|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-407 |
2.73e-172 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 499.28 E-value: 2.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 1 MTETPLEILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKR 80
Cdd:COG0514 1 LRDDALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 81 GIRALSLAGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWGKDFRPAYLECVWL 160
Cdd:COG0514 81 GIRAAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 161 KEEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSLKRSNIAYMVYKT--EDKWRYLEQILHKNTGSS-IVYVRSR 237
Cdd:COG0514 161 RERLPNVPVLALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVPKppDDKLAQLLDFLKEHPGGSgIVYCLSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 238 KSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGR 317
Cdd:COG0514 241 KKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 318 AGRDGKKAFAVMLYN--DYQYQstqkKFLLHQTDVP--FLKLLYAKLNAYFQIAYGEG---EEIVHHFQFS--------D 382
Cdd:COG0514 321 AGRDGLPAEALLLYGpeDVAIQ----RFFIEQSPPDeeRKRVERAKLDAMLAYAETTGcrrQFLLRYFGEElaepcgncD 396
|
410 420
....*....|....*....|....*
gi 1390593022 383 FCmrykLNPQQVANGLAllEAQSVL 407
Cdd:COG0514 397 NC----LGPPETFDGTE--AAQKAL 415
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
8-386 |
1.33e-104 |
|
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: 325.19 E-value: 1.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 8 ILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRALSL 87
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 88 AGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIvrDFIKSMP----VNLIVIDEAHCISHWGKDFRPAYLECVWLKEE 163
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKISASN--RLLQTLEerkgITLIAVDEAHCISQWGHDFRPDYKALGSLKQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 164 FPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSLKRSNIAYMVykTEDKWRYLEQIL-----HKNTGSSIVYVRSRK 238
Cdd:TIGR00614 160 FPNVPVMALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEV--RRKTPKILEDLLrfirkEFEGKSGIIYCPSRK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 239 STVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRA 318
Cdd:TIGR00614 238 KVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390593022 319 GRDGKKAFAVMLYNdyqyqstqkkfllhQTDVPFLK-LLYAKLNAYFQIAYGEGEEIVHHFQFSDFCMR 386
Cdd:TIGR00614 318 GRDGLPSECHLFYA--------------PADMNRLRrLLMEEPDGNFRTYKLKLYEMMEYCLNSSTCRR 372
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
4-332 |
1.29e-101 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 321.66 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 4 TPLEILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIR 83
Cdd:PRK11057 12 LAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 84 ALSLAGALSYTDLERILNNAVLGNYKFLYLSPERLqqeIVRDFIKSM---PVNLIVIDEAHCISHWGKDFRPAYLECVWL 160
Cdd:PRK11057 92 AACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERL---MMDNFLEHLahwNPALLAVDEAHCISQWGHDFRPEYAALGQL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 161 KEEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSLKRSNIAYMV---YKTEDK-WRYLEQILHKntgSSIVYVRS 236
Cdd:PRK11057 169 RQRFPTLPFMALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTLvekFKPLDQlMRYVQEQRGK---SGIIYCNS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 237 RKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAG 316
Cdd:PRK11057 246 RAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETG 325
|
330
....*....|....*.
gi 1390593022 317 RAGRDGKKAFAVMLYN 332
Cdd:PRK11057 326 RAGRDGLPAEAMLFYD 341
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-199 |
1.72e-92 |
|
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: 284.04 E-value: 1.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRAL 85
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 86 SLAGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMP----VNLIVIDEAHCISHWGKDFRPAYLECVWLK 161
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRLPerkrLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390593022 162 EEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSS 199
Cdd:cd17920 161 RALPGVPILALTATATPEVREDILKRLGLRNPVIFRAS 198
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
10-334 |
9.97e-77 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 265.99 E-value: 9.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 10 KKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRALSLAG 89
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 90 ALSYTDLERILN--NAVLGNYKFLYLSPERL-QQEIVRDFIKSMP----VNLIVIDEAHCISHWGKDFRPAYLECVWLKE 162
Cdd:PLN03137 533 GMEWAEQLEILQelSSEYSKYKLLYVTPEKVaKSDSLLRHLENLNsrglLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 163 EFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSLKRSNIAYMVY-KTEDKWRYLEQILHKN--TGSSIVYVRSRKS 239
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVVpKTKKCLEDIDKFIKENhfDECGIIYCLSRMD 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 240 TVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAG 319
Cdd:PLN03137 693 CEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAG 772
|
330
....*....|....*..
gi 1390593022 320 RDGKKAFAVMLYN--DY 334
Cdd:PLN03137 773 RDGQRSSCVLYYSysDY 789
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-200 |
6.80e-60 |
|
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: 198.63 E-value: 6.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKS----GICIVVSPLIALINDQVEGLkKRG 81
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRrrgpGLTLVVSPLIALMKDQVDAL-PRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 82 IRALSLAGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSM-PVNLIVIDEAHCISHWGKDFRPAYLE-CVW 159
Cdd:cd18018 80 IKAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTpPISLLVVDEAHCISEWSHNFRPDYLRlCRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390593022 160 LKEEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSL 200
Cdd:cd18018 160 LRELLGAPPVLALTATATKRVVEDIASHLGIPESGVVRGPL 200
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
7-200 |
8.33e-53 |
|
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: 180.25 E-value: 8.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 7 EILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRALS 86
Cdd:cd18015 8 DTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISATM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 87 LAGALSYTDLERILNNAVLGN--YKFLYLSPERLQQEivRDFIKSMP-------VNLIVIDEAHCISHWGKDFRPAYLEC 157
Cdd:cd18015 88 LNASSSKEHVKWVHAALTDKNseLKLLYVTPEKIAKS--KRFMSKLEkaynagrLARIAIDEVHCCSQWGHDFRPDYKKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1390593022 158 VWLKEEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSL 200
Cdd:cd18015 166 GILKRQFPNVPILGLTATATSKVLKDVQKILCIQKCLTFTASF 208
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
6-200 |
1.25e-50 |
|
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: 173.81 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYWGYDAFRSPQADIVQAVLE-GKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRA 84
Cdd:cd18017 1 LNALNEYFGHSSFRPVQWKVIRSVLEeRRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 85 LSLAGALSYTDLERILNnavlGNYKFLYLSPERLQQ--EIVRDFikSMPVNLIVIDEAHCISHWGKDFRPAYLECVWLKE 162
Cdd:cd18017 81 CFLGSAQSQNVLDDIKM----GKIRVIYVTPEFVSKglELLQQL--RNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRN 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390593022 163 EFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSSL 200
Cdd:cd18017 155 RLPNVPIVALTATATPSVRDDIIKNLNLRNPQITCTSF 192
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
6-184 |
4.73e-49 |
|
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: 169.96 E-value: 4.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYWGYDAFRSP-QADIVQAVLEGK-NVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIR 83
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 84 ALSLAGALSYTDLERILNN--AVLGNYKFLYLSPERLQ----QEIVRDFIKSMPVNLIVIDEAHCISHWGKDFRPAYLEC 157
Cdd:cd18014 81 VDSLNSKLSAQERKRIIADleSEKPQTKFLYITPEMAAtssfQPLLSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180
....*....|....*....|....*..
gi 1390593022 158 VWLKEEFPKIPILALTASATQRVQNDI 184
Cdd:cd18014 161 GALRSRYGHVPWVALTATATPQVQEDI 187
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
202-331 |
9.38e-48 |
|
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: 163.92 E-value: 9.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 202 RSNIAYMVY---KTEDKWRYLEQILHKN-TGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGD 277
Cdd:cd18794 1 RPNLFYSVRpkdKKDEKLDLLKRIKVEHlGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1390593022 278 VQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVMLY 331
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
1-199 |
1.57e-47 |
|
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: 166.16 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 1 MTETPLEILKKYWGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKSGICIVVSPLIALINDQVEGLKKR 80
Cdd:cd18016 1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 81 GIRALSLAGALSYTDLERILNNAVLGN--YKFLYLSPERLQ-----QEIVRDFIKSMPVNLIVIDEAHCISHWGKDFRPA 153
Cdd:cd18016 81 DIPATYLTGDKTDAEATKIYLQLSKKDpiIKLLYVTPEKISasnrlISTLENLYERKLLARFVIDEAHCVSQWGHDFRPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390593022 154 YLECVWLKEEFPKIPILALTASATQRVQNDIVQLMQMNDAQVIKSS 199
Cdd:cd18016 161 YKRLNMLRQKFPSVPMMALTATATPRVQKDILNQLKMLRPQVFTMS 206
|
|
| DpdF |
NF041063 |
protein DpdF; |
8-331 |
2.69e-45 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 172.40 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 8 ILKKYWGYDAFRSP-QADIVQAVL---EGKNVLALMPTGGGKSIAFQVPALLKS---GICIVVSPLIALINDQ----VEG 76
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVRAALlapPGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerraREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 77 LKKRGIRalsLAGALSYT-DL---------ERILNnavlGNYKFLYLSPERLQ---QEIVRDFIKSMPVNLIVIDEAHCI 143
Cdd:NF041063 210 LRRAGPD---LGGPLAWHgGLsaeeraairQRIRD----GTQRILFTSPESLTgslRPALFDAAEAGLLRYLVVDEAHLV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 144 SHWGKDFRPAY-----LECVWLKEEFPKIPI--LALTASATQRVQNDIVQLM-QMNDAQVIKSSLKRSNIAYMVYKTEDK 215
Cdd:NF041063 283 DQWGDGFRPEFqllagLRRSLLRLAPSGRPFrtLLLSATLTESTLDTLETLFgPPGPFIVVSAVQLRPEPAYWVAKCDSE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 216 WRYLEQILHKNTGS---SIVYVRSRKSTVEMAEYLNTKGLT--ATyFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMG 290
Cdd:NF041063 363 EERRERVLEALRHLprpLILYVTKVEDAEAWLQRLRAAGFRrvAL-FHGDTPDAERERLIEQWRENELDIVVATSAFGLG 441
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1390593022 291 IDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVMLY 331
Cdd:NF041063 442 MDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIY 482
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-323 |
1.61e-28 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 120.00 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 1 MTETPLEILKKYW---GYDAFRSPQADIVQA-VLEGKNVLALMPTGGGKS-IA--FQVPALLKSGICIVVSPLIALINDQ 73
Cdd:COG1204 3 VAELPLEKVIEFLkerGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTlIAelAILKALLNGGKALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 74 VEGLKKR----GIRAlslagALSYTDLERilNNAVLGNYKFLYLSPERLQQEIVR--DFIKSmpVNLIVIDEAHCIshwG 147
Cdd:COG1204 83 YREFKRDfeelGIKV-----GVSTGDYDS--DDEWLGRYDILVATPEKLDSLLRNgpSWLRD--VDLVVVDEAHLI---D 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 148 KDFRPAYLECVW--LKEEFPKIPILALtaSATqrVQN--DIVQLMqmnDAQVIKSS----------LKRSNIAY--MVYK 211
Cdd:COG1204 151 DESRGPTLEVLLarLRRLNPEAQIVAL--SAT--IGNaeEIAEWL---DAELVKSDwrpvplnegvLYDGVLRFddGSRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 212 TEDKWRYL-EQILHKNtGSSIVYVRSRKSTVEMAEYL------------------------NTKGLTATYF--------- 257
Cdd:COG1204 224 SKDPTLALaLDLLEEG-GQVLVFVSSRRDAESLAKKLadelkrrltpeereeleelaeellEVSEETHTNEkladclekg 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390593022 258 ----HGGLTTEQKSLkMQMWML-GDVQVMVATNAFGMGIDRPdVRTVIHWDI------PPTLEDYFQEAGRAGRDGK 323
Cdd:COG1204 303 vafhHAGLPSELRRL-VEDAFReGLIKVLVATPTLAAGVNLP-ARRVIIRDTkrggmvPIPVLEFKQMAGRAGRPGY 377
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
19-182 |
1.88e-28 |
|
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: 111.57 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 19 RSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL------LKSGICIVVSPLIALINDQVEGLKKRGIrALSLAGALS 92
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKLGK-GLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 93 YTDLERILNNAVLGNYKFLYLSPERLQQEIV-RDFIKSmpVNLIVIDEAHCISHWGkdFRPAYLECVWLKEefPKIPILA 171
Cdd:pfam00270 80 LGGDSRKEQLEKLKGPDILVGTPGRLLDLLQeRKLLKN--LKLLVLDEAHRLLDMG--FGPDLEEILRRLP--KKRQILL 153
|
170
....*....|.
gi 1390593022 172 LTASATQRVQN 182
Cdd:pfam00270 154 LSATLPRNLED 164
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
6-333 |
2.06e-25 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 109.08 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKyWGYDAFrSP-QADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL--LKSGI-----CIVVSP---LIALINDQV 74
Cdd:COG0513 14 LKALAE-LGYTTP-TPiQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLALQVAEEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 75 EGL-KKRGIRALSLAGALSYTD-LERILNNA--VLGnykflylSPERLqqeivRDFIKSMPVNL-----IVIDEAhcish 145
Cdd:COG0513 92 RKLaKYLGLRVATVYGGVSIGRqIRALKRGVdiVVA-------TPGRL-----LDLIERGALDLsgvetLVLDEA----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 146 wgkD------FRPAylecvwLKEefpkipILALTA--------SATqrVQNDIVQLMQ--MNDAQVIK---SSLKRSNIA 206
Cdd:COG0513 155 ---DrmldmgFIED------IER------ILKLLPkerqtllfSAT--MPPEIRKLAKryLKNPVRIEvapENATAETIE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 207 YMVYKT--EDKWRYLEQIL-HKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQ-----KSLKMqmwmlGDV 278
Cdd:COG0513 218 QRYYLVdkRDKLELLRRLLrDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQreralDAFRN-----GKI 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1390593022 279 QVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVMLYND 333
Cdd:COG0513 293 RVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTP 347
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
14-189 |
9.57e-24 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 99.49 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 14 GYDAFRSPQADIVQAVLEG-KNVLALMPTGGGKSIAFQVPALL-----KSGICIVVSPLIALINDQVEGLKKRGIR-ALS 86
Cdd:smart00487 5 GFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSlGLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 87 LAGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWGkdFRPAYLECvwLKEEFPK 166
Cdd:smart00487 85 VVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--LKLLPKN 160
|
170 180
....*....|....*....|...
gi 1390593022 167 IPILALTASATQRVQNDIVQLMQ 189
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLN 183
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
214-322 |
9.92e-23 |
|
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: 93.43 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 214 DKWRYLEQILHKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDR 293
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 1390593022 294 PDVRTVIHWDIPPTLEDYFQEAGRAGRDG 322
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
242-322 |
2.70e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.12 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 242 EMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRD 321
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81
|
.
gi 1390593022 322 G 322
Cdd:smart00490 82 G 82
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
6-330 |
1.87e-21 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 97.32 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYwGYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALL--------KSG---IcIVVSP---LIALIN 71
Cdd:PRK11192 13 LEALQDK-GYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQhlldfprrKSGpprI-LILTPtreLAMQVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 72 DQVEGL-KKRGIRALSLAGALSYTDLERILNnavlGNYKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWG--K 148
Cdd:PRK11192 91 DQARELaKHTHLDIATITGGVAYMNHAEVFS----ENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGfaQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 149 DFRPAYLECVWLKEefpkipilALTASAT----------QRVQNDIVQLmqmnDAQviKSSLKRSNIAYMVYKTED---K 215
Cdd:PRK11192 167 DIETIAAETRWRKQ--------TLLFSATlegdavqdfaERLLNDPVEV----EAE--PSRRERKKIHQWYYRADDlehK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 216 WRYLEQIL-HKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRP 294
Cdd:PRK11192 233 TALLCHLLkQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDID 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 1390593022 295 DVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVML 330
Cdd:PRK11192 313 DVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
207-331 |
6.80e-21 |
|
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: 88.72 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 207 YMVYKTEDKWRYLEQIL--HKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVAT 284
Cdd:cd18787 5 YVVVEEEEKKLLLLLLLleKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVAT 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1390593022 285 NAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVMLY 331
Cdd:cd18787 85 DVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
14-333 |
1.22e-17 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 86.38 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 14 GYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVP-----ALLKSG--------ICIVVSP---LIALINDQVEGL 77
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 78 KKrGI---RALSLAGALSYTDLERILNNAVLgnykfLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWGkdFRPAY 154
Cdd:PLN00206 220 GK-GLpfkTALVVGGDAMPQQLYRIQQGVEL-----IVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG--FRDQV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 155 LECVWLKEEfPKIPILALTAS-ATQRVQNDIVQ-LMQMNDAQVIKSSLKRSNIAYMVYKTEDKWRYLEQILHKN--TGSS 230
Cdd:PLN00206 292 MQIFQALSQ-PQVLLFSATVSpEVEKFASSLAKdIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhfKPPA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 231 IVYVRSRKSTVEMAEYLN-TKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLE 309
Cdd:PLN00206 371 VVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIK 450
|
330 340
....*....|....*....|....
gi 1390593022 310 DYFQEAGRAGRDGKKAFAVMLYND 333
Cdd:PLN00206 451 EYIHQIGRASRMGEKGTAIVFVNE 474
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
22-330 |
1.13e-16 |
|
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: 84.12 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL---LKSGIC--IVVSPLIALINDQVEGLKK------RGIRALSLAGA 90
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLealLEDPGAtaLYLYPTKALARDQLRRLRElaealgLGVRVATYDGD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 91 LSYTDLERILNNA--VLGNykflylsPERLQQEI------VRDFIKSmpVNLIVIDEAH--------------------C 142
Cdd:COG1205 141 TPPEERRWIREHPdiVLTN-------PDMLHYGLlphhtrWARFFRN--LRYVVIDEAHtyrgvfgshvanvlrrlrriC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 143 iSHWGKDfrPAYlecvwlkeefpkipILAltaSAT--------QRVQNDivqlmqmnDAQVIKSSLKRSNIAYMV----- 209
Cdd:COG1205 212 -RHYGSD--PQF--------------ILA---SATignpaehaERLTGR--------PVTVVDEDGSPRGERTFVlwnpp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 210 --YKTEDKWRYLE--QILHKNTGS---SIVYVRSRKSTVEMAEY----LNTKGLT---ATYfHGGLTTEQ-----KSLKM 270
Cdd:COG1205 264 lvDDGIRRSALAEaaRLLADLVREglrTLVFTRSRRGAELLARYarraLREPDLAdrvAAY-RAGYLPEErreieRGLRS 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 271 qmwmlGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVML 330
Cdd:COG1205 343 -----GELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLV 397
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
14-329 |
5.70e-16 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 81.43 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 14 GYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL------LKSGICIVVSP---LIALINDQVEGLKK--RGI 82
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnldpeLKAPQILVLAPtreLAVQVAEAMTDFSKhmRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 83 RALSLAGALSYTDLERILNNA---VLGnykflylSPERLQQEIVRDFIKSMPVNLIVIDEAHcishwgKDFRPAYLECVw 159
Cdd:PRK11634 105 NVVALYGGQRYDVQLRALRQGpqiVVG-------TPGRLLDHLKRGTLDLSKLSGLVLDEAD------EMLRMGFIEDV- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 160 lKEEFPKIPILALTASATQRVQNDIVQLMQ--MNDAQV--IKSSL-KRSNIA---YMVY---KTEDKWRYLEQilhKNTG 228
Cdd:PRK11634 171 -ETIMAQIPEGHQTALFSATMPEAIRRITRrfMKEPQEvrIQSSVtTRPDISqsyWTVWgmrKNEALVRFLEA---EDFD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 229 SSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTL 308
Cdd:PRK11634 247 AAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDS 326
|
330 340
....*....|....*....|.
gi 1390593022 309 EDYFQEAGRAGRDGKKAFAVM 329
Cdd:PRK11634 327 ESYVHRIGRTGRAGRAGRALL 347
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
19-374 |
1.59e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.07 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 19 RSPQADIVQAVL-----EGKNVLALMPTGGGKSI--AFQVPALLKSGICIVVSPLIALINDQVEGLKKRGIRALSLAGAL 91
Cdd:COG1061 82 RPYQQEALEALLaalerGGGRGLVVAPTGTGKTVlaLALAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGGKK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 92 SYTDLERILNNAVLGNYKFLylsperlqQEIVRDFiksmpvNLIVIDEAHcisHWGkdfRPAYLECVwlkEEFPKIPILA 171
Cdd:COG1061 162 DSDAPITVATYQSLARRAHL--------DELGDRF------GLVIIDEAH---HAG---APSYRRIL---EAFPAAYRLG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 172 LTAS--------------ATQRVQNDIVQLMQMN-----DAQVIKSSLKRSNIAYMVYKTEDKWRY----------LEQI 222
Cdd:COG1061 219 LTATpfrsdgreillflfDGIVYEYSLKEAIEDGylappEYYGIRVDLTDERAEYDALSERLREALaadaerkdkiLREL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 223 L--HKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVI 300
Cdd:COG1061 299 LreHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAI 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390593022 301 HWDipPT--LEDYFQEAGRAGRDGK-KAFAVMlyndyqyqstqkkFLLHQTDVPFLKLLYAKLNAYFQIAYGEGEEI 374
Cdd:COG1061 379 LLR--PTgsPREFIQRLGRGLRPAPgKEDALV-------------YDFVGNDVPVLEELAKDLRDLAGYRVEFLDEE 440
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
32-174 |
2.91e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.51 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 32 GKNVLALMPTGGGKSIAFQVPALL-----KSGICIVVsPLIALINDQVEGLKKRGIRALSLAGALSYTDLERILNNAvLG 106
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLlllkkGKKVLVLV-PTKALALQTAERLRELFGPGIRVAVLVGGSSAEEREKNK-LG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390593022 107 NYKFLYLSPERLQ---QEIVRDFIKsmPVNLIVIDEAHCISHWGKDFRPAYLeCVWlKEEFPKIPILALTA 174
Cdd:cd00046 79 DADIIIATPDMLLnllLREDRLFLK--DLKLIIVDEAHALLIDSRGALILDL-AVR-KAGLKNAQVILLSA 145
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
18-324 |
1.05e-13 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 74.04 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 18 FRSPQADIVQA---VLEGKNVLALMPTGGGKSIAFQVPA--------LLKSG---ICIVVSPLIALindqVEGLKKRgir 83
Cdd:PTZ00110 150 FTEPTPIQVQGwpiALSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTREL----AEQIREQ--- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 84 alslagALSYTDLERILNNAVLGNYkflylsPERLQQEIVR--------------DFIKSMPVNL-----IVIDEAHCIS 144
Cdd:PTZ00110 223 ------CNKFGASSKIRNTVAYGGV------PKRGQIYALRrgveiliacpgrliDFLESNVTNLrrvtyLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 145 HWG---------KDFRPAYLECVW---------------LKEEFPKIPILALTASATQRVQNDIVqlmqmndaqVIKSSL 200
Cdd:PTZ00110 291 DMGfepqirkivSQIRPDRQTLMWsatwpkevqslardlCKEEPVHVNVGSLDLTACHNIKQEVF---------VVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 201 KRSNIAymvyktedkwRYLEQILhKNTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQV 280
Cdd:PTZ00110 362 KRGKLK----------MLLQRIM-RDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1390593022 281 MVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKK 324
Cdd:PTZ00110 431 MIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAK 474
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
230-330 |
2.67e-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: 67.67 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 230 SIVYVRSRKSTVEMAEYLNTK--------GLTATYfHGGLTTEQK-----SLKMqmwmlGDVQVMVATNAFGMGIDRPDV 296
Cdd:cd18797 38 TIVFCRSRKLAELLLRYLKARlveegplaSKVASY-RAGYLAEDRreieaELFN-----GELLGVVATNALELGIDIGGL 111
|
90 100 110
....*....|....*....|....*....|....
gi 1390593022 297 RTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAVML 330
Cdd:cd18797 112 DAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
22-322 |
8.28e-13 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 71.45 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKS-IAFQV--PALLKSGICIVVSPLIALINDQVEGLKKrgIRALSLAGALSYTDLER 98
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTlIAYSAiyETFLAGLKSIYIVPLRSLAMEKYEELSR--LRSLGMRVKISIGDYDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 99 ilNNAVLGNYKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCIshwGKDFRPAYLECVWLKEEF--PKIPILALTASA 176
Cdd:PRK01172 105 --PPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHII---GDEDRGPTLETVLSSARYvnPDARILALSATV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 177 TqrvqnDIVQLMQMNDAQVIKSSLK----RSNIAY---MVYKTEDKWRYLEQILHKNT----GSSIVYVRSRKSTVEMAE 245
Cdd:PRK01172 180 S-----NANELAQWLNASLIKSNFRpvplKLGILYrkrLILDGYERSQVDINSLIKETvndgGQVLVFVSSRKNAEDYAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 246 YL---------------NTKGLT----------ATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPdVRTVI 300
Cdd:PRK01172 255 MLiqhfpefndfkvsseNNNVYDdslnemlphgVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-ARLVI 333
|
330 340 350
....*....|....*....|....*....|.
gi 1390593022 301 HWDIPPTLEDYF---------QEAGRAGRDG 322
Cdd:PRK01172 334 VRDITRYGNGGIrylsnmeikQMIGRAGRPG 364
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
18-141 |
1.05e-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: 66.84 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 18 FRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVP---ALLK-SGIC-IVVSPLIALINDQVEGLKK------RGIRALS 86
Cdd:cd17923 1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPileALLRdPGSRaLYLYPTKALAQDQLRSLRElleqlgLGIRVAT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390593022 87 LAGALSYTDLERILNNA---VLGNYKFLYLS---PERLQQEIVRDfiksmpVNLIVIDEAH 141
Cdd:cd17923 81 YDGDTPREERRAIIRNPpriLLTNPDMLHYAllpHHDRWARFLRN------LRYVVLDEAH 135
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
231-332 |
1.34e-12 |
|
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: 63.49 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 231 IVYVRSRKSTVEMAEYLntkgltatyfhggltteqkslkmqmwmlgdvQVMVATNAFGMGIDRPDVRTVIHWDIPPTLED 310
Cdd:cd18785 7 IVFTNSIEHAEEIASSL-------------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAAS 55
|
90 100
....*....|....*....|..
gi 1390593022 311 YFQEAGRAGRDGKKAFAVMLYN 332
Cdd:cd18785 56 YIQRVGRAGRGGKDEGEVILFV 77
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
208-322 |
3.59e-11 |
|
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: 61.80 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 208 MVYKTEDKWRYLEQILHKNTGSSIVYVRSRKSTVEMAEYLntKGltATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAF 287
Cdd:cd18795 24 MNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDL--AG--IAFHHAGLTREDRELVEELFREGLIKVLVATSTL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1390593022 288 GMGIDRPdVRTVI-----HWD------IPPTleDYFQEAGRAGRDG 322
Cdd:cd18795 100 AAGVNLP-ARTVIikgtqRYDgkgyreLSPL--EYLQMIGRAGRPG 142
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
21-177 |
5.58e-11 |
|
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: 61.58 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 21 PQADIVQA-VLEGKNVLALMPTGGGKSIAFQ---VPALLKSGICIVVSPLIALINDQVEGLKKRGIRALSLagALSYTDL 96
Cdd:cd18028 5 PQAEAVRAgLLKGENLLISIPTASGKTLIAEmamVNTLLEGGKALYLVPLRALASEKYEEFKKLEEIGLKV--GISTGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 97 ERilNNAVLGNYKFLYLSPE------RLQQEIVRDfiksmpVNLIVIDEAHCIShwgKDFRPAYLECVW--LKEEFPKIP 168
Cdd:cd18028 83 DE--DDEWLGDYDIIVATYEkfdsllRHSPSWLRD------VGVVVVDEIHLIS---DEERGPTLESIVarLRRLNPNTQ 151
|
....*....
gi 1390593022 169 ILALtaSAT 177
Cdd:cd18028 152 IIGL--SAT 158
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
230-328 |
6.85e-11 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 64.46 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 230 SIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLE 309
Cdd:PTZ00424 270 AIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPE 349
|
90
....*....|....*....
gi 1390593022 310 DYFQEAGRAGRDGKKAFAV 328
Cdd:PTZ00424 350 NYIHRIGRSGRFGRKGVAI 368
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
3-320 |
1.22e-10 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 64.45 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 3 ETPLEILKKYwGYDAFRSPQADIVQA-VLEGKNVLALMPTGGGKS----IAFQVPALLKSGICIVVSPLIALINDQVEGL 77
Cdd:PRK00254 10 ERIKRVLKER-GIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTlvaeIVMVNKLLREGGKAVYLVPLKALAEEKYREF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 78 K---KRGIRALSLAGALSYTDlerilnnAVLGNYKFLYLSPERLQQeIVR---DFIKSmpVNLIVIDEAHCIshwGKDFR 151
Cdd:PRK00254 89 KdweKLGLRVAMTTGDYDSTD-------EWLGKYDIIIATAEKFDS-LLRhgsSWIKD--VKLVVADEIHLI---GSYDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 152 PAYLECVwLKEEFPKIPILALTASAtqrvqNDIVQLMQMNDAQVIKSSLK----RSNIAYM---------VYKTEDKWRY 218
Cdd:PRK00254 156 GATLEMI-LTHMLGRAQILGLSATV-----GNAEELAEWLNAELVVSDWRpvklRKGVFYQgflfwedgkIERFPNSWES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 219 LEQILHKNTGSSIVYVRSRKST-----------------------VEMAEYLNT--------KGLTA--TYFHGGLTTEQ 265
Cdd:PRK00254 230 LVYDAVKKGKGALVFVNTRRSAekealelakkikrfltkpelralKELADSLEEnptneklkKALRGgvAFHHAGLGRTE 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390593022 266 KSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIH---------WDIPPTLEDYfQEAGRAGR 320
Cdd:PRK00254 310 RVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRdtkrysnfgWEDIPVLEIQ-QMMGRAGR 372
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
14-320 |
2.03e-10 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 63.29 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 14 GYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLKsgicivvspliaLINDQVEGLKKRGIRAL------SL 87
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQH------------LITRQPHAKGRRPVRALiltptrEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 88 AGAL-----SYTDLERILNNAVLG----NYKFLYL---------SPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWG-- 147
Cdd:PRK10590 88 AAQIgenvrDYSKYLNIRSLVVFGgvsiNPQMMKLrggvdvlvaTPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGfi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 148 KDFRPAylecvwLKEEFPKIPILALTASATQRVQNDIVQLMQmNDAQViksSLKRSNIA--------YMVYKTEdKWRYL 219
Cdd:PRK10590 168 HDIRRV------LAKLPAKRQNLLFSATFSDDIKALAEKLLH-NPLEI---EVARRNTAseqvtqhvHFVDKKR-KRELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 220 EQILHK-NTGSSIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRT 298
Cdd:PRK10590 237 SQMIGKgNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
|
330 340
....*....|....*....|..
gi 1390593022 299 VIHWDIPPTLEDYFQEAGRAGR 320
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGR 338
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
21-178 |
1.09e-09 |
|
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: 58.04 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 21 PQADIV-QAVLEGKNVLALMPTGGGKSIAFQ---VPALLKSGICIV-VSPLIALINDQVEGLKKRGIRALSLAGALSytd 95
Cdd:cd17921 5 IQREALrALYLSGDSVLVSAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLT--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 96 LERILNNAVLGNYKFLYLSPERLQ-------QEIVRDfiksmpVNLIVIDEAHCIshwGKDFRPAYLE--CVWLKEEFPK 166
Cdd:cd17921 82 GDPSVNKLLLAEADILVATPEKLDlllrnggERLIQD------VRLVVVDEAHLI---GDGERGVVLEllLSRLLRINKN 152
|
170
....*....|..
gi 1390593022 167 IPILALTASATQ 178
Cdd:cd17921 153 ARFVGLSATLPN 164
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
22-328 |
2.02e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 60.31 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKSIAFQVPA---LLKSGI----------CIVVSPLIALI----NDQVEGLKKRGIRA 84
Cdd:PRK01297 114 QAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIinqLLQTPPpkerymgeprALIIAPTRELVvqiaKDAAALTKYTGLNV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 85 LSLAGALsytDLERILNNAVLGNYKFLYLSPERL-----QQEIVRDFIKSMpvnliVIDEAHCISHWGkdFRPAYLECVw 159
Cdd:PRK01297 194 MTFVGGM---DFDKQLKQLEARFCDILVATPGRLldfnqRGEVHLDMVEVM-----VLDEADRMLDMG--FIPQVRQII- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 160 lKEEFPKIPILALTASATqrVQNDIVQLMQMNDAQVIKSSLKRSNIA--------YMVYKTeDKWRYLEQILHKNTGSSI 231
Cdd:PRK01297 263 -RQTPRKEERQTLLFSAT--FTDDVMNLAKQWTTDPAIVEIEPENVAsdtveqhvYAVAGS-DKYKLLYNLVTQNPWERV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 232 VYVRSRKSTVE-MAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLED 310
Cdd:PRK01297 339 MVFANRKDEVRrIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDD 418
|
330
....*....|....*...
gi 1390593022 311 YFQEAGRAGRDGKKAFAV 328
Cdd:PRK01297 419 YVHRIGRTGRAGASGVSI 436
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
21-335 |
1.97e-07 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 54.19 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 21 PQADIVQA-VLEGKNVLALMPTGGGKSIAFQVpALLKS----GICIVVSPLIALIN---DQVEGLKKRGIRAlslagALS 92
Cdd:PRK02362 27 PQAEAVEAgLLDGKNLLAAIPTASGKTLIAEL-AMLKAiargGKALYIVPLRALASekfEEFERFEELGVRV-----GIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 93 YTDLERilNNAVLGNYKFLYLSPERLQQeIVR---DFIKSmpVNLIVIDEAHCIshwGKDFRPAYLECVW--LKEEFPKI 167
Cdd:PRK02362 101 TGDYDS--RDEWLGDNDIIVATSEKVDS-LLRngaPWLDD--ITCVVVDEVHLI---DSANRGPTLEVTLakLRRLNPDL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 168 PILALtaSATqrVQN--DIVQLMqmnDAQVIKSSLKRSNIAYMVY-----KTEDKWRYLEQILHKNT-----------GS 229
Cdd:PRK02362 173 QVVAL--SAT--IGNadELADWL---DAELVDSEWRPIDLREGVFyggaiHFDDSQREVEVPSKDDTlnlvldtleegGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 230 SIVYVRSRKSTVEMAEYLN---TKGLT---------------------------------ATYFHGGLTTEQKSLKMQMW 273
Cdd:PRK02362 246 CLVFVSSRRNAEGFAKRAAsalKKTLTaaeraelaelaeeirevsdtetskdladcvakgAAFHHAGLSREHRELVEDAF 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390593022 274 MLGDVQVMVATNAFGMGIDRPDVRTVIH-WD--------IP-PTLEdYFQEAGRAGRDGKKAF--AVMLYNDYQ 335
Cdd:PRK02362 326 RDRLIKVISSTPTLAAGLNLPARRVIIRdYRrydggagmQPiPVLE-YHQMAGRAGRPGLDPYgeAVLLAKSYD 398
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
529-565 |
2.40e-07 |
|
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: 48.06 E-value: 2.40e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1390593022 529 FKQMLRFLDDDKKCKSQQLLAYFGEE-NTQPCGICSVC 565
Cdd:pfam16124 28 LQAMVAYCENTTDCRRKQLLRYFGEEfDSEPCGNCDNC 65
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
6-140 |
7.15e-07 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 50.13 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 6 LEILKKYwgydAFRSP---QADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL--LKSGICIVVSPLIALI---------- 70
Cdd:cd00268 2 LKALKKL----GFEKPtpiQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQALVlaptrelamq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 71 -NDQVEGL-KKRGIRALSLAGALSYTDLERILNNA---VLGnykflylSPERLQqeivrDFIKSMPVNL-----IVIDEA 140
Cdd:cd00268 78 iAEVARKLgKGTGLKVAAIYGGAPIKKQIEALKKGpdiVVG-------TPGRLL-----DLIERGKLDLsnvkyLVLDEA 145
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
22-328 |
1.38e-06 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 51.49 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKSIAFQV---------PALL----KSGICIVVSPL----IALINDQVEGLKKRGIRA 84
Cdd:PRK04537 36 QALTLPVALPGGDVAGQAQTGTGKTLAFLVavmnrllsrPALAdrkpEDPRALILAPTrelaIQIHKDAVKFGADLGLRF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 85 LSLAGALSYTDLERILNNAVlgnyKFLYLSPERLQqeivrDFIKSMPV------NLIVIDEAHCISHWG--KDFRpayle 156
Cdd:PRK04537 116 ALVYGGVDYDKQRELLQQGV----DVIIATPGRLI-----DYVKQHKVvslhacEICVLDEADRMFDLGfiKDIR----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 157 cvWLKEEFPKI---PILALTASATQRVQNDIVQLMQMNDAQVIKS-SLKRSNIAYMVY--KTEDKWRYLEQILHKNTGS- 229
Cdd:PRK04537 182 --FLLRRMPERgtrQTLLFSATLSHRVLELAYEHMNEPEKLVVETeTITAARVRQRIYfpADEEKQTLLLGLLSRSEGAr 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 230 SIVYVRSRKSTVEMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLE 309
Cdd:PRK04537 260 TMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAE 339
|
330
....*....|....*....
gi 1390593022 310 DYFQEAGRAGRDGKKAFAV 328
Cdd:PRK04537 340 DYVHRIGRTARLGEEGDAI 358
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
32-79 |
1.69e-06 |
|
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: 48.35 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1390593022 32 GKNVLALMPTGGGKSIAFQVPAL-------LKSGICIVVSPLIALINDQVEGLKK 79
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssladepEKGVQVLYISPLKALINDQERRLEE 55
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
18-141 |
6.42e-06 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 46.51 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 18 FRSPQADIVQAVLEG-----KNVLALMPTGGGKS-IAFQVPALL-KSGI---CIVVSPLIALINDQVEGLKKRGIRALSL 87
Cdd:pfam04851 4 LRPYQIEAIENLLESikngqKRGLIVMATGSGKTlTAAKLIARLfKKGPikkVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390593022 88 AGALSYTDLERILNNA--VLGNYKFLYLSPERLQQEIVRDFIksmpvNLIVIDEAH 141
Cdd:pfam04851 84 GEIISGDKKDESVDDNkiVVTTIQSLYKALELASLELLPDFF-----DVIIIDEAH 134
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
205-333 |
1.05e-05 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase 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: 350198 [Multi-domain] Cd Length: 159 Bit Score: 45.80 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 205 IAYMVYKTEDK---WRYLEQILHKNTGSSIVYVR-------SRKSTVEMAEYLnTKGLTATY----FHGGLTTEQKSLKM 270
Cdd:cd18811 2 ITTYLIFHTRLdkvYEFVREEIAKGRQAYVIYPLieeseklDLKAAVAMYEYL-KERFRPELnvglLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390593022 271 QMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDipptlEDYF------QEAGRAGRDGKKAFAVMLYND 333
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIED-----AERFglsqlhQLRGRVGRGDHQSYCLLVYKD 144
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
18-175 |
1.24e-05 |
|
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: 46.66 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 18 FRSPQADIVQAVLEGKNVLALMPTGGGKS-IAF--------QVPALLKSGIcIVVSPLIALINDQVEGLKKRGIRALSLA 88
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTfVAVlicehhlkKFPAGRKGKV-VFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 89 GALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMP-VNLIVIDEAHcisHWGKDFrpAYLECV--WLKEEF- 164
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSdFSLLVFDECH---NTTKNH--PYNEIMfrYLDQKLg 156
|
170
....*....|....
gi 1390593022 165 PKIP---ILALTAS 175
Cdd:cd17927 157 SSGPlpqILGLTAS 170
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
219-330 |
1.34e-05 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 45.27 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 219 LEQILHK-----NTGSSIVYVRSRKSTVEMAEYLNT-----KGLTATYFHGGLTTEQK-----SLKMQMWML-----GDV 278
Cdd:cd18802 12 LIEILREyfpktPDFRGIIFVERRATAVVLSRLLKEhpstlAFIRCGFLIGRGNSSQRkrslmTQRKQKETLdkfrdGEL 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1390593022 279 QVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKaFAVML 330
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK-YILMV 142
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
39-175 |
4.21e-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: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 39 MPTGGGKS-IAFQVPALLKSGICIVVSPLIALINDQVEGLKK-RGIRALSLAGALSYTDLERIlnNAVLGNYKFLYLSPE 116
Cdd:cd17926 25 LPTGSGKTlTALALIAYLKELRTLIVVPTDALLDQWKERFEDfLGDSSIGLIGGGKKKDFDDA--NVVVATYQSLSNLAE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390593022 117 RlQQEIVRDFiksmpvNLIVIDEAHCIShwGKDFRpaylECVwlkEEFPKIPILALTAS 175
Cdd:cd17926 103 E-EKDLFDQF------GLLIVDEAHHLP--AKTFS----EIL---KELNAKYRLGLTAT 145
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
125-328 |
8.01e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 45.35 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 125 DFIKSMPVNL-----IVIDEAHCISHWG--KDFRpaylecvWLkeeFPKIPI----LALTASAT--QRVQNdiVQLMQMN 191
Cdd:PRK04837 146 DYAKQNHINLgaiqvVVLDEADRMFDLGfiKDIR-------WL---FRRMPPanqrLNMLFSATlsYRVRE--LAFEHMN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 192 DAQ--VIKSSLKRS-NIAYMVY--KTEDKWRYLEQILHKN-TGSSIVYVRSRKSTVEMAEYLNTKGLTAtyfhgGLTT-- 263
Cdd:PRK04837 214 NPEyvEVEPEQKTGhRIKEELFypSNEEKMRLLQTLIEEEwPDRAIIFANTKHRCEEIWGHLAADGHRV-----GLLTgd 288
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390593022 264 --EQKSLK-MQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGRDGKKAFAV 328
Cdd:PRK04837 289 vaQKKRLRiLEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSI 356
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
30-140 |
9.16e-05 |
|
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: 43.73 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 30 LEGKNVLALMPTGGGKSIAFQVPALLK-------SGI-CIVVSP---LIALINDQVEGL-KKRGIRALSLAGALSytdlE 97
Cdd:cd17957 25 LHGRDLLACAPTGSGKTLAFLIPILQKlgkprkkKGLrALILAPtreLASQIYRELLKLsKGTGLRIVLLSKSLE----A 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1390593022 98 RILNNAVLGN-YKFLYLSPERLqqeivRDFIKSMPVNL-----IVIDEA 140
Cdd:cd17957 101 KAKDGPKSITkYDILVSTPLRL-----VFLLKQGPIDLssveyLVLDEA 144
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
19-175 |
1.15e-04 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 19 RSPQADIVQAVLEgKNVLALMPTGGGKS-IA--------FQVPALLKSG-ICIVVSPLIALINDQVEGLKKR-GIRALSL 87
Cdd:cd18034 4 RSYQLELFEAALK-RNTIVVLPTGSGKTlIAvmlikemgELNRKEKNPKkRAVFLVPTVPLVAQQAEAIRSHtDLKVGEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 88 AGALSYTDLERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHcisHWGKD--FRPAYLEC--VWLKEE 163
Cdd:cd18034 83 SGEMGVDKWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECH---HATGDhpYARIMKEFyhLEGRTS 159
|
170
....*....|..
gi 1390593022 164 FPKipILALTAS 175
Cdd:cd18034 160 RPR--ILGLTAS 169
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
252-319 |
2.61e-04 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 44.53 E-value: 2.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390593022 252 LTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAG 319
Cdd:PRK09751 302 FIARSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
238-333 |
3.08e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain] Cd Length: 160 Bit Score: 41.87 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 238 KSTVEMAEYLntKGLTATY----FHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDipptlEDYF- 312
Cdd:cd18792 45 KSIEALAEEL--KELVPEArvalLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED-----ADRFg 117
|
90 100
....*....|....*....|....*.
gi 1390593022 313 -----QEAGRAGRDGKKAFAVMLYND 333
Cdd:cd18792 118 lsqlhQLRGRVGRGKHQSYCYLLYPD 143
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
217-320 |
3.63e-04 |
|
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: 41.48 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 217 RYLEQILHKNtgSSIVYVRSRKSTVEMAEYLNT---KGLTATYF---HGGLTTEQ-----KSLKMqmwmlGDVQVMVATN 285
Cdd:cd18796 30 EVIFLLERHK--STLVFTNTRSQAERLAQRLRElcpDRVPPDFIalhHGSLSRELreeveAALKR-----GDLKVVVATS 102
|
90 100 110
....*....|....*....|....*....|....*
gi 1390593022 286 AFGMGIDRPDVRTVIHWDIPPTLEDYFQEAGRAGR 320
Cdd:cd18796 103 SLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
258-322 |
7.36e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 42.62 E-value: 7.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390593022 258 HGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPdVRTVI-----------HWDIPPTleDYFQEAGRAGRDG 322
Cdd:COG4581 306 HAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMP-ARTVVftklskfdgerHRPLTAR--EFHQIAGRAGRRG 378
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
258-333 |
7.39e-04 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase 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: 350197 [Multi-domain] Cd Length: 151 Bit Score: 40.40 E-value: 7.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390593022 258 HGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTVIHWDIPP-TLEDYFQEAGRAGRDGKKAFAVMLYND 333
Cdd:cd18810 58 HGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKfGLAQLYQLRGRVGRSKERAYAYFLYPD 134
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
19-198 |
1.58e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 40.15 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 19 RSPQADIVQAVLEGKNVLALMPTGGGKSIAF---------QVPALLKSGICIVVSPLIALINDQVEGLKK---RGIRALS 86
Cdd:cd18036 4 RNYQLELVLPALRGKNTIICAPTGSGKTRVAvyicrhhleKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKyfrKGYKVTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 87 LAGALSytdlERILNNAVLGNYKFLYLSPERLQQEIVRDFIKSMP----VNLIVIDEAHcisHWGKD-------FRpaYL 155
Cdd:cd18036 84 LSGDSS----HKVSFGQIVKASDVIICTPQILINNLLSGREEERVylsdFSLLIFDECH---HTQKEhpynkimRM--YL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1390593022 156 EcVWLKEEFPKIPILALTAS-------ATQRVQNDIVQLMQMNDAQVIKS 198
Cdd:cd18036 155 D-KKLSSQGPLPQILGLTASpgvggarSFEEALEHILKLCANLDASVIAT 203
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
22-73 |
1.71e-03 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) 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: 350713 [Multi-domain] Cd Length: 204 Bit Score: 40.29 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLK-----SGI-CIVVSP---LIALINDQ 73
Cdd:cd17955 26 QKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRlsedpYGIfALVLTPtreLAYQIAEQ 86
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
14-147 |
2.23e-03 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain] Cd Length: 193 Bit Score: 39.84 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 14 GYDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLK------SGICIVVSP---LIALINDQVEGLKKRGIR- 83
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcltehrNPSALILTPtreLAVQIEDQAKELMKGLPPm 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390593022 84 --ALSLAGALSYTDLERILNNAvlgnyKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHCISHWG 147
Cdd:cd17962 89 ktALLVGGLPLPPQLYRLQQGV-----KVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMG 149
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
15-72 |
3.36e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 40.64 E-value: 3.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 15 YDAFRSPQADIVQAVLEGKNVLALMPTGGGKSIAFQVPAL-----------LKSGI-CIVVSPLIALIND 72
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIdelfrlgregeLEDKVyCLYVSPLRALNND 99
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
242-341 |
3.53e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 38.77 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 242 EMAEYLNTKGLTATYFHGGLTTEQKSLKMQMWMLGDVQVMVATNAFGMGIDRPDVRTV--IHWDIPPTLEDY---FQEAG 316
Cdd:cd18790 42 DLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVaiLDADKEGFLRSEtslIQTIG 121
|
90 100
....*....|....*....|....*..
gi 1390593022 317 RAGR--DGKkafaVMLYNDYQYQSTQK 341
Cdd:cd18790 122 RAARnvNGK----VILYADKITDSMQK 144
|
|
| DEXDc_FANCM |
cd18033 |
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ... |
18-187 |
3.96e-03 |
|
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain] Cd Length: 182 Bit Score: 38.84 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 18 FRSPQADIVQAVLEgKNVLALMPTGGGKSIAFQVPAL-----LKSGICIVVSPLIALINDQVEGLKK-RGI---RALSLA 88
Cdd:cd18033 3 LRDYQFTIVQKALF-QNTLVALPTGLGKTFIAAVVMLnyyrwFPKGKIVFMAPTKPLVSQQIEACYKiTGIpssQTAELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 89 GALSYTDLERILNNAvlgnyKFLYLSPERLQQEIVRDFIKSMPVNLIVIDEAHcisHWGKDFrpAYLECVWLKEEFPK-I 167
Cdd:cd18033 82 GSVPPTKRAELWASK-----RVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAH---RATGNY--AYCQVVRELMRYNShF 151
|
170 180
....*....|....*....|...
gi 1390593022 168 PILALTA---SATQRVQNDIVQL 187
Cdd:cd18033 152 RILALTAtpgSKLEAVQQVIDNL 174
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
33-141 |
4.80e-03 |
|
C-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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 38.51 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593022 33 KNVLALMPTGGGKSIAFQVP---ALLKSGICIVV--SPLIALINDQVEGLKKR-----GIRALSLAGalSYT-DLERILN 101
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAmfrAFNKYPGSKVVyiAPLKALVRERVDDWKKRfeeklGKKVVELTG--DVTpDMKALAD 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1390593022 102 NAVlgnykfLYLSPE------RLQQeiVRDFIKSmpVNLIVIDEAH 141
Cdd:cd18022 96 ADI------IITTPEkwdgisRSWQ--TREYVQQ--VSLIIIDEIH 131
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
22-65 |
8.09e-03 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 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: 350700 [Multi-domain] Cd Length: 198 Bit Score: 38.11 E-value: 8.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1390593022 22 QADIVQAVLEGKNVLALMPTGGGKSIAFQVPA--LL-------KSGI-CIVVSP 65
Cdd:cd17942 17 QAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLyklkfkpRNGTgVIIISP 70
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
18-65 |
8.66e-03 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 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: 350699 [Multi-domain] Cd Length: 198 Bit Score: 38.04 E-value: 8.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390593022 18 FRSP---QADIVQAVLEGKNVLALMPTGGGKSIAFQVPALLK---------SGI-CIVVSP 65
Cdd:cd17941 10 FIKMteiQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpeDGLgALIISP 70
|
|
| |
