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Conserved domains on  [gi|27371129|gb|AAH23303|]
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Ddx10 protein, partial [Mus musculus]

Protein Classification

DEADc_DDX10 and SF2_C_DEAD domain-containing protein (domain architecture ID 12782903)

protein containing domains DEADc_DDX10, SF2_C_DEAD, and DUF4217

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
80-277 3.71e-143

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


:

Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 415.15  E-value: 3.71e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMNAI 239
Cdd:cd17941  81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27371129 240 IENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVH 277
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
69-472 3.03e-118

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


:

Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 363.34  E-value: 3.03e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLqwTSTDGLGVLIIS 148
Cdd:COG0513  29 PEFASLGLSPELLQALKDLGFEEPTPIQLAAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQKILKS--VERKYVSALILA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 149 PTRELAYQTFEVLRKVGKNH-DFSAGLIIGGKDLKHEAERIN-NINILVCTPGRLLQHMDETIcFHATNLQMLVLDEADR 226
Cdd:COG0513 107 PTRELAVQIAEELRKLGKNLgGLRVAVVYGGVSIRKQIEALKrGVDIVVATPGRLLDLIKRGK-LDLSGVETLVLDEADR 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 227 ILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYSTPATLEQNYIICE-LHQKISVLF 305
Cdd:COG0513 186 MLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIRELARRYLNDPVEIEVSVEKLERTLKKIKQFYLEVEsEEEKLELLL 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 306 SFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVN 385
Cdd:COG0513 266 KLLKDEDEGRVIVFVRTKRLVEELAESLRKR--GFKVAALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVS 343
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 386 WVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQGMVQQLLQ-KKVPVKEIKINPEKLIDVQKKLESFLAQDQD 464
Cdd:COG0513 344 HVINYDLPLDPEDYVHRIGRTGRAGRKGVAISFVTEEEEVKKLKRIEKrLERKLPSAVLLPLDEPEDAKLLKTTRPGLEE 423

                ....*...
gi 27371129 465 LKERAQRC 472
Cdd:COG0513 424 ESDISDEI 431
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
451-510 1.50e-17

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


:

Pssm-ID: 339021  Cd Length: 60  Bit Score: 76.65  E-value: 1.50e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   451 VQKKLESFLAQDQDLKERAQRCFVSYIR--SVYLMKDkeVFNVSKLPITEYALSLGLAVAPR 510
Cdd:pfam13959   1 IQLQLEKLVLKDRELKELAQKAFVSYVRaySTHLLKD--IFNVKKLDLGHLAKSFGLLEAPK 60
 
Name Accession Description Interval E-value
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
80-277 3.71e-143

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 415.15  E-value: 3.71e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMNAI 239
Cdd:cd17941  81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27371129 240 IENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVH 277
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
69-472 3.03e-118

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


Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 363.34  E-value: 3.03e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLqwTSTDGLGVLIIS 148
Cdd:COG0513  29 PEFASLGLSPELLQALKDLGFEEPTPIQLAAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQKILKS--VERKYVSALILA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 149 PTRELAYQTFEVLRKVGKNH-DFSAGLIIGGKDLKHEAERIN-NINILVCTPGRLLQHMDETIcFHATNLQMLVLDEADR 226
Cdd:COG0513 107 PTRELAVQIAEELRKLGKNLgGLRVAVVYGGVSIRKQIEALKrGVDIVVATPGRLLDLIKRGK-LDLSGVETLVLDEADR 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 227 ILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYSTPATLEQNYIICE-LHQKISVLF 305
Cdd:COG0513 186 MLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIRELARRYLNDPVEIEVSVEKLERTLKKIKQFYLEVEsEEEKLELLL 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 306 SFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVN 385
Cdd:COG0513 266 KLLKDEDEGRVIVFVRTKRLVEELAESLRKR--GFKVAALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVS 343
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 386 WVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQGMVQQLLQ-KKVPVKEIKINPEKLIDVQKKLESFLAQDQD 464
Cdd:COG0513 344 HVINYDLPLDPEDYVHRIGRTGRAGRKGVAISFVTEEEEVKKLKRIEKrLERKLPSAVLLPLDEPEDAKLLKTTRPGLEE 423

                ....*...
gi 27371129 465 LKERAQRC 472
Cdd:COG0513 424 ESDISDEI 431
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
69-436 2.98e-76

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 251.64  E-value: 2.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEAL----YRLQwtstdglgV 144
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdvkrFRVQ--------A 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  145 LIISPTRELAYQTFEVLRKVGKnhdFSAGLII----GGK-------DLKHEAerinniNILVCTPGRLLQHMD-ETIcfH 212
Cdd:PRK11776  76 LVLCPTRELADQVAKEIRRLAR---FIPNIKVltlcGGVpmgpqidSLEHGA------HIIVGTPGRILDHLRkGTL--D 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  213 ATNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWV---HEKakystpATLE 289
Cdd:PRK11776 145 LDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVestHDL------PAIE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  290 QNYIICELHQKISVLFSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVL 369
Cdd:PRK11776 219 QRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQ--GFSALALHGDLEQRDRDQVLVRFANRSCSVL 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27371129  370 FATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQ--GMVQQLLQKKV 436
Cdd:PRK11776 297 VATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQraNAIEDYLGRKL 365
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
93-263 3.25e-61

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: 333969 [Multi-domain]  Cd Length: 165  Bit Score: 201.69  E-value: 3.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    93 TEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQwtstDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSA 172
Cdd:pfam00270   1 TPIQAQAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALNKKD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   173 GLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHatNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQTLLF 252
Cdd:pfam00270  77 ASLLGGDSRKEQLEKLKGPDILVGTPGRLLDLLRERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 27371129   253 SATQTKSVKDL 263
Cdd:pfam00270 155 SATLPRNLEDL 165
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
13-413 1.28e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 202.06  E-value: 1.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   13 RPDPVRSFNRWKKKHSHRQHQKKERRKQLKKP--EWQVEregisrlmqNYEKINVNEITRFSDFPLSKKTLKGLQEAQYR 90
Cdd:PRK01297  38 APATKAAAPAAAAPRAEKPKKDKPRRERKPKPasLWKLE---------DFVVEPQEGKTRFHDFNLAPELMHAIHDLGFP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   91 LVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLG---VLIISPTRELAYQTFEVLRKVGKN 167
Cdd:PRK01297 109 YCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGeprALIIAPTRELVVQIAKDAAALTKY 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  168 HDFSAGLIIGGKDLKHEAERI--NNINILVCTPGRLLQhMDETICFHATNLQMLVLDEADRILDMGFADTMNAIIENLPK 245
Cdd:PRK01297 189 TGLNVMTFVGGMDFDKQLKQLeaRFCDILVATPGRLLD-FNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPR 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  246 K--RQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYStpATLEQNYIICELHQKISVLFSFLRSHLKKKSIVFFSSC 323
Cdd:PRK01297 268 KeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVAS--DTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRK 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  324 KEVQylyRVFCRL-RPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHR 402
Cdd:PRK01297 346 DEVR---RIEERLvKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHR 422
                        410
                 ....*....|.
gi 27371129  403 AGRTARYKEDG 413
Cdd:PRK01297 423 IGRTGRAGASG 433
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
288-419 4.69e-46

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 159.60  E-value: 4.69e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 288 LEQNYIICELHQKISVLF-SFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRA 366
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 27371129 367 AVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLIL 419
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEXDc smart00487
DEAD-like helicases superfamily;
93-274 3.70e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.88  E-value: 3.70e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129     93 TEIQKQTIGLALQG-KDVLGAAKTGSGKTLAFLVPVLEALYRlqwtsTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFS 171
Cdd:smart00487  10 RPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    172 AGLIIGGKDLKHEAERINN--INILVCTPGRLLQHMDETICFHAtNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQT 249
Cdd:smart00487  85 VVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQL 163
                          170       180
                   ....*....|....*....|....*
gi 27371129    250 LLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:smart00487 164 LLLSATPPEEIENLLELFLNDPVFI 188
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
299-410 1.58e-25

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: 333970 [Multi-domain]  Cd Length: 111  Bit Score: 101.13  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   299 QKISVLFSFL-RSHLKKKSIVFFSSCKEVQYLyrVFCRLRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAAR 377
Cdd:pfam00271   1 EKLEALLELLkLKERGGKVLIFSNTKKRLELL--ELLLEKEGIKVARLHGDLSQEEREEILEDFRNGKIDVLVATDVAAR 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 27371129   378 GLDFPAVNWVLQFDCPEDANTYIHRAGRTARYK 410
Cdd:pfam00271  79 GLDLPDVNLVINYDLPWNPASYIQRIGRAGRAG 111
HELICc smart00490
helicase superfamily c-terminal domain;
327-410 6.01e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 6.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    327 QYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRT 406
Cdd:smart00490   1 EELAELLKEL--GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 27371129    407 ARYK 410
Cdd:smart00490  79 GRAG 82
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
451-510 1.50e-17

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


Pssm-ID: 339021  Cd Length: 60  Bit Score: 76.65  E-value: 1.50e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   451 VQKKLESFLAQDQDLKERAQRCFVSYIR--SVYLMKDkeVFNVSKLPITEYALSLGLAVAPR 510
Cdd:pfam13959   1 IQLQLEKLVLKDRELKELAQKAFVSYVRaySTHLLKD--IFNVKKLDLGHLAKSFGLLEAPK 60
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
96-460 3.46e-15

ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273594 [Multi-domain]  Cd Length: 591  Bit Score: 78.96  E-value: 3.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLGVlIISPTRELAYQTFEVLRKVGKNhdfsAGLI 175
Cdd:TIGR01389  18 QEEIISHVLDGRDVLVVMPTGGGKSLCYQVP---ALLL------KGLTV-VISPLISLMKDQVDQLRAAGVA----AAYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   176 IGGKDLKhEAERI------NNINILVCTPGRLLQ-HMDETIcfHATNLQMLVLDEADRILDMG--FADTMNAI---IENL 243
Cdd:TIGR01389  84 NSTLSAK-EQQDIekalvnGELKLLYVAPERLEQdYFLNML--QRIPIALVAVDEAHCVSQWGhdFRPEYQRLgslAERF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   244 PKkRQTLLFSATQTKSVKD--LARLSLKDPEyvwvHEKAKYSTPatlEQNYIICELHQKISVLFSFLRSHLKKKSIVFFS 321
Cdd:TIGR01389 161 PQ-VPRIALTATADAETRQdiRELLRLADAN----EFITSFDRP---NLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYAS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   322 SCKEVQYLYRVFCRlrPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIH 401
Cdd:TIGR01389 233 SRKKVEELAERLES--QGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQ 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   402 RAGRTARYKEDGEALLILLPSEeqgmvQQLLQKKVpvkEIKINPEKLIDVQ-KKLESFLA 460
Cdd:TIGR01389 311 EAGRAGRDGLPAEAILLYSPAD-----IALLKRRI---EQSEADDDYKQIErEKLRAMIA 362
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
96-458 4.51e-15

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


Pssm-ID: 223588 [Multi-domain]  Cd Length: 590  Bit Score: 78.49  E-value: 4.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLgVLIISPTRELAYQTFEVLRKVGKNhdfsAGLI 175
Cdd:COG0514  22 QQEIIDALLSGKDTLVVMPTGGGKSLCYQIP---ALLL------EGL-TLVVSPLISLMKDQVDQLEAAGIR----AAYL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 176 IGGKDlKHEAERI------NNINILVCTPGRLLQ-HMDETICfhATNLQMLVLDEADRILDMGFA-----DTMNAIIENL 243
Cdd:COG0514  88 NSTLS-REERQQVlnqlksGQLKLLYISPERLMSpRFLELLK--RLPISLVAIDEAHCISQWGHDfrpdyRRLGRLRAGL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 244 PKKrQTLLFSATQTKSVKD--LARLSLKDPEyvwvhekaKYSTPATLEQNYIicELHQKISVL--FSFLRSHLKKKS--- 316
Cdd:COG0514 165 PNP-PVLALTATATPRVRDdiREQLGLQDAN--------IFRGSFDRPNLAL--KVVEKGEPSdqLAFLATVLPQLSksg 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 317 IVFFSSCKEVQYLYRvfcRLRP-GISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPED 395
Cdd:COG0514 234 IIYCLTRKKVEELAE---WLRKnGISAGAYHAGLSNEERERVQQAFLNDEIKVMVATNAFGMGIDKPDVRFVIHYDLPGS 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27371129 396 ANTYIHRAGRTARykeDGE-ALLILLPSEEQGMVQQ--LLQKKVPVKEIKINPEKLIDVQKKLESF 458
Cdd:COG0514 311 IESYYQETGRAGR---DGLpAEAILLYSPEDIRWQRylIEQSKPDEEQKQIELAKLRQMIAYCETQ 373
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
96-435 1.25e-14

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


Pssm-ID: 129701 [Multi-domain]  Cd Length: 470  Bit Score: 76.73  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYrlqwtsTDGLGvLIISPTRELAYQTFEVLrkvgKNHDFSAGLI 175
Cdd:TIGR00614  16 QLEVINAVLLGRDCFVVMPTGGGKSLCYQLP---ALC------SDGIT-LVISPLISLMEDQVLQL----KASGIPATFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   176 IGGKDLKHEAE-----RINNINILVCTP------GRLLQHMDETIcfhatNLQMLVLDEADRILDMG--FADT---MNAI 239
Cdd:TIGR00614  82 NSSQSKEQQKNvltdlKDGKIKLLYVTPekcsasNRLLQTLEERK-----GITLIAVDEAHCISQWGhdFRPDykaLGSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   240 IENLPKKRQTLLfSATQTKSV-KDLAR-LSLKDPE-----------YVWVHEKakysTPATLEQnyiicelhqkisvLFS 306
Cdd:TIGR00614 157 KQKFPNVPIMAL-TATASPSVrEDILRqLNLKNPQifctsfdrpnlYYEVRRK----TPKILED-------------LLR 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   307 FLRSHLKKKS-IVFFSSCKEVQylyRVFCRLRP-GISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAV 384
Cdd:TIGR00614 219 FIRKEFKGKSgIIYCPSRKKSE---QVTASLQNlGIAAGAYHAGLEISARDDVHHKFQRDEIQVVVATVAFGMGINKPDV 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   385 NWVLQFDCPEDANTYIHRAGRTARYKEDGEALLI-----------LLPSEEQGMVQQLLQKK 435
Cdd:TIGR00614 296 RFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFyapadinrlrrLLMEEPDGQQRTYKLKL 357
 
Name Accession Description Interval E-value
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
80-277 3.71e-143

DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350699 [Multi-domain]  Cd Length: 198  Bit Score: 415.15  E-value: 3.71e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17941   1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLGALIISPTRELAMQIFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMNAI 239
Cdd:cd17941  81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAI 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27371129 240 IENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVH 277
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISVH 198
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
69-472 3.03e-118

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


Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 363.34  E-value: 3.03e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLqwTSTDGLGVLIIS 148
Cdd:COG0513  29 PEFASLGLSPELLQALKDLGFEEPTPIQLAAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQKILKS--VERKYVSALILA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 149 PTRELAYQTFEVLRKVGKNH-DFSAGLIIGGKDLKHEAERIN-NINILVCTPGRLLQHMDETIcFHATNLQMLVLDEADR 226
Cdd:COG0513 107 PTRELAVQIAEELRKLGKNLgGLRVAVVYGGVSIRKQIEALKrGVDIVVATPGRLLDLIKRGK-LDLSGVETLVLDEADR 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 227 ILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYSTPATLEQNYIICE-LHQKISVLF 305
Cdd:COG0513 186 MLDMGFIDDIEKILKALPPDRQTLLFSATMPDDIRELARRYLNDPVEIEVSVEKLERTLKKIKQFYLEVEsEEEKLELLL 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 306 SFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVN 385
Cdd:COG0513 266 KLLKDEDEGRVIVFVRTKRLVEELAESLRKR--GFKVAALHGDLPQEERDRALEKFKDGELRVLVATDVAARGLDIPDVS 343
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 386 WVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQGMVQQLLQ-KKVPVKEIKINPEKLIDVQKKLESFLAQDQD 464
Cdd:COG0513 344 HVINYDLPLDPEDYVHRIGRTGRAGRKGVAISFVTEEEEVKKLKRIEKrLERKLPSAVLLPLDEPEDAKLLKTTRPGLEE 423

                ....*...
gi 27371129 465 LKERAQRC 472
Cdd:COG0513 424 ESDISDEI 431
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
80-274 1.38e-82

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 259.21  E-value: 1.38e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17942   1 TLKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTGVIIISPTRELALQIYG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMNA 238
Cdd:cd17942  81 VAKELLKYHSQTFGIVIGGANRKAEAEKLgKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27371129 239 IIENLPKKRQTLLFSATQTKSVKDLARLSLKD-PEYV 274
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDLARISLKKkPLYV 197
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
80-274 1.23e-80

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 253.90  E-value: 1.23e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDETIcFHATNLQMLVLDEADRILDMGFADTMNA 238
Cdd:cd00268  81 VARKLGKGTGLKVAAIYGGAPIKKQIEALkKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27371129 239 IIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
69-436 2.98e-76

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 251.64  E-value: 2.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEAL----YRLQwtstdglgV 144
Cdd:PRK11776   4 TAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdvkrFRVQ--------A 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  145 LIISPTRELAYQTFEVLRKVGKnhdFSAGLII----GGK-------DLKHEAerinniNILVCTPGRLLQHMD-ETIcfH 212
Cdd:PRK11776  76 LVLCPTRELADQVAKEIRRLAR---FIPNIKVltlcGGVpmgpqidSLEHGA------HIIVGTPGRILDHLRkGTL--D 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  213 ATNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWV---HEKakystpATLE 289
Cdd:PRK11776 145 LDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVestHDL------PAIE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  290 QNYIICELHQKISVLFSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVL 369
Cdd:PRK11776 219 QRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQ--GFSALALHGDLEQRDRDQVLVRFANRSCSVL 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27371129  370 FATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQ--GMVQQLLQKKV 436
Cdd:PRK11776 297 VATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQraNAIEDYLGRKL 365
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
69-408 8.96e-72

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 239.07  E-value: 8.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIIS 148
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  149 PTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERIN-NINILVCTPGRLLQHMDETiCFHATNLQMLVLDEADRI 227
Cdd:PRK11192  81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSeNQDIVVATPGRLLQYIKEE-NFDCRAVETLILDEADRM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  228 LDMGFADTMNAIIENLPKKRQTLLFSAT-QTKSVKDLARLSLKDPEYVWVH----EKAKystpatLEQNYIICE-LHQKI 301
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATlEGDAVQDFAERLLNDPVEVEAEpsrrERKK------IHQWYYRADdLEHKT 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  302 SVLFSFLRSHLKKKSIVFFSSCKEVQYLyRVFCRLRpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDF 381
Cdd:PRK11192 234 ALLCHLLKQPEVTRSIVFVRTRERVHEL-AGWLRKA-GINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDI 311
                        330       340
                 ....*....|....*....|....*..
gi 27371129  382 PAVNWVLQFDCPEDANTYIHRAGRTAR 408
Cdd:PRK11192 312 DDVSHVINFDMPRSADTYLHRIGRTGR 338
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
81-271 3.23e-68

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 221.36  E-value: 3.23e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEalyRLQWTSTDGLG--VLIISPTRELAYQTF 158
Cdd:cd17947   2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILE---RLLYRPKKKAAtrVLVLVPTRELAMQCF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 159 EVLRKVGKNHDFSAGLIIGGKDLK-HEAERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMN 237
Cdd:cd17947  79 SVLQQLAQFTDITFALAVGGLSLKaQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELK 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 27371129 238 AIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17947 159 EILRLCPRTRQTMLFSATMTDEVKDLAKLSLNKP 192
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
93-274 1.58e-64

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


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 212.45  E-value: 1.58e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  93 TEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQ--WTSTDGLGVLIISPTRELAYQTFEVLRKVGKN-HD 169
Cdd:cd17949  15 TAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEprVDRSDGTLALVLVPTRELALQIYEVLEKLLKPfHW 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 170 FSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFADTMNAIIE------- 241
Cdd:cd17949  95 IVPGYLIGGEKRKSEKARLrKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEllddkrs 174
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27371129 242 ------NLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17949 175 kaggekSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
80-274 1.17e-62

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 207.04  E-value: 1.17e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYR--LQWTSTDgLGVLIISPTRELAYQT 157
Cdd:cd17960   1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKrkANLKKGQ-VGALIISPTRELATQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 158 FEVLRKVGKNHD--FSAGLIIGGKDLKHEAERI--NNINILVCTPGRL---LQHMDETICFhaTNLQMLVLDEADRILDM 230
Cdd:cd17960  80 YEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFkrNGPNILVGTPGRLeelLSRKADKVKV--KSLEVLVLDEADRLLDL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27371129 231 GFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17960 158 GFEADLNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
93-263 3.25e-61

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: 333969 [Multi-domain]  Cd Length: 165  Bit Score: 201.69  E-value: 3.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    93 TEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQwtstDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSA 172
Cdd:pfam00270   1 TPIQAQAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALNKKD----NGPQALVLAPTRELAEQIYEELKKLGKGLGLKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   173 GLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHatNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQTLLF 252
Cdd:pfam00270  77 ASLLGGDSRKEQLEKLKGPDILVGTPGRLLDLLRERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLL 154
                         170
                  ....*....|.
gi 27371129   253 SATQTKSVKDL 263
Cdd:pfam00270 155 SATLPRNLEDL 165
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
71-441 2.52e-60

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 212.12  E-value: 2.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYR---LQWTSTDGLGVLII 147
Cdd:PRK04537  11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSrpaLADRKPEDPRALIL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  148 SPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLL----QHmdETICFHATnlQMLVLD 222
Cdd:PRK04537  91 APTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQgVDVIIATPGRLIdyvkQH--KVVSLHAC--EICVLD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  223 EADRILDMGFADTMNAIIENLPKK--RQTLLFSATQTKSVKDLARLSLKDPEYVWVheKAKYSTPATLEQNYIICELHQK 300
Cdd:PRK04537 167 EADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVV--ETETITAARVRQRIYFPADEEK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  301 ISVLFSFLRSHLKKKSIVFFSSCKEVQYLYRVFcrLRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLD 380
Cdd:PRK04537 245 QTLLLGLLSRSEGARTMVFVNTKAFVERVARTL--ERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLH 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27371129  381 FPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEAllILLPSEEQGM----VQQLLQKKVPVKEI 441
Cdd:PRK04537 323 IDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDA--ISFACERYAMslpdIEAYIEQKIPVEPV 385
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
71-274 1.97e-59

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 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: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 198.30  E-value: 1.97e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEalyRLQWTSTD-GLGVLIISP 149
Cdd:cd17959   3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIE---KLKAHSPTvGARALILSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 150 TRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDEtICFHATNLQMLVLDEADRIL 228
Cdd:cd17959  80 TRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALaSNPDIIIATPGRLLHLLVE-MNLKLSSVEYVVFDEADRLF 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27371129 229 DMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
71-271 2.95e-58

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 195.23  E-value: 2.95e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyrlqWTSTDGLGVLIISPT 150
Cdd:cd17954   2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL----LENPQRFFALVLAPT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 151 RELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILD 229
Cdd:cd17954  78 RELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALaKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLN 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 230 MGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17954 158 MDFEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
13-413 1.28e-57

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 202.06  E-value: 1.28e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   13 RPDPVRSFNRWKKKHSHRQHQKKERRKQLKKP--EWQVEregisrlmqNYEKINVNEITRFSDFPLSKKTLKGLQEAQYR 90
Cdd:PRK01297  38 APATKAAAPAAAAPRAEKPKKDKPRRERKPKPasLWKLE---------DFVVEPQEGKTRFHDFNLAPELMHAIHDLGFP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   91 LVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLG---VLIISPTRELAYQTFEVLRKVGKN 167
Cdd:PRK01297 109 YCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGeprALIIAPTRELVVQIAKDAAALTKY 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  168 HDFSAGLIIGGKDLKHEAERI--NNINILVCTPGRLLQhMDETICFHATNLQMLVLDEADRILDMGFADTMNAIIENLPK 245
Cdd:PRK01297 189 TGLNVMTFVGGMDFDKQLKQLeaRFCDILVATPGRLLD-FNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPR 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  246 K--RQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYStpATLEQNYIICELHQKISVLFSFLRSHLKKKSIVFFSSC 323
Cdd:PRK01297 268 KeeRQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVAS--DTVEQHVYAVAGSDKYKLLYNLVTQNPWERVMVFANRK 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  324 KEVQylyRVFCRL-RPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHR 402
Cdd:PRK01297 346 DEVR---RIEERLvKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHR 422
                        410
                 ....*....|.
gi 27371129  403 AGRTARYKEDG 413
Cdd:PRK01297 423 IGRTGRAGASG 433
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
76-274 6.95e-57

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 191.64  E-value: 6.95e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  76 LSKKTLKGLQEAQYRLVTEIQKQTIGLALQ-GKDVLGAAKTGSGKTLAFLVPVLEALYR-LQWTSTDGLGVLIISPTREL 153
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNtKPAGRRSGVSALIISPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 154 AYQTFEVLRKV-GKNHDFSAGLIIGGKDLKHEAERI--NNINILVCTPGRLLQHMDET---ICFhaTNLQMLVLDEADRI 227
Cdd:cd17964  81 ALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLrrGRPDILVATPGRLIDHLENPgvaKAF--TDLDYLVLDEADRL 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27371129 228 LDMGFADTMNAIIENLPKK----RQTLLFSATQTKSVKDLARLSL-KDPEYV 274
Cdd:cd17964 159 LDMGFRPDLEQILRHLPEKnadpRQTLLFSATVPDEVQQIARLTLkKDYKFI 210
PTZ00110 PTZ00110
helicase; Provisional
67-421 1.17e-56

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 201.16  E-value: 1.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   67 EITRFSDFplskkTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPV---LEALYRLQWTstDGLG 143
Cdd:PTZ00110 133 EYTSFPDY-----ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAivhINAQPLLRYG--DGPI 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  144 VLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGG--KDLKHEAERiNNINILVCTPGRLLQHMDETIcfhaTNLQ---M 218
Cdd:PTZ00110 206 VLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGvpKRGQIYALR-RGVEILIACPGRLIDFLESNV----TNLRrvtY 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  219 LVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLAR-LSLKDPEYVWVHEkAKYSTPATLEQNYIICEL 297
Cdd:PTZ00110 281 LVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARdLCKEEPVHVNVGS-LDLTACHNIKQEVFVVEE 359
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  298 HQKISVLFSFLRSHLKK--KSIVFFSSCKEVQYLYRVFcRLRpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIA 375
Cdd:PTZ00110 360 HEKRGKLKMLLQRIMRDgdKILIFVETKKGADFLTKEL-RLD-GWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVA 437
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 27371129  376 ARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLP 421
Cdd:PTZ00110 438 SRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
69-450 4.90e-55

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 193.65  E-value: 4.90e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyrLQWTSTDGLGV---- 144
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYL--LSHPAPEDRKVnqpr 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  145 -LIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDETIcFHATNLQMLVLD 222
Cdd:PRK04837  86 aLIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESgVDILIGTTGRLIDYAKQNH-INLGAIQVVVLD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  223 EADRILDMGFADTMNAIIENLP--KKRQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYSTPATLEQNYIICElhQK 300
Cdd:PRK04837 165 EADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNE--EK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  301 ISVLFSFLRSHLKKKSIVFFS---SCKEV-QYL----YRVfcrlrpGIsilaLHGRQQQMRRMEVYNEFVRKRAAVLFAT 372
Cdd:PRK04837 243 MRLLQTLIEEEWPDRAIIFANtkhRCEEIwGHLaadgHRV------GL----LTGDVAQKKRLRILEEFTRGDLDILVAT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  373 DIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEAllILLPSEEQGM----VQQLLQKKVPVKeiKINPEKL 448
Cdd:PRK04837 313 DVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHS--ISLACEEYALnlpaIETYIGHSIPVS--KYDSDAL 388

                 ..
gi 27371129  449 ID 450
Cdd:PRK04837 389 LT 390
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
71-276 1.73e-54

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 185.12  E-value: 1.73e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyrlqwtSTDGLGV--LIIS 148
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL------SEDPYGIfaLVLT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 149 PTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNI-NILVCTPGRLLQHM----DETICFHatNLQMLVLDE 223
Cdd:cd17955  75 PTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRpHIVVATPGRLADHLrssdDTTKVLS--RVKFLVLDE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27371129 224 ADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPeYVWV 276
Cdd:cd17955 153 ADRLLTGSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKP-FFWE 204
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
69-463 7.13e-52

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 189.67  E-value: 7.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwTSTDGLGVLIIS 148
Cdd:PRK11634   6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD----PELKAPQILVLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  149 PTRELAYQTFEVLRKVGKN-HDFSAGLIIGGK--DLKHEAERiNNINILVCTPGRLLQHMDETIcFHATNLQMLVLDEAD 225
Cdd:PRK11634  82 PTRELAVQVAEAMTDFSKHmRGVNVVALYGGQryDVQLRALR-QGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDEAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  226 RILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVheKAKYSTPATLEQNYIICELHQKISVLF 305
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI--QSSVTTRPDISQSYWTVWGMRKNEALV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  306 SFLRSHLKKKSIVFF---SSCKEVQYLYRvfcrlRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFP 382
Cdd:PRK11634 238 RFLEAEDFDAAIIFVrtkNATLEVAEALE-----RNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  383 AVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLI-------LLPSEEQGMvqqllqkKVPVKEIKINPEKLIDvQKKL 455
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFvenrerrLLRNIERTM-------KLTIPEVELPNAELLG-KRRL 384

                 ....*...
gi 27371129  456 ESFLAQDQ 463
Cdd:PRK11634 385 EKFAAKVQ 392
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
71-437 1.23e-51

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 185.40  E-value: 1.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGV--LIIS 148
Cdd:PRK10590   3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVraLILT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  149 PTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQhMDETICFHATNLQMLVLDEADRI 227
Cdd:PRK10590  83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLrGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  228 LDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVwvhEKAKYSTPA-TLEQNYIICELHQKISVLFS 306
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEI---EVARRNTASeQVTQHVHFVDKKRKRELLSQ 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  307 FLRSHLKKKSIVFFSSCKEVQYLYRVFCrlRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNW 386
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLN--KDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPH 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27371129  387 VLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQGM--VQQLLQKKVP 437
Cdd:PRK10590 317 VVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLrdIEKLLKKEIP 369
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
68-433 2.98e-49

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 180.37  E-value: 2.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   68 ITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLE--ALYRLQWTSTD-GLGV 144
Cdd:PLN00206 120 ILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcCTIRSGHPSEQrNPLA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  145 LIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDEticfHATNLQ---MLV 220
Cdd:PLN00206 200 MVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQgVELIVGTPGRLIDLLSK----HDIELDnvsVLV 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  221 LDEADRILDMGFADTMNAIIENLPKKrQTLLFSATQTKSVKDLARLSLKDPEYVWVHEKAKYStpATLEQNYIICELHQK 300
Cdd:PLN00206 276 LDEVDCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPN--KAVKQLAIWVETKQK 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  301 ISVLFSFLRS--HLKKKSIVFFSSCKEVQYLYRVFcRLRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARG 378
Cdd:PLN00206 353 KQKLFDILKSkqHFKPPAVVFVSSRLGADLLANAI-TVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRG 431
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27371129  379 LDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEAlLILLPSEEQGMVQQLLQ 433
Cdd:PLN00206 432 VDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTA-IVFVNEEDRNLFPELVA 485
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
71-276 1.32e-48

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 169.59  E-value: 1.32e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLG------V 144
Cdd:cd17967   2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVGRGRrkaypsA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 145 LIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMD-ETICFhaTNLQMLVLD 222
Cdd:cd17967  82 LILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLlRGCDILVATPGRLVDFIErGRISL--SSIKFLVLD 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27371129 223 EADRILDMGFADTMNAIIE--NLPKK--RQTLLFSATQTKSVKDLARLSLKDpeYVWV 276
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEhpDMPPKgeRQTLMFSATFPREIQRLAADFLKN--YIFL 215
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
71-271 7.00e-48

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 167.09  E-value: 7.00e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwTSTDGLGVLIISPT 150
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKID----PKKDVIQALILVPT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 151 RELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDETICfHATNLQMLVLDEADRILD 229
Cdd:cd17940  77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQtVHVLVGTPGRILDLAKKGVA-DLSHCKTLVLDEADKLLS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 230 MGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17940 156 QDFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNP 197
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
81-271 9.44e-48

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: 166.61  E-value: 9.44e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQwtSTDGLGVLIISPTRELAYQTFEV 160
Cdd:cd17957   2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPR--KKKGLRALILAPTRELASQIYRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 161 LRKVGKNHDFSAGLIIGG--KDLKHEAERINNINILVCTPGRLLQHM-DETICFhaTNLQMLVLDEADRILDMGFADTMN 237
Cdd:cd17957  80 LLKLSKGTGLRIVLLSKSleAKAKDGPKSITKYDILVSTPLRLVFLLkQGPIDL--SSVEYLVLDEADKLFEPGFREQTD 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 27371129 238 AIIENLP-KKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17957 158 EILAACTnPNLQRSLFSATIPSEVEELARSVMKDP 192
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
288-419 4.69e-46

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 159.60  E-value: 4.69e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 288 LEQNYIICELHQKISVLF-SFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRA 366
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 27371129 367 AVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLIL 419
Cdd:cd18787  79 RVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
81-274 8.38e-45

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 159.41  E-value: 8.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRL----QWTSTDGLGVLIISPTRELAYQ 156
Cdd:cd17945   2 LRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLppldEETKDDGPYALILAPTRELAQQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 157 TFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDEticfHATNL---QMLVLDEADRILDMGF 232
Cdd:cd17945  82 IEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNgCEILIATPGRLLDCLER----RLLVLnqcTYVVLDEADRMIDMGF 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129 233 ADTMNAIIENLP--------------------KKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17945 158 EPQVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
DEXDc smart00487
DEAD-like helicases superfamily;
93-274 3.70e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.88  E-value: 3.70e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129     93 TEIQKQTIGLALQG-KDVLGAAKTGSGKTLAFLVPVLEALYRlqwtsTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFS 171
Cdd:smart00487  10 RPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR-----GKGGRVLVLVPTRELAEQWAEELKKLGPSLGLK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    172 AGLIIGGKDLKHEAERINN--INILVCTPGRLLQHMDETICFHAtNLQMLVLDEADRILDMGFADTMNAIIENLPKKRQT 249
Cdd:smart00487  85 VVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDKLSLS-NVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQL 163
                          170       180
                   ....*....|....*....|....*
gi 27371129    250 LLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:smart00487 164 LLLSATPPEEIENLLELFLNDPVFI 188
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
59-276 1.93e-43

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 157.05  E-value: 1.93e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  59 NYEKINVN--------EITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEA 130
Cdd:cd18052  25 KYDEIPVEvtgrnpppAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 131 LYRLQWTSTDGLGV-----LIISPTRELAYQTFEVLRKvgknhdFSAGLII------GGKDLKHEAERI-NNINILVCTP 198
Cdd:cd18052 105 MMKEGLTASSFSEVqepqaLIVAPTRELANQIFLEARK------FSYGTCIrpvvvyGGVSVGHQIRQIeKGCHILVATP 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 199 GRLLQHMD-ETICFhaTNLQMLVLDEADRILDMGFADTMNAIIE--NLPKK--RQTLLFSATQTKSVKDLARLSLKdPEY 273
Cdd:cd18052 179 GRLLDFIGrGKISL--SKLKYLILDEADRMLDMGFGPEIRKLVSepGMPSKedRQTLMFSATFPEEIQRLAAEFLK-EDY 255

                ...
gi 27371129 274 VWV 276
Cdd:cd18052 256 LFL 258
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
68-271 3.71e-42

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 152.15  E-value: 3.71e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  68 ITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyRLQWTSTDGLG--VL 145
Cdd:cd17953  11 IQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHI-KDQRPVKPGEGpiGL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 146 IISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHE-AERINNINILVCTPGRLLqhmdETICFHA---TNLQ---M 218
Cdd:cd17953  90 IMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQiAELKRGAEIVVCTPGRMI----DILTANNgrvTNLRrvtY 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27371129 219 LVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17953 166 VVLDEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
81-271 2.65e-41

DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350724 [Multi-domain]  Cd Length: 197  Bit Score: 148.67  E-value: 2.65e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVL---EALYRLQwtSTDGLGVLIISPTRELAYQT 157
Cdd:cd17966   2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhiNAQPPLE--RGDGPIVLVLAPTRELAQQI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 158 FEVLRKVGKNHDFSAGLIIGG-------KDLKHEAErinninILVCTPGRLLQHMDETicfhATNLQ---MLVLDEADRI 227
Cdd:cd17966  80 QQEANKFGGSSRLRNTCVYGGapkgpqiRDLRRGVE------ICIATPGRLIDFLDQG----KTNLRrvtYLVLDEADRM 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27371129 228 LDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17966 150 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
81-271 5.42e-41

DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 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: 350709 [Multi-domain]  Cd Length: 206  Bit Score: 148.26  E-value: 5.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPV----LEALYRLQWTSTDGLGVLIISPTRELAYQ 156
Cdd:cd17951   2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLimfaLEQEKKLPFIKGEGPYGLIVCPSRELARQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 157 TFEVLRKVGKNhdFSAG--------LIIGGKDLKHEAERINN-INILVCTPGRLlQHMDETICFHATNLQMLVLDEADRI 227
Cdd:cd17951  82 THEVIEYYCKA--LQEGgypqlrclLCIGGMSVKEQLEVIRKgVHIVVATPGRL-MDMLNKKKINLDICRYLCLDEADRM 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27371129 228 LDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17951 159 IDMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKP 202
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
81-271 5.72e-40

DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor 3B-Associated 125 kDa Protein, RHELP, or RNAHP) is an NTPase with a preference for ATP, the hydrolysis of which is enhanced by various RNA substrates. It acts as a non-processive RNA helicase with protein displacement and RNA annealing activities. DDX42 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350710 [Multi-domain]  Cd Length: 197  Bit Score: 145.25  E-value: 5.72e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVL-EALYRLQWTSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17952   2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvHIMDQRELEKGEGPIAVIVAPTRELAQQIYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKNHDFSAGLIIGG-------KDLKHEAErinninILVCTPGRLLQHmdetICFHATNLQ---MLVLDEADRILD 229
Cdd:cd17952  82 EAKKFGKAYNLRVVAVYGGgskweqaKALQEGAE------IVVATPGRLIDM----VKKKATNLQrvtYLVLDEADRMFD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 230 MGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17952 152 MGFEYQVRSIVGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
76-271 3.51e-39

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 143.11  E-value: 3.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  76 LSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTS--TDGLGVLIISPTREL 153
Cdd:cd17961   1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESgeEQGTRALILVPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 154 AYQTFEVLRKVGK---NHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDM 230
Cdd:cd17961  81 AQQVSKVLEQLTAycrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27371129 231 GFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNP 201
PTZ00424 PTZ00424
helicase 45; Provisional
59-427 1.27e-37

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 144.58  E-value: 1.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   59 NYEKInvneITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFlvpVLEALYRLQWtS 138
Cdd:PTZ00424  22 NYDEI----VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATF---VIAALQLIDY-D 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  139 TDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDETiCFHATNLQ 217
Cdd:PTZ00424  94 LNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAgVHMVVGTPGRVYDMIDKR-HLRVDDLK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  218 MLVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWVheKAKYSTPATLEQNYIICEL 297
Cdd:PTZ00424 173 LFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILV--KKDELTLEGIRQFYVAVEK 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  298 HQ-KISVLFSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLRPGISilALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAA 376
Cdd:PTZ00424 251 EEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVS--CMHGDMDQKDRDLIMREFRSGSTRVLITTDLLA 328
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 27371129  377 RGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEEQGM 427
Cdd:PTZ00424 329 RGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQL 379
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
80-274 1.27e-37

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 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: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 138.55  E-value: 1.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRlqwtSTDGLGVLIISPTRELAYQTFE 159
Cdd:cd17943   1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDL----ERRHPQVLILAPTREIAVQIHD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 160 VLRKVGKN-HDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLqHMDETICFHATNLQMLVLDEADRILDMGFADTMNA 238
Cdd:cd17943  77 VFKKIGKKlEGLKCEVFIGGTPVKEDKKKLKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27371129 239 IIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
81-289 1.34e-37

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 139.68  E-value: 1.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLAL-QGKDVLGAAKTGSGKTLAFLVPVLEALYRLQ-----WTSTDGLGVLIISPTRELA 154
Cdd:cd17946   2 LRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSQKssngvGGKQKPLRALILTPTRELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 155 YQTFEVLRKVGKNHDFSAGLIIGG-------KDLKHEAErinninILVCTPGRLLQHMDETiCFHATNLQ---MLVLDEA 224
Cdd:cd17946  82 VQVKDHLKAIAKYTNIKIASIVGGlavqkqeRLLKKRPE------IVVATPGRLWELIQEG-NEHLANLKslrFLVLDEA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129 225 DRILDMGFADTMNAIIENLP-------KKRQTLLFSATQTKSVKDLARLSLKDpeyvwvhEKAKYSTPATLE 289
Cdd:cd17946 155 DRMLEKGHFAELEKILELLNkdragkkRKRQTFVFSATLTLDHQLPLKLNSKK-------KKKKKEKKQKLE 219
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
71-276 3.68e-37

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 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: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 137.45  E-value: 3.68e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwtstdglgVLIISPT 150
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIVV-----------ALILEPS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 151 RELAYQTFEVLRKVGK---NHDFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQH-MDETICFhaTNLQMLVLDEAD 225
Cdd:cd17938  70 RELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLeSGVDIVVGTPGRLEDLiKTGKLDL--SSVRFFVLDEAD 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27371129 226 RILDMGFADTMNAIIENLPK-----KR-QTLLFSAT-QTKSVKDLARLSLKDPeyVWV 276
Cdd:cd17938 148 RLLSQGNLETINRIYNRIPKitsdgKRlQVIVCSATlHSFEVKKLADKIMHFP--TWV 203
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
59-265 9.31e-37

DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 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: 350809 [Multi-domain]  Cd Length: 249  Bit Score: 137.86  E-value: 9.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  59 NYEKINVN--------EITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEA 130
Cdd:cd18051   3 KYEDIPVEatgencppHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 131 LY-----RLQWTSTDGLG-------VLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLK---HEAERinNINILV 195
Cdd:cd18051  83 IYeqgpgESLPSESGYYGrrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGqqmRDLER--GCHLLV 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27371129 196 CTPGRLLQhMDETICFHATNLQMLVLDEADRILDMGFADTMNAIIE--NLPKK--RQTLLFSATQTKSVKDLAR 265
Cdd:cd18051 161 ATPGRLVD-MLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPTgeRQTLMFSATFPKEIQMLAR 233
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
76-271 1.44e-33

DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350721 [Multi-domain]  Cd Length: 196  Bit Score: 126.92  E-value: 1.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  76 LSKKTLKGLQEAQYRLVTEIQKQTIGLALQG--KDVLGAAKTGSGKTLAFLVPVLEAL-YRLQWTStdglgVLIISPTRE 152
Cdd:cd17963   1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVdPTLKSPQ-----ALCLAPTRE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 153 LAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEaERINNiNILVCTPGRLLQHMDeTICFHATNLQMLVLDEADRILDM-G 231
Cdd:cd17963  76 LARQIGEVVEKMGKFTGVKVALAVPGNDVPRG-KKITA-QIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTqG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27371129 232 FADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNA 192
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
60-274 1.52e-33

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 128.13  E-value: 1.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  60 YEKINVNEITRFsdFPLSKKTLKGLQEAQyrlvteiqkqTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSt 139
Cdd:cd17956   2 LKNLQNNGITSA--FPVQAAVIPWLLPSS----------KSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPR- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 140 dgLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERI---------NNINILVCTPGRLLQHMDETIC 210
Cdd:cd17956  69 --LRALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLlvdtsgrylSRVDILVATPGRLVDHLNSTPG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 211 FHATNLQMLVLDEADRILDMGFAD----TMNAI----------------IENLPKKRQTLLFSATQTKSVKDLARLSLKD 270
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFQDwletVMKALgrptapdlgsfgdanlLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226

                ....
gi 27371129 271 PEYV 274
Cdd:cd17956 227 PRLF 230
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
84-271 3.04e-33

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development.Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 126.12  E-value: 3.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  84 LQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVL-EALyrlqwTSTDGLGVLIISPTRELAYQTFEVLR 162
Cdd:cd17962   5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIiRCL-----TEHRNPSALILTPTRELAVQIEDQAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 163 KVGKNH-DFSAGLIIGGKDLKHEAERI-NNINILVCTPGRLLQHMDETiCFHATNLQMLVLDEADRILDMGFADTMNAII 240
Cdd:cd17962  80 ELMKGLpPMKTALLVGGLPLPPQLYRLqQGVKVIIATPGRLLDILKQS-SVELDNIKIVVVDEADTMLKMGFQQQVLDIL 158
                       170       180       190
                ....*....|....*....|....*....|.
gi 27371129 241 ENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17962 159 ENISHDHQTILVSATIPRGIEQLAGQLLQNP 189
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
73-271 4.37e-32

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 123.20  E-value: 4.37e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  73 DFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwTSTDGLGVLIISPTRE 152
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRID----TTVRETQALVLAPTRE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 153 LAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERIN-NINILVCTPGRLLqHMDETICFHATNLQMLVLDEADRILDMG 231
Cdd:cd17939  77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQyGPHIVVGTPGRVF-DMLQRRSLRTDKIKMFVLDEADEMLSRG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27371129 232 FADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd17939 156 FKDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
68-270 8.98e-31

DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 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: 350807 [Multi-domain]  Cd Length: 234  Bit Score: 120.50  E-value: 8.98e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  68 ITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTST-DGLGVLI 146
Cdd:cd18049  23 VLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERgDGPICLV 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 147 ISPTRELAYQTFEVLRKVGKNHDFSAGLIIGG-------KDLKHEAErinninILVCTPGRLLQHMDETicfhATNLQ-- 217
Cdd:cd18049 103 LAPTRELAQQVQQVAAEYGRACRLKSTCIYGGapkgpqiRDLERGVE------ICIATPGRLIDFLEAG----KTNLRrc 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371129 218 -MLVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKD 270
Cdd:cd18049 173 tYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
68-270 1.20e-30

DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 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: 350808  Cd Length: 271  Bit Score: 121.27  E-value: 1.20e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  68 ITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTST-DGLGVLI 146
Cdd:cd18050  61 VFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERgDGPICLV 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 147 ISPTRELAYQTFEVLRKVGKNHDFSAGLIIGG-------KDLKHEAErinninILVCTPGRLLQHMDETicfhATNLQ-- 217
Cdd:cd18050 141 LAPTRELAQQVQQVADDYGKSSRLKSTCIYGGapkgpqiRDLERGVE------ICIATPGRLIDFLEAG----KTNLRrc 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371129 218 -MLVLDEADRILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKD 270
Cdd:cd18050 211 tYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
81-274 3.90e-30

DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350716 [Multi-domain]  Cd Length: 197  Bit Score: 117.57  E-value: 3.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  81 LKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRLQWTST-----DGLGVLIISPTRELAY 155
Cdd:cd17958   2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLP---GFIHLDLQPIpreqrNGPGVLVLTPTRELAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 156 QTFEVLRKVGKNhDFSAGLIIGGKDLKHEAERINN-INILVCTPGRL--LQhMDETIcfHATNLQMLVLDEADRILDMGF 232
Cdd:cd17958  79 QIEAECSKYSYK-GLKSVCVYGGGNRNEQIEDLSKgVDIIIATPGRLndLQ-MNNVI--NLKSITYLVLDEADRMLDMGF 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 233 ADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd17958 155 EPQIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
80-269 1.32e-28

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 113.40  E-value: 1.32e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  80 TLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLG--VLIISPTRELAYQT 157
Cdd:cd17944   1 TIKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkVLVLAPTRELANQV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 158 FEVLRKVGKNhdFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMdETICFHATNLQMLVLDEADRILDMGFADTM 236
Cdd:cd17944  81 TKDFKDITRK--LSVACFYGGTPYQQQIFAIRNgIDILVGTPGRIKDHL-QNGRLDLTKLKHVVLDEVDQMLDMGFAEQV 157
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27371129 237 NAIIENLPKKR-----QTLLFSATQTKSVKDLARLSLK 269
Cdd:cd17944 158 EEILSVSYKKDsednpQTLLFSATCPDWVYNVAKKYMK 195
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
69-276 1.12e-26

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 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: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 107.82  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  69 TRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwTSTDGLGVLIIS 148
Cdd:cd17950   2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE----PVDGQVSVLVIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 149 PTRELAYQ-TFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNI--NILVCTPGRLLQHMDETIcFHATNLQMLVLDEAD 225
Cdd:cd17950  78 HTRELAFQiSNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLKNKcpHIVVGTPGRILALVREKK-LKLSHVKHFVLDECD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371129 226 RI---LDMGfADtMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYVWV 276
Cdd:cd17950 157 KMleqLDMR-RD-VQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
71-271 5.70e-26

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are 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: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 105.61  E-value: 5.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYrlqwTSTDGLGVLIISPT 150
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQID----TSLKATQALVLAPT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 151 RELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQHMDETIcFHATNLQMLVLDEADRILD 229
Cdd:cd18046  77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAgPHIVVGTPGRVFDMINRRY-LRTDYIKMFVLDEADEMLS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 230 MGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
71-271 1.32e-25

DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 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: 350803 [Multi-domain]  Cd Length: 201  Bit Score: 104.47  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyRLQWTSTDglgVLIISPT 150
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL-DIQVRETQ---ALILSPT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 151 RELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINN-INILVCTPGRLLQhMDETICFHATNLQMLVLDEADRILD 229
Cdd:cd18045  77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYgQHIVSGTPGRVFD-MIRRRSLRTRHIKMLVLDEADEMLN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27371129 230 MGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDP 271
Cdd:cd18045 156 KGFKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
299-410 1.58e-25

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: 333970 [Multi-domain]  Cd Length: 111  Bit Score: 101.13  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   299 QKISVLFSFL-RSHLKKKSIVFFSSCKEVQYLyrVFCRLRPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAAR 377
Cdd:pfam00271   1 EKLEALLELLkLKERGGKVLIFSNTKKRLELL--ELLLEKEGIKVARLHGDLSQEEREEILEDFRNGKIDVLVATDVAAR 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 27371129   378 GLDFPAVNWVLQFDCPEDANTYIHRAGRTARYK 410
Cdd:pfam00271  79 GLDLPDVNLVINYDLPWNPASYIQRIGRAGRAG 111
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
84-263 2.81e-24

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 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: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 101.67  E-value: 2.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  84 LQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyrLQWTSTDGLG-----VLIISPTRELAYQTF 158
Cdd:cd17948   5 LQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRL--LRYKLLAEGPfnaprGLVITPSRELAEQIG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 159 EVLRKVGKNHDFSAGLIIGGKDLKheaeRINN-----INILVCTPGRLLQHMDETIcFHATNLQMLVLDEADRILDMGFA 233
Cdd:cd17948  83 SVAQSLTEGLGLKVKVITGGRTKR----QIRNphfeeVDILVATPGALSKLLTSRI-YSLEQLRHLVLDEADTLLDDSFN 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 27371129 234 DTMNAIIENLP-------------KKRQTLLFSATQTKSVKDL 263
Cdd:cd17948 158 EKLSHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEV 200
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
106-255 7.42e-21

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: 89.00  E-value: 7.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 106 GKDVLGAAKTGSGKTLAFLVPVLEALyrlqwtSTDGLGVLIISPTRELAYQTFEVLRKVGKnHDFSAGLIIGGKDLKH-E 184
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAALLLL------LKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEErE 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27371129 185 AERINNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADRIL-DMGFADTMNAIIENLPKKR-QTLLFSAT 255
Cdd:cd00046  74 KNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLiDSRGALILDLAVRKAGLKNaQVILLSAT 146
HELICc smart00490
helicase superfamily c-terminal domain;
327-410 6.01e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 6.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    327 QYLYRVFCRLrpGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRT 406
Cdd:smart00490   1 EELAELLKEL--GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 27371129    407 ARYK 410
Cdd:smart00490  79 GRAG 82
DUF4217 pfam13959
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ...
451-510 1.50e-17

Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.


Pssm-ID: 339021  Cd Length: 60  Bit Score: 76.65  E-value: 1.50e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   451 VQKKLESFLAQDQDLKERAQRCFVSYIR--SVYLMKDkeVFNVSKLPITEYALSLGLAVAPR 510
Cdd:pfam13959   1 IQLQLEKLVLKDRELKELAQKAFVSYVRaySTHLLKD--IFNVKKLDLGHLAKSFGLLEAPK 60
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
112-259 1.44e-16

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 79.73  E-value: 1.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 112 AAKTGSGKTLAFLVPVLEALYR--LQWTSTDGLG-----------VLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGG 178
Cdd:cd17965  67 AAETGSGKTLAYLAPLLDYLKRqeQEPFEEAEEEyesakdtgrprSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 179 KDLKHE--AERINN-INILVCTPGRL--LQHMDETICFHATNLqmlVLDEADRILDMGFADTMNAIIENLPKKRQTLLFS 253
Cdd:cd17965 147 FGPSYQrlQLAFKGrIDILVTTPGKLasLAKSRPKILSRVTHL---VVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCS 223

                ....*.
gi 27371129 254 ATQTKS 259
Cdd:cd17965 224 ATIPKE 229
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
68-274 3.04e-16

DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) 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: 350806 [Multi-domain]  Cd Length: 229  Bit Score: 78.14  E-value: 3.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  68 ITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQG--KDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTdglgVL 145
Cdd:cd18048  17 VKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ----CL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 146 IISPTRELAYQTFEVLRKVGKnhdFSAGLII--------GGKDLKHEAErinninILVCTPGRLLQHMDETICFHATNLQ 217
Cdd:cd18048  93 CLSPTFELALQTGKVVEEMGK---FCVGIQViyairgnrPGKGTDIEAQ------IVIGTPGTVLDWCFKLRLIDVTNIS 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27371129 218 MLVLDEADRILDM-GFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd18048 164 VFVLDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNII 221
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
96-478 9.73e-16

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 224126 [Multi-domain]  Cd Length: 851  Bit Score: 80.91  E-value: 9.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQwTSTdglgVLIISPTRELAYQTFEVLRKVgkNHDFSAGLI 175
Cdd:COG1205  75 QVDALRLIREGRNVVVTTGTGSGKTESFLLPILDHLLRDP-SAR----ALLLYPTNALANDQAERLREL--ISDLPGKVT 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 176 IGGKDLKHEAER-----INNINILVCTPG----RLLQHMDETIcFHATNLQMLVLDEA---------------DRILDMg 231
Cdd:COG1205 148 FGRYTGDTPPEErraiiRNPPDILLTNPDmlhyLLLRNHDAWL-WLLRNLKYLVVDELhtyrgvqgsevalllRRLLRR- 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 232 fadtmnaiIENLPKKRQTLLFSATqTKSVKDLARLSLKDPEYVWVHE------KAKYSTPATLEQNYIICELHQKISVLF 305
Cdd:COG1205 226 --------LRRYGSPLQIICTSAT-LANPGEFAEELFGRDFEVPVDEdgsprgLRYFVRREPPIRELAESIRRSALAELA 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 306 SFLRSHLKK--KSIVFFSSCKEVQYLYRVFCR--LRPGI----SILALHG--RQQQMRRMEvyNEFVRKRAAVLFATDIA 375
Cdd:COG1205 297 TLAALLVRNgiQTLVFFRSRKQVELLYLSPRRrlVREGGklldAVSTYRAglHREERRRIE--AEFKEGELLGVIATNAL 374
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 376 ARGLDFPAVNWVLQFDCPED-ANTYIHRAGRTARYKEDGEALLILlpsEEQGMVQQLLQK--------KVPVKEIKINPE 446
Cdd:COG1205 375 ELGIDIGSLDAVIAYGYPGVsVLSFRQRAGRAGRRGQESLVLVVL---RSDPLDSYYLRHpeelletgFGPVESVRVDDN 451
                       410       420       430
                ....*....|....*....|....*....|...
gi 27371129 447 KLIDVQKKLESfLAQDQDLKER-AQRCFVSYIR 478
Cdd:COG1205 452 NEYLLDGHLLC-ADAELPLKDReLLPSDGSLEE 483
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
71-274 2.88e-15

DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 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: 350805 [Multi-domain]  Cd Length: 205  Bit Score: 74.76  E-value: 2.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  71 FSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQG--KDVLGAAKTGSGKTLAFLVPVLEAL-YRLQWTStdglgVLII 147
Cdd:cd18047   3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVePANKYPQ-----CLCL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 148 SPTRELAYQTFEVLRKVGKnhdFSAGLIIGGKDLKHEAERINNI--NILVCTPGRLLQHMDETICFHATNLQMLVLDEAD 225
Cdd:cd18047  78 SPTYELALQTGKVIEQMGK---FYPELKLAYAVRGNKLERGQKIseQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEAD 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27371129 226 -RILDMGFADTMNAIIENLPKKRQTLLFSATQTKSVKDLARLSLKDPEYV 274
Cdd:cd18047 155 vMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVI 204
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
96-460 3.46e-15

ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273594 [Multi-domain]  Cd Length: 591  Bit Score: 78.96  E-value: 3.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLGVlIISPTRELAYQTFEVLRKVGKNhdfsAGLI 175
Cdd:TIGR01389  18 QEEIISHVLDGRDVLVVMPTGGGKSLCYQVP---ALLL------KGLTV-VISPLISLMKDQVDQLRAAGVA----AAYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   176 IGGKDLKhEAERI------NNINILVCTPGRLLQ-HMDETIcfHATNLQMLVLDEADRILDMG--FADTMNAI---IENL 243
Cdd:TIGR01389  84 NSTLSAK-EQQDIekalvnGELKLLYVAPERLEQdYFLNML--QRIPIALVAVDEAHCVSQWGhdFRPEYQRLgslAERF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   244 PKkRQTLLFSATQTKSVKD--LARLSLKDPEyvwvHEKAKYSTPatlEQNYIICELHQKISVLFSFLRSHLKKKSIVFFS 321
Cdd:TIGR01389 161 PQ-VPRIALTATADAETRQdiRELLRLADAN----EFITSFDRP---NLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYAS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   322 SCKEVQYLYRVFCRlrPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIH 401
Cdd:TIGR01389 233 SRKKVEELAERLES--QGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQ 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   402 RAGRTARYKEDGEALLILLPSEeqgmvQQLLQKKVpvkEIKINPEKLIDVQ-KKLESFLA 460
Cdd:TIGR01389 311 EAGRAGRDGLPAEAILLYSPAD-----IALLKRRI---EQSEADDDYKQIErEKLRAMIA 362
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
96-458 4.51e-15

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


Pssm-ID: 223588 [Multi-domain]  Cd Length: 590  Bit Score: 78.49  E-value: 4.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLgVLIISPTRELAYQTFEVLRKVGKNhdfsAGLI 175
Cdd:COG0514  22 QQEIIDALLSGKDTLVVMPTGGGKSLCYQIP---ALLL------EGL-TLVVSPLISLMKDQVDQLEAAGIR----AAYL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 176 IGGKDlKHEAERI------NNINILVCTPGRLLQ-HMDETICfhATNLQMLVLDEADRILDMGFA-----DTMNAIIENL 243
Cdd:COG0514  88 NSTLS-REERQQVlnqlksGQLKLLYISPERLMSpRFLELLK--RLPISLVAIDEAHCISQWGHDfrpdyRRLGRLRAGL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 244 PKKrQTLLFSATQTKSVKD--LARLSLKDPEyvwvhekaKYSTPATLEQNYIicELHQKISVL--FSFLRSHLKKKS--- 316
Cdd:COG0514 165 PNP-PVLALTATATPRVRDdiREQLGLQDAN--------IFRGSFDRPNLAL--KVVEKGEPSdqLAFLATVLPQLSksg 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 317 IVFFSSCKEVQYLYRvfcRLRP-GISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPED 395
Cdd:COG0514 234 IIYCLTRKKVEELAE---WLRKnGISAGAYHAGLSNEERERVQQAFLNDEIKVMVATNAFGMGIDKPDVRFVIHYDLPGS 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27371129 396 ANTYIHRAGRTARykeDGE-ALLILLPSEEQGMVQQ--LLQKKVPVKEIKINPEKLIDVQKKLESF 458
Cdd:COG0514 311 IESYYQETGRAGR---DGLpAEAILLYSPEDIRWQRylIEQSKPDEEQKQIELAKLRQMIAYCETQ 373
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
96-435 1.25e-14

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


Pssm-ID: 129701 [Multi-domain]  Cd Length: 470  Bit Score: 76.73  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYrlqwtsTDGLGvLIISPTRELAYQTFEVLrkvgKNHDFSAGLI 175
Cdd:TIGR00614  16 QLEVINAVLLGRDCFVVMPTGGGKSLCYQLP---ALC------SDGIT-LVISPLISLMEDQVLQL----KASGIPATFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   176 IGGKDLKHEAE-----RINNINILVCTP------GRLLQHMDETIcfhatNLQMLVLDEADRILDMG--FADT---MNAI 239
Cdd:TIGR00614  82 NSSQSKEQQKNvltdlKDGKIKLLYVTPekcsasNRLLQTLEERK-----GITLIAVDEAHCISQWGhdFRPDykaLGSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   240 IENLPKKRQTLLfSATQTKSV-KDLAR-LSLKDPE-----------YVWVHEKakysTPATLEQnyiicelhqkisvLFS 306
Cdd:TIGR00614 157 KQKFPNVPIMAL-TATASPSVrEDILRqLNLKNPQifctsfdrpnlYYEVRRK----TPKILED-------------LLR 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   307 FLRSHLKKKS-IVFFSSCKEVQylyRVFCRLRP-GISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAV 384
Cdd:TIGR00614 219 FIRKEFKGKSgIIYCPSRKKSE---QVTASLQNlGIAAGAYHAGLEISARDDVHHKFQRDEIQVVVATVAFGMGINKPDV 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   385 NWVLQFDCPEDANTYIHRAGRTARYKEDGEALLI-----------LLPSEEQGMVQQLLQKK 435
Cdd:TIGR00614 296 RFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFyapadinrlrrLLMEEPDGQQRTYKLKL 357
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
113-421 1.27e-11

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: 66.30  E-value: 1.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 113 AKTGSGKTLAFLvpvLEALYRLQWTSTDGlgVLIISPTRELAYQTFEVLRKVGKnHDFSAGLIIGGKDLKH-----EAER 187
Cdd:cd09639   6 APTGYGKTEAAL---LWALHSLKSQKADR--VIIALPTRATINAMYRRAKEAFG-ETGLYHSSILSSRIKEmgdseEFEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 188 INNIN-----------ILVCTPGRLLQHMDETICFHATNL-----QMLVLDEADRIldmgfADTMNAIIENL-----PKK 246
Cdd:cd09639  80 LFPLYihsndtlfldpITVCTIDQVLKSVFGEFGHYEFTLasianSLLIFDEVHFY-----DEYTLALILAVlevlkDND 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 247 RQTLLFSATQTKSVKDLARlslkDPEYVWVHEKakYSTPATLEQNYIICELHQ--KISVLFSFLRSHLKKKSI-VFFSSC 323
Cdd:cd09639 155 VPILLMSATLPKFLKEYAE----KIGYVEENEP--LDLKPNERAPFIKIESDKvgEISSLERLLEFIKKGGSVaIIVNTV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 324 KEVQYLYRVFCRLRPGISILALHGRQQQMRRM----EVYNEFVRKRAAVLFATDIAARGLDFpAVNWVLQFDCPEDAntY 399
Cdd:cd09639 229 DRAQEFYQQLKEKGPEEEIMLIHSRFTEKDRAkkeaELLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS--L 305
                       330       340
                ....*....|....*....|...
gi 27371129 400 IHRAGRTARY-KEDGEALLILLP 421
Cdd:cd09639 306 IQRLGRLHRYgEKNGEEVYIITD 328
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
96-423 1.83e-11

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 67.05  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLgVLIISPTRELAYQTFEVLRKVGknhdFSAGLI 175
Cdd:PRK11057  30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIP---ALVL------DGL-TLVVSPLISLMKDQVDQLLANG----VAAACL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  176 IGGKDLKHEAERIN-----NINILVCTPGRLLqhMDETI-CFHATNLQMLVLDEADRILDMG--FADTMNAI------IE 241
Cdd:PRK11057  96 NSTQTREQQLEVMAgcrtgQIKLLYIAPERLM--MDNFLeHLAHWNPALLAVDEAHCISQWGhdFRPEYAALgqlrqrFP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  242 NLPkkrqTLLFSATQTKSV-KDLAR-LSLKDP-EYVwvhekAKYSTPATleqNYIICELHQKISVLFSFLRSHLKKKSIV 318
Cdd:PRK11057 174 TLP----FMALTATADDTTrQDIVRlLGLNDPlIQI-----SSFDRPNI---RYTLVEKFKPLDQLMRYVQEQRGKSGII 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  319 FFSSCKEVQYLYRVFCRlrPGISILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANT 398
Cdd:PRK11057 242 YCNSRAKVEDTAARLQS--RGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIES 319
                        330       340
                 ....*....|....*....|....*...
gi 27371129  399 YIHRAGRTARykeDG---EALLILLPSE 423
Cdd:PRK11057 320 YYQETGRAGR---DGlpaEAMLFYDPAD 344
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];
115-420 5.77e-11

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


Pssm-ID: 223989 [Multi-domain]  Cd Length: 442  Bit Score: 64.77  E-value: 5.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 115 TGSGKTLAFLvpvlEALYRLqwtstdGLGVLIISPTRELAYQTFEVLRKVGKNHDfSAGLIIGG-KDLKHEAERINNINI 193
Cdd:COG1061  64 TGAGKTVVAA----EAIAEL------KRSTLVLVPTKELLDQWAEALKKFLLLND-EIGIYGGGeKELEPAKVTVATVQT 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 194 LVctpgrLLQHMDEticFHATNLQMLVLDEADRILDMGFADtmnaIIENLPKKRQTLLFSATQ----------------- 256
Cdd:COG1061 133 LA-----RRQLLDE---FLGNEFGLIIFDEVHHLPAPSYRR----ILELLSAAYPRLGLTATPeredggrigdlfdligp 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 257 ---TKSVKDLARLS-LKDPEYVWVH---------------------EKAKYSTPATLEQNYIICELHQKISVLFSFLRSH 311
Cdd:COG1061 201 ivyEVSLKELIDEGyLAPYKYVEIKvtltedeereyakesarfrelLRARGTLRAENEARRIAIASERKIAAVRGLLLKH 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 312 LK-KKSIVFFSSCKEVQYLYRVFcrLRPGISIlALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQF 390
Cdd:COG1061 281 ARgDKTLIFASDVEHAYEIAKLF--LAPGIVE-AITGETPKEEREAILERFRTGGIKVLVTVKVLDEGVDIPDADVLIIL 357
                       330       340       350
                ....*....|....*....|....*....|
gi 27371129 391 DCPEDANTYIHRAGRTARYKEDGEALLILL 420
Cdd:COG1061 358 RPTGSRRLFIQRLGRGLRPAEGKEDTLALD 387
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
93-405 1.05e-10

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


Pssm-ID: 224122 [Multi-domain]  Cd Length: 814  Bit Score: 64.97  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  93 TEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTST-DGLGVLIISPTRELAYQTFEVLRKVGKnhdfS 171
Cdd:COG1201  24 TPPQRYAIPEIHSGENVLIIAPTGSGKTEAAFLPVINELLSLGKGKLeDGIYALYISPLKALNNDIRRRLEEPLR----E 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 172 AGLIIggkDLKH----EAER---INNI-NILVCTP---------GRLLQHMdeticfhaTNLQMLVLDEadrildmgfad 234
Cdd:COG1201 100 LGIEV---AVRHgdtpQSEKqkmLKNPpHILITTPeslaillnsPKFRELL--------RDVRYVIVDE----------- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 235 tMNAIIENlpkKRQTLL------------------FSATQtKSVKDLAR-LSLKDPEY--VWVHEKAKYSTPATLEQNYI 293
Cdd:COG1201 158 -IHALAES---KRGVQLalslerlrelagdfqrigLSATV-GPPEEVAKfLVGFGDPCeiVDVSAAKKLEIKVISPVEDL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 294 ICELHQKISV---LFSFLRSHlkKKSIVFFSSCKEVQylyRVFCRLRP--GISILALHGRQQQMRRMEVYNEFVRKRAAV 368
Cdd:COG1201 233 IYDEELWAALyerIAELVKKH--RTTLIFTNTRSGAE---RLAFRLKKlgPDIIEVHHGSLSRELRLEVEERLKEGELKA 307
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 27371129 369 LFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGR 405
Cdd:COG1201 308 VVATSSLELGIDIGDIDLVIQLGSPKSVNRFLQRIGR 344
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
96-224 1.29e-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: 60.68  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRlQWTSTdglgVLIISPTRELAYQTFEVLRKVgkNHDFSAGLI 175
Cdd:cd17923   5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR-DPGSR----ALYLYPTKALAQDQLRSLREL--LEQLGLGIR 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27371129 176 IG---GkDLKHEAER---INNINILVCTPGRL----LQHMDETICFhATNLQMLVLDEA 224
Cdd:cd17923  78 VAtydG-DTPREERRaiiRNPPRILLTNPDMLhyalLPHHDRWARF-LRNLRYVVLDEA 134
cas3_core TIGR01587
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ...
113-412 3.23e-10

CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.


Pssm-ID: 273707 [Multi-domain]  Cd Length: 359  Bit Score: 62.09  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   113 AKTGSGKTLAFLvpvLEALYRLQWTSTDGlgVLIISPTRELA---YQTFEVLRKVGKNHDFSAGLIIGGK------DLKH 183
Cdd:TIGR01587   6 APTGYGKTEAAL---LWALHSIKSQKADR--VIIALPTRATInamYRRAKELFGSELVGLHHSSSFSRIKemgdseEFEH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   184 EAER--INNIN-----ILVCTPGRLLQHMDETICFHATNL-----QMLVLDEADRIldmgfADTMNAIIENL-----PKK 246
Cdd:TIGR01587  81 LFPLyiHSNDKlfldpITVCTIDQVLKSVFGEFGHYEFTLasianSLLIFDEVHFY-----DEYTLALILAVlevlkDND 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   247 RQTLLFSATQTKSVKDLARlslkDPEYVWVHEKAKYSTPATLEQNYIICELHQ---KISVLFSFLRSHLKKKSI-VFFSS 322
Cdd:TIGR01587 156 VPILLMSATLPKFLKEYAE----KIGYVEFNEPLDLKEERRFENHRFILIESDkvgEISSLERLLEFIKKGGSIaIIVNT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   323 CKEVQYLYRVFCRLRPGISILALHGRQQQMRR----MEVYNEFVRKRAA-VLFATDIAARGLDFpAVNWVLQFDCPEDAn 397
Cdd:TIGR01587 232 VDRAQEFYQQLKEKAPEEEIILYHSRFTEKDRakkeAELLREMKKSNEKfVIVATQVIEASLDI-SADVMITELAPIDS- 309
                         330
                  ....*....|....*
gi 27371129   398 tYIHRAGRTARYKED 412
Cdd:TIGR01587 310 -LIQRLGRLHRYGRK 323
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
91-265 7.27e-09

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


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 55.73  E-value: 7.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  91 LVTEIQKQTI-GLALQGKDVLGAAKTGSGKTLAflvpVLEALYRLqWTSTDGLgVLIISPTRELAYQTFEVLRKVGKNHD 169
Cdd:cd17921   1 LLNPIQREALrALYLSGDSVLVSAPTSSGKTLI----AELAILRA-LATSGGK-AVYIAPTRALVNQKEADLRERFGPLG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 170 FSAGLIIGgkDLKHEAERINNINILVCTP----GRLLQHMDETIcfhaTNLQMLVLDEADRILDMGFADTMNAIIENLP- 244
Cdd:cd17921  75 KNVGLLTG--DPSVNKLLLAEADILVATPekldLLLRNGGERLI----QDVRLVVVDEAHLIGDGERGVVLELLLSRLLr 148
                       170       180
                ....*....|....*....|...
gi 27371129 245 --KKRQTLLFSATqTKSVKDLAR 265
Cdd:cd17921 149 inKNARFVGLSAT-LPNAEDLAE 170
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
362-421 1.10e-08

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.32  E-value: 1.10e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 362 VRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDgEALLILLP 421
Cdd:cd18785  19 IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD-EGEVILFV 77
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
115-255 3.32e-08

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 52.69  E-value: 3.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 115 TGSGKTLaFLVPVLEALYRLqwtstdglGVLIISPTRELAYQTFEVLRKVGKNHDFSaglIIGGKDLKHeaerINNINIL 194
Cdd:cd17926  27 TGSGKTL-TALALIAYLKEL--------RTLIVVPTDALLDQWKERFEDFLGDSSIG---LIGGGKKKD----FDDANVV 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27371129 195 VCTPGRLLQHMDETICFHATNLQMLVlDEADRILdmgfADTMNAIIENLPKKRQtLLFSAT 255
Cdd:cd17926  91 VATYQSLSNLAEEEKDLFDQFGLLIV-DEAHHLP----AKTFSEILKELNAKYR-LGLTAT 145
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
106-163 9.44e-08

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: 51.82  E-value: 9.44e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27371129 106 GKDVLGAAKTGSGKTLAFLVPVLEALYRLQWtstDGLGVLIISPTRELAYQTFEVLRK 163
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE---KGVQVLYISPLKALINDQERRLEE 55
ResIII pfam04851
Type III restriction enzyme, res subunit;
115-255 9.52e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 309815 [Multi-domain]  Cd Length: 162  Bit Score: 51.90  E-value: 9.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   115 TGSGKTLAFLvpvleALYRLQWTSTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLkheaERINNINIL 194
Cdd:pfam04851  32 TGSGKTLTAA-----KLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEIGEIISGDKKD----ESVDDNKIV 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129   195 VCTPGRLLQHMDETICFHATNLQMLVL-DEADRildmGFADTMNAIIENLPKKRQtLLFSAT 255
Cdd:pfam04851 103 VTTIQSLYKALELASLELLPDFFDVIIiDEAHR----SGASSYRNILEYFKPAFL-LGLTAT 159
recG TIGR00643
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
84-382 1.38e-07

ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273192 [Multi-domain]  Cd Length: 630  Bit Score: 54.65  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    84 LQEAQYRLVTEIQ---KQTIGLA--LQGkDVlgaaktGSGKTLAFLVPVLEALyrlqwtsTDGLGVLIISPTRELAYQTF 158
Cdd:TIGR00643 236 LTRAQKRVVKEILqdlKSDVPMNrlLQG-DV------GSGKTLVAALAMLAAI-------EAGYQVALMAPTEILAEQHY 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   159 EVLRKVGKNHDFSAGLIIG---GKDLKHEAERI--NNINILVCTPGrLLQhmdETICFHatNLQMLVLDEADR------- 226
Cdd:TIGR00643 302 NSLRNLLAPLGIEVALLTGslkGKRRKELLETIasGQIHLVVGTHA-LIQ---EKVEFK--RLALVIIDEQHRfgveqrk 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   227 -------------ILDMG------------FADTMNAIIENLPKKRQ---TLLFSATQTKSVkdlarlslkdpeYVWVHE 278
Cdd:TIGR00643 376 klrekgqggftphVLVMSatpiprtlaltvYGDLDTSIIDELPPGRKpitTVLIKHDEKDIV------------YEFIEE 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129   279 KAKYStpatlEQNYIICELHQKISVLFSflrshlkkksivffsscKEVQYLYRVFCRLRPGISILALHGRQQQMRRMEVY 358
Cdd:TIGR00643 444 EIAKG-----RQAYVVYPLIEESEKLDL-----------------KAAEALYERLKKAFPKYNVGLLHGRMKSDEKEAVM 501
                         330       340
                  ....*....|....*....|....
gi 27371129   359 NEFVRKRAAVLFATDIAARGLDFP 382
Cdd:TIGR00643 502 EEFREGEVDILVATTVIEVGVDVP 525
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
297-419 1.40e-07

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 50.82  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 297 LHQKISVLFSFLRSHLKKKS------IVFFSSCKE-VQYLYRVFCRLRPGISILALHGR--------QQQMRRMEVYNEF 361
Cdd:cd18801   7 IHPKLEKLEEIVKEHFKKKQegsdtrVIIFSEFRDsAEEIVNFLSKIRPGIRATRFIGQasgksskgMSQKEQKEVIEQF 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27371129 362 VRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARyKEDGEALLIL 419
Cdd:cd18801  87 RKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
Cas3 COG1203
CRISPR/Cas system-associated endonuclease/helicase Cas3 [Defense mechanisms];
113-462 1.45e-06

CRISPR/Cas system-associated endonuclease/helicase Cas3 [Defense mechanisms];


Pssm-ID: 224124 [Multi-domain]  Cd Length: 733  Bit Score: 51.31  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 113 AKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLiisPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLK---------H 183
Cdd:COG1203 221 APTGYGKTEASLILALALLDEKIKLKSRVIYVL---PFRTIIEDMYRRAKEIFGLFSVIGKSLHSSSKEPlllepdqdiL 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 184 EAERINNIN------ILVCTPgrLLQHMDETICFHATNLQML-----VLDEADRILDmgfaDTMNAIIENLPKKR----- 247
Cdd:COG1203 298 LTLTTNDSYkklllaLIVVTP--IQILIFSVKGFKFEFLALLltslvILDEVHLYAD----ETMLAALLALLEALaeagv 371
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 248 QTLLFSATQTKSVKDL--ARLSLKDPEYVWVHEKAKYSTPAtLEQNYIICELHQKISVLFSFLRSHLK--KKSIVFFSSC 323
Cdd:COG1203 372 PVLLMSATLPPFLKEKlkKALGKGREVVENAKFCPKEDEPG-LKRKERVDVEDGPQEELIELISEEVKegKKVLVIVNTV 450
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 324 KEVQYLYRvfcRLRPGI-SILALHGRQQQMRR----MEVYNEFVRKRAAVLFATDIAARGLDFpAVNWVLQFDCPEDAnt 398
Cdd:COG1203 451 DRAIELYE---KLKEKGpKVLLLHSRFTLKDReekeRELKKLFKQNEGFIVVATQVIEAGVDI-DFDVLITELAPIDS-- 524
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27371129 399 YIHRAGRTARYKEDGEALLILLPSEEQGmvqQLLQKKVPVKEIKINPEKLIDVQKKLESFLAQD 462
Cdd:COG1203 525 LIQRAGRVNRHGKKENGKIYVYNDEERG---PYLKYSYEKLEKKLKSLEELPLEIINGDSLLSD 585
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
96-272 2.38e-06

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 48.41  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLeaLYRLQwtsTDGLGvLIISPTREL-AYQTFEVLRKVgknhdfSAGL 174
Cdd:cd18018  17 QEEAIARLLSGRSTLVVLPTGAGKSLCYQLPAL--LLRRR---GPGLT-LVVSPLIALmKDQVDALPRAI------KAAA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 175 IIGG---KDLKHEAERINN--INILVCTPGRLLQHMDETICFHATNLQMLVLDEADRILDMGFA---DTM--NAIIENLP 244
Cdd:cd18018  85 LNSSltrEERRRILEKLRAgeVKILYVSPERLVNESFRELLRQTPPISLLVVDEAHCISEWSHNfrpDYLrlCRVLRELL 164
                       170       180
                ....*....|....*....|....*...
gi 27371129 245 KKRQTLLFSATQTKSVKDLARLSLKDPE 272
Cdd:cd18018 165 GAPPVLALTATATKRVVEDIASHLGIPE 192
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
96-157 3.50e-06

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 50.24  E-value: 3.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQT 157
Cdd:TIGR04121  18 QLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDI 79
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
103-226 5.56e-06

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 47.43  E-value: 5.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 103 ALQGKDVLGAAKTGSGKTlafLVPVLEALYRLQWTSTDGLG-VLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDL 181
Cdd:cd17927  14 ALKGKNTIICLPTGSGKT---FVAVLICEHHLKKFPAGRKGkVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSE 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 27371129 182 KHEAER-INNINILVCTPGRLLQHMDETICFHATNLQMLVLDEADR 226
Cdd:cd17927  91 NVSVEQiVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
96-274 1.09e-05

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 46.37  E-value: 1.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPvleALYRlqwtstDGLgVLIISPTreLAYQTFEVLRKvgKNHDFSAGLI 175
Cdd:cd17920  17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLL------DGV-TLVVSPL--ISLMQDQVDRL--QQLGIRAAAL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 176 IGGKDLKHEAERINNI-----NILVCTPGRLLQ-HMDETIC--FHATNLQMLVLDEADRIL--------DMGFadtMNAI 239
Cdd:cd17920  83 NSTLSPEEKREVLLRIkngqyKLLYVTPERLLSpDFLELLQrlPERKRLALIVVDEAHCVSqwghdfrpDYLR---LGRL 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27371129 240 IENLPKKrQTLLFSATQTKSVKD--LARLSLKDPEYV 274
Cdd:cd17920 160 RRALPGV-PILALTATATPEVREdiLKRLGLRNPVIF 195
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
348-408 1.77e-05

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 44.89  E-value: 1.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27371129 348 RQQQmrrmEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRtAR 408
Cdd:cd18802  77 RKQK----ETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-AR 132
DECH_helic TIGR03817
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood ...
96-165 2.39e-05

helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.


Pssm-ID: 274800 [Multi-domain]  Cd Length: 742  Bit Score: 47.42  E-value: 2.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129    96 QKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALyrlqwTSTDGLGVLIISPTRELAYQTFEVLRKVG 165
Cdd:TIGR03817  41 QARAAELAHAGRHVVVATGTASGKSLAYQLPVLSAL-----ADDPRATALYLAPTKALAADQLRAVRELT 105
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
101-246 3.65e-05

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


Pssm-ID: 224125 [Multi-domain]  Cd Length: 766  Bit Score: 46.99  E-value: 3.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 101 GLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRlqwtstDGLGVLIISPTRELAYQTFEVLRKVgKNHDFSAGLIIGGKD 180
Cdd:COG1204  42 KGLLSDENVLISAPTGSGKTLIALLAILSTLLE------GGGKVVYIVPLKALAEEKYEEFSRL-EELGIRVGISTGDYD 114
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27371129 181 LKHeaERINNINILVCTPGR---LLQHMDETIcfhaTNLQMLVLDEADRILDmgfaDTMNAIIENLPKK 246
Cdd:COG1204 115 LDD--ERLARYDVIVTTPEKldsLTRKRPSWI----EEVDLVVIDEIHLLGD----RTRGPVLESIVAR 173
PRK13767 PRK13767
ATP-dependent helicase; Provisional
88-154 3.77e-05

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 46.80  E-value: 3.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27371129   88 QYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRL--QWTSTDGLGVLIISPTRELA 154
Cdd:PRK13767  29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLgrEGELEDKVYCLYVSPLRALN 97
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
108-226 5.32e-05

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: 44.33  E-value: 5.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 108 DVLGAAKTGSGKTLAFLVPVLEALYRlqwtstdGLGVLIISPTRELAYQTFEVLRKVGKnhDFSAGLIIGGKDLKHEAEr 187
Cdd:cd17918  38 DRLLSGDVGSGKTLVALGAALLAYKN-------GKQVAILVPTEILAHQHYEEARKFLP--FINVELVTGGTKAQILSG- 107
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 27371129 188 innINILVCTPGrlLQHMDEticfHATNLQMLVLDEADR 226
Cdd:cd17918 108 ---ISLLVGTHA--LLHLDV----KFKNLDLVIVDEQHR 137
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
95-226 1.16e-04

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 43.27  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  95 IQKQTIGLALQGKDVLGAAKTGSGKTLaflVPVLEALYRLQwtsTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGL 174
Cdd:cd18035   5 LYQVLIAAVALNGNTLIVLPTGLGKTI---IAILVAADRLT---KKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27371129 175 iIGGKDLKHEAERINNINILVCTPgrllQHMDETICFHATNLQ---MLVLDEADR 226
Cdd:cd18035  79 -TGEVKPEERAERWDASKIIVATP----QVIENDLLAGRITLDdvsLLIFDEAHH 128
comFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) ...
83-411 1.39e-04

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 226583 [Multi-domain]  Cd Length: 441  Bit Score: 44.76  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  83 GLQEAQYRLVTEIQKQtiglalqgKDVLGAAKTGSGKTlAFLVPVLEALYRlqwtstDGLGVLIISPTRELAYQTFEVLR 162
Cdd:COG4098 101 GQKKASNQLVQYIKQK--------EDTLVWAVTGAGKT-EMIFQGIEQALN------QGGRVCIASPRVDVCLELYPRLK 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 163 KVGKNHDFSAgliiggkdLKHEAERINNINILVCTPGRLLQhmdeticFHATnLQMLVLDEADrildmGFADTMN----- 237
Cdd:COG4098 166 QAFSNCDIDL--------LYGDSDSYFRAPLVVATTHQLLR-------FKQA-FDLLIIDEVD-----AFPFSDDqslqy 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 238 AIIENLPKKRQTLLFSATQTK------------SVKDLARL---SLKDPEYVWVHEKAKYstpatLEQNYIIcelhqkiS 302
Cdd:COG4098 225 AVKKARKKEGATIYLTATPTKklerkilkgnlrILKLPARFhgkPLPVPKFVWIGNWNKK-----LQRNKLP-------L 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 303 VLFSFLRSHLKKKS--IVFFSSCKEVQYLYRVFCRLRPGISILALHGRQQQmrRMEVYNEFVRKRAAVLFATDIAARGLD 380
Cdd:COG4098 293 KLKRWLEKQRKTGRpvLIFFPEIETMEQVAAALKKKLPKETIASVHSEDQH--RKEKVEAFRDGKITLLITTTILERGVT 370
                       330       340       350
                ....*....|....*....|....*....|....
gi 27371129 381 FPAVNwVLQFDCPEDANT---YIHRAGRTARYKE 411
Cdd:COG4098 371 FPNVD-VFVLGAEHRVFTesaLVQIAGRVGRSLE 403
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
115-224 1.85e-04

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 43.02  E-value: 1.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 115 TGSGKTL-AFLvpVLEALYRLQ-WTSTDGLGVLIISPTRELAYQTFEVLR-----KVGKnhdFSAGLIIGGKDLKHEAER 187
Cdd:cd18034  25 TGSGKTLiAVM--LIKEMGELNrKEKNPKKRAVFLVPTVPLVAQQAEAIRshtdlKVGE---YSGEMGVDKWTKERWKEE 99
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 27371129 188 INNINILVCTPGRL---LQHMdeTICFHATNLqmLVLDEA 224
Cdd:cd18034 100 LEKYDVLVMTAQILldaLRHG--FLSLSDINL--LIFDEC 135
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
84-226 1.99e-04

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


Pssm-ID: 224121 [Multi-domain]  Cd Length: 677  Bit Score: 44.51  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  84 LQEAQYRLVTEIQKqtiGLA--------LQGkDVlgaaktGSGKTLaflVPVLEALYrlqwTSTDGLGVLIISPTRELAY 155
Cdd:COG1200 263 LTNAQKRVIKEILA---DLAspvpmnrlLQG-DV------GSGKTV---VALLAMLA----AIEAGYQAALMAPTEILAE 325
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27371129 156 QTFEVLRKVGKNHDFSAGLIIG---GKDLKHEAERINN--INILVCTPGrLLQhmdETICFHatNLQMLVLDEADR 226
Cdd:COG1200 326 QHYESLRKWLEPLGIRVALLTGslkGKARKEILEQLASgeIDIVVGTHA-LIQ---DKVEFH--NLGLVIIDEQHR 395
DEXHc_RecG cd17992
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ...
84-226 2.19e-04

DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain]  Cd Length: 225  Bit Score: 42.90  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129  84 LQEAQYRLVTEI---QKQTIGLA--LQGkDVlgaaktGSGKTL-AFLvpvleALYRlqwTSTDGLGVLIISPTRELAYQT 157
Cdd:cd17992  46 LTGAQKRVIDEIlrdLASEKPMNrlLQG-DV------GSGKTVvAAL-----AMLA---AVENGYQVALMAPTEILAEQH 110
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27371129 158 FEVLRKVGKNHDFSAGLIIG---GKDLKHEAERINN--INILVCTPGrLLQhmdETICFHatNLQMLVLDEADR 226
Cdd:cd17992 111 YDSLKKLLEPLGIRVALLTGstkAKEKREILEKIASgeIDIVIGTHA-LIQ---EDVEFH--NLGLVIIDEQHR 178
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
104-255 2.71e-04

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: 41.94  E-value: 2.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 104 LQGKDVLGAAKTGSGKTLAFLVPVLEALYRlqwtstdGLGVLIISPTRELA---YQTFEVLRKVGKNHDFSAGliiggkD 180
Cdd:cd18028  15 LKGENLLISIPTASGKTLIAEMAMVNTLLE-------GGKALYLVPLRALAsekYEEFKKLEEIGLKVGISTG------D 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 181 LKHEAERINNINILVCTPGR---LLQHMDETIcfhaTNLQMLVLDEADRILDMGFADTMNAII---ENLPKKRQTLLFSA 254
Cdd:cd18028  82 YDEDDEWLGDYDIIVATYEKfdsLLRHSPSWL----RDVGVVVVDEIHLISDEERGPTLESIVarlRRLNPNTQIIGLSA 157

                .
gi 27371129 255 T 255
Cdd:cd18028 158 T 158
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
298-419 3.19e-04

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


Pssm-ID: 224036 [Multi-domain]  Cd Length: 542  Bit Score: 43.48  E-value: 3.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27371129 298 HQKISVLFSFLRSHLKKKS----IVFFSSCKEVQYLYRVFCRLRPGISILAL--------HGRQQQMRRmEVYNEFVRKR 365
Cdd:COG1111 347 HPKLEKLREILKEQLEKNGdsrvIVFTEYRDTAEEIVNFLKKIGIKARVRFIgqasregdKGMSQKEQK-EIIDQFRKGE 425
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27371129 366 AAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARyKEDGEALLIL 419
Cdd:COG1111 426 YNVLVATSVGEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KRKGRVVVLV 478
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
93-228 3.21e-04

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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.