|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
14-437 |
3.51e-176 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 521.62 E-value: 3.51e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 14 RRVRSTLKKVFGFDSFKtPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLAL 93
Cdd:COG0514 3 DDALEVLKRVFGYDSFR-PGQEEIIEAVLAG-RDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 94 KVRVSSLNSKLSAQERKDLLADLEReePQTKILYITPEMAASSSFQpslnSLLSRHLLSYLVVDEAHCVSQWGHDFRPDY 173
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRA--GELKLLYVAPERLLNPRFL----ELLRRLKISLFAIDEAHCISQWGHDFRPDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 174 LRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElISDPYGNLKDFcLKALGQE 253
Cdd:COG0514 155 RRLGELRERLPNVPVLALTATATPRVRADIAEQLGLEDP-RVFVGSFDRPNLRLEVVPKP-PDDKLAQLLDF-LKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 254 AdkglsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIH 333
Cdd:COG0514 232 S-------GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 334 WNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKAsdkatilAFDALVTFCEELGCRH 413
Cdd:COG0514 305 YDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERKRVERA-------KLDAMLAYAETTGCRR 377
|
410 420
....*....|....*....|....
gi 1622881391 414 AAIAKYFGDAPPACAKGCDHCQNP 437
Cdd:COG0514 378 QFLLRYFGEELAEPCGNCDNCLGP 401
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
17-221 |
4.38e-130 |
|
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: 391.06 E-value: 4.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 17 RSTLKKVFGFDSFKTPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVR 96
Cdd:cd18014 1 RSTLKKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 97 VSSLNSKLSAQERKDLLADLEREEPQTKILYITPEMAASSSFQPSLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADLESEKPQTKFLYITPEMAATSSFQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622881391 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 |
7.56e-130 |
|
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: 405.23 E-value: 7.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 17 RSTLKKVFGFDSFKtPLQENATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVR 96
Cdd:TIGR01389 2 QQVLKRTFGYDDFR-PGQEEIISHVLDGR-DVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 97 VSSLNSKLSAQERKDLLADLEREEpqTKILYITPEMAASSSFQpslnSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR01389 80 AAYLNSTLSAKEQQDIEKALVNGE--LKLLYVAPERLEQDYFL----NMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKElisdpygNLKDFCLKALGQEadK 256
Cdd:TIGR01389 154 GSLAERFPQVPRIALTATADAETRQDIRELLRLADA-NEFITSFDRPNLRFSVVKKN-------NKQKFLLDYLKKH--R 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNI 336
Cdd:TIGR01389 224 GQSG--IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkEVAKLQEKRGNKASDKatilaFDALVTFCEELGCRHAAI 416
Cdd:TIGR01389 302 PGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDDYKQIEREK-----LRAMIAYCETQTCRRAYI 374
|
410 420 430
....*....|....*....|....*....|.
gi 1622881391 417 AKYFGDAPPACAKGCDHC-QNPMAVRRQLEA 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 |
7.89e-127 |
|
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: 392.98 E-value: 7.89e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 18 STLKKVFGFDSFKtPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVRV 97
Cdd:TIGR00614 1 KILKKYFGLSSFR-PVQLEVINAVLLG-RDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 98 SSLNSKLSAQERKDLLADLEreEPQTKILYITPE-MAASSSFqpsLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:TIGR00614 79 TFLNSAQTKEQQLNVLTDLK--DGKIKLLYVTPEkISASNRL---LQTLEERKGITLIAVDEAHCISQWGHDFRPDYKAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPvAIFKTPCFRANLFYDVQFKelisdpYGNLKDFCLKALgQEADK 256
Cdd:TIGR00614 154 GSLKQKFPNVPVMALTATASPSVREDILRQLNLLNP-QIFCTSFDRPNLYYEVRRK------TPKILEDLLRFI-RKEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 257 GLSGcgIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNI 336
Cdd:TIGR00614 226 GKSG--IIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 337 AKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqvSFLIRKEVakLQEKRGNKASDKATILafdALVTFCEELG-CRHAA 415
Cdd:TIGR00614 304 PKSMESYYQESGRAGRDGLPSECHLFYAPAD----MNRLRRLL--MEEPDGNFRTYKLKLY---EMMEYCLNSStCRRLI 374
|
410 420
....*....|....*....|..
gi 1622881391 416 IAKYFGD---APPACAKGCDHC 434
Cdd:TIGR00614 375 LLSYFGEkgfNKSFCIMGTEKC 396
|
|
| RecQ5 |
pfam06959 |
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ... |
626-826 |
2.16e-119 |
|
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.
Pssm-ID: 399738 Cd Length: 202 Bit Score: 363.03 E-value: 2.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 626 SCSAQAVPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSRPFQTATELMETTRIREQAPQPKRGGEHEPPSRPCGLLDEDR 705
Cdd:pfam06959 2 SCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDEDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 706 SEPLPGPRGEVPGGSAHCGGPSPEKKAKSSSGGSSLAKGRASKKQQLLAAAAHKDSQSIARFFCRREESPALLASAPEAE 785
Cdd:pfam06959 82 SEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSSVAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRAE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622881391 786 GACPSCEGVQGPLMAPEKYTGEEDGAGGRSPAPPQTEECLR 826
Cdd:pfam06959 162 GASPSCEGVQGPPMAPEKCTGEEDGAQGHLAAPPQTEECTR 202
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
17-220 |
2.78e-99 |
|
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: 2.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 17 RSTLKKVFGFDSFKtPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVR 96
Cdd:cd17920 1 EQILKEVFGYDEFR-PGQLEAINAVLAG-RDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 97 VSSLNSKLSAQERKDllADLEREEPQTKILYITPEMAASSSFQPSLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYLRL 176
Cdd:cd17920 79 AAALNSTLSPEEKRE--VLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622881391 177 GALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPC 220
Cdd:cd17920 157 GRLRRALPGVPILALTATATPEVREDILKRLGLRNPV-IFRASF 199
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-437 |
9.62e-99 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 323.20 E-value: 9.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 6 TTFPLDPERRVRSTLKKVFGFDSFKtPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQD 85
Cdd:PRK11057 3 QAEVLNLESLAKQVLQETFGYQQFR-PGQQEIIDAVLSG-RDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 86 QVDHLLALKVRVSSLNSKLSAQERKDLLADLEREepQTKILYITPEMAASSSFqpsLNSLLSRHLlSYLVVDEAHCVSQW 165
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTREQQLEVMAGCRTG--QIKLLYIAPERLMMDNF---LEHLAHWNP-ALLAVDEAHCISQW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 166 GHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP---VAIFKTPCFRANLFYdvQFKelisdPYGNL 242
Cdd:PRK11057 155 GHDFRPEYAALGQLRQRFPTLPFMALTATADDTTRQDIVRLLGLNDPliqISSFDRPNIRYTLVE--KFK-----PLDQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 243 KDFCLKALGQeadkglsgCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMG 322
Cdd:PRK11057 228 MRYVQEQRGK--------SGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 323 VDKANVRFVIHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KEVAKLQEKRGNKasdkatila 398
Cdd:PRK11057 300 INKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIERHK--------- 367
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622881391 399 FDALVTFCEELGCRHAAIAKYFGDAPPACAKGCDHCQNP 437
Cdd:PRK11057 368 LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDP 406
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
21-434 |
1.97e-98 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 336.48 E-value: 1.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 21 KKVFGFDSFKTPLQE--NATMAvvkgNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVRVS 98
Cdd:PLN03137 453 KKVFGNHSFRPNQREiiNATMS----GYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 99 SLNSKLSAQERKDLLADLEREEPQTKILYITPE-MAASSSFQPSLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLG 177
Cdd:PLN03137 529 SLSAGMEWAEQLEILQELSSEYSKYKLLYVTPEkVAKSDSLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 178 ALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTPCFRANLFYDVQFKelisdpygnlKDFCLkalgQEADKG 257
Cdd:PLN03137 609 ILKQKFPNIPVLALTATATASVKEDVVQALGLVNCV-VFRQSFNRPNLWYSVVPK----------TKKCL----EDIDKF 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 258 L-----SGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVI 332
Cdd:PLN03137 674 IkenhfDECGIIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVI 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 333 HWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRK-EVAKLQEKRG-NKASDKATILAFDA-----LVTF 405
Cdd:PLN03137 754 HHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQgGVEQSPMAMGyNRMASSGRILETNTenllrMVSY 833
|
410 420 430
....*....|....*....|....*....|..
gi 1622881391 406 CE-ELGCRHAAIAKYFGDAPPA--CAKGCDHC 434
Cdd:PLN03137 834 CEnEVDCRRFLQLVHFGEKFDStnCKKTCDNC 865
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
15-219 |
6.08e-68 |
|
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: 6.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 15 RVRSTLKKVFGFDSFKtPLQE---NATMAvvkgNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLL 91
Cdd:cd18015 5 KVKDTLKNVFKLEKFR-PLQLetiNATMA----GRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 92 ALKVRVSSLNSKLSAQERKDLLADLEREEPQTKILYITPE-MAASSSFQPSLNSLLSRHLLSYLVVDEAHCVSQWGHDFR 170
Cdd:cd18015 80 KLGISATMLNASSSKEHVKWVHAALTDKNSELKLLYVTPEkIAKSKRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622881391 171 PDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVaIFKTP 219
Cdd:cd18015 160 PDYKKLGILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCL-TFTAS 207
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
222-363 |
3.92e-67 |
|
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: 220.54 E-value: 3.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 222 RANLFYDVQFKELISDPYGNLKdfclkalgQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLV 301
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLK--------RIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDV 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622881391 302 QNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 363
Cdd:cd18794 73 QRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
14-212 |
8.37e-66 |
|
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: 220.08 E-value: 8.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 14 RRVRSTLKKVFGFDSFKTPlQENATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLAL 93
Cdd:cd18016 3 KEMMKIFHKKFGLHQFRTN-QLEAINAALLGE-DCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 94 KVRVSSLNSKLSAQERKDLLADLEREEPQTKILYITPE-MAASSSFQPSLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPD 172
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDPIIKLLYVTPEkISASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622881391 173 YLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKP 212
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRP 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
19-219 |
2.21e-64 |
|
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: 215.58 E-value: 2.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 19 TLKKVFGFDSFKtPLQENATMAVVKGNKDVFVcMPTGAGKSLCYQLPALL----AKGITIVVSPLIALIQDQVDHLLALk 94
Cdd:cd18018 3 LLRRVFGHPSFR-PGQEEAIARLLSGRSTLVV-LPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 95 VRVSSLNSKLSAQERKDLLADLEREEpqTKILYITPEMAASSSFqpsLNSLLSRHLLSYLVVDEAHCVSQWGHDFRPDYL 174
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGE--VKILYVSPERLVNESF---RELLRQTPPISLLVVDEAHCISEWSHNFRPDYL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622881391 175 RLG-ALRSRLGHAPCVALTATATPQVQEDVfaALHLKKP-VAIFKTP 219
Cdd:cd18018 155 RLCrVLRELLGAPPVLALTATATKRVVEDI--ASHLGIPeSGVVRGP 199
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
18-213 |
5.93e-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: 186.13 E-value: 5.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 18 STLKKVFGFDSFKtPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLALKVRV 97
Cdd:cd18017 2 NALNEYFGHSSFR-PVQWKVIRSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 98 SSLNSKLSAQERKDLLADLEReepqtkILYITPEMAASSsfqPSLNSLLSRHLlSYLVVDEAHCVSQWGHDFRPDYLRLG 177
Cdd:cd18017 81 CFLGSAQSQNVLDDIKMGKIR------VIYVTPEFVSKG---LELLQQLRNGI-TLIAIDEAHCVSQWGHDFRSSYRHLG 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622881391 178 ALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPV 213
Cdd:cd18017 151 SIRNRLPNVPIVALTATATPSVRDDIIKNLNLRNPQ 186
|
|
| DpdF |
NF041063 |
protein DpdF; |
9-370 |
3.50e-53 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 200.14 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 9 PLDPerrvrsTLKKVFGFDSFKTPLQENATMAVVKGNKD--VFVCMPTGAGKSLCYQLPALLAK---GITIVVSPLIALI 83
Cdd:NF041063 126 PGDP------FLAEALGFTHYRSPGQREAVRAALLAPPGstLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 84 QDQ-------VDHLLALKVRVSSLNSKLSAQERKDLLADLEREEpQtKILYITPEmAASSSFQPSLNSLLSRHLLSYLVV 156
Cdd:NF041063 200 IDQerrarelLRRAGPDLGGPLAWHGGLSAEERAAIRQRIRDGT-Q-RILFTSPE-SLTGSLRPALFDAAEAGLLRYLVV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 157 DEAHCVSQWGHDFRPDYLRLGALRSRL------GHAP-CVALTATATPQVQE------------DVFAALHLKKPVAIFK 217
Cdd:NF041063 277 DEAHLVDQWGDGFRPEFQLLAGLRRSLlrlapsGRPFrTLLLSATLTESTLDtletlfgppgpfIVVSAVQLRPEPAYWV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 218 TPCFRANlfydvqfkelisdpygNLKDFCLKALgQEADKGLsgcgIVYCRTREACEQLAIELSCRGVN-AKAYHAGLKAS 296
Cdd:NF041063 357 AKCDSEE----------------ERRERVLEAL-RHLPRPL----ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDA 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622881391 297 ERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 370
Cdd:NF041063 416 ERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
31-201 |
1.96e-30 |
|
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: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 31 TPLQENAtMAVVKGNKDVFVCMPTGAGKSLCYQLPAL------LAKGITIVVSPLIALIQDQVDHLLAL-KVRVSSLNSK 103
Cdd:pfam00270 1 TPIQAEA-IPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLgKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 104 LSAQERKDLLADLEReepqTKILYITPEMAASSSfqpSLNSLLSRhlLSYLVVDEAHCVSQWGhdFRPDYLR-LGALRSr 182
Cdd:pfam00270 80 LGGDSRKEQLEKLKG----PDILVGTPGRLLDLL---QERKLLKN--LKLLVLDEAHRLLDMG--FGPDLEEiLRRLPK- 147
|
170
....*....|....*....
gi 1622881391 183 lgHAPCVALTATATPQVQE 201
Cdd:pfam00270 148 --KRQILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
22-229 |
2.75e-27 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 110.27 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 22 KVFGFDSFkTPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA-----KGITIVVSPLIALIQDQVDHLLAL--- 93
Cdd:smart00487 2 EKFGFEPL-RPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLgps 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 94 -KVRVSSLNSKLSAQERKDLLadlerEEPQTKILYITPEMAasssFQPSLNSLLSRHLLSYLVVDEAHCVSQWGhdFRPD 172
Cdd:smart00487 81 lGLKVVGLYGGDSKREQLRKL-----ESGKTDILVTTPGRL----LDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622881391 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, ... |
9-357 |
4.79e-21 |
|
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: 99.14 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 9 PLDPerRVRSTLKKvFGFD---SFktplQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVVSPLI 80
Cdd:COG1205 40 WLPP--ELRAALKK-RGIErlySH----QAEAIEAARAG-KNVVIATPTASGKSLAYLLPVLEAlledPGATaLYLYPTK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 81 ALIQDQVDHLLAL------KVRVSSLNSKLSAQERKDLladleREEPQtkILYITPEMaasssfqpsLN-SLLSRHL--- 150
Cdd:COG1205 112 ALARDQLRRLRELaealglGVRVATYDGDTPPEERRWI-----REHPD--IVLTNPDM---------LHyGLLPHHTrwa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 151 -----LSYLVVDEAHC---V--SQWGHDFRpdylRLGALRSRLGHAP-CVALTAT-ATPQvqedVFAalhlkkpvaifkt 218
Cdd:COG1205 176 rffrnLRYVVIDEAHTyrgVfgSHVANVLR----RLRRICRHYGSDPqFILASATiGNPA----EHA------------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 219 pcfrANLFyDVQFkELISD---PYGNlKDFCL-----------KALGQEA--------DKGLSgcGIVYCRTREACEQLA 276
Cdd:COG1205 235 ----ERLT-GRPV-TVVDEdgsPRGE-RTFVLwnpplvddgirRSALAEAarlladlvREGLR--TLVFTRSRRGAELLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 277 IEL------SCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIhwniaksMAGY------- 343
Cdd:COG1205 306 RYArralrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVV-------LAGYpgtrasf 378
|
410
....*....|....
gi 1622881391 344 YQESGRAGRDGKPS 357
Cdd:COG1205 379 WQQAGRAGRRGQDS 392
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
273-354 |
2.09e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 83.42 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 273 EQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAKSMAGYYQESGRAGR 352
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1622881391 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 |
1.27e-17 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 80.53 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 45 NKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIQDQ---VDHLLALKVRVSSLNSKLSAQERKdlladlE 117
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEERE------K 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622881391 118 REEPQTKILYITPEMaasssFQPSLNSLLSRHL--LSYLVVDEAHCVSQWGHDFRPDYLRLgaLRSRLGHAPCVALTAT 194
Cdd:cd00046 75 NKLGDADIIIATPDM-----LLNLLLREDRLFLkdLKLIIVDEAHALLIDSRGALILDLAV--RKAGLKNAQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
247-354 |
1.56e-17 |
|
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: 79.18 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 247 LKALGQEADKGLSGCGIVYCRTREACEqLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:pfam00271 3 LEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLP 81
|
90 100
....*....|....*....|....*...
gi 1622881391 327 NVRFVIHWNIAKSMAGYYQESGRAGRDG 354
Cdd:pfam00271 82 DVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
12-399 |
8.49e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 78.40 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 12 PERRVRSTLKKvFGFDSFkTPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGITIV-VSPLIALIQDQVD 88
Cdd:COG1204 7 PLEKVIEFLKE-RGIEEL-YPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILkaLLNGGKALyIVPLRALASEKYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 89 HL------LALKVRVSSlnsklSAQERKDllADLEREEpqtkILYITPEMAAS-SSFQPslnSLLSRhlLSYLVVDEAHC 161
Cdd:COG1204 85 EFkrdfeeLGIKVGVST-----GDYDSDD--EWLGRYD----ILVATPEKLDSlLRNGP---SWLRD--VDLVVVDEAHL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 162 VsqwGHDFR-PDY------LRLGALRSRLghapcVALTATAT-PQVQEDVFAALHLK---KPVAIfktpcfRANLFYD-- 228
Cdd:COG1204 149 I---DDESRgPTLevllarLRRLNPEAQI-----VALSATIGnAEEIAEWLDAELVKsdwRPVPL------NEGVLYDgv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 229 VQFKELISDPYGNLKDFCLKALGQEadkglsGCGIVYCRTREACEQLAIELS---------------------------- 280
Cdd:COG1204 215 LRFDDGSRRSKDPTLALALDLLEEG------GQVLVFVSSRRDAESLAKKLAdelkrrltpeereeleelaeellevsee 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 281 ---------C--RGVnakAYH-AGLKASERTLVQnDWMEE-KVPVIVATISFGMGVdkaN--VRFVI----HWNIAKSMA 341
Cdd:COG1204 289 thtnekladCleKGV---AFHhAGLPSELRRLVE-DAFREgLIKVLVATPTLAAGV---NlpARRVIirdtKRGGMVPIP 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622881391 342 G--YYQESGRAGRDGK-P---SWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATILAF 399
Cdd:COG1204 362 VleFKQMAGRAGRPGYdPygeAILVAKSSDEADELFERYILGEPEPIRSKLANESALRTHLLAL 425
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
263-357 |
1.38e-13 |
|
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: 68.82 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 263 IVYCRTREACEQLAIELSCRGVNAK-------AYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWN 335
Cdd:cd18797 39 IVFCRSRKLAELLLRYLKARLVEEGplaskvaSYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|..
gi 1622881391 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 |
1.47e-13 |
|
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: 69.92 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 46 KDVFVCMPTGAGKSLCYQLPALLA----KGIT-IVVSPLIALIQDQVDHLLAL------KVRVSSLNSKLSAQERKDLLa 114
Cdd:cd17923 16 RSVVVTTGTASGKSLCYQLPILEAllrdPGSRaLYLYPTKALAQDQLRSLRELleqlglGIRVATYDGDTPREERRAII- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622881391 115 dleREEPQtkILYITPEMaasssfqpsLNSLLSRH---------LLSYLVVDEAH 160
Cdd:cd17923 95 ---RNPPR--ILLTNPDM---------LHYALLPHhdrwarflrNLRYVVLDEAH 135
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
45-160 |
1.99e-13 |
|
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: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 45 NKDVFVCMPTGAGKSLCYQLPALL------AKGITIV-VSPLIALIQDQVDHL------LALKVRVSSLNSKLSAQERKD 111
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSsladepEKGVQVLyISPLKALINDQERRLeepldeIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622881391 112 LLADLereePQtkILYITPEmaasssfqpSLNSLLS----RHLLS---YLVVDEAH 160
Cdd:cd17922 81 QLKNP----PG--ILITTPE---------SLELLLVnkklRELFAglrYVVVDEIH 121
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
247-355 |
1.05e-11 |
|
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: 63.30 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 247 LKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKA 326
Cdd:cd18787 15 LLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIP 94
|
90 100
....*....|....*....|....*....
gi 1622881391 327 NVRFVIHWNIAKSMAGYYQESGRAGRDGK 355
Cdd:cd18787 95 GVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
35-352 |
1.11e-09 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 62.35 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 35 ENATMAVVKGNKDVFVCMPTGAGKSL----CYQlpALLAKGITIVVSPLIALIQDQVDHLLALkvrvssLNSKLSAQERK 110
Cdd:COG1061 90 EALLAALERGGGRGLVVAPTGTGKTVlalaLAA--ELLRGKRVLVLVPRRELLEQWAEELRRF------LGDPLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 111 DLLADlereepqtkILYITPEMAASssfQPSLNSLLSRhlLSYLVVDEAHcvsqwghdfrpdylRLGA-----LRSRLGH 185
Cdd:COG1061 162 DSDAP---------ITVATYQSLAR---RAHLDELGDR--FGLVIIDEAH--------------HAGApsyrrILEAFPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 186 APCVALtaTATPqVQEDvfaalhlKKPVAIFktpcFRANLFYDVQFKELISD--------------------PYGNLKDF 245
Cdd:COG1061 214 AYRLGL--TATP-FRSD-------GREILLF----LFDGIVYEYSLKEAIEDgylappeyygirvdltderaEYDALSER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 246 CLKALGQEAD------------KGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVI 313
Cdd:COG1061 280 LREALAADAErkdkilrellreHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRIL 359
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622881391 314 VATISFGMGVDKANVRFVIHWNIAKSMAGYYQesgRAGR 352
Cdd:COG1061 360 VTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ---RLGR 395
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
263-354 |
2.72e-09 |
|
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: 56.79 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 263 IVYCRTREACEQLAIELSCrgvnAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVD--------KANVRFVIHW 334
Cdd:cd18795 47 LVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviiKGTQRYDGKG 122
|
90 100
....*....|....*....|
gi 1622881391 335 NIAKSMAGYYQESGRAGRDG 354
Cdd:cd18795 123 YRELSPLEYLQMIGRAGRPG 142
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
8-355 |
5.59e-09 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 59.39 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 8 FPLDPErrVRSTLKKVfGFDSFkTPLQEnATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGI-----TIVVSP-- 78
Cdd:COG0513 7 LGLSPP--LLKALAEL-GYTTP-TPIQA-QAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 79 -LIALIQDQVDHLLA-LKVRVSSL--NSKLSAQERKdlladLEReepQTKILYITP----EMAASSSFqpSLNSLlsrhl 150
Cdd:COG0513 82 eLALQVAEELRKLAKyLGLRVATVygGVSIGRQIRA-----LKR---GVDIVVATPgrllDLIERGAL--DLSGV----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 151 lSYLVVDEAhcvsqwghD------FRPDylrlgaLRSRLGHAPCVALT----ATATPQVQEdvFAALHLKKPVAIFKTPC 220
Cdd:COG0513 147 -ETLVLDEA--------DrmldmgFIED------IERILKLLPKERQTllfsATMPPEIRK--LAKRYLKNPVRIEVAPE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 221 FRAN-----LFYDVQFKElisdpygnlKDFCLKALGQEADKGLsgcGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKA 295
Cdd:COG0513 210 NATAetieqRYYLVDKRD---------KLELLRRLLRDEDPER---AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQ 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622881391 296 SERTLVQNDWMEEKVPVIVATisfgmGVDKANVRFVIHWNIAKSMagyyqES--------GRAGRDGK 355
Cdd:COG0513 278 GQRERALDAFRNGKIRVLVATdvaarGIDIDDVSHVINYDLPEDP-----EDyvhrigrtGRAGAEGT 340
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
240-354 |
8.70e-09 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 59.40 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 240 GNLKDFcLKALGQEADKGLsgcgiVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISF 319
Cdd:PTZ00110 364 GKLKML-LQRIMRDGDKIL-----IFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
|
90 100 110
....*....|....*....|....*....|....*
gi 1622881391 320 GMGVDKANVRFVIHWNIAKSMAGYYQESGRAGRDG 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 |
1.28e-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: 52.29 E-value: 1.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622881391 365 RNDRDQVSFLIRKEVAKLQEKRGNKASdkatilaFDALVTFCEELG-CRHAAIAKYFGDA--PPACaKGCDHC 434
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEERKEVELQK-------LQAMVAYCENTTdCRRKQLLRYFGEEfdSEPC-GNCDNC 65
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
31-195 |
2.70e-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: 54.58 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 31 TPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLA----KGITIVVSPLIALIqDQVdhllalkvrVSSLNSKLSA 106
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRAlatsGGKAVYIAPTRALV-NQK---------EADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 107 QERKDLLADLE-----REEPQTKILYITPEMaasssfqpsLNSLLSRH------LLSYLVVDEAHCVSQwghdfrPDY-- 173
Cdd:cd17921 73 LGKNVGLLTGDpsvnkLLLAEADILVATPEK---------LDLLLRNGgerliqDVRLVVVDEAHLIGD------GERgv 137
|
170 180
....*....|....*....|....*
gi 1622881391 174 ---LRLGALRSRLGHAPCVALTATA 195
Cdd:cd17921 138 vleLLLSRLLRINKNARFVGLSATL 162
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
261-355 |
1.92e-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: 49.24 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 261 CGIVYCRTREACEQLAIELScrgvnakayhaglkasertlvqndwmeekvpVIVATISFGMGVDKANVRFVIHWNIAKSM 340
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90
....*....|....*
gi 1622881391 341 AGYYQESGRAGRDGK 355
Cdd:cd18785 54 ASYIQRVGRAGRGGK 68
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
252-352 |
2.78e-07 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 54.51 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 252 QEADKGLSGCGIVYCRTREACEQLAIELscrGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVD--KANVR 329
Cdd:COG1202 420 TKSSKGYRGQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDfpASQVI 496
|
90 100
....*....|....*....|....*...
gi 1622881391 330 FV-----IHWniaKSMAGYYQESGRAGR 352
Cdd:COG1202 497 FDslamgIEW---LSVQEFHQMLGRAGR 521
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
263-355 |
3.43e-06 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 50.60 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 263 IVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAKSMAG 342
Cdd:PTZ00424 271 IIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPEN 350
|
90
....*....|...
gi 1622881391 343 YYQESGRAGRDGK 355
Cdd:PTZ00424 351 YIHRIGRSGRFGR 363
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
31-167 |
5.17e-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: 48.77 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 31 TPLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLP---ALLA----KGITIVVSPLIALI-------QDQV-DHLLALK- 94
Cdd:cd17946 14 TPIQALALPAAIRDGKDVIGAAETGSGKTLAFGIPileRLLSqkssNGVGGKQKPLRALIltptrelAVQVkDHLKAIAk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 95 ---VRVSSLNSKLSAQERKDLLadleREEPQtkILYITP----EMAASSsfqpslNSLLSR-HLLSYLVVDEAHCVSQWG 166
Cdd:cd17946 94 ytnIKIASIVGGLAVQKQERLL----KKRPE--IVVATPgrlwELIQEG------NEHLANlKSLRFLVLDEADRMLEKG 161
|
.
gi 1622881391 167 H 167
Cdd:cd17946 162 H 162
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
10-211 |
7.71e-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: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 10 LDPerRVRSTLKKVfGFDSfKTPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPA----LLAKGITIVVSPLIALI-- 83
Cdd:cd17961 1 LDP--RLLKAIAKL-GWEK-PTLIQSKAIPLALEG-KDILARARTGSGKTAAYALPIiqkiLKAKAESGEEQGTRALIlv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 84 -----QDQV-DHLLAL------KVRVSSLNSKLSAQERKDLLADLereePQtkILYITPEMAASssfQPSLNSLLSRHLL 151
Cdd:cd17961 76 ptrelAQQVsKVLEQLtaycrkDVRVVNLSASSSDSVQRALLAEK----PD--IVVSTPARLLS---HLESGSLLLLSTL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622881391 152 SYLVVDEAHCVSQWGHDfrpdylrlGALRSRLGHAP----CVALTATATPQVQEdvfaalhLKK 211
Cdd:cd17961 147 KYLVIDEADLVLSYGYE--------EDLKSLLSYLPknyqTFLMSATLSEDVEA-------LKK 195
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
47-159 |
5.60e-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: 45.70 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 47 DVFVCMPTGAGKSLCYQLP---ALLAKGIT----IVVSPLIALIQdQVDHLL-----ALKVRVSSLNSKLS-AQERKDLL 113
Cdd:cd17956 38 DLCVSAPTGSGKTLAYVLPivqALSKRVVPrlraLIVVPTKELVQ-QVYKVFeslckGTGLKVVSLSGQKSfKKEQKLLL 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622881391 114 ADLERE-EPQTKILYITP-----EMAASSSFqpSLNSllsrhlLSYLVVDEA 159
Cdd:cd17956 117 VDTSGRyLSRVDILVATPgrlvdHLNSTPGF--TLKH------LRFLVIDEA 160
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
22-159 |
6.73e-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: 44.87 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 22 KVFGFDSFkTPLQEnATMAVVKGNKDVFVCMPTGAGKSLCYQLPAL--LAKGIT---------IVVSP---LIALIQDQV 87
Cdd:cd17960 6 AELGFTSM-TPVQA-ATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLeiLLKRKAnlkkgqvgaLIISPtreLATQIYEVL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622881391 88 DHLLA---LKVRVSSLNSKLSAQERkdlLADLEREEPQtkILYITP----EMAASSSFQPSLNSllsrhlLSYLVVDEA 159
Cdd:cd17960 84 QSFLEhhlPKLKCQLLIGGTNVEED---VKKFKRNGPN--ILVGTPgrleELLSRKADKVKVKS------LEVLVLDEA 151
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
32-194 |
6.77e-05 |
|
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: 43.83 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 32 PLQENATMAVVKGNKDVF--VCMPTGAGKSLC-YQLPALLAKGITIVVSPLIALIQDQVDHLLALKVRVSSlnSKLSAQE 108
Cdd:cd17926 3 PYQEEALEAWLAHKNNRRgiLVLPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSI--GLIGGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 109 RKDLladlereePQTKILYITPEMAASSSFQPSLNSllsrHLLSYLVVDEAH--CVSQWGHdfrpdylrlgaLRSRLGHA 186
Cdd:cd17926 81 KKDF--------DDANVVVATYQSLSNLAEEEKDLF----DQFGLLIVDEAHhlPAKTFSE-----------ILKELNAK 137
|
....*...
gi 1622881391 187 PCVALTAT 194
Cdd:cd17926 138 YRLGLTAT 145
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
40-160 |
2.17e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 42.66 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 40 AVVKGNKDVFVCMPTGAGKSLCY-QLPALLAK----GITIVVSPLIALIQDQVDHLLALKVRVSSLNSKLSAQERKdlla 114
Cdd:pfam04851 18 SIKNGQKRGLIVMATGSGKTLTAaKLIARLFKkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKD---- 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622881391 115 dleREEPQTKILYITPEMAASSSFQPSLnsLLSRHLLSYLVVDEAH 160
Cdd:pfam04851 94 ---ESVDDNKIVVTTIQSLYKALELASL--ELLPDFFDVIIIDEAH 134
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
26-160 |
4.19e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.49 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 26 FDSFkTPLQENATMAVVKGnKDVFVCMPTGAGKSLCYQLPAL-----------LAKGITIV-VSPLIALIQDQVDHLLA- 92
Cdd:PRK13767 30 FGTF-TPPQRYAIPLIHEG-KNVLISSPTGSGKTLAAFLAIIdelfrlgregeLEDKVYCLyVSPLRALNNDIHRNLEEp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 93 LK---------------VRVSSLNSKLSAQERKDLLadleREEPQtkILYITPEmaassSFQPSLNSLLSRHLLS---YL 154
Cdd:PRK13767 108 LTeireiakergeelpeIRVAIRTGDTSSYEKQKML----KKPPH--ILITTPE-----SLAILLNSPKFREKLRtvkWV 176
|
....*.
gi 1622881391 155 VVDEAH 160
Cdd:PRK13767 177 IVDEIH 182
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
262-356 |
4.75e-04 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 44.01 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 262 GIVYCRTREACEQLAIELS-CRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAKSM 340
Cdd:PLN00206 370 AVVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTI 449
|
90
....*....|....*.
gi 1622881391 341 AGYYQESGRAGRDGKP 356
Cdd:PLN00206 450 KEYIHQIGRASRMGEK 465
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
633-916 |
5.13e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 633 PPEPNEYDIPPASHVYSLKPKRVGagfPKGSRPFQTATElmettRIREQAPQPKRG-----------GEHEPPSRPCGLL 701
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPA---PRPSEPAVTSRA-----RRPDAPPQSARPrapvddrgdprGPAPPSPLPPDTH 2622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 702 DEDRSEPLPGPRGEVPGGSAHCGGPSPEKKAKSSSGGSSLAKGRASKKQQllAAAAHKDSQSIARFFCRREESPALLASA 781
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR--AAQASSPPQRPRRRAARPTVGSLTSLAD 2700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 782 PEAEGACPscEGVQGPLMAPEKYTGEEDGAGGRSPAPPQTEEclrERPSTCLPRDQGTPEVQPTPAkdTWKGKRPPSQQE 861
Cdd:PHA03247 2701 PPPPPPTP--EPAPHALVSATPLPPGPAAARQASPALPAAPA---PPAVPAGPATPGGPARPARPP--TTAGPPAPAPPA 2773
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622881391 862 NPESQPQKRLRPSAKPSVLAEVKGSVLASD----------QGTLNPTAQDPCQLSAPGISLKEAA 916
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRESLPSPWDpadppaavlaPAAALPPAASPAGPLPPPTSAQPTA 2838
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
41-194 |
1.59e-03 |
|
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: 40.81 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 41 VVKGNKDVFVCMPTGAGKSLC--YQLPALLA---KGITIVVSPLIALIQDQVDHLLAlkvRVSSlNSKLSAQErkdLLAD 115
Cdd:cd18025 12 IVDRRESALIVAPTSSGKTFIsyYCMEKVLResdDGVVVYVAPTKALVNQVVAEVYA---RFSK-KYPPSGKS---LWGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 116 LERE----EPQT-KILYITPEMAASSSFQPSLNSLLSRhlLSYLVVDEAHCVSQWGHDFRPDYLRLgalrsrLGHAPCVA 190
Cdd:cd18025 85 FTRDyrhnNPMNcQVLITVPECLEILLLSPHNASWVPR--IKYVIFDEIHSIGQSEDGAVWEQLLL------LIPCPFLA 156
|
....
gi 1622881391 191 LTAT 194
Cdd:cd18025 157 LSAT 160
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
259-356 |
2.50e-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: 39.55 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 259 SGCGIVYCRTREACEQLAIELscrgvNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIHWNIAK 338
Cdd:cd18796 49 SQAERLAQRLRELCPDRVPPD-----FIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPK 123
|
90
....*....|....*...
gi 1622881391 339 SMAGYYQESGRAGRDGKP 356
Cdd:cd18796 124 SVARLLQRLGRSGHRPGA 141
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
34-160 |
3.75e-03 |
|
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: 39.72 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 34 QENATMAVVKGnKDVFVCMPTGAGKS-----LC----YQLPAlLAKGITIVVSPLIALIQDQVD----HLLALKVRVSSL 100
Cdd:cd17927 7 QLELAQPALKG-KNTIICLPTGSGKTfvavlICehhlKKFPA-GRKGKVVFLANKVPLVEQQKEvfrkHFERPGYKVTGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622881391 101 NSKLSAQERKDLLADlereepQTKILYITPemaasssfQPSLNSLL-----SRHLLSYLVVDEAH 160
Cdd:cd17927 85 SGDTSENVSVEQIVE------SSDVIIVTP--------QILVNDLKsgtivSLSDFSLLVFDECH 135
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
25-131 |
4.18e-03 |
|
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: 39.66 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 25 GFDSFKT--PLQENATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKG-------------ITIV-VSPLIALIQDQVD 88
Cdd:cd18019 11 AFEGFKSlnRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGkhrnpdgtinldaFKIVyIAPMKALVQEMVG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622881391 89 HLLAlkvRVSSLNSKLSaqerkDLLAD--LEREE-PQTKILYITPE 131
Cdd:cd18019 91 NFSK---RLAPYGITVA-----ELTGDqqLTKEQiSETQIIVTTPE 128
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
34-197 |
4.64e-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: 39.11 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 34 QENATMAVVK---GNKDVFVCMPTGAGKSLCY--QLPALLAKGIT-IVVSPLIALIQdqvdHLLA-LKVR----VSSLNS 102
Cdd:cd17929 1 QRKAYEAIVSslgGFKTFLLHGVTGSGKTEVYieLIEKVLAKGKQvLVLVPEISLTP----QLIKrFKKRfgdkVAVLHS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 103 KLSAQERKDLLADLEREEPQTKIlyitpeMAASSSFQPSLNsllsrhlLSYLVVDEAHcVSQWGHDFRPDY-LRLGAL-R 180
Cdd:cd17929 77 KLSDKERADEWRKIKRGEAKVVI------GARSALFAPFKN-------LGLIIVDEEH-DSSYKQDSGPRYhARDVAIyR 142
|
170
....*....|....*..
gi 1622881391 181 SRLGHAPCValTATATP 197
Cdd:cd17929 143 AKLENAPVV--LGSATP 157
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
779-881 |
4.75e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 40.81 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 779 ASAPEAEGACPSCEGVQGPLMAPEKYTGEED----GAGGRSPAPPQTEECLRER--PSTCLPRDQGTPEVQPtpAKDTWK 852
Cdd:PHA03377 584 STGPRDMAPPSTGPRQQAKCKDGPPASGPHEkqppSSAPRDMAPSVVRMFLRERllEQSTGPKPKSFWEMRA--GRDGSG 661
|
90 100
....*....|....*....|....*....
gi 1622881391 853 GKRPPSQQENPESQPQKRlRPSAKPSVLA 881
Cdd:PHA03377 662 IQQEPSSRRQPATQSTPP-RPSWLPSVFV 689
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
267-354 |
6.48e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 40.33 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 267 RTREACEQLAielSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVIH-WNIAKSMAG--- 342
Cdd:PRK02362 290 SDTETSKDLA---DCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRdYRRYDGGAGmqp 366
|
90
....*....|....*..
gi 1622881391 343 -----YYQESGRAGRDG 354
Cdd:PRK02362 367 ipvleYHQMAGRAGRPG 383
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
628-897 |
8.01e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 628 SAQAVPPEPNEYDIPPA-SHVYSLKPKRVGAGFPKGSRPFQTATELMETTRIREQAPQPKRGGEHEPPSRPCGLLDEDRS 706
Cdd:PHA03247 2746 AGPATPGGPARPARPPTtAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 707 EPLPGPRGEVPGGSAHCGGPSPEKKAKSSSGGSSLAKGRASKKQQLLAAAAhkdsqSIARFFCRREESPALlasapeaeg 786
Cdd:PHA03247 2826 GPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPA-----APARPPVRRLARPAV--------- 2891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622881391 787 aCPSCEGVQGPLMAPEKYtgeedgaggRSPAPPQTeeclrerpstclPRDQGTPEVQPTPAkdtwkgkrPPSQqenPESQ 866
Cdd:PHA03247 2892 -SRSTESFALPPDQPERP---------PQPQAPPP------------PQPQPQPPPPPQPQ--------PPPP---PPPR 2938
|
250 260 270
....*....|....*....|....*....|.
gi 1622881391 867 PQKRLRPSAKPSVLAEVKGSVLASDQGTLNP 897
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVP 2969
|
|
| |
