NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19114484|ref|NP_593572|]
View 

exosome RNA helicase subunit Mtl1 [Schizosaccharomyces pombe]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000858)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to Homo sapiens exosome RNA helicase MTR4 and Arabidopsis thaliana chloroplastic DExH-box ATP-dependent RNA helicase DExH15

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Dob10 super family cl34780
Superfamily II RNA helicase [Replication, recombination and repair];
119-1000 1.28e-161

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


The actual alignment was detected with superfamily member COG4581:

Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 494.84  E-value: 1.28e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  119 AKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFG--DVG 196
Cdd:COG4581   19 AEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERFGaeNVG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  197 LMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNAL 276
Cdd:COG4581   99 LLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  277 QFARWISEIHkQPCHVVYTDYRPTPL-QHFIYPqgaDGIYMLvdeknkfktenFKKVLEVLDHSTRQEnysksskkvkks 355
Cdd:COG4581  179 EFAEWLTRVR-GETAVVVSEERPVPLeFHYLVT---PRLFPL-----------FRVNPELLRPPSRHE------------ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  356 sslerIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAinqlsEEDRGLRQFEEMRSLLLRG 435
Cdd:COG4581  232 -----VIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEF-----AEDFSVLFGKTLSRLLRRG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  436 IGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDT 515
Cdd:COG4581  302 IAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDT 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  516 KGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLmrIEEISPE---DILKKSFYQFQNMESLPLIKEELMQL 592
Cdd:COG4581  382 EGHVVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMVLNL--LARPGLErarELLEDSFAQFQADRSVVGLARRAREL 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  593 KNEetsinipnetavkefhdlklqLEKYGEEIqkvmtHPDncLPYLQSgrliqiklggiifpwgvlvnvikrefDPNTRE 672
Cdd:COG4581  460 ERA---------------------LAGVVERL-----ACD--LGDLQE--------------------------YFALRQ 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  673 QVAPHE-------TYVLDVLLPISsnsmsnhkvnpSILVPPRPnetplyeivsVLLTAvcnissiriymprelnsneskL 745
Cdd:COG4581  486 PLSPLEalerespAYALDVVSVPE-----------ATLEDPRP----------VLLAQ---------------------D 523
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  746 RAYRRvnEVIEEFK-EIPYLDPLEhmhiesstlslSLRklEILEPK-LFDSPYYKDSKHRAEYHEFRKKLNLRaqikdis 823
Cdd:COG4581  524 RRARG--EAAAAMKaAIEYDERME-----------RLE--EVLRPHpLHECPLERAFELYRETHPWVRDIELR------- 581
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  824 tkiTNTEAiiqlRELKIRQRVLRRLGFCTLENVIDiKGRVACEITSgdellLVELIFQGFFNQMPPEEIAAALSCFVYED 903
Cdd:COG4581  582 ---PKSVA----RDFDRFCELLREYGYLDDLTLTS-EGLLLRYLYD-----AAEALRQGVPDDLDPEELAALISWLVEEV 648
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  904 KSEVSTLNLKEPFKKmyltIIEAakRIATVSLESKLQFNESDylHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVR 983
Cdd:COG4581  649 RRVDSSEWERLPSPA----NRRA--FVLVNALFRRLELLERR--HGLPELDPGLAGAWASGADLAEVLDATDLDAGDFVR 720
                        890       900
                 ....*....|....*....|
gi 19114484  984 TFRRL---DELLKQLEHAAI 1000
Cdd:COG4581  721 WVRQVidpDPELRRTARAAV 740
 
Name Accession Description Interval E-value
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
119-1000 1.28e-161

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 494.84  E-value: 1.28e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  119 AKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFG--DVG 196
Cdd:COG4581   19 AEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERFGaeNVG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  197 LMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNAL 276
Cdd:COG4581   99 LLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  277 QFARWISEIHkQPCHVVYTDYRPTPL-QHFIYPqgaDGIYMLvdeknkfktenFKKVLEVLDHSTRQEnysksskkvkks 355
Cdd:COG4581  179 EFAEWLTRVR-GETAVVVSEERPVPLeFHYLVT---PRLFPL-----------FRVNPELLRPPSRHE------------ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  356 sslerIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAinqlsEEDRGLRQFEEMRSLLLRG 435
Cdd:COG4581  232 -----VIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEF-----AEDFSVLFGKTLSRLLRRG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  436 IGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDT 515
Cdd:COG4581  302 IAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDT 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  516 KGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLmrIEEISPE---DILKKSFYQFQNMESLPLIKEELMQL 592
Cdd:COG4581  382 EGHVVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMVLNL--LARPGLErarELLEDSFAQFQADRSVVGLARRAREL 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  593 KNEetsinipnetavkefhdlklqLEKYGEEIqkvmtHPDncLPYLQSgrliqiklggiifpwgvlvnvikrefDPNTRE 672
Cdd:COG4581  460 ERA---------------------LAGVVERL-----ACD--LGDLQE--------------------------YFALRQ 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  673 QVAPHE-------TYVLDVLLPISsnsmsnhkvnpSILVPPRPnetplyeivsVLLTAvcnissiriymprelnsneskL 745
Cdd:COG4581  486 PLSPLEalerespAYALDVVSVPE-----------ATLEDPRP----------VLLAQ---------------------D 523
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  746 RAYRRvnEVIEEFK-EIPYLDPLEhmhiesstlslSLRklEILEPK-LFDSPYYKDSKHRAEYHEFRKKLNLRaqikdis 823
Cdd:COG4581  524 RRARG--EAAAAMKaAIEYDERME-----------RLE--EVLRPHpLHECPLERAFELYRETHPWVRDIELR------- 581
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  824 tkiTNTEAiiqlRELKIRQRVLRRLGFCTLENVIDiKGRVACEITSgdellLVELIFQGFFNQMPPEEIAAALSCFVYED 903
Cdd:COG4581  582 ---PKSVA----RDFDRFCELLREYGYLDDLTLTS-EGLLLRYLYD-----AAEALRQGVPDDLDPEELAALISWLVEEV 648
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  904 KSEVSTLNLKEPFKKmyltIIEAakRIATVSLESKLQFNESDylHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVR 983
Cdd:COG4581  649 RRVDSSEWERLPSPA----NRRA--FVLVNALFRRLELLERR--HGLPELDPGLAGAWASGADLAEVLDATDLDAGDFVR 720
                        890       900
                 ....*....|....*....|
gi 19114484  984 TFRRL---DELLKQLEHAAI 1000
Cdd:COG4581  721 WVRQVidpDPELRRTARAAV 740
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
94-298 7.65e-156

DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain]  Cd Length: 205  Bit Score: 458.83  E-value: 7.65e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   94 ALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIY 173
Cdd:cd18024    1 CTHEVALPPDYDYTPISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  174 TSPIKSLSNQKYRELLSEFGDVGLMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWE 253
Cdd:cd18024   81 TSPIKALSNQKYRELQEEFGDVGLMTGDVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19114484  254 ETLILLPDAIRFIFLSATLPNALQFARWISEIHKQPCHVVYTDYR 298
Cdd:cd18024  161 ETIILLPDKVRYVFLSATIPNARQFAEWICKIHKQPCHVVYTDYR 205
rRNA_proc-arch pfam13234
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating ...
566-826 2.61e-72

rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating cofactor. This arch domain is carried in Mtr4 and Ski2 (the cytosolic homolog of Mtr4). The arch domain is required for proper 5.8S rRNA processing, and appears to function independently of canonical helicase activity.


Pssm-ID: 463813  Cd Length: 267  Bit Score: 240.65  E-value: 2.61e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    566 EDILKKSFYQFQNMESLPLIKEELMQLKNEETSINIPNETAVKEFHDLKLQLEKYGEEIQKVMTHPDNCLPYLQSGRLIQ 645
Cdd:pfam13234    1 EYMLKRSFSQFQNQASLPELEKKLKELEKELASIKIPDEEDIKEYYDLRQQLEKLNEDIREVILHPPYGLPFLQPGRLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    646 IKL-GGIIFPWGVLVNVIKRefdPNTREQVAPHETYVLDVLLPISSNSM-----SNHKVNPSILVPPRPNETPLYEIVSV 719
Cdd:pfam13234   81 VKDnGDQDFGWGVVVNFKKR---KKNGKAEPPQESYIVDVLLVLALVSSpedldKFNDVNPEGFRPAPPGEKGEMEVVPV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    720 LLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKE-IPYLDPLEHMHIESSTLSLSLRKLEILEPKLFDSPYYK 798
Cdd:pfam13234  158 PLSDIEAISSVRLKLPKDLRPAEAREAVLKALQELKRRFPDgIPLLDPIEDMKIKDDEFKELLRKIEVLESRLESHPLHK 237
                          250       260
                   ....*....|....*....|....*...
gi 19114484    799 DSKHRAEYHEFRKKLNLRAQIKDISTKI 826
Cdd:pfam13234  238 SPRLEELYALYHEKVELQEEIKELKKEI 265
PRK01172 PRK01172
ATP-dependent DNA helicase;
124-582 9.17e-37

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 148.49  E-value: 9.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   124 FELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYREL--LSEFG-DVGLMTG 200
Cdd:PRK01172   21 FELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELsrLRSLGmRVKISIG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   201 DVSINPS----ASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETL----ILLPDAiRFIFLSATL 272
Cdd:PRK01172  101 DYDDPPDfikrYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLssarYVNPDA-RILALSATV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   273 PNALQFARWISeihkqpCHVVYTDYRPTPLQHFIypqgadgIY---MLVDEKNKFKTENFKKVLEVLDHSTRqenyskss 349
Cdd:PRK01172  180 SNANELAQWLN------ASLIKSNFRPVPLKLGI-------LYrkrLILDGYERSQVDINSLIKETVNDGGQ-------- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   350 kkvkksssleriinmvlsnrydpIIVFCFSKKECEINAHQFGKL--DLNDTENKELVTEIFDSAINQlseedrglrqfee 427
Cdd:PRK01172  239 -----------------------VLVFVSSRKNAEDYAEMLIQHfpEFNDFKVSSENNNVYDDSLNE------------- 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   428 mrsLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGR 507
Cdd:PRK01172  283 ---MLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   508 AGRRGIDTKGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLMRIEEI----SPEDILK---KSFYQFQNME 580
Cdd:PRK01172  360 AGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMGSQRKVRFNTLAAISMglasSMEDLILfynETLMAIQNGV 439

                  ..
gi 19114484   581 SL 582
Cdd:PRK01172  440 DE 441
DEXDc smart00487
DEAD-like helicases superfamily;
123-305 2.54e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 119.13  E-value: 2.54e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484     123 PFELDPFQSTAIKCV-ERMESVLVSAHTSAGKTVIAEYAIAQALKNRQ--RVIYTSPIKSLSNQKYRELLSEFGD----- 194
Cdd:smart00487    6 FEPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPSlglkv 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484     195 VGLMTGDVS-------INPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIF 267
Cdd:smart00487   86 VGLYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLL 165
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 19114484     268 LSATLPNALQFARWisEIHKQPCHVVYTDYRPTPLQHF 305
Cdd:smart00487  166 LSATPPEEIENLLE--LFLNDPVFIDVGFTPLEPIEQF 201
 
Name Accession Description Interval E-value
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
119-1000 1.28e-161

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 494.84  E-value: 1.28e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  119 AKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFG--DVG 196
Cdd:COG4581   19 AEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFFDLVERFGaeNVG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  197 LMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNAL 276
Cdd:COG4581   99 LLTGDASVNPDAPIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVWEEPIIHLPARVQLVLLSATVGNAE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  277 QFARWISEIHkQPCHVVYTDYRPTPL-QHFIYPqgaDGIYMLvdeknkfktenFKKVLEVLDHSTRQEnysksskkvkks 355
Cdd:COG4581  179 EFAEWLTRVR-GETAVVVSEERPVPLeFHYLVT---PRLFPL-----------FRVNPELLRPPSRHE------------ 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  356 sslerIINMVLSNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELVTEIFDSAinqlsEEDRGLRQFEEMRSLLLRG 435
Cdd:COG4581  232 -----VIEELDRGGLLPAIVFIFSRRGCDEAAQQLLSARLTTKEERAEIREAIDEF-----AEDFSVLFGKTLSRLLRRG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  436 IGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDT 515
Cdd:COG4581  302 IAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDT 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  516 KGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLmrIEEISPE---DILKKSFYQFQNMESLPLIKEELMQL 592
Cdd:COG4581  382 EGHVVVLAPEHDDPKKFARLASARPEPLRSSFRPSYNMVLNL--LARPGLErarELLEDSFAQFQADRSVVGLARRAREL 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  593 KNEetsinipnetavkefhdlklqLEKYGEEIqkvmtHPDncLPYLQSgrliqiklggiifpwgvlvnvikrefDPNTRE 672
Cdd:COG4581  460 ERA---------------------LAGVVERL-----ACD--LGDLQE--------------------------YFALRQ 485
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  673 QVAPHE-------TYVLDVLLPISsnsmsnhkvnpSILVPPRPnetplyeivsVLLTAvcnissiriymprelnsneskL 745
Cdd:COG4581  486 PLSPLEalerespAYALDVVSVPE-----------ATLEDPRP----------VLLAQ---------------------D 523
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  746 RAYRRvnEVIEEFK-EIPYLDPLEhmhiesstlslSLRklEILEPK-LFDSPYYKDSKHRAEYHEFRKKLNLRaqikdis 823
Cdd:COG4581  524 RRARG--EAAAAMKaAIEYDERME-----------RLE--EVLRPHpLHECPLERAFELYRETHPWVRDIELR------- 581
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  824 tkiTNTEAiiqlRELKIRQRVLRRLGFCTLENVIDiKGRVACEITSgdellLVELIFQGFFNQMPPEEIAAALSCFVYED 903
Cdd:COG4581  582 ---PKSVA----RDFDRFCELLREYGYLDDLTLTS-EGLLLRYLYD-----AAEALRQGVPDDLDPEELAALISWLVEEV 648
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  904 KSEVSTLNLKEPFKKmyltIIEAakRIATVSLESKLQFNESDylHQFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVR 983
Cdd:COG4581  649 RRVDSSEWERLPSPA----NRRA--FVLVNALFRRLELLERR--HGLPELDPGLAGAWASGADLAEVLDATDLDAGDFVR 720
                        890       900
                 ....*....|....*....|
gi 19114484  984 TFRRL---DELLKQLEHAAI 1000
Cdd:COG4581  721 WVRQVidpDPELRRTARAAV 740
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
94-298 7.65e-156

DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain]  Cd Length: 205  Bit Score: 458.83  E-value: 7.65e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   94 ALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIY 173
Cdd:cd18024    1 CTHEVALPPDYDYTPISAHKPPGNPARTYPFTLDPFQKTAIACIERNESVLVSAHTSAGKTVVAEYAIAQSLRDKQRVIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  174 TSPIKSLSNQKYRELLSEFGDVGLMTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWE 253
Cdd:cd18024   81 TSPIKALSNQKYRELQEEFGDVGLMTGDVTINPNASCLVMTTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19114484  254 ETLILLPDAIRFIFLSATLPNALQFARWISEIHKQPCHVVYTDYR 298
Cdd:cd18024  161 ETIILLPDKVRYVFLSATIPNARQFAEWICKIHKQPCHVVYTDYR 205
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
118-295 3.53e-86

DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L 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: 350785 [Multi-domain]  Cd Length: 179  Bit Score: 274.91  E-value: 3.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  118 PAKTYPFELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGL 197
Cdd:cd18027    1 PAFKWPFELDVFQKQAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  198 MTGDVSINPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPNALQ 277
Cdd:cd18027   81 ITGDVQLNPEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDHVSIILLSATVPNTVE 160
                        170
                 ....*....|....*...
gi 19114484  278 FARWISEIHKQPCHVVYT 295
Cdd:cd18027  161 FADWIGRIKKKNIYVIST 178
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
119-596 2.70e-73

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 252.12  E-value: 2.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  119 AKTYPFELDPFQSTAI-KCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYREL---LSEFG- 193
Cdd:COG1204   16 KERGIEELYPPQAEALeAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKYREFkrdFEELGi 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  194 DVGLMTGDVSINP----SASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWE---ETLILLPDAIRFI 266
Cdd:COG1204   96 KVGVSTGDYDSDDewlgRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEvllARLRRLNPEAQIV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  267 FLSATLPNALQFARWIseihkqPCHVVYTDYRPTPLQHFIYpqgadgiymlVDEKNKFKTENFKKVLEVLDhstrqenys 346
Cdd:COG1204  176 ALSATIGNAEEIAEWL------DAELVKSDWRPVPLNEGVL----------YDGVLRFDDGSRRSKDPTLA--------- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  347 ksskkvkkssslerIINMVLSNRyDPIIVFCFSKKECEINAHQFGKLdLNDTENKELVTEIfDSAINQLSEEDRGLRQFE 426
Cdd:COG1204  231 --------------LALDLLEEG-GQVLVFVSSRRDAESLAKKLADE-LKRRLTPEEREEL-EELAEELLEVSEETHTNE 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  427 EMRSLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNnfrWLTSGEYMQMSG 506
Cdd:COG1204  294 KLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKRGGMV---PIPVLEFKQMAG 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  507 RAGRRGIDTKGLSIVILDQS--IDEQAARCLmNGQADVLNSAFHLSYGMILNLMRI---------EEIspEDILKKSFYQ 575
Cdd:COG1204  371 RAGRPGYDPYGEAILVAKSSdeADELFERYI-LGEPEPIRSKLANESALRTHLLALiasgfansrEEL--LDFLENTFYA 447
                        490       500
                 ....*....|....*....|...
gi 19114484  576 FQNMESLP--LIKEELMQLKNEE 596
Cdd:COG1204  448 YQYDKGDLeeVVDDALEFLLENG 470
rRNA_proc-arch pfam13234
rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating ...
566-826 2.61e-72

rRNA-processing arch domain; Mtr4 is the essential RNA helicase, and is an exosome-activating cofactor. This arch domain is carried in Mtr4 and Ski2 (the cytosolic homolog of Mtr4). The arch domain is required for proper 5.8S rRNA processing, and appears to function independently of canonical helicase activity.


Pssm-ID: 463813  Cd Length: 267  Bit Score: 240.65  E-value: 2.61e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    566 EDILKKSFYQFQNMESLPLIKEELMQLKNEETSINIPNETAVKEFHDLKLQLEKYGEEIQKVMTHPDNCLPYLQSGRLIQ 645
Cdd:pfam13234    1 EYMLKRSFSQFQNQASLPELEKKLKELEKELASIKIPDEEDIKEYYDLRQQLEKLNEDIREVILHPPYGLPFLQPGRLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    646 IKL-GGIIFPWGVLVNVIKRefdPNTREQVAPHETYVLDVLLPISSNSM-----SNHKVNPSILVPPRPNETPLYEIVSV 719
Cdd:pfam13234   81 VKDnGDQDFGWGVVVNFKKR---KKNGKAEPPQESYIVDVLLVLALVSSpedldKFNDVNPEGFRPAPPGEKGEMEVVPV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    720 LLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKE-IPYLDPLEHMHIESSTLSLSLRKLEILEPKLFDSPYYK 798
Cdd:pfam13234  158 PLSDIEAISSVRLKLPKDLRPAEAREAVLKALQELKRRFPDgIPLLDPIEDMKIKDDEFKELLRKIEVLESRLESHPLHK 237
                          250       260
                   ....*....|....*....|....*...
gi 19114484    799 DSKHRAEYHEFRKKLNLRAQIKDISTKI 826
Cdd:pfam13234  238 SPRLEELYALYHEKVELQEEIKELKKEI 265
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
125-286 7.47e-57

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: 194.02  E-value: 7.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  125 ELDPFQSTAIKCV-ERMESVLVSAHTSAGKTVIAEYAIAQAL-KNRQRVIYTSPIKSLSNQKYRELLSEFG----DVGLM 198
Cdd:cd17921    1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALaTSGGKAVYIAPTRALVNQKEADLRERFGplgkNVGLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  199 TGDVSINPS----ASCLIMTTEILRAMLYKNSE-IMHEIAWVIFDEVHYMRDKDRGVVWEETLILLP---DAIRFIFLSA 270
Cdd:cd17921   81 TGDPSVNKLllaeADILVATPEKLDLLLRNGGErLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLrinKNARFVGLSA 160
                        170
                 ....*....|....*.
gi 19114484  271 TLPNALQFARWISEIH 286
Cdd:cd17921  161 TLPNAEDLAEWLGVED 176
DSHCT pfam08148
DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box ...
855-1023 1.49e-53

DSHCT (NUC185) domain; This C terminal domain is found in DOB1/SK12/helY-like DEAD box helicases.


Pssm-ID: 462374  Cd Length: 154  Bit Score: 183.81  E-value: 1.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    855 NVIDIKGRVACEITSGDELLLVELIFQGFFNQMPPEEIAAALSCFVYEDKSEVSTLnLKEPFKKMYLTIIEAAKRIATVS 934
Cdd:pfam08148    1 DVVTLKGRVACEIRSENELLLTELLFSGVFDDLDPEELAALLSAFVFEEKRREPYL-PSPELAEALRLLEEIAHRIAVSR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    935 LesklqfnesdylhqFKPDIMEPVSLWINGASFQEICIVSKLYEGSIVRTFRRLDELLKQLEHAAIVLGNNELKEKSVLT 1014
Cdd:pfam08148   80 F--------------LDFGLMEVVYAWARGASFAEICKLTDLDEGDIVRLIRRLDELLRQIANAAKIIGDPELREKAEEA 145

                   ....*....
gi 19114484   1015 EQKLHRDII 1023
Cdd:pfam08148  146 IELIKRDIV 154
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
298-522 3.91e-53

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: 182.37  E-value: 3.91e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  298 RPTPLQHFIYPQGADGIYMLVDEKNKFKTENFKKVlevldhstrqenysksskkvkkssslerIINMVLSNRydPIIVFC 377
Cdd:cd18795    1 RPVPLEEYVLGFNGLGIKLRVDVMNKFDSDIIVLL----------------------------KIETVSEGK--PVLVFC 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  378 FSKKECEINAhqfgkldlndtenkelvteifdsainqlseedrglrqfeemrsLLLRGIGIHHSGLLPILKELVEILFQE 457
Cdd:cd18795   51 SSRKECEKTA-------------------------------------------KDLAGIAFHHAGLTREDRELVEELFRE 87
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114484  458 GLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGIDTKGLSIVI 522
Cdd:cd18795   88 GLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELSPLEYLQMIGRAGRPGFDTRGEAIIM 152
KOW_Mtr4 cd13154
KOW_Mtr4 is an inserted domain in Mtr4 globular domain; Mtr4 is a conserved helicase with a ...
637-765 4.00e-48

KOW_Mtr4 is an inserted domain in Mtr4 globular domain; Mtr4 is a conserved helicase with a core DExH region that cooperates with the eukaryotic nuclear exosome in RNA processing and degradation. KOW_Mtr4 motif might be involved in presenting RNA substrates to the helicase core. KOW domain is known as an RNA-binding motif that is shared so far among some families of ribosomal proteins, the essential bacterial transcriptional elongation factor NusG, the eukaryotic chromatin elongation factor Spt5, the higher eukaryotic KIN17 proteins and Mtr4. KOW motif is located at the extended insertion of Mtr4 protein.


Pssm-ID: 240518  Cd Length: 129  Bit Score: 167.37  E-value: 4.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  637 YLQSGRLIQIKLGGIIFPWGVLVNVIKREFDPNTREQVAPHETYVLDVLLPISSNSMSNhKVNPSILVPPRPNETPLYEI 716
Cdd:cd13154    1 FLQPGRLVKVKVGDDDFGWGVVVNFQKRPNKKNGSENSPPQESYVVDVLLNCSSGSSIN-NGSPSGIRPPGPGEKGEMEV 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 19114484  717 VSVLLTAVCNISSIRIYMPRELNSNESKLRAYRRVNEVIEEFKE-IPYLD 765
Cdd:cd13154   80 VPVLLSLIQAISSIRLYLPKDLRSADARQSVGKSLQEVKRRFPDgLPLLD 129
PRK01172 PRK01172
ATP-dependent DNA helicase;
124-582 9.17e-37

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 148.49  E-value: 9.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   124 FELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYREL--LSEFG-DVGLMTG 200
Cdd:PRK01172   21 FELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELsrLRSLGmRVKISIG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   201 DVSINPS----ASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETL----ILLPDAiRFIFLSATL 272
Cdd:PRK01172  101 DYDDPPDfikrYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLssarYVNPDA-RILALSATV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   273 PNALQFARWISeihkqpCHVVYTDYRPTPLQHFIypqgadgIY---MLVDEKNKFKTENFKKVLEVLDHSTRqenyskss 349
Cdd:PRK01172  180 SNANELAQWLN------ASLIKSNFRPVPLKLGI-------LYrkrLILDGYERSQVDINSLIKETVNDGGQ-------- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   350 kkvkksssleriinmvlsnrydpIIVFCFSKKECEINAHQFGKL--DLNDTENKELVTEIFDSAINQlseedrglrqfee 427
Cdd:PRK01172  239 -----------------------VLVFVSSRKNAEDYAEMLIQHfpEFNDFKVSSENNNVYDDSLNE------------- 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   428 mrsLLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGR 507
Cdd:PRK01172  283 ---MLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   508 AGRRGIDTKGLSIVILDQSIDEQAARCLMNGQADVLNSAFHLSYGMILNLMRIEEI----SPEDILK---KSFYQFQNME 580
Cdd:PRK01172  360 AGRPGYDQYGIGYIYAASPASYDAAKKYLSGEPEPVISYMGSQRKVRFNTLAAISMglasSMEDLILfynETLMAIQNGV 439

                  ..
gi 19114484   581 SL 582
Cdd:PRK01172  440 DE 441
PRK02362 PRK02362
ATP-dependent DNA helicase;
125-529 3.88e-32

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 134.70  E-value: 3.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   125 ELDPFQSTAI-KCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYREL--LSEFG-DVGLMTG 200
Cdd:PRK02362   23 ELYPPQAEAVeAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFerFEELGvRVGISTG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   201 D-------VSINpsaSCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILL----PDaIRFIFLS 269
Cdd:PRK02362  103 DydsrdewLGDN---DIIVATSEKVDSLLRNGAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLrrlnPD-LQVVALS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   270 ATLPNALQFARWI-SEIhkqpchvVYTDYRPTPLQHFIYPQGAdgIYmLVDEKNKFKTENFKKVLevldhstrqenysks 348
Cdd:PRK02362  179 ATIGNADELADWLdAEL-------VDSEWRPIDLREGVFYGGA--IH-FDDSQREVEVPSKDDTL--------------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   349 skkvkksssleriiNMVLsnryDPI------IVFCFSKKECEINAHQFGKLdlndteNKELVTEIFDSAINQLSEEDRGL 422
Cdd:PRK02362  234 --------------NLVL----DTLeeggqcLVFVSSRRNAEGFAKRAASA------LKKTLTAAERAELAELAEEIREV 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   423 RQFEEMRSL---LLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSGN-NFRWLTS 498
Cdd:PRK02362  290 SDTETSKDLadcVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGaGMQPIPV 369
                         410       420       430
                  ....*....|....*....|....*....|.
gi 19114484   499 GEYMQMSGRAGRRGIDTKGLSiVILDQSIDE 529
Cdd:PRK02362  370 LEYHQMAGRAGRPGLDPYGEA-VLLAKSYDE 399
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
128-277 1.53e-30

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 118.50  E-value: 1.53e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    128 PFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQ---RVIYTSPIKSLSNQKYRELLSEFGDVGL----MTG 200
Cdd:pfam00270    2 PIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDngpQALVLAPTRELAEQIYEELKKLGKGLGLkvasLLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    201 DVSINP------SASCLIMTTEILRAMLyKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPN 274
Cdd:pfam00270   82 GDSRKEqleklkGPDILVGTPGRLLDLL-QERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLPR 160

                   ...
gi 19114484    275 ALQ 277
Cdd:pfam00270  161 NLE 163
DEXDc smart00487
DEAD-like helicases superfamily;
123-305 2.54e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 119.13  E-value: 2.54e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484     123 PFELDPFQSTAIKCV-ERMESVLVSAHTSAGKTVIAEYAIAQALKNRQ--RVIYTSPIKSLSNQKYRELLSEFGD----- 194
Cdd:smart00487    6 FEPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELKKLGPSlglkv 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484     195 VGLMTGDVS-------INPSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIF 267
Cdd:smart00487   86 VGLYGGDSKreqlrklESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLL 165
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 19114484     268 LSATLPNALQFARWisEIHKQPCHVVYTDYRPTPLQHF 305
Cdd:smart00487  166 LSATPPEEIENLLE--LFLNDPVFIDVGFTPLEPIEQF 201
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
127-298 9.82e-30

DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350783 [Multi-domain]  Cd Length: 192  Bit Score: 117.08  E-value: 9.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  127 DPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALK--NRQRVIYTSPIKSLSNQKYRELLSEFGD---------V 195
Cdd:cd18025    3 DAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLResDDGVVVYVAPTKALVNQVVAEVYARFSKkyppsgkslW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  196 GLMTGDVSINPSASCLIMTT--EILRAMLY--KNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPdaIRFIFLSAT 271
Cdd:cd18025   83 GVFTRDYRHNNPMNCQVLITvpECLEILLLspHNASWVPRIKYVIFDEIHSIGQSEDGAVWEQLLLLIP--CPFLALSAT 160
                        170       180       190
                 ....*....|....*....|....*....|
gi 19114484  272 LPNALQFARWISEI---HKQPCHVVYTDYR 298
Cdd:cd18025  161 IGNPQKFHEWLQSVqraRKAELKKIEHNHR 190
PRK00254 PRK00254
ski2-like helicase; Provisional
125-522 4.24e-28

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 121.85  E-value: 4.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   125 ELDPFQSTAIKC-VERMESVLVSAHTSAGKTVIAEYAIA-QALKNRQRVIYTSPIKSLSNQKYRELlSEFGDVGL----M 198
Cdd:PRK00254   23 ELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVnKLLREGGKAVYLVPLKALAEEKYREF-KDWEKLGLrvamT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   199 TGDVSINPS----ASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIFLSATLPN 274
Cdd:PRK00254  102 TGDYDSTDEwlgkYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQILGLSATVGN 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   275 ALQFARWISeihkqpCHVVYTDYRPTPLQHFIYPQG----ADGiymlvdeknkfKTENFKKVLEVLdhstrqenyskssk 350
Cdd:PRK00254  182 AEELAEWLN------AELVVSDWRPVKLRKGVFYQGflfwEDG-----------KIERFPNSWESL-------------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   351 kvkkssslerIINMVlsNRYDPIIVFCFSKKECEINAHQFGKLDLNDTENKELvteifdSAINQLSEEDRGLRQFEEMRS 430
Cdd:PRK00254  231 ----------VYDAV--KKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPEL------RALKELADSLEENPTNEKLKK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   431 LLLRGIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFTKAQKFSgnNFRW--LTSGEYMQMSGRA 508
Cdd:PRK00254  293 ALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYS--NFGWedIPVLEIQQMMGRA 370
                         410
                  ....*....|....
gi 19114484   509 GRRGIDTKGLSIVI 522
Cdd:PRK00254  371 GRPKYDEVGEAIIV 384
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
125-282 4.33e-25

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 103.18  E-value: 4.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  125 ELDPFQSTAI-KCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYREL--LSEFG-DVGLMTG 200
Cdd:cd18028    1 ELYPPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFkkLEEIGlKVGISTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  201 DVSIN----PSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLI---LLPDAIRFIFLSATLP 273
Cdd:cd18028   81 DYDEDdewlGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVArlrRLNPNTQIIGLSATIG 160

                 ....*....
gi 19114484  274 NALQFARWI 282
Cdd:cd18028  161 NPDELAEWL 169
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
130-284 2.97e-22

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: 95.89  E-value: 2.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  130 QSTAIK-CVERMESVLVSAHTSAGKTVIAEYAIAQALK-------NRQRVIYTSPIKSLSNQKYRELLSEFGDVGL---- 197
Cdd:cd18023    6 QSEVFPdLLYSDKNFVVSAPTGSGKTVLFELAILRLLKernplpwGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLscae 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  198 MTGDVSINPS---ASC-LIMTT-EILRAMLYK---NSEIMHEIAWVIFDEVHYMRDKdRGVVWE-------------ETL 256
Cdd:cd18023   86 LTGDTEMDDTfeiQDAdIILTTpEKWDSMTRRwrdNGNLVQLVALVLIDEVHIIKEN-RGATLEvvvsrmktlssssELR 164
                        170       180
                 ....*....|....*....|....*...
gi 19114484  257 ILLPDAIRFIFLSATLPNALQFARWISE 284
Cdd:cd18023  165 GSTVRPMRFVAVSATIPNIEDLAEWLGD 192
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
141-282 3.53e-17

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: 79.93  E-value: 3.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQALKNRQ----RVIYTSPIKSLSNQKYR---ELLSEFG---DVGLMTGDVS------- 203
Cdd:cd17922    2 RNVLIAAPTGSGKTEAAFLPALSSLADEPekgvQVLYISPLKALINDQERrleEPLDEIDleiPVAVRHGDTSqsekakq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  204 -INPSaSCLIMTTEILRAMLY--KNSEIMHEIAWVIFDEVHYMRDKDRGVVWEETLILL-----PDAIRfIFLSATLPNA 275
Cdd:cd17922   82 lKNPP-GILITTPESLELLLVnkKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLrkltgRPLRR-IGLSATLGNL 159

                 ....*..
gi 19114484  276 LQFARWI 282
Cdd:cd17922  160 EEAAAFL 166
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
125-510 4.79e-16

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 83.02  E-value: 4.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  125 ELDPFQSTAIK--CVERMESVLVSAhTSAGKTVIAEYA-IAQALKNRQRVIYTSPIKSLSNQKYRELLSEFG---DVGLM 198
Cdd:COG1202  209 ELLPVQSLAVEngLLEGKDQLVVSA-TATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGdglDVSIR 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  199 TGDVSIN-------PSASCLIMTTE----ILRAmlyknSEIMHEIAWVIFDEVHYMRDKDRGVVWeETLI-----LLPDA 262
Cdd:COG1202  288 VGASRIRddgtrfdPNADIIVGTYEgidhALRT-----GRDLGDIGTVVIDEVHMLEDPERGHRL-DGLIarlkyYCPGA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  263 iRFIFLSATLPNALQFARwiseihKQPCHVVYTDYRPTPLQ-HFIYpqgadgiymlVDEKNKfktenfkkvlevldhstr 341
Cdd:COG1202  362 -QWIYLSATVGNPEELAK------KLGAKLVEYEERPVPLErHLTF----------ADGREK------------------ 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  342 qenysksskkvkkssslERIINMVLSNRYDPI---------IVFCFSKKECEINAHQFGkldlndtenkelvteiFDSAi 412
Cdd:COG1202  407 -----------------IRIINKLVKREFDTKsskgyrgqtIIFTNSRRRCHEIARALG----------------YKAA- 452
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  413 nqlseedrglrqfeemrslllrgigIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLF-TKAQkfsGN 491
Cdd:COG1202  453 -------------------------PYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFdSLAM---GI 504
                        410
                 ....*....|....*....
gi 19114484  492 NfrWLTSGEYMQMSGRAGR 510
Cdd:COG1202  505 E--WLSVQEFHQMLGRAGR 521
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
141-271 6.84e-15

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: 72.82  E-value: 6.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQ-ALKNRQRVIYTSPIKSLSNQKYRELLSEFG---DVGLMTGDVS-------INPSAS 209
Cdd:cd00046    2 ENVLITAPTGSGKTLAALLAALLlLLKKGKKVLVLVPTKALALQTAERLRELFGpgiRVAVLVGGSSaeereknKLGDAD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114484  210 CLIMTTE-ILRAMLYKNSEIMHEIAWVIFDEVHyMRDKDRGVVWEETLIL----LPDAiRFIFLSAT 271
Cdd:cd00046   82 IIIATPDmLLNLLLREDRLFLKDLKLIIVDEAH-ALLIDSRGALILDLAVrkagLKNA-QVILLSAT 146
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
141-299 1.61e-13

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 70.32  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQALKNRQRV-IYTSPIKSLSNQKYRELLSEFGDVGL----MTGDVSINP-----SASC 210
Cdd:cd18026   34 RNLVYSLPTSGGKTLVAEILMLKRLLERRKKaLFVLPYVSIVQEKVDALSPLFEELGFrvegYAGNKGRSPpkrrkSLSV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  211 LIMTTEilRAMLYKNSEI----MHEIAWVIFDEVHYMRDKDRGVVWEETLILL----PDAIRFIFLSATLPNALQFARWI 282
Cdd:cd18026  114 AVCTIE--KANSLVNSLIeegrLDELGLVVVDELHMLGDGHRGALLELLLTKLlyaaQKNIQIVGMSATLPNLEELASWL 191
                        170
                 ....*....|....*..
gi 19114484  283 SeihkqpCHVVYTDYRP 299
Cdd:cd18026  192 R------AELYTTNFRP 202
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
128-282 3.57e-12

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 66.13  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  128 PFQSTAIKCVERM-ESVLVSAHTSAGKTVIAEYAIAQALKN--RQRVIYTSPIKSLSNQKYRELLSEFGDVG-----LMT 199
Cdd:cd18021    6 PIQTQVFNSLYNTdDNVFVGAPTGSGKTVCAELALLRHWRQnpKGRAVYIAPMQELVDARYKDWRAKFGPLLgkkvvKLT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  200 GDVSINP---SASCLIMTTEILRAML---YKNSEIMHEIAWVIFDEVHyMRDKDRGVVWEETL-------ILLPDAIRFI 266
Cdd:cd18021   86 GETSTDLkllAKSDVILATPEQWDVLsrrWKQRKNVQSVELFIADELH-LIGGENGPVYEVVVsrmryisSQLEKPIRIV 164
                        170
                 ....*....|....*.
gi 19114484  267 FLSATLPNALQFARWI 282
Cdd:cd18021  165 GLSSSLANARDVGEWL 180
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
141-282 7.18e-12

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 65.47  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQALKNR--QRVIYTSPIKSLSNQKYRELLSEFGDV-GL----MTGDVSINP----SAS 209
Cdd:cd18022   18 NNVLLGAPTGSGKTIAAELAMFRAFNKYpgSKVVYIAPLKALVRERVDDWKKRFEEKlGKkvveLTGDVTPDMkalaDAD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  210 CLIMTTE----ILRAmlYKNSEIMHEIAWVIFDEVHyMRDKDRGVVWEetLIL---------LPDAIRFIFLSATLPNAL 276
Cdd:cd18022   98 IIITTPEkwdgISRS--WQTREYVQQVSLIIIDEIH-LLGSDRGPVLE--VIVsrmnyissqTEKPVRLVGLSTALANAG 172

                 ....*.
gi 19114484  277 QFARWI 282
Cdd:cd18022  173 DLANWL 178
HELICc smart00490
helicase superfamily c-terminal domain;
435-512 4.27e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 59.92  E-value: 4.27e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114484     435 GIGIHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMP-ARTVLFTKAqkfsgnnfrWLTSGEYMQMSGRAGRRG 512
Cdd:smart00490   13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGRAG 82
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
128-301 9.12e-11

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 66.28  E-value: 9.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  128 PFQSTAIKCVERMESVLVSAHTSAGKT------VIAEYA---IAQALKNRQRVIYTSPIKSLSNQKYREL---LSEFGD- 194
Cdd:COG1201   27 PPQREAWPAIAAGESTLLIAPTGSGKTlaaflpALDELArrpRPGELPDGLRVLYISPLKALANDIERNLrapLEEIGEa 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  195 ---------VGLMTGDVSI--------NPsASCLIMTTEILRAML-YKNS-EIMHEIAWVIFDEVHYMRDKDRGVVWEET 255
Cdd:COG1201  107 aglplpeirVGVRTGDTPAserqrqrrRP-PHILITTPESLALLLtSPDArELLRGVRTVIVDEIHALAGSKRGVHLALS 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19114484  256 L----ILLPDAIRFIFLSATLPNALQFARWIS-EIHKQPCHVVYTDYRPTP 301
Cdd:COG1201  186 LerlrALAPRPLQRIGLSATVGPLEEVARFLVgYEDPRPVTIVDAGAGKKP 236
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
130-280 1.84e-10

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: 61.06  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  130 QSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQAL--KNRQRVIYTSPIKSLSN---QKYRELLSEFG---DVGLMTGD 201
Cdd:cd17923    5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALlrDPGSRALYLYPTKALAQdqlRSLRELLEQLGlgiRVATYDGD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  202 VSINPS-------ASCLIMTTEILRAMLYKNSEIMHEIA----WVIFDEVHYMRdkdrGVVWEETLILL----------P 260
Cdd:cd17923   85 TPREERraiirnpPRILLTNPDMLHYALLPHHDRWARFLrnlrYVVLDEAHTYR----GVFGSHVALLLrrlrrlcrryG 160
                        170       180
                 ....*....|....*....|
gi 19114484  261 DAIRFIFLSATLPNALQFAR 280
Cdd:cd17923  161 ADPQFILTSATIGNPAEHAR 180
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
141-282 8.64e-10

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 59.37  E-value: 8.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQALKNRQR-----------VIYTSPIKSLSNQ---KYRELLSEFG-DVGLMTGDVSIN 205
Cdd:cd18020   18 ENMLICAPTGAGKTNIAMLTILHEIRQHVNqggvikkddfkIVYIAPMKALAAEmveKFSKRLAPLGiKVKELTGDMQLT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  206 PS---ASCLIMTT-EILRAMLYKNS---EIMHEIAWVIFDEVHYMRDkDRGVVWE----ETLILLPDA---IRFIFLSAT 271
Cdd:cd18020   98 KKeiaETQIIVTTpEKWDVVTRKSSgdvALSQLVRLLIIDEVHLLHD-DRGPVIEslvaRTLRQVESTqsmIRIVGLSAT 176
                        170
                 ....*....|.
gi 19114484  272 LPNALQFARWI 282
Cdd:cd18020  177 LPNYLDVADFL 187
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
119-279 1.25e-09

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 58.58  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  119 AKTYPFELDPFQSTAIKCV-------ERMESvLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSE 191
Cdd:cd17918    9 CKSLPFSLTKDQAQAIKDIekdlhspEPMDR-LLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  192 FGD--VGLMTGDV--SINPSASCLIMTTEILRAmlyknSEIMHEIAWVIFDEVHYMrdkdrGVVWEETLILLpDAIRFIF 267
Cdd:cd17918   88 LPFinVELVTGGTkaQILSGISLLVGTHALLHL-----DVKFKNLDLVIVDEQHRF-----GVAQREALYNL-GATHFLE 156
                        170
                 ....*....|...
gi 19114484  268 LSAT-LPNALQFA 279
Cdd:cd17918  157 ATATpIPRTLALA 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
50-271 1.76e-09

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 61.58  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   50 IIENLSDSSVNKEYAKNSLKLSDAVSESKYLNPLLKDKRHDRSFALHKVVVPDDYDYIPLNKHIPSDPPAKTYPFELDPF 129
Cdd:COG1061    5 GIAERGADKLRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  130 QSTAIKCVERMES------VLVSAhTSAGKTVIAeYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGlmTGDVS 203
Cdd:COG1061   85 QQEALEALLAALErgggrgLVVAP-TGTGKTVLA-LALAAELLRGKRVLVLVPRRELLEQWAEELRRFLGDPL--AGGGK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114484  204 INPSASCLIMTTEILRAMLYKNsEIMHEIAWVIFDEVHYMRDKdrgvVWEETLILLPDAIRfIFLSAT 271
Cdd:COG1061  161 KDSDAPITVATYQSLARRAHLD-ELGDRFGLVIIDEAHHAGAP----SYRRILEAFPAAYR-LGLTAT 222
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
126-274 4.18e-09

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 57.77  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  126 LDPFQSTAIKC-VERMESVLVSAHTSAGKTVIAEYAIAQAL-KNRQR----------VIYTSPIKSLSNQKYREL---LS 190
Cdd:cd18019   18 LNRIQSKLFPAaFETDENLLLCAPTGAGKTNVALLTILREIgKHRNPdgtinldafkIVYIAPMKALVQEMVGNFskrLA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  191 EFG-DVGLMTGDVSINP---SASCLIMTT-EILRAMLYKNSEIMHE--IAWVIFDEVHYMRDkDRGVVWE-------ETL 256
Cdd:cd18019   98 PYGiTVAELTGDQQLTKeqiSETQIIVTTpEKWDIITRKSGDRTYTqlVRLIIIDEIHLLHD-DRGPVLEsivartiRQI 176
                        170
                 ....*....|....*...
gi 19114484  257 ILLPDAIRFIFLSATLPN 274
Cdd:cd18019  177 EQTQEYVRLVGLSATLPN 194
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
111-525 5.10e-09

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: 60.23  E-value: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  111 KHIPSdPPAKTYPFE--LDP----------------FQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQA-LKNRQ-R 170
Cdd:COG1205   25 RTIPA-REARYAPWPdwLPPelraalkkrgierlysHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlLEDPGaT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  171 VIYTSPIKSLSN---QKYRELLSEFG---DVGLMTGDVS------INPSASCLIMTTEIL-RAMLYknseimHEIAW--- 234
Cdd:COG1205  104 ALYLYPTKALARdqlRRLRELAEALGlgvRVATYDGDTPpeerrwIREHPDIVLTNPDMLhYGLLP------HHTRWarf 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  235 ------VIFDEVH-YmrdkdRGV----VweeTLIL---------LPDAIRFIFLSATLPNALQFARWISEihkQPCHVVY 294
Cdd:COG1205  178 frnlryVVIDEAHtY-----RGVfgshV---ANVLrrlrricrhYGSDPQFILASATIGNPAEHAERLTG---RPVTVVD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  295 TDYRPTPLQHFIY---PQGADGIYmlvdeknkfktenfkkvlevldHSTRQEnysksskkvkksssLERIINMVLSNRYd 371
Cdd:COG1205  247 EDGSPRGERTFVLwnpPLVDDGIR----------------------RSALAE--------------AARLLADLVREGL- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  372 PIIVFCFSKKECEInahqfgkldlndtenkelvteIFDSAINQLSEEDRGLRqfeemrslllrgIGIHHSGLLPILKELV 451
Cdd:COG1205  290 RTLVFTRSRRGAEL---------------------LARYARRALREPDLADR------------VAAYRAGYLPEERREI 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  452 EILFQEGLVRILFATETFSIGLNMP---ArTVLftkaqkfSGNnfrwltSGEYM---QMSGRAGRRGIDtkGLSIVI--- 522
Cdd:COG1205  337 ERGLRSGELLGVVSTNALELGIDIGgldA-VVL-------AGY------PGTRAsfwQQAGRAGRRGQD--SLVVLVagd 400

                 ....*
gi 19114484  523 --LDQ 525
Cdd:COG1205  401 dpLDQ 405
SF2_C_suv3 cd18805
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ...
462-514 6.46e-08

C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain]  Cd Length: 135  Bit Score: 52.56  E-value: 6.46e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19114484  462 ILFATETFSIGLNMPARTVLFTKAQKFSGNNFRWLTSGEYMQMSGRAGRRGID 514
Cdd:cd18805   73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGRFGSH 125
PRK13767 PRK13767
ATP-dependent helicase; Provisional
125-250 3.28e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.51  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   125 ELDPFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAI---------AQALKNRQRVIYTSPIKSLSNQKYR--------- 186
Cdd:PRK13767   32 TFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIidelfrlgrEGELEDKVYCLYVSPLRALNNDIHRnleepltei 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   187 -ELLSEFGD------VGLMTGDVSINPSAS-------CLIMTTEILRAMLY--KNSEIMHEIAWVIFDEVHYMRDKDRGV 250
Cdd:PRK13767  112 rEIAKERGEelpeirVAIRTGDTSSYEKQKmlkkpphILITTPESLAILLNspKFREKLRTVKWVIVDEIHSLAENKRGV 191
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
358-512 4.07e-06

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: 46.43  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484    358 LERIINMVLSNRYDPIIVFCFSKKECEInahqfgkldlndtenkelvteifdsainqlseedrglrqfEEMRSLLLRGIG 437
Cdd:pfam00271    3 LEALLELLKKERGGKVLIFSQTKKTLEA----------------------------------------ELLLEKEGIKVA 42
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114484    438 IHHSGLLPILKELVEILFQEGLVRILFATETFSIGLNMPARTVLFtkaqkfsgnNFR-WLTSGEYMQMSGRAGRRG 512
Cdd:pfam00271   43 RLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVI---------NYDlPWNPASYIQRIGRAGRAG 109
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
143-281 4.09e-06

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 48.10  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  143 VLVSAHTSAGKTVIAEYAIAQALKNR-QRVIYTSP----IKSLSNQKYRELLSEFGD-VGL-MTGDVSINPSASCLIMTT 215
Cdd:cd17990   20 VVLEAPPGAGKTTRVPLALLAELWIAgGKIIVLEPrrvaARAAARRLATLLGEAPGEtVGYrVRGESRVGRRTRVEVVTE 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  216 EILRAMLYKNSEiMHEIAWVIFDEVHyMRDKDR----GVVWEETLILLPDaIRFIFLSATLPNALQFARW 281
Cdd:cd17990  100 GVLLRRLQRDPE-LSGVGAVILDEFH-ERSLDAdlalALLLEVQQLLRDD-LRLLAMSATLDGDGLAALL 166
DEXQc_Suv3 cd17913
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA ...
149-252 8.03e-06

DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350671 [Multi-domain]  Cd Length: 142  Bit Score: 46.40  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  149 TSAGKTviaeYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFGDVGLMTGD-VSINPSASCLIMTTEilraMLYKNSE 227
Cdd:cd17913   10 TNSGKT----YHALQRLKSAKSGVYCGPLRLLAWEVYERLNAEGVPCDLVTGQeRREVEGATHVSCTVE----MASISEP 81
                         90       100
                 ....*....|....*....|....*
gi 19114484  228 ImhEIAwVIfDEVHYMRDKDRGVVW 252
Cdd:cd17913   82 Y--DVA-VI-DEIQMIGDPQRGWAW 102
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
144-272 1.02e-05

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 46.53  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  144 LVSAHTSAGKTVIAEYAIAQALKnrQRVIYTSPIKSLSNQKYRELLSEFGD--VGLMTGDVSI-NPSASCLIMTTEILRA 220
Cdd:cd17926   22 ILVLPTGSGKTLTALALIAYLKE--LRTLIVVPTDALLDQWKERFEDFLGDssIGLIGGGKKKdFDDANVVVATYQSLSN 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19114484  221 MLYKNSEIMHEIAWVIFDEVHYMrdkdRGVVWEETLILLPDAIRFiFLSATL 272
Cdd:cd17926  100 LAEEEKDLFDQFGLLIVDEAHHL----PAKTFSEILKELNAKYRL-GLTATP 146
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
143-276 3.33e-05

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 45.75  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  143 VLVSAHTSAGKTviaEYAIAQALKNR-----QRVIYTSPIKSLSNQ---KYRELLSEFGD---VGLMTGDVSIN------ 205
Cdd:cd17930    4 VILEAPTGSGKT---EAALLWALKLAarggkRRIIYALPTRATINQmyeRIREILGRLDDedkVLLLHSKAALEllesde 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  206 -PSASCLIMTTEILRAMLYKNSEIM---------------------HEIAW--VIFDEVH-----YMRdkdrGVVweETL 256
Cdd:cd17930   81 ePDDDPVEAVDWALLLKRSWLAPIVvttidqllesllkykhferrlHGLANsvVVLDEVQaydpeYMA----LLL--KAL 154
                        170       180
                 ....*....|....*....|..
gi 19114484  257 ILLPDA--IRFIFLSATLPNAL 276
Cdd:cd17930  155 LELLGElgGPVVLMTATLPALL 176
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
145-282 5.05e-05

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 47.61  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   145 VSAHTSAGKTVIA-EYAIAQALKNR------------QRVIYTSPIKSLSNQKYREL---LSEFGD-------------V 195
Cdd:PRK09751    1 VIAPTGSGKTLAAfLYALDRLFREGgedtreahkrktSRILYISPIKALGTDVQRNLqipLKGIADerrrrgetevnlrV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484   196 GLMTGDVSINPSA-------SCLIMTTEILRAMLY-KNSEIMHEIAWVIFDEVHYMRDKDRG----VVWEETLILLPDAI 263
Cdd:PRK09751   81 GIRTGDTPAQERSkltrnppDILITTPESLYLMLTsRARETLRGVETVIIDEVHAVAGSKRGahlaLSLERLDALLHTSA 160
                         170
                  ....*....|....*....
gi 19114484   264 RFIFLSATLPNALQFARWI 282
Cdd:PRK09751  161 QRIGLSATVRSASDVAAFL 179
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
368-512 6.71e-05

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: 43.74  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  368 NRYDPIIVFCFSKKECEinahqfgkldlndtenkelvteifdsainQLSEEdrglrqfeemrsllLRGIGIH----HSGL 443
Cdd:cd18794   28 HLGGSGIIYCLSRKECE-----------------------------QVAAR--------------LQSKGISaaayHAGL 64
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  444 LPILKELVEILFQEGLVRILFATETFSIGLNMP-ARTVLFTKAQKfsgnnfrwlTSGEYMQMSGRAGRRG 512
Cdd:cd18794   65 EPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPdVRFVIHYSLPK---------SMESYYQESGRAGRDG 125
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
141-241 8.03e-04

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 43.57  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  141 ESVLVSAHTSAGKTVIAEYAIAQALKNRQ-RVIYTSPIKSLSNQ---KYRELLS-EFGDVGLMTGDVSINP------SAS 209
Cdd:COG1111   18 KNTLVVLPTGLGKTAVALLVIAERLHKKGgKVLFLAPTKPLVEQhaeFFKEALNiPEDEIVVFTGEVSPEKrkelweKAR 97
                         90       100       110
                 ....*....|....*....|....*....|..
gi 19114484  210 CLIMTTEILRAMLYKNSEIMHEIAWVIFDEVH 241
Cdd:COG1111   98 IIVATPQVIENDLIAGRIDLDDVSLLIFDEAH 129
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
133-240 2.36e-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: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  133 AIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQRVIYTSPIKSLSNQKYRELLSEFG--DVGLMTGDVSINPSASC 210
Cdd:cd17925    9 LVETIDAKEDLLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPRIDVCLELAPRLKAAFPgaAIVLLHGGSEDQYQRSP 88
                         90       100       110
                 ....*....|....*....|....*....|..
gi 19114484  211 L-IMTT-EILRamlYKnseimHEIAWVIFDEV 240
Cdd:cd17925   89 LvIATThQLLR---FY-----RAFDLLIIDEV 112
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
143-276 5.71e-03

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 40.11  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  143 VLVSAHTSAGKTVIAEYAIAQALKNRQ--RVIYTSPIKSLSNQKYRELLSEFGDVGLmtGDVSINPSASCLIMTTE---I 217
Cdd:cd09639    2 LVIEAPTGYGKTEAALLWALHSLKSQKadRVIIALPTRATINAMYRRAKEAFGETGL--YHSSILSSRIKEMGDSEefeH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  218 LRAMLYKNS--------------EIM---------HEI-------AWVIFDEVHYMRDKDRGVVWEETLILLPDAIRFIF 267
Cdd:cd09639   80 LFPLYIHSNdtlfldpitvctidQVLksvfgefghYEFtlasianSLLIFDEVHFYDEYTLALILAVLEVLKDNDVPILL 159

                 ....*....
gi 19114484  268 LSATLPNAL 276
Cdd:cd09639  160 MSATLPKFL 168
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
128-273 8.41e-03

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 38.72  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  128 PFQSTAIKCVERMESVLVSAHTSAGKTVIAEYAIAQALKNRQ-----RVIYTSPIKSLSNQKYRE-------------LL 189
Cdd:cd17957   15 PIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRkkkglRALILAPTRELASQIYREllklskgtglrivLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114484  190 SEFGDVGLMTGDVSINpSASCLIMTTEILRAMLYKNSEIMHEIAWVIFDEVhymrDK--DRGVVwEETLILL-----PDA 262
Cdd:cd17957   95 SKSLEAKAKDGPKSIT-KYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA----DKlfEPGFR-EQTDEILaactnPNL 168
                        170
                 ....*....|.
gi 19114484  263 IRFIFlSATLP 273
Cdd:cd17957  169 QRSLF-SATIP 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH