|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
14-449 |
2.90e-180 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 516.62 E-value: 2.90e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 14 RRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL 93
Cdd:COG0514 3 DDALEVLKRVFGYDSFR-PGQEEIIEAVLAG-RDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 94 KVRVSSLNSKLSAQERKELLADLERekPQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRA--GELKLLYVAPERLLNPRFL----ELLRRLKISLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElISDPYGNLKDFcLKALGQE 253
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDP-RVFVGSFDRPNLRLEVVPKP-PDDKLAQLLDF-LKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 254 AdkglsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAH 333
Cdd:COG0514 232 S-------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 334 WNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKAsdkatimAFDALVTFCEELGCRH 413
Cdd:COG0514 305 YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERA-------KLDAMLAYAETTGCRR 377
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2462558841 414 AAIAKYFGDALPACAKGCDHCQNPT-------AVRRRLEALER 449
Cdd:COG0514 378 QFLLRYFGEELAEPCGNCDNCLGPPetfdgteAAQKALSCVYR 420
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
17-221 |
6.73e-136 |
|
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: 392.60 E-value: 6.73e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 17 RSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 97 VSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462558841 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCF 221
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDIFAQLRLKKPVAIFKTPCF 205
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
17-446 |
2.87e-133 |
|
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: 400.22 E-value: 2.87e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 17 RSTLKKVFGFDSFKtPLQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:TIGR01389 2 QQVLKRTFGYDDFR-PGQEEIISHVLDGR-DVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 97 VSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFQptlnSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNG--ELKLLYVAPERLEQDYFL----NMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElisdpygNLKDFCLKALGQEadK 256
Cdd:TIGR01389 154 GSLAERFPQVPRIALTATADAETRQDIRELLRLADA-NEFITSFDRPNLRFSVVKKN-------NKQKFLLDYLKKH--R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 336
Cdd:TIGR01389 224 GQSG--IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkEVAKLQEKRGNKASDKatimaFDALVTFCEELGCRHAAI 416
Cdd:TIGR01389 302 PGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDDYKQIEREK-----LRAMIAYCETQTCRRAYI 374
|
410 420 430
....*....|....*....|....*....|.
gi 2462558841 417 AKYFGDALPACAKGCDHC-QNPTAVRRRLEA 446
Cdd:TIGR01389 375 LRYFGENEVEPCGNCDNClDPPKSYDATVEA 405
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
18-434 |
2.29e-131 |
|
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: 391.06 E-value: 2.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 18 STLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRV 97
Cdd:TIGR00614 1 KILKKYFGLSSFR-PVQLEVINAVLLG-RDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 98 SSLNSKLSAQERKELLADLEreKPQTKILYITPE-MAASSSFqptLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR00614 79 TFLNSAQTKEQQLNVLTDLK--DGKIKLLYVTPEkISASNRL---LQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKelisdpYGNLKDFCLKALgQEADK 256
Cdd:TIGR00614 154 GSLKQKFPNVPVMALTATASPSVREDILRQLNLLNP-QIFCTSFDRPNLYYEVRRK------TPKILEDLLRFI-RKEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNI 336
Cdd:TIGR00614 226 GKSG--IIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqvSFLIRKEVakLQEKRGNKASDKATIMafdALVTFCEELG-CRHAA 415
Cdd:TIGR00614 304 PKSMESYYQESGRAGRDGLPSECHLFYAPAD----MNRLRRLL--MEEPDGNFRTYKLKLY---EMMEYCLNSStCRRLI 374
|
410 420
....*....|....*....|....*.
gi 2462558841 416 IAKYFGD-------ALPACAKGCDHC 434
Cdd:TIGR00614 375 LLSYFGEkgfnksfCIMGTEKCCDNC 400
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
6-434 |
6.82e-104 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 338.41 E-value: 6.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 6 TTFPFdpERRVRSTLKKVFGFDSFKtPLQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PLN03137 440 RNFPW--TKKLEVNNKKVFGNHSFR-PNQREIINATMSGY-DVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 86 QVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQ 164
Cdd:PLN03137 516 QIMNLLQANIPAASLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEkVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQ 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 165 WGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPCFRANLFYDVQFKelisdpygnlKD 244
Cdd:PLN03137 596 WGHDFRPDYQGLGILKQKFPNIPVLALTATATASVKEDVVQALGLVNCV-VFRQSFNRPNLWYSVVPK----------TK 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 245 FCLkalgQEADKGL-----SGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISF 319
Cdd:PLN03137 665 KCL----EDIDKFIkenhfDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAF 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 320 GMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRK-EVAKLQEKRG-NKASDKATIM 397
Cdd:PLN03137 741 GMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQgGVEQSPMAMGyNRMASSGRIL 820
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462558841 398 AFDA-----LVTFCE-ELGCRHAAIAKYFGDALPA--CAKGCDHC 434
Cdd:PLN03137 821 ETNTenllrMVSYCEnEVDCRRFLQLVHFGEKFDStnCKKTCDNC 865
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
17-220 |
9.21e-104 |
|
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: 310.24 E-value: 9.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 17 RSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVR 96
Cdd:cd17920 1 EQILKEVFGYDEFR-PGQLEAINAVLAG-RDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 97 VSSLNSKLSAQERKEllADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd17920 79 AAALNSTLSPEEKRE--VLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462558841 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPC 220
Cdd:cd17920 157 GRLRRALPGVPILALTATATPEVREDILKRLGLRNPV-IFRASF 199
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-448 |
2.90e-103 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 323.20 E-value: 2.90e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 6 TTFPFDPERRVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PRK11057 3 QAEVLNLESLAKQVLQETFGYQQFR-PGQQEIIDAVLSG-RDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 86 QVDHLLTLKVRVSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFqptLNSLVSRHLlSYLVVDEAHCVSQW 165
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTG--QIKLLYIAPERLMMDNF---LEHLAHWNP-ALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 166 GHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP---VAIFKTPCFRANLFYdvQFKelisdPYGNL 242
Cdd:PRK11057 155 GHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPliqISSFDRPNIRYTLVE--KFK-----PLDQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 243 KDFCLKALGQeadkglsgCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMG 322
Cdd:PRK11057 228 MRYVQEQRGK--------SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 323 VDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KEVAKLQEKRGNKasdkatima 398
Cdd:PRK11057 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIERHK--------- 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2462558841 399 FDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTavrRRLEALE 448
Cdd:PRK11057 368 LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP---KQYDGLE 414
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
15-219 |
6.93e-71 |
|
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: 226.09 E-value: 6.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 15 RVRSTLKKVFGFDSFKtPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLK 94
Cdd:cd18015 5 KVKDTLKNVFKLEKFR-PLQLETINATMAG-RDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 95 VRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:cd18015 83 ISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEkIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRPDY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462558841 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTP 219
Cdd:cd18015 163 KKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCL-TFTAS 207
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
14-212 |
1.41e-69 |
|
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: 222.39 E-value: 1.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 14 RRVRSTLKKVFGFDSFKTPlQESATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL 93
Cdd:cd18016 3 KEMMKIFHKKFGLHQFRTN-QLEAINAALLGE-DCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 94 KVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPE-MAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPD 172
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEkISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462558841 173 YLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP 212
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRP 200
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
222-363 |
4.13e-68 |
|
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: 215.92 E-value: 4.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 222 RANLFYDVQFKELISDPYGNLKdfclkalgQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLV 301
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLK--------RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDV 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558841 302 QNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 363
Cdd:cd18794 73 QRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
19-219 |
3.68e-66 |
|
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: 213.27 E-value: 3.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 19 TLKKVFGFDSFKtPLQESATMAVVKGNKDVFVcMPTGAGKSLCYQLPALL----AKGITIVVSPLIALIQDQVDHLLTLk 94
Cdd:cd18018 3 LLRRVFGHPSFR-PGQEEAIARLLSGRSTLVV-LPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 95 VRVSSLNSKLSAQERKELLADLEREkpQTKILYITPEMAASSSFQPTLNSLVSrhlLSYLVVDEAHCVSQWGHDFRPDYL 174
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAG--EVKILYVSPERLVNESFRELLRQTPP---ISLLVVDEAHCISEWSHNFRPDYL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462558841 175 RLG-ALRSRLGHAPCVALTATATPQVQEDVfaALHLKKP-VAIFKTP 219
Cdd:cd18018 155 RLCrVLRELLGAPPVLALTATATKRVVEDI--ASHLGIPeSGVVRGP 199
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-370 |
2.70e-55 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 199.37 E-value: 2.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 9 PFDPerrvrsTLKKVFGFDSFKTPLQESATMAVVKGNKD--VFVCMPTGAGKSLCYQLPALLAK---GITIVVSPLIALI 83
Cdd:NF041063 126 PGDP------FLAEALGFTHYRSPGQREAVRAALLAPPGstLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 84 QDQVDHLLTLKVRVSSLNSK-------LSAQERKELLADLEREkpQTKILYITPEmAASSSFQPTLNSLVSRHLLSYLVV 156
Cdd:NF041063 200 IDQERRARELLRRAGPDLGGplawhggLSAEERAAIRQRIRDG--TQRILFTSPE-SLTGSLRPALFDAAEAGLLRYLVV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 157 DEAHCVSQWGHDFRPDYLRLGALRSRL------GHAP-CVALTATATPQVQE------------DVFAALHLKKPVAIFK 217
Cdd:NF041063 277 DEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFrTLLLSATLTESTLDtletlfgppgpfIVVSAVQLRPEPAYWV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 218 TPCFRANlfydvqfkelisdpygNLKDFCLKALgQEADKGLsgcgIVYCRTREACEQLAIELSCRGVN-AKAYHAGLKAS 296
Cdd:NF041063 357 AKCDSEE----------------ERRERVLEAL-RHLPRPL----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDA 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558841 297 ERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 370
Cdd:NF041063 416 ERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
18-213 |
2.70e-54 |
|
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: 181.90 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 18 STLKKVFGFDSFKtPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVdhlLTLKVR- 96
Cdd:cd18017 2 NALNEYFGHSSFR-PVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQV---LQLVMSn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 97 VSSlnSKLSAQERKELLADLEREKpqTKILYITPEMAASSsfqPTLNSLVSRHLlSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18017 78 IPA--CFLGSAQSQNVLDDIKMGK--IRVIYVTPEFVSKG---LELLQQLRNGI-TLIAIDEAHCVSQWGHDFRSSYRHL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462558841 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPV 213
Cdd:cd18017 150 GSIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQ 186
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
31-201 |
6.17e-31 |
|
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: 118.11 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESAtMAVVKGNKDVFVCMPTGAGKSLCYQLPAL------LAKGITIVVSPLIALIQDQVDHLLTL-KVRVSSLNSK 103
Cdd:pfam00270 1 TPIQAEA-IPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 104 LSAQERKELLADLERekpqTKILYITPEMAASSsfqptLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPDYLR-LGALRSr 182
Cdd:pfam00270 80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDL-----LQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEiLRRLPK- 147
|
170
....*....|....*....
gi 2462558841 183 lgHAPCVALTATATPQVQE 201
Cdd:pfam00270 148 --KRQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
22-229 |
9.58e-28 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.27 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 22 KVFGFDSFkTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA-----KGITIVVSPLIALIQDQVDHLLTL--- 93
Cdd:smart00487 2 EKFGFEPL-RPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLgps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 94 -KVRVSSLNSKLSAQERKELLadlerEKPQTKILYITPEMAasssFQPTLNSLVSRHLLSYLVVDEAHCVSQWGhdFRPD 172
Cdd:smart00487 81 lGLKVVGLYGGDSKREQLRKL-----ESGKTDILVTTPGRL----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558841 173 YLRLgaLRSRLGHAPCVALTATATPQVQEdvFAALHLKKPvaIFKTPCFRANLFYDV 229
Cdd:smart00487 150 LEKL--LKLLPKNVQLLLLSATPPEEIEN--LLELFLNDP--VFIDVGFTPLEPIEQ 200
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
5-357 |
7.71e-20 |
|
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: 93.36 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 5 HTTFPFDPERRVRSTLKKvFGFD---SFktplQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVV 76
Cdd:COG1205 34 YAPWPDWLPPELRAALKK-RGIErlySH----QAEAIEAARAG-KNVVIATPTASGKSLAYLLPVLEAlledPGATaLYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 77 SPLIALIQDQVDHLLTL------KVRVSSLNSKLSAQERKELladleREKPQtkILYITPEMaasssfqptLN-SLVSRH 149
Cdd:COG1205 108 YPTKALARDQLRRLRELaealglGVRVATYDGDTPPEERRWI-----REHPD--IVLTNPDM---------LHyGLLPHH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 150 L--------LSYLVVDEAHC---V--SQWGHDFRpdylRLGALRSRLGHAP-CVALTAT-ATPQvqedVFAalhlkkpva 214
Cdd:COG1205 172 TrwarffrnLRYVVIDEAHTyrgVfgSHVANVLR----RLRRICRHYGSDPqFILASATiGNPA----EHA--------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 215 ifktpcfrANLFyDVQFkELISD---PYGNlKDFCL-----------KALGQEA--------DKGLSgcGIVYCRTREAC 272
Cdd:COG1205 235 --------ERLT-GRPV-TVVDEdgsPRGE-RTFVLwnpplvddgirRSALAEAarlladlvREGLR--TLVFTRSRRGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 273 EQLAIEL------SCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFV--AHWniAKSMAGYY 344
Cdd:COG1205 302 ELLARYArralrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVvlAGY--PGTRASFW 379
|
410
....*....|...
gi 2462558841 345 QESGRAGRDGKPS 357
Cdd:COG1205 380 QQAGRAGRRGQDS 392
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
273-354 |
1.74e-18 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 79.95 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 273 EQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGR 352
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2462558841 353 DG 354
Cdd:smart00490 81 AG 82
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
45-194 |
1.26e-17 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 79.75 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 45 NKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIQDQ---VDHLLTLKVRVSSLNSKLSAQERKELLADLE 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558841 118 rekpqtKILYITPEMAASSSFQptlNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLgaLRSRLGHAPCVALTAT 194
Cdd:cd00046 81 ------DIIIATPDMLLNLLLR---EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
247-354 |
1.66e-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: 75.32 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 247 LKALGQEADKGLSGCGIVYCRTREACEqLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 2462558841 327 NVRFVAHWNIAKSMAGYYQESGRAGRDG 354
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
45-160 |
9.00e-14 |
|
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: 69.15 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 45 NKDVFVCMPTGAGKSLCYQLPALL------AKGITIV-VSPLIALIQDQVDHL------LTLKVRVSSLNSKLSAQERKE 111
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLeepldeIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462558841 112 LLadlerEKPQTkILYITPEmaassSFQPTLNSLVSRHLLS---YLVVDEAH 160
Cdd:cd17922 81 QL-----KNPPG-ILITTPE-----SLELLLVNKKLRELFAglrYVVVDEIH 121
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-355 |
1.46e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 73.01 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 12 PERRVRSTLKKvFGFDSFkTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGITIV-VSPLIALIQDQVD 88
Cdd:COG1204 7 PLEKVIEFLKE-RGIEEL-YPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 89 HL------LTLKVRVSSLNsklsAQERKELLADlerekpqTKILYITPEMAAS-SSFQPtlnSLVSRhlLSYLVVDEAHC 161
Cdd:COG1204 85 EFkrdfeeLGIKVGVSTGD----YDSDDEWLGR-------YDILVATPEKLDSlLRNGP---SWLRD--VDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 162 VsqwGHDFR-PDY------LRLGALRSRLghapcVALTATAT-PQVQEDVFAALHLK---KPVAIfktpcfRANLFYD-- 228
Cdd:COG1204 149 I---DDESRgPTLevllarLRRLNPEAQI-----VALSATIGnAEEIAEWLDAELVKsdwRPVPL------NEGVLYDgv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 229 VQFKELISDPYGNLKDFCLKALGQEadkglsGCGIVYCRTREACEQLAIELS---------------------------- 280
Cdd:COG1204 215 LRFDDGSRRSKDPTLALALDLLEEG------GQVLVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 281 ---------C--RGVnakAYH-AGLKASERTLVQnDWMEE-KVPVIVATISFGMGVdkaN--VRFV----AHWNIAKSMA 341
Cdd:COG1204 289 thtnekladCleKGV---AFHhAGLPSELRRLVE-DAFREgLIKVLVATPTLAAGV---NlpARRViirdTKRGGMVPIP 361
|
410
....*....|....*.
gi 2462558841 342 G--YYQESGRAGRDGK 355
Cdd:COG1204 362 VleFKQMAGRAGRPGY 377
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
263-357 |
1.15e-12 |
|
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: 65.36 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 263 IVYCRTREACEQLAIELSCRGVNAK-------AYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWN 335
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 2462558841 336 IAKSMAGYYQESGRAGRDGKPS 357
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDS 140
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
46-160 |
1.30e-12 |
|
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: 66.45 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 46 KDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVVSPLIALIQDQVDHL------LTLKVRVSSLNSKLSAQERKELLa 114
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAllrdPGSRaLYLYPTKALAQDQLRSLrelleqLGLGIRVATYDGDTPREERRAII- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462558841 115 dleREKPQtkILYITPEMaasssfqptLNSLVSRH---------LLSYLVVDEAH 160
Cdd:cd17923 95 ---RNPPR--ILLTNPDM---------LHYALLPHhdrwarflrNLRYVVLDEAH 135
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
263-354 |
5.36e-10 |
|
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: 57.95 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 263 IVYCRTREACEQLAIELSCrgvnAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVD--------KANVRFVAHW 334
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|
gi 2462558841 335 NIAKSMAGYYQESGRAGRDG 354
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPG 142
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
247-355 |
8.21e-10 |
|
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: 56.75 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 247 LKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:cd18787 15 LLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIP 94
|
90 100
....*....|....*....|....*....
gi 2462558841 327 NVRFVAHWNIAKSMAGYYQESGRAGRDGK 355
Cdd:cd18787 95 GVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
43-324 |
3.21e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 59.65 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 43 KGNKDVFVCMPTGAGKSL----CYQlpALLAKGITIVVSPLIALIQDQVDHLLTLkvrvssLNSKLSAQERKELLADler 118
Cdd:COG1061 98 RGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------LGDPLAGGGKKDSDAP--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 119 ekpqtkILYITPEMAASssfQPTLNSLVSRhlLSYLVVDEAHcvsqwghdfrpdylRLGA-----LRSRLGHAPCVALta 193
Cdd:COG1061 167 ------ITVATYQSLAR---RAHLDELGDR--FGLVIIDEAH--------------HAGApsyrrILEAFPAAYRLGL-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 194 TATPqVQEDvfaalhlKKPVAIFktpcFRANLFYDVQFKELISD--------------------PYGNLKDFCLKALGQE 253
Cdd:COG1061 220 TATP-FRSD-------GREILLF----LFDGIVYEYSLKEAIEDgylappeyygirvdltderaEYDALSERLREALAAD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 254 AD------------KGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGM 321
Cdd:COG1061 288 AErkdkilrellreHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
|
...
gi 2462558841 322 GVD 324
Cdd:COG1061 368 GVD 370
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-195 |
1.76e-08 |
|
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: 54.19 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIqDQVDHLLTLKVRVSSLNSKL-- 104
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALV-NQKEADLRERFGPLGKNVGLlt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 105 -SAQERKELLADLErekpqtkILYITPEMAASssfqpTLNSLVSRHL--LSYLVVDEAHCVSQwghdfrPDY-----LRL 176
Cdd:cd17921 82 gDPSVNKLLLAEAD-------ILVATPEKLDL-----LLRNGGERLIqdVRLVVVDEAHLIGD------GERgvvleLLL 143
|
170
....*....|....*....
gi 2462558841 177 GALRSRLGHAPCVALTATA 195
Cdd:cd17921 144 SRLLRINKNARFVGLSATL 162
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
240-354 |
2.70e-08 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 56.32 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 240 GNLKDFcLKALGQEADKGLsgcgiVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISF 319
Cdd:PTZ00110 364 GKLKML-LQRIMRDGDKIL-----IFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
|
90 100 110
....*....|....*....|....*....|....*
gi 2462558841 320 GMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDG 354
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
365-434 |
3.18e-08 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 50.37 E-value: 3.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558841 365 RNDRDQVSFLIRKEVAKLQEKRGNKASdkatimaFDALVTFCEELG-CRHAAIAKYFGDALPA--CaKGCDHC 434
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQK-------LQAMVAYCENTTdCRRKQLLRYFGEEFDSepC-GNCDNC 65
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
252-352 |
1.00e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 54.90 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 252 QEADKGLSGCGIVYCRTREACEQLAIELscrGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDkanvrFV 331
Cdd:COG1202 420 TKSSKGYRGQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVD-----FP 491
|
90 100 110
....*....|....*....|....*....|
gi 2462558841 332 AHWNIAKSMA-G--------YYQESGRAGR 352
Cdd:COG1202 492 ASQVIFDSLAmGiewlsvqeFHQMLGRAGR 521
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
31-316 |
1.14e-07 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 54.00 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPAL--LAKGI-----TIVVSP---LIALIQDQVDHLLT-LKVRVSS 99
Cdd:COG0513 26 TPIQAQAIPLILAG-RDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLALQVAEELRKLAKyLGLRVAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 100 L--NSKLSAQERKelladLEReKPQtkILYITP----EMAASSSFqptlnSLvsrHLLSYLVVDEAhcvsqwghD----- 168
Cdd:COG0513 105 VygGVSIGRQIRA-----LKR-GVD--IVVATPgrllDLIERGAL-----DL---SGVETLVLDEA--------Drmldm 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 169 -FRPDylrlgaLRSRLGHAPCVALT----ATATPQVQEdvFAALHLKKPVAIFKTPCFRAN-----LFYDVQFKElisdp 238
Cdd:COG0513 161 gFIED------IERILKLLPKERQTllfsATMPPEIRK--LAKRYLKNPVRIEVAPENATAetieqRYYLVDKRD----- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558841 239 ygnlKDFCLKALGQEADKGLsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVAT 316
Cdd:COG0513 228 ----KLELLRRLLRDEDPER---AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVAT 298
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
261-355 |
8.18e-07 |
|
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: 46.93 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 261 CGIVYCRTREACEQLAIELScrgvnakayhaglkasertlvqndwmeekvpVIVATISFGMGVDKANVRFVAHWNIAKSM 340
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|....*
gi 2462558841 341 AGYYQESGRAGRDGK 355
Cdd:cd18785 54 ASYIQRVGRAGRGGK 68
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
32-194 |
2.46e-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: 47.30 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 32 PLQESATMAVVKGNKDVF--VCMPTGAGKSLC-YQLPALLAKGITIVVSPLIALIQDQVDHLLTLkvrvsslnskLSAQE 108
Cdd:cd17926 3 PYQEEALEAWLAHKNNRRgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDF----------LGDSS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 109 RKELLADLEREKPQTKILYITPEMAASSSFQPTLNSlvsrHLLSYLVVDEAH--CVSQWGHdfrpdylrlgaLRSRLGHA 186
Cdd:cd17926 73 IGLIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLF----DQFGLLIVDEAHhlPAKTFSE-----------ILKELNAK 137
|
....*...
gi 2462558841 187 PCVALTAT 194
Cdd:cd17926 138 YRLGLTAT 145
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
31-211 |
3.22e-06 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 47.96 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPA----LLAKGITIVVSPLIALI-------QDQV-DHLLTL----- 93
Cdd:cd17961 18 TLIQSKAIPLALEG-KDILARARTGSGKTAAYALPIiqkiLKAKAESGEEQGTRALIlvptrelAQQVsKVLEQLtaycr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 94 -KVRVSSLNSKLSAQERKELLADlereKPQtkILYITPEMAASssfQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDfrpd 172
Cdd:cd17961 97 kDVRVVNLSASSSDSVQRALLAE----KPD--IVVSTPARLLS---HLESGSLLLLSTLKYLVIDEADLVLSYGYE---- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462558841 173 ylrlGALRSRLGHAP----CVALTATATPQVQEdvfaalhLKK 211
Cdd:cd17961 164 ----EDLKSLLSYLPknyqTFLMSATLSEDVEA-------LKK 195
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
31-167 |
4.11e-06 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 48.00 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLP---ALLA----KGITIVVSPLIALI-------QDQV-DHLLTLK- 94
Cdd:cd17946 14 TPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPileRLLSqkssNGVGGKQKPLRALIltptrelAVQVkDHLKAIAk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 95 ---VRVSSLNSKLSAQERKELLadleREKPQtkILYITP----EMAASSsfQPTLNSLvsrHLLSYLVVDEAHCVSQWGH 167
Cdd:cd17946 94 ytnIKIASIVGGLAVQKQERLL----KKRPE--IVVATPgrlwELIQEG--NEHLANL---KSLRFLVLDEADRMLEKGH 162
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
22-159 |
1.26e-05 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 46.42 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 22 KVFGFDSFkTPLQeSATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGIT---------IVVSPLIALIQdQVDHL 90
Cdd:cd17960 6 AELGFTSM-TPVQ-AATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLKRKAnlkkgqvgaLIISPTRELAT-QIYEV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558841 91 LT--LKVRVSSLNSKL--SAQERKELLADLEREKPQtkILYITP----EMAASSSFQPTLNSlvsrhlLSYLVVDEA 159
Cdd:cd17960 83 LQsfLEHHLPKLKCQLliGGTNVEEDVKKFKRNGPN--ILVGTPgrleELLSRKADKVKVKS------LEVLVLDEA 151
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
263-355 |
1.52e-05 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 47.51 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 263 IVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAG 342
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|...
gi 2462558841 343 YYQESGRAGRDGK 355
Cdd:PTZ00424 351 YIHRIGRSGRFGR 363
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
47-159 |
1.59e-05 |
|
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350714 [Multi-domain] Cd Length: 231 Bit Score: 46.47 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 47 DVFVCMPTGAGKSLCYQLP---ALLAKGIT----IVVSPLIALIQdQVDHLLT-----LKVRVSSLNSKLS-AQERKELL 113
Cdd:cd17956 38 DLCVSAPTGSGKTLAYVLPivqALSKRVVPrlraLIVVPTKELVQ-QVYKVFEslckgTGLKVVSLSGQKSfKKEQKLLL 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462558841 114 ADLERE---KPQtkILYITP-----EMAASSSFqpTLNSlvsrhlLSYLVVDEA 159
Cdd:cd17956 117 VDTSGRylsRVD--ILVATPgrlvdHLNSTPGF--TLKH------LRFLVIDEA 160
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
25-216 |
1.82e-04 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 43.13 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 25 GFDSFKT--PLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKG-------------ITIV-VSPLIALIQDQVd 88
Cdd:cd18019 11 AFEGFKSlnRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGkhrnpdgtinldaFKIVyIAPMKALVQEMV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 89 hlLTLKVRVSSLNSKLSaqerkELLADLEREKPQ---TKILYITPE---MAASSSFQPTLNSLVsrhllSYLVVDEAHCV 162
Cdd:cd18019 90 --GNFSKRLAPYGITVA-----ELTGDQQLTKEQiseTQIIVTTPEkwdIITRKSGDRTYTQLV-----RLIIIDEIHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558841 163 sqwgHDFRPDYLRlgALRSR------LGHAPC--VALTATaTPQVqEDVFAALHLKKPVAIF 216
Cdd:cd18019 158 ----HDDRGPVLE--SIVARtirqieQTQEYVrlVGLSAT-LPNY-EDVATFLRVDPKKGLF 211
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
40-160 |
2.79e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.50 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 40 AVVKGNKDVFVCMPTGAGKSLCY-QLPALLAK----GITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKella 114
Cdd:pfam04851 18 SIKNGQKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKD---- 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462558841 115 dleREKPQTKILYITPEMAASSSFQPTLNSLVSRHLlsYLVVDEAH 160
Cdd:pfam04851 94 ---ESVDDNKIVVTTIQSLYKALELASLELLPDFFD--VIIIDEAH 134
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
41-194 |
4.23e-04 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 41.58 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 41 VVKGNKDVFVCMPTGAGKSLC--YQLPALLA---KGITIVVSPLIALIQDQVdhlltlkVRVSSLNSKLSAQERKELLAD 115
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFIsyYCMEKVLResdDGVVVYVAPTKALVNQVV-------AEVYARFSKKYPPSGKSLWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 116 LERE----KPQT-KILYITPEMAASSSFQPTLNSLVSRhlLSYLVVDEAHCVSQWGHDFRPDYLRLgalrsrLGHAPCVA 190
Cdd:cd18025 85 FTRDyrhnNPMNcQVLITVPECLEILLLSPHNASWVPR--IKYVIFDEIHSIGQSEDGAVWEQLLL------LIPCPFLA 156
|
....
gi 2462558841 191 LTAT 194
Cdd:cd18025 157 LSAT 160
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
22-211 |
5.15e-04 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 41.41 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 22 KVFGFDSfKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGI---------TIVVSP---LIALIQDQV 87
Cdd:cd17964 10 TRMGFET-MTPVQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIqsLLNTKpagrrsgvsALIISPtreLALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 88 DHLLTL--KVRVSSLnskLSAQERKELLADLEREKPQtkILYITP----EMAASSSFQPTLNSlvsrhlLSYLVVDEAHC 161
Cdd:cd17964 89 KKLLQGlrKLRVQSA---VGGTSRRAELNRLRRGRPD--ILVATPgrliDHLENPGVAKAFTD------LDYLVLDEADR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558841 162 VSQWGhdFRPDylrlgaLRSRLGHAPCVALT--------ATATPQVQEdvFAALHLKK 211
Cdd:cd17964 158 LLDMG--FRPD------LEQILRHLPEKNADprqtllfsATVPDEVQQ--IARLTLKK 205
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
34-160 |
9.87e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 40.49 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 34 QESATMAVVKGnKDVFVCMPTGAGKS-----LC----YQLPAlLAKGITIVVSPLIALIQDQVD----HLLTLKVRVSSL 100
Cdd:cd17927 7 QLELAQPALKG-KNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEvfrkHFERPGYKVTGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558841 101 NSKLSAQERKELLADlerekpQTKILYITPemaasssfQPTLNSL-----VSRHLLSYLVVDEAH 160
Cdd:cd17927 85 SGDTSENVSVEQIVE------SSDVIIVTP--------QILVNDLksgtiVSLSDFSLLVFDECH 135
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
32-163 |
1.08e-03 |
|
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: 40.01 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 32 PLQESATMAVVKGNKDVFVCMPTGAGKSLCYQL---PALLAKGITIVVSPLIALIQDQVDH-----LLTLKVRVSSlnsk 103
Cdd:cd18028 4 PPQAEAVRAGLLKGENLLISIPTASGKTLIAEMamvNTLLEGGKALYLVPLRALASEKYEEfkkleEIGLKVGIST---- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558841 104 LSAQERKELLADLErekpqtkILYITPEmaasssfqpTLNSLVsRH------LLSYLVVDEAHCVS 163
Cdd:cd18028 80 GDYDEDDEWLGDYD-------IIVATYE---------KFDSLL-RHspswlrDVGVVVVDEIHLIS 128
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
262-356 |
1.43e-03 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 41.31 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 262 GIVYCRTREACEQLAIELS-CRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSM 340
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90
....*....|....*.
gi 2462558841 341 AGYYQESGRAGRDGKP 356
Cdd:PLN00206 450 KEYIHQIGRASRMGEK 465
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
37-128 |
2.26e-03 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 40.27 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 37 ATMAVVK-GNKDVFV-CMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTL--------KVRVSSLnSKLSA 106
Cdd:TIGR03158 4 ATFEALQsKDADIIFnTAPTGAGKTLAWLTPLLHGENDTIALYPTNALIEDQTEAIKEFvdvfkperDVNLLHV-SKATL 82
|
90 100
....*....|....*....|..
gi 2462558841 107 QERKELLADLEREKPQTKILYI 128
Cdd:TIGR03158 83 KDIKEYANDKVGSSKGEKLYNL 104
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
34-163 |
3.40e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 39.12 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 34 QESATMAVVKGNKDVFVCMPTGAGKSLCYQL----PALLAKGITIVVSPLIALIQDQVDHLltlkvrvSSLNSKLSAQER 109
Cdd:cd18026 22 KECLSLPGLLEGRNLVYSLPTSGGKTLVAEIlmlkRLLERRKKALFVLPYVSIVQEKVDAL-------SPLFEELGFRVE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558841 110 kELLADLEREKP----QTKILYITPEMAASssfqpTLNSLV---SRHLLSYLVVDEAHCVS 163
Cdd:cd18026 95 -GYAGNKGRSPPkrrkSLSVAVCTIEKANS-----LVNSLIeegRLDELGLVVVDELHMLG 149
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
31-215 |
3.53e-03 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 38.72 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 31 TPLQESAtMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA-------KGI-TIVVSPLIALIQDQVDHLLTLkvrvsSLNS 102
Cdd:cd17957 14 TPIQMQA-IPILLHGRDLLACAPTGSGKTLAFLIPILQKlgkprkkKGLrALILAPTRELASQIYRELLKL-----SKGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 103 KLSAQERKELLADLEREKPQTK----ILYITPeMAASSSFQptlNSLVSRHLLSYLVVDEAhcvsqwghD--FRPDYLR- 175
Cdd:cd17957 88 GLRIVLLSKSLEAKAKDGPKSItkydILVSTP-LRLVFLLK---QGPIDLSSVEYLVLDEA--------DklFEPGFREq 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462558841 176 ----LGALRSrlgHAPCVAL-TATATPQVQEdvFAALHLKKPVAI 215
Cdd:cd17957 156 tdeiLAACTN---PNLQRSLfSATIPSEVEE--LARSVMKDPIRI 195
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
34-197 |
4.08e-03 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 38.34 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 34 QESATMAVVK---GNKDVFVCMPTGAGKSLCY--QLPALLAKGIT-IVVSPLIALIQDQVDHLltlKVR----VSSLNSK 103
Cdd:cd17929 1 QRKAYEAIVSslgGFKTFLLHGVTGSGKTEVYieLIEKVLAKGKQvLVLVPEISLTPQLIKRF---KKRfgdkVAVLHSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 104 LSAQERKELLADLEREKPQTKIlyitpeMAASSSFQPTLNslvsrhlLSYLVVDEAHcVSQWGHDFRPDY-LRLGAL-RS 181
Cdd:cd17929 78 LSDKERADEWRKIKRGEAKVVI------GARSALFAPFKN-------LGLIIVDEEH-DSSYKQDSGPRYhARDVAIyRA 143
|
170
....*....|....*.
gi 2462558841 182 RLGHAPCValTATATP 197
Cdd:cd17929 144 KLENAPVV--LGSATP 157
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
37-160 |
4.67e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 39.47 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 37 ATMAVVK-GNKDVFV-CMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQ---------------VDHLLTLKVRVSS 99
Cdd:cd09710 4 ATFEALQsKDADIIFnTAPTGAGKTLAWLTPLLHGENKAIALYPTNALIEDQteaikefvddanprhQVKSLSASDITLW 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558841 100 LNSKLSAQERKELLADLEREKPQTK---ILYITPEMAASSSFQ----PTLNSLVSRHLLSYLVVDEAH 160
Cdd:cd09710 84 PNDKNVGSSKGEKLYNLLRNDIGTStpiILLTNPDIFVYLTRFayidRGDIAAGFYTKFSTVIFDEFH 151
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
43-160 |
5.05e-03 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 38.57 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 43 KGNKDVFVCMPTGAGKSLCYQLPAL--LAKGIT------------IVVSPLIALIQDQVDHLLTlkvRVSSLNSKLsaqe 108
Cdd:cd18020 15 KTNENMLICAPTGAGKTNIAMLTILheIRQHVNqggvikkddfkiVYIAPMKALAAEMVEKFSK---RLAPLGIKV---- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558841 109 rKELLADLE---REKPQTKILYITPE----MAASSSFQPTLNSLVsrhllSYLVVDEAH 160
Cdd:cd18020 88 -KELTGDMQltkKEIAETQIIVTTPEkwdvVTRKSSGDVALSQLV-----RLLIIDEVH 140
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
259-356 |
5.49e-03 |
|
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: 37.63 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558841 259 SGCGIVYCRTREACEQLAIELscrgvNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAK 338
Cdd:cd18796 49 SQAERLAQRLRELCPDRVPPD-----FIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPK 123
|
90
....*....|....*...
gi 2462558841 339 SMAGYYQESGRAGRDGKP 356
Cdd:cd18796 124 SVARLLQRLGRSGHRPGA 141
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
6-60 |
6.45e-03 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 39.54 E-value: 6.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558841 6 TTFPFDPERR--VRSTLKKVFGFDSFktPLQESATMAVVKGnKDVFVCMPTGAGKSL 60
Cdd:COG4581 2 TLSPARADARleALADFAEERGFELD--PFQEEAILALEAG-RSVLVAAPTGSGKTL 55
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
18-67 |
6.57e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 38.34 E-value: 6.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462558841 18 STLKKVFGFDSfKTPLQESATMAVVKGnKDVFVCMPTGAGKSLCYQLPAL 67
Cdd:cd17949 3 SHLKSKMGIEK-PTAIQKLAIPVLLQG-RDVLVRSQTGSGKTLAYLLPII 50
|
|
| |
