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Conserved domains on  [gi|18421145|ref|NP_568499|]
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RECQ helicase SIM [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecQ super family cl33925
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
155-684 1.76e-132

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0514:

Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 404.52  E-value: 1.76e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 155 RVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVS 234
Cdd:COG0514   4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 235 ACFLGSGqLD----NCIEEKAMQGMYQIIYVCPEtvvRLIKP--LQKLAKThGIALFAIDEAHCVSKWGHDFRPHYRKLS 308
Cdd:COG0514  84 AAFLNSS-LSaeerREVLRALRAGELKLLYVAPE---RLLNPrfLELLRRL-KISLFAIDEAHCISQWGHDFRPDYRRLG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 309 VLRENFCasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFSV--KHSRTKFASsyakdfqn 386
Cdd:COG0514 159 ELRERLP---------NVPVLALTATATPRVRADIAEQLGL-EDPRVFVGSFDRPNLRLEVvpKPPDDKLAQ-------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 387 LVDLYSEKKNSTGkklavisreseeqtdfgshdsenihetdydedeedqenslakknssngkelseayledetdifqsvd 466
Cdd:COG0514 221 LLDFLKEHPGGSG------------------------------------------------------------------- 233

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 467 dwdvacgefcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDN 546
Cdd:COG0514 234 ----------------------------------IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRD 279

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 547 KLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVL---YADLSRAPTLLP-SRRSKEQTEQA 622
Cdd:COG0514 280 EVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLlygPEDVAIQRFFIEqSPPDEERKRVE 359

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421145 623 YKMLSDCFRYgMNTSQCRAKILVEYFGEEFsSKKCNSCDVCTeGPPELVDVREEANLLFQVI 684
Cdd:COG0514 360 RAKLDAMLAY-AETTGCRRQFLLRYFGEEL-AEPCGNCDNCL-GPPETFDGTEAAQKALSCV 418
UBA_like_SF super family cl21463
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
 8-42 7.38e-05

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


The actual alignment was detected with superfamily member cd14327:

Pssm-ID: 473871 [Multi-domain]  Cd Length: 38  Bit Score: 40.75  E-value: 7.38e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18421145   8 LVMKIVEMGFEKLDALEAVKAVGGKSCDDAVEYIL 42
Cdd:cd14327   2 AVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLF 36
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
155-684 1.76e-132

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 404.52  E-value: 1.76e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 155 RVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVS 234
Cdd:COG0514   4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 235 ACFLGSGqLD----NCIEEKAMQGMYQIIYVCPEtvvRLIKP--LQKLAKThGIALFAIDEAHCVSKWGHDFRPHYRKLS 308
Cdd:COG0514  84 AAFLNSS-LSaeerREVLRALRAGELKLLYVAPE---RLLNPrfLELLRRL-KISLFAIDEAHCISQWGHDFRPDYRRLG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 309 VLRENFCasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFSV--KHSRTKFASsyakdfqn 386
Cdd:COG0514 159 ELRERLP---------NVPVLALTATATPRVRADIAEQLGL-EDPRVFVGSFDRPNLRLEVvpKPPDDKLAQ-------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 387 LVDLYSEKKNSTGkklavisreseeqtdfgshdsenihetdydedeedqenslakknssngkelseayledetdifqsvd 466
Cdd:COG0514 221 LLDFLKEHPGGSG------------------------------------------------------------------- 233

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 467 dwdvacgefcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDN 546
Cdd:COG0514 234 ----------------------------------IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRD 279

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 547 KLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVL---YADLSRAPTLLP-SRRSKEQTEQA 622
Cdd:COG0514 280 EVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLlygPEDVAIQRFFIEqSPPDEERKRVE 359

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421145 623 YKMLSDCFRYgMNTSQCRAKILVEYFGEEFsSKKCNSCDVCTeGPPELVDVREEANLLFQVI 684
Cdd:COG0514 360 RAKLDAMLAY-AETTGCRRQFLLRYFGEEL-AEPCGNCDNCL-GPPETFDGTEAAQKALSCV 418
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
 158-663 2.86e-113

ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129701 [Multi-domain]  Cd Length: 470  Bit Score: 354.08  E-value: 2.86e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   158 SILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACF 237
Cdd:TIGR00614   1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   238 LGSGQLDNCIEE---KAMQGMYQIIYVCPETVVRLIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKLSVLRENF 314
Cdd:TIGR00614  81 LNSAQTKEQQLNvltDLKDGKIKLLYVTPEKISASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   315 CasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFSVKHSRTKFAssyakdfQNLVDLysek 394
Cdd:TIGR00614 161 P---------NVPVMALTATASPSVREDILRQLNL-LNPQIFCTSFDRPNLYYEVRRKTPKIL-------EDLLRF---- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   395 knstgkklavISRESEEQTDfgshdsenihetdydedeedqenslakknssngkelseayledetdifqsvddwdvacge 474
Cdd:TIGR00614 220 ----------IRKEFEGKSG------------------------------------------------------------ 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   475 fcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVAT 554
Cdd:TIGR00614 230 --------------------------IIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVAT 283

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   555 IAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVLY---ADLSRAPTLLPSRRSKEQTEQAYKMLSDCFR 631
Cdd:TIGR00614 284 VAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFyapADMNRLRRLLMEEPDGNFRTYKLKLYEMMEY 363

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 18421145   632 YgMNTSQCRAKILVEYFGE---------EFSSKKCNSCDVC 663
Cdd:TIGR00614 364 C-LNSSTCRRLILLSYFGEkgfnksfciMGTEKCCDNCCKR 403
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 158-360 1.63e-85

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: 270.94  E-value: 1.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 158 SILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACF 237
Cdd:cd17920   2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 238 LGSGQLDNC---IEEKAMQGMYQIIYVCPETVVR--LIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKLSVLRE 312
Cdd:cd17920  82 LNSTLSPEEkreVLLRIKNGQYKLLYVTPERLLSpdFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18421145 313 NFcasnlefleYDVPIMALTATATVNVQEDILESLHLsKETKIVLTSF 360
Cdd:cd17920 162 AL---------PGVPILALTATATPEVREDILKRLGL-RNPVIFRASF 199
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 159-677 5.77e-81

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 272.74  E-value: 5.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  159 ILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACFL 238
Cdd:PRK11057  16 VLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  239 GSG-----QLDncIEEKAMQGMYQIIYVCPETVVrLIKPLQKLAKTHgIALFAIDEAHCVSKWGHDFRPHYRKLSVLREN 313
Cdd:PRK11057  96 NSTqtreqQLE--VMAGCRTGQIKLLYIAPERLM-MDNFLEHLAHWN-PALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  314 FCasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFsvkhsrtkfassyakdfqNLVDLYse 393
Cdd:PRK11057 172 FP---------TLPFMALTATADDTTRQDIVRLLGL-NDPLIQISSFDRPNIRY------------------TLVEKF-- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  394 kknstgKKLAVISRESEEQtdfgshdsenihetdydedeedqenslakknssNGKelseayledetdifqsvddwdvaCG 473
Cdd:PRK11057 222 ------KPLDQLMRYVQEQ---------------------------------RGK-----------------------SG 239

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  474 efcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVA 553
Cdd:PRK11057 240 ---------------------------IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  554 TIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVLYADLSRAPTLlpsRRSKEQTEQAykMLSDCFRYG 633
Cdd:PRK11057 293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWL---RRCLEEKPAG--QQQDIERHK 367

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18421145  634 MN-------TSQCRAKILVEYFGeEFSSKKCNSCDVCTEgPPELVDVREEA 677
Cdd:PRK11057 368 LNamgafaeAQTCRRLVLLNYFG-EGRQEPCGNCDICLD-PPKQYDGLEDA 416
DpdF NF041063
protein DpdF;
159-602 2.23e-32

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 135.04  E-value: 2.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  159 ILRNRFGISSLRSF-QREAL---------STWVAhkdCLvlaATGSGKSLCFQIPALL---TGKVVVVISPLISLMHDQ- 224
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVraallappgSTLIV---NL---PTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQe 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  225 --CLKLSRHkvSACFLGS-----GQLDncIEEKAM------QGMYQIIYVCPETVVR-LIKPLQKLAKTHGIALFAIDEA 290
Cdd:NF041063 204 rrARELLRR--AGPDLGGplawhGGLS--AEERAAirqrirDGTQRILFTSPESLTGsLRPALFDAAEAGLLRYLVVDEA 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  291 HCVSKWGHDFRPHYRKLSVLRENF---CASNLEFLeydvpIMALTATATvNVQEDILESLHLSKETKIVLT-SFFRPNLQ 366
Cdd:NF041063 280 HLVDQWGDGFRPEFQLLAGLRRSLlrlAPSGRPFR-----TLLLSATLT-ESTLDTLETLFGPPGPFIVVSaVQLRPEPA 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  367 FSVKhsrtkfassyakdfqnlvdlysekknstgkklavisreseeqtdfgSHDSENIHEtdydedeedqenslakknssn 446
Cdd:NF041063 354 YWVA----------------------------------------------KCDSEEERR--------------------- 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  447 gkelsEAYLEdetdifqsvddwdvacgefcampscELLEIPVPSekqkdlegltIIYVPTRKESVNIAKYLCGVGLK-AA 525
Cdd:NF041063 367 -----ERVLE-------------------------ALRHLPRPL----------ILYVTKVEDAEAWLQRLRAAGFRrVA 406

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421145  526 AYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAEC-VLYAD 602
Cdd:NF041063 407 LFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSlLIYTP 484
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 170-341 4.50e-29

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: 113.88  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   170 RSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPAL------LTGKVVVVISPLISLMHDQCLKLSR------HKVSACF 237
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKlgkglgLKVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   238 LGSGQLDnciEEKAMQGmYQIIYVCPEtvvRLIKPLQKLAKTHGIALFAIDEAHCVSKWGhdFRPHYRKLsvlrenfcas 317
Cdd:pfam00270  81 GGDSRKE---QLEKLKG-PDILVGTPG---RLLDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI---------- 141

                         170       180
                  ....*....|....*....|....
gi 18421145   318 nLEFLEYDVPIMALTATATVNVQE 341
Cdd:pfam00270 142 -LRRLPKKRQILLLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
162-355 3.24e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.11  E-value: 3.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145    162 NRFGISSLRSFQREALSTWVAH-KDCLVLAATGSGKSLCFQIPALLTGK-----VVVVISPLISLMHDQCLKLSR----- 230
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKrgkggRVLVLVPTRELAEQWAEELKKlgpsl 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145    231 HKVSACFLGSGQLDNcIEEKAMQGMYQIIYVCPETVVRLIKplQKLAKTHGIALFAIDEAHCVSKWGhdFRPHYRKLsvl 310
Cdd:smart00487  82 GLKVVGLYGGDSKRE-QLRKLESGKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--- 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 18421145    311 renfcasnLEFLEYDVPIMALTATATVNVQEDILESLHLSKETKI 355
Cdd:smart00487 154 --------LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
 8-42 7.38e-05

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 40.75  E-value: 7.38e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18421145   8 LVMKIVEMGFEKLDALEAVKAVGGKSCDDAVEYIL 42
Cdd:cd14327   2 AVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLF 36
 
Name Accession Description Interval E-value
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
155-684 1.76e-132

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 404.52  E-value: 1.76e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 155 RVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVS 234
Cdd:COG0514   4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 235 ACFLGSGqLD----NCIEEKAMQGMYQIIYVCPEtvvRLIKP--LQKLAKThGIALFAIDEAHCVSKWGHDFRPHYRKLS 308
Cdd:COG0514  84 AAFLNSS-LSaeerREVLRALRAGELKLLYVAPE---RLLNPrfLELLRRL-KISLFAIDEAHCISQWGHDFRPDYRRLG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 309 VLRENFCasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFSV--KHSRTKFASsyakdfqn 386
Cdd:COG0514 159 ELRERLP---------NVPVLALTATATPRVRADIAEQLGL-EDPRVFVGSFDRPNLRLEVvpKPPDDKLAQ-------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 387 LVDLYSEKKNSTGkklavisreseeqtdfgshdsenihetdydedeedqenslakknssngkelseayledetdifqsvd 466
Cdd:COG0514 221 LLDFLKEHPGGSG------------------------------------------------------------------- 233

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 467 dwdvacgefcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDN 546
Cdd:COG0514 234 ----------------------------------IVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRD 279

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 547 KLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVL---YADLSRAPTLLP-SRRSKEQTEQA 622
Cdd:COG0514 280 EVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLlygPEDVAIQRFFIEqSPPDEERKRVE 359

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421145 623 YKMLSDCFRYgMNTSQCRAKILVEYFGEEFsSKKCNSCDVCTeGPPELVDVREEANLLFQVI 684
Cdd:COG0514 360 RAKLDAMLAY-AETTGCRRQFLLRYFGEEL-AEPCGNCDNCL-GPPETFDGTEAAQKALSCV 418
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
 158-663 2.86e-113

ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129701 [Multi-domain]  Cd Length: 470  Bit Score: 354.08  E-value: 2.86e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   158 SILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACF 237
Cdd:TIGR00614   1 KILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   238 LGSGQLDNCIEE---KAMQGMYQIIYVCPETVVRLIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKLSVLRENF 314
Cdd:TIGR00614  81 LNSAQTKEQQLNvltDLKDGKIKLLYVTPEKISASNRLLQTLEERKGITLIAVDEAHCISQWGHDFRPDYKALGSLKQKF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   315 CasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFSVKHSRTKFAssyakdfQNLVDLysek 394
Cdd:TIGR00614 161 P---------NVPVMALTATASPSVREDILRQLNL-LNPQIFCTSFDRPNLYYEVRRKTPKIL-------EDLLRF---- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   395 knstgkklavISRESEEQTDfgshdsenihetdydedeedqenslakknssngkelseayledetdifqsvddwdvacge 474
Cdd:TIGR00614 220 ----------IRKEFEGKSG------------------------------------------------------------ 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   475 fcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVAT 554
Cdd:TIGR00614 230 --------------------------IIYCPSRKKVEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVAT 283

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   555 IAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVLY---ADLSRAPTLLPSRRSKEQTEQAYKMLSDCFR 631
Cdd:TIGR00614 284 VAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFyapADMNRLRRLLMEEPDGNFRTYKLKLYEMMEY 363

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 18421145   632 YgMNTSQCRAKILVEYFGE---------EFSSKKCNSCDVC 663
Cdd:TIGR00614 364 C-LNSSTCRRLILLSYFGEkgfnksfciMGTEKCCDNCCKR 403
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
 159-677 2.71e-102

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: 329.34  E-value: 2.71e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   159 ILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACFL 238
Cdd:TIGR01389   4 VLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAAAYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   239 GSG---QLDNCIEEKAMQGMYQIIYVCPEtvvRLIKP--LQKLAKTHgIALFAIDEAHCVSKWGHDFRPHYRKLSVLREN 313
Cdd:TIGR01389  84 NSTlsaKEQQDIEKALVNGELKLLYVAPE---RLEQDyfLNMLQRIP-IALVAVDEAHCVSQWGHDFRPEYQRLGSLAER 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   314 FcasnlefleYDVPIMALTATATVNVQEDILESLHLSKETKIVlTSFFRPNLQFSVkhsrtkfassyakdfqnlvdlysE 393
Cdd:TIGR01389 160 F---------PQVPRIALTATADAETRQDIRELLRLADANEFI-TSFDRPNLRFSV-----------------------V 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   394 KKNSTGKKLAVisreseeqtdfgshdsenihetdydedeedqenslakknssngkelseaYLedetdifqsvddwdvacg 473
Cdd:TIGR01389 207 KKNNKQKFLLD-------------------------------------------------YL------------------ 219

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   474 efcampscelleipvpsEKQKDLEGltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVA 553
Cdd:TIGR01389 220 -----------------KKHRGQSG--IIYASSRKKVEELAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVA 280

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   554 TIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVLY---ADLSRAPTLLPSRRSKEQTEQA-YKMLSDC 629
Cdd:TIGR01389 281 TNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLyspADIALLKRRIEQSEADDDYKQIeREKLRAM 360

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 18421145   630 FRYgMNTSQCRAKILVEYFGEEfSSKKCNSCDVCTeGPPELVDVREEA 677
Cdd:TIGR01389 361 IAY-CETQTCRRAYILRYFGEN-EVEPCGNCDNCL-DPPKSYDATVEA 405
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
 158-360 1.63e-85

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: 270.94  E-value: 1.63e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 158 SILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACF 237
Cdd:cd17920   2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 238 LGSGQLDNC---IEEKAMQGMYQIIYVCPETVVR--LIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKLSVLRE 312
Cdd:cd17920  82 LNSTLSPEEkreVLLRIKNGQYKLLYVTPERLLSpdFLELLQRLPERKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLRR 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 18421145 313 NFcasnlefleYDVPIMALTATATVNVQEDILESLHLsKETKIVLTSF 360
Cdd:cd17920 162 AL---------PGVPILALTATATPEVREDILKRLGL-RNPVIFRASF 199
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 159-677 5.77e-81

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 272.74  E-value: 5.77e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  159 ILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACFL 238
Cdd:PRK11057  16 VLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGVAAACL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  239 GSG-----QLDncIEEKAMQGMYQIIYVCPETVVrLIKPLQKLAKTHgIALFAIDEAHCVSKWGHDFRPHYRKLSVLREN 313
Cdd:PRK11057  96 NSTqtreqQLE--VMAGCRTGQIKLLYIAPERLM-MDNFLEHLAHWN-PALLAVDEAHCISQWGHDFRPEYAALGQLRQR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  314 FCasnlefleyDVPIMALTATATVNVQEDILESLHLsKETKIVLTSFFRPNLQFsvkhsrtkfassyakdfqNLVDLYse 393
Cdd:PRK11057 172 FP---------TLPFMALTATADDTTRQDIVRLLGL-NDPLIQISSFDRPNIRY------------------TLVEKF-- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  394 kknstgKKLAVISRESEEQtdfgshdsenihetdydedeedqenslakknssNGKelseayledetdifqsvddwdvaCG 473
Cdd:PRK11057 222 ------KPLDQLMRYVQEQ---------------------------------RGK-----------------------SG 239

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  474 efcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVA 553
Cdd:PRK11057 240 ---------------------------IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  554 TIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVLYADLSRAPTLlpsRRSKEQTEQAykMLSDCFRYG 633
Cdd:PRK11057 293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWL---RRCLEEKPAG--QQQDIERHK 367

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18421145  634 MN-------TSQCRAKILVEYFGeEFSSKKCNSCDVCTEgPPELVDVREEA 677
Cdd:PRK11057 368 LNamgafaeAQTCRRLVLLNYFG-EGRQEPCGNCDICLD-PPKQYDGLEDA 416
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 152-665 8.42e-60

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 221.69  E-value: 8.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   152 WEKRVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRH 231
Cdd:PLN03137  444 WTKKLEVNNKKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQA 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   232 KVSACFLGSG-----QLDNCIEEKAMQGMYQIIYVCPETVVR---LIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPH 303
Cdd:PLN03137  524 NIPAASLSAGmewaeQLEILQELSSEYSKYKLLYVTPEKVAKsdsLLRHLENLNSRGLLARFVIDEAHCVSQWGHDFRPD 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   304 YRKLSVLRENFcasnlefleYDVPIMALTATATVNVQEDILESLHLSkETKIVLTSFFRPNLQFSVkhsrtkfassyakd 383
Cdd:PLN03137  604 YQGLGILKQKF---------PNIPVLALTATATASVKEDVVQALGLV-NCVVFRQSFNRPNLWYSV-------------- 659

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   384 fqnlvdlysekknstgkklavisreseeqtdfgshdsenihetdydedeedqensLAKKNSSngkelseayLEDeTDIFQ 463
Cdd:PLN03137  660 -------------------------------------------------------VPKTKKC---------LED-IDKFI 674

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   464 SVDDWDvACGefcampscelleipvpsekqkdlegltIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDF 543
Cdd:PLN03137  675 KENHFD-ECG---------------------------IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQW 726

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   544 HDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAECVL---YADLSRAPTLL---------- 610
Cdd:PLN03137  727 SKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLyysYSDYIRVKHMIsqggveqspm 806

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18421145   611 ---------PSRRSKEQTEQAYKMLSDCfrygMNTSQCRAKILVEYFGEEFSSKKC-NSCDVCTE 665
Cdd:PLN03137  807 amgynrmasSGRILETNTENLLRMVSYC----ENEVDCRRFLQLVHFGEKFDSTNCkKTCDNCSS 867
DEXHc_RecQ3 cd18017
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ...
 160-360 1.18e-58

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: 198.46  E-value: 1.18e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 160 LRNRFGISSLRSFQREAL-STWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSACFL 238
Cdd:cd18017   4 LNEYFGHSSFRPVQWKVIrSVLEERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 239 GSGQLDNCIEEKAMqGMYQIIYVCPETVVRLIKPLQKLAKthGIALFAIDEAHCVSKWGHDFRPHYRKLSVLRENFCasn 318
Cdd:cd18017  84 GSAQSQNVLDDIKM-GKIRVIYVTPEFVSKGLELLQQLRN--GITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLP--- 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 18421145 319 lefleyDVPIMALTATATVNVQEDILESLHLSKeTKIVLTSF 360
Cdd:cd18017 158 ------NVPIVALTATATPSVRDDIIKNLNLRN-PQITCTSF 192
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
 151-351 7.91e-55

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: 188.34  E-value: 7.91e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 151 SWEKRVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSR 230
Cdd:cd18015   1 PWSGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 231 HKVSACFL---GSGQLDNCIEEKAMQGMYQ--IIYVCPETVV---RLIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRP 302
Cdd:cd18015  81 LGISATMLnasSSKEHVKWVHAALTDKNSElkLLYVTPEKIAkskRFMSKLEKAYNAGRLARIAIDEVHCCSQWGHDFRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18421145 303 HYRKLSVLRENFcasnlefleYDVPIMALTATATVNVQEDILESLHLSK 351
Cdd:cd18015 161 DYKKLGILKRQF---------PNVPILGLTATATSKVLKDVQKILCIQK 200
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
 154-360 1.43e-51

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 179.25  E-value: 1.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 154 KRVNSILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKV 233
Cdd:cd18016   3 KEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 234 SACFLGSGQLDNCIEEKAMQ-----GMYQIIYVCPETVV---RLIKPLQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYR 305
Cdd:cd18016  83 PATYLTGDKTDAEATKIYLQlskkdPIIKLLYVTPEKISasnRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRPDYK 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18421145 306 KLSVLRENFcasnlefleYDVPIMALTATATVNVQEDILESLHLSKeTKIVLTSF 360
Cdd:cd18016 163 RLNMLRQKF---------PSVPMMALTATATPRVQKDILNQLKMLR-PQVFTMSF 207
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
 159-347 8.58e-47

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: 165.89  E-value: 8.58e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 159 ILRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALL----TGKVVVVISPLISLMHDQCLKLSRHKVS 234
Cdd:cd18018   3 LLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLlrrrGPGLTLVVSPLIALMKDQVDALPRAIKA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 235 ACF---LGSGQLDNCIEeKAMQGMYQIIYVCPEtvvRLIKP--LQKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKL-S 308
Cdd:cd18018  83 AALnssLTREERRRILE-KLRAGEVKILYVSPE---RLVNEsfRELLRQTPPISLLVVDEAHCISEWSHNFRPDYLRLcR 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 18421145 309 VLRENFCASnlefleydvPIMALTATATVNVQEDILESL 347
Cdd:cd18018 159 VLRELLGAP---------PVLALTATATKRVVEDIASHL 188
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 492-600 2.22e-44

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: 156.21  E-value: 2.22e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 492 KQKDLEGLTIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIH 571
Cdd:cd18794  25 KVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIH 104

                        90       100
                ....*....|....*....|....*....
gi 18421145 572 YGWLQSLEAYYQEAGRAGRDGELAECVLY 600
Cdd:cd18794 105 YSLPKSMESYYQESGRAGRDGLPSECILF 133
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
 158-361 9.71e-42

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: 151.47  E-value: 9.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 158 SILRNRFGISSLRS-FQREALSTWV-AHKDCLVLAATGSGKSLCFQIPALLTGKVVVVISPLISLMHDQCLKLSRHKVSA 235
Cdd:cd18014   2 STLKKVFGHSDFKSpLQEKATMAVVkGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 236 CFLGS----GQLDNCIEE-KAMQGMYQIIYVCPETV-VRLIKPL-QKLAKTHGIALFAIDEAHCVSKWGHDFRPHYRKLS 308
Cdd:cd18014  82 DSLNSklsaQERKRIIADlESEKPQTKFLYITPEMAaTSSFQPLlSSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLG 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18421145 309 VLRENFCasnlefleyDVPIMALTATATVNVQEDILESLHLSKETKIVLTSFF 361
Cdd:cd18014 162 ALRSRYG---------HVPWVALTATATPQVQEDIFAQLRLKKPVAIFKTPCF 205
DpdF NF041063
protein DpdF;
159-602 2.23e-32

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 135.04  E-value: 2.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  159 ILRNRFGISSLRSF-QREAL---------STWVAhkdCLvlaATGSGKSLCFQIPALL---TGKVVVVISPLISLMHDQ- 224
Cdd:NF041063 130 FLAEALGFTHYRSPgQREAVraallappgSTLIV---NL---PTGSGKSLVAQAPALLasrQGGLTLVVVPTVALAIDQe 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  225 --CLKLSRHkvSACFLGS-----GQLDncIEEKAM------QGMYQIIYVCPETVVR-LIKPLQKLAKTHGIALFAIDEA 290
Cdd:NF041063 204 rrARELLRR--AGPDLGGplawhGGLS--AEERAAirqrirDGTQRILFTSPESLTGsLRPALFDAAEAGLLRYLVVDEA 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  291 HCVSKWGHDFRPHYRKLSVLRENF---CASNLEFLeydvpIMALTATATvNVQEDILESLHLSKETKIVLT-SFFRPNLQ 366
Cdd:NF041063 280 HLVDQWGDGFRPEFQLLAGLRRSLlrlAPSGRPFR-----TLLLSATLT-ESTLDTLETLFGPPGPFIVVSaVQLRPEPA 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  367 FSVKhsrtkfassyakdfqnlvdlysekknstgkklavisreseeqtdfgSHDSENIHEtdydedeedqenslakknssn 446
Cdd:NF041063 354 YWVA----------------------------------------------KCDSEEERR--------------------- 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  447 gkelsEAYLEdetdifqsvddwdvacgefcampscELLEIPVPSekqkdlegltIIYVPTRKESVNIAKYLCGVGLK-AA 525
Cdd:NF041063 367 -----ERVLE-------------------------ALRHLPRPL----------ILYVTKVEDAEAWLQRLRAAGFRrVA 406

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421145  526 AYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGELAEC-VLYAD 602
Cdd:NF041063 407 LFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSlLIYTP 484
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 170-341 4.50e-29

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: 113.88  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   170 RSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPAL------LTGKVVVVISPLISLMHDQCLKLSR------HKVSACF 237
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALealdklDNGPQALVLAPTRELAEQIYEELKKlgkglgLKVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   238 LGSGQLDnciEEKAMQGmYQIIYVCPEtvvRLIKPLQKLAKTHGIALFAIDEAHCVSKWGhdFRPHYRKLsvlrenfcas 317
Cdd:pfam00270  81 GGDSRKE---QLEKLKG-PDILVGTPG---RLLDLLQERKLLKNLKLLVLDEAHRLLDMG--FGPDLEEI---------- 141

                         170       180
                  ....*....|....*....|....
gi 18421145   318 nLEFLEYDVPIMALTATATVNVQE 341
Cdd:pfam00270 142 -LRRLPKKRQILLLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
162-355 3.24e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 104.11  E-value: 3.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145    162 NRFGISSLRSFQREALSTWVAH-KDCLVLAATGSGKSLCFQIPALLTGK-----VVVVISPLISLMHDQCLKLSR----- 230
Cdd:smart00487   2 EKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKrgkggRVLVLVPTRELAEQWAEELKKlgpsl 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145    231 HKVSACFLGSGQLDNcIEEKAMQGMYQIIYVCPETVVRLIKplQKLAKTHGIALFAIDEAHCVSKWGhdFRPHYRKLsvl 310
Cdd:smart00487  82 GLKVVGLYGGDSKRE-QLRKLESGKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKL--- 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 18421145    311 renfcasnLEFLEYDVPIMALTATATVNVQEDILESLHLSKETKI 355
Cdd:smart00487 154 --------LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDV 190
HELICc smart00490
helicase superfamily c-terminal domain;
513-592 3.59e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.56  E-value: 3.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145    513 IAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDG 592
Cdd:smart00490   3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 183-334 1.90e-16

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: 77.06  E-value: 1.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 183 HKDCLVLAATGSGKSLCFQIPALL----TGKVVVVISPLISLMHDQ---CLKLSRHKVSaCFLGSGQLDNCIEEKAMQGM 255
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLlllkKGKKVLVLVPTKALALQTaerLRELFGPGIR-VAVLVGGSSAEEREKNKLGD 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421145 256 YQIIYVCPETVVRLIKPLqKLAKTHGIALFAIDEAHCVSKWGHDFRphyrklsvlreNFCASNLEFLEYDVPIMALTAT 334
Cdd:cd00046  80 ADIIIATPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGAL-----------ILDLAVRKAGLKNAQVILLSAT 146
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 498-592 9.57e-15

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: 71.09  E-value: 9.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   498 GLTIIYVPTRKEsVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQS 577
Cdd:pfam00271  16 GKVLIFSQTKKT-LEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWN 94

                          90
                  ....*....|....*
gi 18421145   578 LEAYYQEAGRAGRDG 592
Cdd:pfam00271  95 PASYIQRIGRAGRAG 109
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 500-593 6.66e-12

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 63.82  E-value: 6.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 500 TIIYVPTRKESVNIAKYLCGVGLKA-------AAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHY 572
Cdd:cd18797  38 TIVFCRSRKLAELLLRYLKARLVEEgplaskvASYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLA 117

                        90       100
                ....*....|....*....|.
gi 18421145 573 GWLQSLEAYYQEAGRAGRDGE 593
Cdd:cd18797 118 GYPGSLASLWQQAGRAGRRGK 138
RecQ_Zn_bind pfam16124
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
 600-664 7.57e-12

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: 61.15  E-value: 7.57e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18421145   600 YADLSRAPTLL-PSRRSKEQTEQAYKMLSDCFRYGMNTSQCRAKILVEYFGEEFSSKKCNSCDVCT 664
Cdd:pfam16124   1 YQDVVRLRFLIeQSEADEERKEVELQKLQAMVAYCENTTDCRRKQLLRYFGEEFDSEPCGNCDNCL 66
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 500-602 4.76e-10

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 58.72  E-value: 4.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 500 TIIYVPTRKESVNIAKYLCGVglkaAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIdkkN-------VRKIIHY 572
Cdd:cd18795  46 VLVFCSSRKECEKTAKDLAGI----AFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGV---NlpartviIKGTQRY 118

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18421145 573 G-----WLQSLEaYYQEAGRAGRDG--ELAECVLYAD 602
Cdd:cd18795 119 DgkgyrELSPLE-YLQMIGRAGRPGfdTRGEAIIMTK 154
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
168-588 6.94e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 59.27  E-value: 6.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 168 SLRSFQREALSTWVA-----HKDCLVLAATGSGKSLCFQ--IPALLTGKVVVVISPLISLMHDQCLKLSRHKVSAcflGS 240
Cdd:COG1061  80 ELRPYQQEALEALLAalergGGRGLVVAPTGTGKTVLALalAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDP---LA 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 241 GQLDNCIEEKAMQGMYQIIYVCPEtvvrlikpLQKLAKTHGiaLFAIDEAHcvskwgHDFRPHYRKlsvLRENFCAsnle 320
Cdd:COG1061 157 GGGKKDSDAPITVATYQSLARRAH--------LDELGDRFG--LVIIDEAH------HAGAPSYRR---ILEAFPA---- 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 321 fleydVPIMALTATatvnvqedilesLHLSKETKIVLTSFFRPNLQFSVKhsrtkfassYAKDFQNLVDLYSekknstgk 400
Cdd:COG1061 214 -----AYRLGLTAT------------PFRSDGREILLFLFDGIVYEYSLK---------EAIEDGYLAPPEY-------- 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 401 kLAVISRESEEQTDFgshdsenihetdydedeedqenslakknSSNGKELSEAYLEDETDIFQSVDDWDVACGEFCAmps 480
Cdd:COG1061 260 -YGIRVDLTDERAEY----------------------------DALSERLREALAADAERKDKILRELLREHPDDRK--- 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 481 celleipvpsekqkdleglTIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMG 560
Cdd:COG1061 308 -------------------TLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG 368

                       410       420
                ....*....|....*....|....*...
gi 18421145 561 IDKKNVRKIIHYGWLQSLEAYYQEAGRA 588
Cdd:COG1061 369 VDVPRLDVAILLRPTGSPREFIQRLGRG 396
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 169-305 1.17e-08

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: 54.62  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 169 LRSFQREALSTWVAHKD----CLVLaATGSGKSLC-FQIPALLTGKVVVVISPLISLMH---DQCLKLSRHKVSaCFLGS 240
Cdd:cd17926   1 LRPYQEEALEAWLAHKNnrrgILVL-PTGSGKTLTaLALIAYLKELRTLIVVPTDALLDqwkERFEDFLGDSSI-GLIGG 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 241 GQLDNCIEEKAMQGMYQIIYVCPETvVRLIKPLQklakthgiALFAIDEAH--CVSKWGH---DFRPHYR 305
Cdd:cd17926  79 GKKKDFDDANVVVATYQSLSNLAEE-EKDLFDQF--------GLLIVDEAHhlPAKTFSEilkELNAKYR 139
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
498-627 1.36e-08

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 58.75  E-value: 1.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 498 GLTIIYVPTRKESVNIAKYLcgvGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFG----------------MGI 561
Cdd:COG1202 428 GQTIIFTNSRRRCHEIARAL---GYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAagvdfpasqvifdslaMGI 504

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421145 562 DkknvrkiihygWLqSLEAYYQEAGRAGRDGelaecvlYADLSRApTLLPS-----RRSKEQTE--QAYKMLS 627
Cdd:COG1202 505 E-----------WL-SVQEFHQMLGRAGRPD-------YHDRGKV-YLLVEpgksyHRSMEMTEdeVAFKLLK 557
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 154-230 1.58e-08

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: 58.31  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 154 KRVNSILRNRfGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALLT-----GKVVVVISPLISLMHDQCLKL 228
Cdd:COG1205  43 PELRAALKKR-GIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARDQLRRL 121


                ..
gi 18421145 229 SR 230
Cdd:COG1205 122 RE 123
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 492-590 2.47e-07

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: 50.58  E-value: 2.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 492 KQKDLEGLTIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIH 571
Cdd:cd18787  22 LEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVIN 101

                        90
                ....*....|....*....
gi 18421145 572 YGWLQSLEAYYQEAGRAGR 590
Cdd:cd18787 102 YDLPRDAEDYVHRIGRTGR 120
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 546-600 2.78e-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: 48.47  E-value: 2.78e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18421145 546 NKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGEL-AECVLY 600
Cdd:cd18785  21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDeGEVILF 76
ResIII pfam04851
Type III restriction enzyme, res subunit;
168-334 3.56e-07

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 50.75  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   168 SLRSFQREALSTWVA-----HKDCLVLAATGSGKSLC-FQIPALLTGKV----VVVISPLISL---MHDQCLKLSRHKVS 234
Cdd:pfam04851   3 ELRPYQIEAIENLLEsikngQKRGLIVMATGSGKTLTaAKLIARLFKKGpikkVLFLVPRKDLleqALEEFKKFLPNYVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145   235 ACFLGSGQldnciEEKAMQGMYQIIYVCPETVVRLIKPLQKLAKTHGIALFAIDEAHcvskwgHDFRPHYRKLsvlrenf 314
Cdd:pfam04851  83 IGEIISGD-----KKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH------RSGASSYRNI------- 144

                         170       180
                  ....*....|....*....|
gi 18421145   315 casnLEFLEYDVpIMALTAT 334
Cdd:pfam04851 145 ----LEYFKPAF-LLGLTAT 159
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 500-593 1.34e-06

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: 52.15  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 500 TIIYVPTRKESVNIAKYL------CGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDkknvrkI---- 569
Cdd:COG1205 291 TLVFTRSRRGAELLARYArralrePDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGID------Iggld 364

                        90       100
                ....*....|....*....|....*.
gi 18421145 570 --IHYGWLQSLEAYYQEAGRAGRDGE 593
Cdd:COG1205 365 avVLAGYPGTRASFWQQAGRAGRRGQ 390
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
498-593 1.64e-06

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 51.30  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 498 GLTIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVAT-IAfGMGIDKKNVRKIIHYGWLQ 576
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATdVA-ARGIDIDDVSHVINYDLPE 320

                        90       100
                ....*....|....*....|
gi 18421145 577 SLEAYYQEAG---RAGRDGE 593
Cdd:COG0513 321 DPEDYVHRIGrtgRAGAEGT 340
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
163-590 3.67e-06

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 50.66  E-value: 3.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 163 RFGISSLRSFQREALSTWVAHKDCLVLAA-TGSGKSLCFQIP---ALLTGKVVVVISPLISLMHDQCLKLSRH------K 232
Cdd:COG1204  17 ERGIEELYPPQAEALEAGLLEGKNLVVSApTASGKTLIAELAilkALLNGGKALYIVPLRALASEKYREFKRDfeelgiK 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 233 VSACflgSGQLDNCIEEKamqGMYQIIYVCPETVVRLI----KPLQKlakthgIALFAIDEAHCVskwGHDFR-PHYR-K 306
Cdd:COG1204  97 VGVS---TGDYDSDDEWL---GRYDILVATPEKLDSLLrngpSWLRD------VDLVVVDEAHLI---DDESRgPTLEvL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 307 LSVLREnfcasnlefLEYDVPIMALTATATvNVqEDILESLhlskeTKIVLTSFFRPN-LQFSV-KHSRTKFASSYAKDF 384
Cdd:COG1204 162 LARLRR---------LNPEAQIVALSATIG-NA-EEIAEWL-----DAELVKSDWRPVpLNEGVlYDGVLRFDDGSRRSK 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 385 QNLVDLYSEKKNSTGKKLAVIS--RESEeqtdfgshdsenihetdydedeedqenSLAKKNSsngKELSEAYLEDETDIF 462
Cdd:COG1204 226 DPTLALALDLLEEGGQVLVFVSsrRDAE---------------------------SLAKKLA---DELKRRLTPEEREEL 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 463 QSVDDwdvacgefcampscELLEIPVPSEKQKDLegltiiyvptrkesvniAKYL-CGVglkaAAYNASLPKKHLRQVHQ 541
Cdd:COG1204 276 EELAE--------------ELLEVSEETHTNEKL-----------------ADCLeKGV----AFHHAGLPSELRRLVED 320

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421145 542 DFHDNKLQVVVAT--IAFGMGIDKKNVrkIIH------YGWLQSLEaYYQEAGRAGR 590
Cdd:COG1204 321 AFREGLIKVLVATptLAAGVNLPARRV--IIRdtkrggMVPIPVLE-FKQMAGRAGR 374
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 169-224 5.38e-06

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: 47.58  E-value: 5.38e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421145 169 LRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPAL-----LTGKVVVVISPLISLMHDQ 224
Cdd:cd17923   1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeallrDPGSRALYLYPTKALAQDQ 61
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
 8-42 7.38e-05

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 40.75  E-value: 7.38e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18421145   8 LVMKIVEMGFEKLDALEAVKAVGGKSCDDAVEYIL 42
Cdd:cd14327   2 AVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLF 36
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
 173-290 8.59e-05

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 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: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 44.33  E-value: 8.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 173 QREALSTWVAHKDCLVLAATGSGKSLCFQIPALL-----------TGKVVVVISPLISLMHD---QCLKLSRH---KVSA 235
Cdd:cd17952  17 QAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVhimdqrelekgEGPIAVIVAPTRELAQQiylEAKKFGKAynlRVVA 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18421145 236 CFLGSGQLDNCieeKAMQGMYQIIYVCPETVVRLIKplQKLAKTHGIALFAIDEA 290
Cdd:cd17952  97 VYGGGSKWEQA---KALQEGAEIVVATPGRLIDMVK--KKATNLQRVTYLVLDEA 146
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 185-365 1.26e-04

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: 44.16  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 185 DCLVLAATGSGKSLCFQIPAL--LTGKVV-----VVISP---LISLMHDQCLKLSRH-KVSACFLGSgqlDNCIEEKAMQ 253
Cdd:cd17956  38 DLCVSAPTGSGKTLAYVLPIVqaLSKRVVprlraLIVVPtkeLVQQVYKVFESLCKGtGLKVVSLSG---QKSFKKEQKL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 254 GMYQI---------IYVCpeTVVRLikpLQKLAKTHGIAL-----FAIDEAHCVSK-----W--GHDFRPHYRKLSVLRE 312
Cdd:cd17956 115 LLVDTsgrylsrvdILVA--TPGRL---VDHLNSTPGFTLkhlrfLVIDEADRLLNqsfqdWleTVMKALGRPTAPDLGS 189

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18421145 313 NFCASNLEFLEYDVPIMALTATATVNVQEdiLESLHLsketkivltsfFRPNL 365
Cdd:cd17956 190 FGDANLLERSVRPLQKLLFSATLTRDPEK--LSSLKL-----------HRPRL 229
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 173-230 1.33e-04

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: 1.33e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421145 173 QREALSTWVAHKDCLVLAATGSGKSLCFQIPALL-------TGKV-VVVISP---LISLMHDQCLKLSR 230
Cdd:cd17957  17 QMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQklgkprkKKGLrALILAPtreLASQIYRELLKLSK 85
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 162-290 1.34e-04

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: 43.97  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 162 NRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPAL---------LTGKV-VVVISP---LISLMHDQCLKL 228
Cdd:cd00268   6 KKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekllpepkkKGRGPqALVLAPtreLAMQIAEVARKL 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18421145 229 SRHK--VSACFLGSGQLDNciEEKAMQGMYQIIyVC-PETVVRLIKplQKLAKTHGIALFAIDEA 290
Cdd:cd00268  86 GKGTglKVAAIYGGAPIKK--QIEALKKGPDIV-VGtPGRLLDLIE--RGKLDLSNVKYLVLDEA 145
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
 500-619 1.70e-04

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 45.22  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  500 TIIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLE 579
Cdd:PRK11634 248 AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSE 327

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18421145  580 AYYQEAGRAGRDGELAECVLYADlSRAPTLLpsrRSKEQT 619
Cdd:PRK11634 328 SYVHRIGRTGRAGRAGRALLFVE-NRERRLL---RNIERT 363
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 521-593 2.51e-04

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 44.39  E-value: 2.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421145  521 GLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEAYYQEAGRAGRDGE 593
Cdd:PLN00206 392 GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGE 464
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
 522-626 4.80e-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: 41.56  E-value: 4.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 522 LKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKII-----HYGwlqsLEAYYQEAGRAGRDGELAE 596
Cdd:cd18810  52 ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFG----LAQLYQLRGRVGRSKERAY 127

                        90       100       110
                ....*....|....*....|....*....|
gi 18421145 597 CVLyadlsraptLLPSRrsKEQTEQAYKML 626
Cdd:cd18810 128 AYF---------LYPDQ--KKLTEDALKRL 146
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
172-220 1.01e-03

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 42.62  E-value: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18421145 172 FQREALSTWVAHKDCLVLAATGSGKSL-----CFQipALLTGKVVVVISPLISL 220
Cdd:COG4581  29 FQEEAILALEAGRSVLVAAPTGSGKTLvaefaIFL--ALARGRRSFYTAPIKAL 80
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 167-295 1.51e-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: 40.88  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 167 SSLRSFQREALSTWVAHKDCLVLAATGSGKS-----LC----FQIPALLTGKVVVVIsPLISLMHDQCLKLSRH------ 231
Cdd:cd17927   1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTfvavlICehhlKKFPAGRKGKVVFLA-NKVPLVEQQKEVFRKHferpgy 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18421145 232 KVSACflgSGQL-DNCIEEKAMQGmYQIIYVCPETVVRLIKPLQKLAKTHgIALFAIDEAHCVSK 295
Cdd:cd17927  80 KVTGL---SGDTsENVSVEQIVES-SDVIIVTPQILVNDLKSGTIVSLSD-FSLLVFDECHNTTK 139
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
 185-249 1.76e-03

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members 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: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 40.53  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 185 DCLVLAATGSGKSLCFQIPALL------------TGKVVVVISP---LISLMHDQCLKLSRHKV-SACFLGSGQLDNCIE 248
Cdd:cd17958  29 DLIGVAQTGTGKTLAYLLPGFIhldlqpipreqrNGPGVLVLTPtreLALQIEAECSKYSYKGLkSVCVYGGGNRNEQIE 108


                .
gi 18421145 249 E 249
Cdd:cd17958 109 D 109
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 172-294 1.79e-03

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: 40.32  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 172 FQREALSTWVAHKDCLVLAA-TGSGKSLCFQIPALLT----GKVVVVISPLISL---MHDQCLKLSRHKVSAC--FLGSG 241
Cdd:cd17921   5 IQREALRALYLSGDSVLVSApTSSGKTLIAELAILRAlatsGGKAVYIAPTRALvnqKEADLRERFGPLGKNVglLTGDP 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18421145 242 QLDNCIEEKAmqgmyQIIYVCPETV-VRLIKPLQKLAKTHGiaLFAIDEAHCVS 294
Cdd:cd17921  85 SVNKLLLAEA-----DILVATPEKLdLLLRNGGERLIQDVR--LVVVDEAHLIG 131
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
 174-235 1.99e-03

DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain]  Cd Length: 143  Bit Score: 39.59  E-value: 1.99e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18421145 174 REALSTWVAHKDCLVLAATGSGKS-LCFQI--PALLTGKVVVVISPLIslmhDQCLKLSRHKVSA 235
Cdd:cd17925   7 NALVETIDAKEDLLVWAVTGAGKTeMLFPAiaQALRQGGRVAIASPRI----DVCLELAPRLKAA 67
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 500-590 2.13e-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: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 500 TIIYVPTRKESVNIAKYL------CGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYG 573
Cdd:cd18796  41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120

                        90
                ....*....|....*..
gi 18421145 574 WLQSLEAYYQEAGRAGR 590
Cdd:cd18796 121 SPKSVARLLQRLGRSGH 137
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 184-363 3.35e-03

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 39.65  E-value: 3.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 184 KDCLVLAATGSGKSLCFQI---------PALLTGKVVVV-ISPLISLMhDQCLKLSRHKVsacflgsGQLD-NCIEEKAM 252
Cdd:cd18023  18 KNFVVSAPTGSGKTVLFELailrllkerNPLPWGNRKVVyIAPIKALC-SEKYDDWKEKF-------GPLGlSCAELTGD 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 253 QGMYQ--------IIYVCPE---TVVRLIKPLQKLAKThgIALFAIDEAHCVSkwghDFRPHYRKLSVLRENFCASNLEF 321
Cdd:cd18023  90 TEMDDtfeiqdadIILTTPEkwdSMTRRWRDNGNLVQL--VALVLIDEVHIIK----ENRGATLEVVVSRMKTLSSSSEL 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18421145 322 LEYDVPIMALTA-TATVNVQEDILESLHLSKETKIVLTSFFRP 363
Cdd:cd18023 164 RGSTVRPMRFVAvSATIPNIEDLAEWLGDNPAGCFSFGESFRP 206
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 184-224 3.82e-03

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: 39.10  E-value: 3.82e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 18421145 184 KDCLVLAATGSGKSLCFQIPAL-------LTGKVVVVISPLISLMHDQ 224
Cdd:cd17922   2 RNVLIAAPTGSGKTEAAFLPALssladepEKGVQVLYISPLKALINDQ 49
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 160-205 4.22e-03

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 39.49  E-value: 4.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18421145 160 LRNRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPAL 205
Cdd:cd17949   5 LKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPII 50
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 162-290 5.30e-03

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 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: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 39.28  E-value: 5.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 162 NRFGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPALL-----------TGKVVVVISP---LISLMHDQCLK 227
Cdd:cd17953  28 KKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRhikdqrpvkpgEGPIGLIMAPtreLALQIYVECKK 107

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 228 LSRH---KVSACFLGSGQLDNCIEEKamQGMYqiIYVCpeTVVRLIKPLQ----KLAKTHGIALFAIDEA 290
Cdd:cd17953 108 FSKAlglRVVCVYGGSGISEQIAELK--RGAE--IVVC--TPGRMIDILTanngRVTNLRRVTYVVLDEA 171
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
161-198 7.38e-03

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 40.09  E-value: 7.38e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 18421145 161 RNRFGisSLRSFQREALSTWVAHKDCLVLAATGSGKSL 198
Cdd:COG1201  19 AARFG--APTPPQREAWPAIAAGESTLLIAPTGSGKTL 54
PTZ00110 PTZ00110
helicase; Provisional
 501-592 7.48e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 39.76  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145  501 IIYVPTRKESVNIAKYLCGVGLKAAAYNASLPKKHLRQVHQDFHDNKLQVVVATIAFGMGIDKKNVRKIIHYGWLQSLEA 580
Cdd:PTZ00110 381 LIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIED 460

                         90
                 ....*....|..
gi 18421145  581 YYQEAGRAGRDG 592
Cdd:PTZ00110 461 YVHRIGRTGRAG 472
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
 173-216 7.83e-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: 38.43  E-value: 7.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18421145 173 QREALSTWVAHKDCLVLAATGSGKSLCFQIPAL----------LTGKVVVVISP 216
Cdd:cd17941  17 QRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLeklyrerwtpEDGLGALIISP 70
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
 164-290 8.02e-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: 38.50  E-value: 8.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421145 164 FGISSLRSFQREALSTWVAHKDCLVLAATGSGKSLCFQIPA--LLT--------GKVVVVISPLISL---MHDQCLKLSR 230
Cdd:cd17942   8 MGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAieLLYklkfkprnGTGVIIISPTRELalqIYGVAKELLK 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421145 231 HKVSACFLGSGQLDNCIE-EKAMQGMYQIIyvcpETVVRLIKPLQKLAK--THGIALFAIDEA 290
Cdd:cd17942  88 YHSQTFGIVIGGANRKAEaEKLGKGVNILV----ATPGRLLDHLQNTKGflYKNLQCLIIDEA 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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