 90
Cdd:COG1204 16 KERGIEELYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALasekYREFKRDFEELGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 91 RAArldasLSVDDSREVTQALRDGSlklLYVAperfNNERFTALLRE-----LRISLFAVDEAHCVsewGHNFR-PDY-L 163
Cdd:COG1204 96 KVG-----VSTGDYDSDDEWLGRYD---ILVA----TPEKLDSLLRNgpswlRDVDLVVVDEAHLI---DDESRgPTLeV 160
|
170 180
....*....|....*....|
gi 2111050890 164 KLAKAARDLSAERILALTAT 183
Cdd:COG1204 161 LLARLRRLNPEAQIVALSAT 180
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
29-149 |
5.48e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 50.28 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 29 QREVLDALLGPNAAALAVfPTGGGKSLCYQLPAL--LLE--GIT-VVVSPLIALMKDQIDALAR------QGIRAARLDA 97
Cdd:cd17923 5 QAEAIEAARAGRSVVVTT-GTASGKSLCYQLPILeaLLRdpGSRaLYLYPTKALAQDQLRSLRElleqlgLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2111050890 98 slsvDDSREVTQALRDGSLKLLYVAPERF------NNERFTALLRELRisLFAVDEAH 149
Cdd:cd17923 84 ----DTPREERRAIIRNPPRILLTNPDMLhyallpHHDRWARFLRNLR--YVVLDEAH 135
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
285-333 |
3.02e-06 |
|
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: 45.39 E-value: 3.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2111050890 285 MASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDG 333
Cdd:cd18785 19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGG 67
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
25-183 |
3.53e-06 |
|
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: 46.92 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 25 FRPGQREVLDALLGPNAAALAVF--PTGGGKSLC-YQLPALLLEGITVVVSPLIALMKDQIDALARQGIRAA-RLDASLS 100
Cdd:cd17926 1 LRPYQEEALEAWLAHKNNRRGILvlPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSiGLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 101 VDD--SREVTQALRDgSLKLLyVAPERFNNERFtallrelriSLFAVDEAHcvsewghnfRPDYLKLAKAARDLSAERIL 178
Cdd:cd17926 81 KKDfdDANVVVATYQ-SLSNL-AEEEKDLFDQF---------GLLIVDEAH---------HLPAKTFSEILKELNAKYRL 140
|
....*
gi 2111050890 179 ALTAT 183
Cdd:cd17926 141 GLTAT 145
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
223-371 |
4.77e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 49.56 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 223 EARDAFLLGRLgSRAPGP-TIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMG 301
Cdd:PRK04537 242 EEKQTLLLGLL-SRSEGArTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2111050890 302 IDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELFACPD---DVPSLENFALGDTPTREAIQSLVTEL 371
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERyamSLPDIEAYIEQKIPVEPVTAELLTPL 393
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
219-343 |
6.19e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 46.49 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 219 PVHAEARDAFLLGRLGSrapgpTIVYVTQQKTAERVAAFLAT------EGLPASAYHAGLEPEVRERVQESWMASANGIV 292
Cdd:cd18796 24 GADAYAEVIFLLERHKS-----TLVFTNTRSQAERLAQRLRElcpdrvPPDFIALHHGSLSRELREEVEAALKRGDLKVV 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2111050890 293 VATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAG-RDGAPSVVELFAC 343
Cdd:cd18796 99 VATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAASKGRLVPT 150
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
24-184 |
2.26e-05 |
|
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: 45.33 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 24 DFRPGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPALLL----EGITVVVSPLIAL----MKDQIDALARQGIRAARL 95
Cdd:cd17921 1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALvnqkEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 96 DASLSVDDsrevtqaLRDGSLKLLYVAPERFNNerftaLLR------ELRISLFAVDEAHCVSEwghnfrPDY-----LK 164
Cdd:cd17921 81 TGDPSVNK-------LLLAEADILVATPEKLDL-----LLRnggerlIQDVRLVVVDEAHLIGD------GERgvvleLL 142
|
170 180
....*....|....*....|
gi 2111050890 165 LAKAARDLSAERILALTATA 184
Cdd:cd17921 143 LSRLLRINKNARFVGLSATL 162
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
242-351 |
3.71e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 46.83 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 242 IVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLES 321
Cdd:PRK01297 339 MVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
|
90 100 110
....*....|....*....|....*....|...
gi 2111050890 322 YSQEIGRAGRDGAPSVVELFACPDD---VPSLE 351
Cdd:PRK01297 419 YVHRIGRTGRAGASGVSISFAGEDDafqLPEIE 451
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
236-333 |
4.22e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 44.08 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 236 RAPGPTIVYVTQQKTAERVAAFLAteGlpASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGID----KADVRAVY 311
Cdd:cd18795 41 SEGKPVLVFCSSRKECEKTAKDLA--G--IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlparTVIIKGTQ 116
|
90 100
....*....|....*....|....*..
gi 2111050890 312 HYNlPKGLESYS-----QEIGRAGRDG 333
Cdd:cd18795 117 RYD-GKGYRELSpleylQMIGRAGRPG 142
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
277-353 |
1.16e-04 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 44.96 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 277 RERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLESYSQEIGRAGRDGAPSVVELFACPD---DVPSLENF 353
Cdd:PRK04837 294 RLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEyalNLPAIETY 373
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
27-183 |
1.66e-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: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 27 PGQREVLDALLGPNAAALAVFPTGGGKSLCYQLPAL--LLEGITVV-VSPLIALMKDQID---ALARQGIRAArldasLS 100
Cdd:cd18028 4 PPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVntLLEGGKALyLVPLRALASEKYEefkKLEEIGLKVG-----IS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 101 VDDSREvtqalRDGSLKLLYVAPERFnnERFTALLRE----LR-ISLFAVDEAHCVSEWGHNFRPDYLkLAKAARDLSAE 175
Cdd:cd18028 79 TGDYDE-----DDEWLGDYDIIVATY--EKFDSLLRHspswLRdVGVVVVDEIHLISDEERGPTLESI-VARLRRLNPNT 150
|
....*...
gi 2111050890 176 RILALTAT 183
Cdd:cd18028 151 QIIGLSAT 158
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
241-339 |
6.00e-04 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 42.62 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 241 TIVYVtqqKTAERVA---AFLATEGLPaSAYHAGlepevrERVQESWMAS----ANGIV---VATIAFGMGIDKADVRAV 310
Cdd:PRK11192 248 SIVFV---RTRERVHelaGWLRKAGIN-CCYLEG------EMVQAKRNEAikrlTDGRVnvlVATDVAARGIDIDDVSHV 317
|
90 100 110
....*....|....*....|....*....|...
gi 2111050890 311 YHYNLPKGLESYSQEIGRAGRDG----APSVVE 339
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGrkgtAISLVE 350
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
239-331 |
7.90e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 42.57 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 239 GPTIVYVTQQKTAERVAAFLateGLPASAYHAGLEPEVRERVQESWmasANG---IVVATIAFGMGIDKADVRAVYHyNL 315
Cdd:COG1202 428 GQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRF---ADQelaAVVTTAALAAGVDFPASQVIFD-SL 500
|
90 100
....*....|....*....|.
gi 2111050890 316 PKGLE-----SYSQEIGRAGR 331
Cdd:COG1202 501 AMGIEwlsvqEFHQMLGRAGR 521
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
40-149 |
9.74e-04 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 40.26 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 40 NAAALAVFPTGGGKSLCYQLPALL------LEGITVV-VSPLIALMKDQIDALARQgirAARLDASLSVDD-SREVTQAL 111
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLEEP---LDEIDLEIPVAVrHGDTSQSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2111050890 112 RDGSLK----LLYVAPERF----NNERFTALLRELRisLFAVDEAH 149
Cdd:cd17922 78 KAKQLKnppgILITTPESLelllVNKKLRELFAGLR--YVVVDEIH 121
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
29-153 |
2.24e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 40.03 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 29 QREVLDALLGPNAAALAVFPTGGGKSLCYQLPAL-LLEG---------ITVVVSPLIALMKDQID----ALARQGIRAAR 94
Cdd:cd18023 6 QSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILrLLKErnplpwgnrKVVYIAPIKALCSEKYDdwkeKFGPLGLSCAE 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2111050890 95 LDASLSVDDSREVTQAlrdgslKLLYVAPERF--------NNERFTALLRelrisLFAVDEAHCVSE 153
Cdd:cd18023 86 LTGDTEMDDTFEIQDA------DIILTTPEKWdsmtrrwrDNGNLVQLVA-----LVLIDEVHIIKE 141
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
241-341 |
2.51e-03 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 40.99 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 241 TIVYVTQQKTAERVAAFLATEGLPASAYHAGLEPEVRERVQESWMASANGIVVATIAFGMGIDKADVRAVYHYNLPKGLE 320
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327
|
90 100
....*....|....*....|.
gi 2111050890 321 SYSQEIGRAGRDGAPSVVELF 341
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLF 348
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
25-183 |
3.53e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 25 FRPGQREVLDALL----GPNAAALAVFPTGGGKSLCY-QLPALLLE----GITVVVSPLIALMKDQIDALARQGIRAARL 95
Cdd:pfam04851 4 LRPYQIEAIENLLesikNGQKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111050890 96 DASLSVD-DSREVTQAlrdgslKLLYVAPERFNNERFTALLREL--RISLFAVDEAHcvsewgHNFRPDYLKLAKAardL 172
Cdd:pfam04851 84 GEIISGDkKDESVDDN------KIVVTTIQSLYKALELASLELLpdFFDVIIIDEAH------RSGASSYRNILEY---F 148
|
170
....*....|.
gi 2111050890 173 SAERILALTAT 183
Cdd:pfam04851 149 KPAFLLGLTAT 159
|
|
| |
