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Conserved domains on  [gi|555017726|gb|ESL62160|]
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ATP-dependent RNA helicase srmB [Klebsiella pneumoniae BIDMC 22]

Protein Classification

ATP-dependent RNA helicase SrmB( domain architecture ID 11485262)

ATP-dependent RNA helicase SrmB is a DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature; exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
20-434 0e+00

ATP-dependent RNA helicase SrmB; Provisional


:

Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 868.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:PRK11192  17 QDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILTPTRELAMQVADQAREL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:PRK11192  97 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAETR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEGDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRE 259
Cdd:PRK11192 177 WRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 260 RVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRT 339
Cdd:PRK11192 257 RVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRT 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 340 GRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKRAQKKKDEKEKPRVKKRH 419
Cdd:PRK11192 337 GRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRH 416
                        410
                 ....*....|....*
gi 555017726 420 RDTKNIGKRRKPSAA 434
Cdd:PRK11192 417 RDTKNIGKRRKPSGT 431
 
Name Accession Description Interval E-value
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
20-434 0e+00

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 868.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:PRK11192  17 QDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILTPTRELAMQVADQAREL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:PRK11192  97 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAETR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEGDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRE 259
Cdd:PRK11192 177 WRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 260 RVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRT 339
Cdd:PRK11192 257 RVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRT 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 340 GRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKRAQKKKDEKEKPRVKKRH 419
Cdd:PRK11192 337 GRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRH 416
                        410
                 ....*....|....*
gi 555017726 420 RDTKNIGKRRKPSAA 434
Cdd:PRK11192 417 RDTKNIGKRRKPSGT 431
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
20-430 2.00e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 476.95  E-value: 2.00e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLdfpRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:COG0513   18 AELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLD---PSRPRAPQALILAPTRELALQVAEELRKL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:COG0513   95 AKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKLLP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDiEHKTKLLVNLLQQPEATRAIVFVRKRE 259
Cdd:COG0513  175 KERQTLLFSATMP-PEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDK-RDKLELLRRLLRDEDPERAIVFCNTKR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 260 RVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRT 339
Cdd:COG0513  253 GADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRT 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 340 GRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKRAQKKKDEKEKprvKKRH 419
Cdd:COG0513  333 GRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGPK---GERK 409
                        410
                 ....*....|.
gi 555017726 420 RDTKNIGKRRK 430
Cdd:COG0513  410 ARRGKRRRRKR 420
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
20-211 3.05e-82

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: 251.59  E-value: 3.05e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:cd00268    6 KKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd00268   86 GKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSALP 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd00268  166 KDRQTLLFSATLP-EEVKELAKKFLKNPVRIE 196
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
39-191 9.69e-50

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 166.65  E-value: 9.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   39 LDGRDILGSAPTGTGKTAAYLLPALQHLldfpRKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMN 118
Cdd:pfam00270  12 LEGRDVLVQAPTGSGKTLAFLLPALEAL----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555017726  119 HAEVFsENQDIVVATTGRLLQYIKEENFdCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATL 191
Cdd:pfam00270  88 QLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
DEXDc smart00487
DEAD-like helicases superfamily;
42-223 2.71e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.11  E-value: 2.71e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726    42 RDILGSAPTGTGKTAAYLLPALQHLldfprKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAY-MNHA 120
Cdd:smart00487  25 RDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKrEQLR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   121 EVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATLEGDaIKDFA 200
Cdd:smart00487 100 KLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSATPPEE-IENLL 178
                          170       180
                   ....*....|....*....|...
gi 555017726   201 ERLLEEPVEVSANPSTRERKKIH 223
Cdd:smart00487 179 ELFLNDPVFIDVGFTPLEPIEQF 201
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
39-99 4.15e-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: 49.09  E-value: 4.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726   39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAmqvADHAREL 99
Cdd:TIGR04121  26 LEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYITPLRALA---VDIARNL 83
 
Name Accession Description Interval E-value
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
20-434 0e+00

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 868.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:PRK11192  17 QDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILTPTRELAMQVADQAREL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:PRK11192  97 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAAETR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEGDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRE 259
Cdd:PRK11192 177 WRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLKQPEVTRSIVFVRTRE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 260 RVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRT 339
Cdd:PRK11192 257 RVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRT 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 340 GRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKRAQKKKDEKEKPRVKKRH 419
Cdd:PRK11192 337 GRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEKKTGKPSKKVLAKRAEKKEKEKEKPKVKKRH 416
                        410
                 ....*....|....*
gi 555017726 420 RDTKNIGKRRKPSAA 434
Cdd:PRK11192 417 RDTKNIGKRRKPSGT 431
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
20-430 2.00e-167

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 476.95  E-value: 2.00e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLdfpRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:COG0513   18 AELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLD---PSRPRAPQALILAPTRELALQVAEELRKL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:COG0513   95 AKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIERILKLLP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDiEHKTKLLVNLLQQPEATRAIVFVRKRE 259
Cdd:COG0513  175 KERQTLLFSATMP-PEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDK-RDKLELLRRLLRDEDPERAIVFCNTKR 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 260 RVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRT 339
Cdd:COG0513  253 GADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRT 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 340 GRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKRAQKKKDEKEKprvKKRH 419
Cdd:COG0513  333 GRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLKGKKAGRGGRPGPK---GERK 409
                        410
                 ....*....|.
gi 555017726 420 RDTKNIGKRRK 430
Cdd:COG0513  410 ARRGKRRRRKR 420
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
39-386 1.63e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 292.09  E-value: 1.63e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHL-LDFPRKKSgppriLILTPTRELAMQVADHARELAKHTH-LDIATITGGVAY 116
Cdd:PRK11776  39 LAGKDVIAQAKTGSGKTAAFGLGLLQKLdVKRFRVQA-----LVLCPTRELADQVAKEIRRLARFIPnIKVLTLCGGVPM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 117 MNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATLeGDAI 196
Cdd:PRK11776 114 GPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQTLLFSATY-PEGI 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 197 KDFAERLLEEPVEVSANpSTRERKKIHQWYYRADDiEHKTKLLVNLLQ--QPEATraIVFVRKRERVHELANWLREAGIN 274
Cdd:PRK11776 193 AAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSP-DERLPALQRLLLhhQPESC--VVFCNTKKECQEVADALNAQGFS 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 275 TCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKGTAISLVEA 354
Cdd:PRK11776 269 ALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAP 348
                        330       340       350
                 ....*....|....*....|....*....|..
gi 555017726 355 HDHLLLGKIGRYIEEPLKARVIDELRPTTRAP 386
Cdd:PRK11776 349 EEMQRANAIEDYLGRKLNWEPLPSLSPLSGVP 380
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
39-420 5.63e-85

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 266.45  E-value: 5.63e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFP---RKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVA 115
Cdd:PRK04837  43 LAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapeDRKVNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDG 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 116 YMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIetiagetRW--RKQ-------TML 186
Cdd:PRK04837 123 YDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGFIKDI-------RWlfRRMppanqrlNML 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 187 FSATLEGdAIKDFAERLLEEPVEVSANPSTRERKKIHQ-WYYRADdiEHKTKLLVNLLQQPEATRAIVFVRKRERVHELA 265
Cdd:PRK04837 196 FSATLSY-RVRELAFEHMNNPEYVEVEPEQKTGHRIKEeLFYPSN--EEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIW 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 266 NWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKK 345
Cdd:PRK04837 273 GHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGAS 352
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555017726 346 GTAISLVEAHDHLLLGKIGRYIEEPLkarvidelrPTTRAPSEKLTGK--PSKKVLAKRAQKKKDEKEKPRVKKRHR 420
Cdd:PRK04837 353 GHSISLACEEYALNLPAIETYIGHSI---------PVSKYDSDALLTDlpKPLRLTRPRTGNGPRRSGAPRNRRRRK 420
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
2-411 1.81e-83

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 268.64  E-value: 1.81e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   2 TVTTFSELELDENLLEALQDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALqHLLDfPRKKSgpPRILI 81
Cdd:PRK11634   4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLD-PELKA--PQILV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  82 LTPTRELAMQVADHARELAKHTH-LDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEAD 160
Cdd:PRK11634  80 LAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 161 RMLDMGFAQDIETIAGETRWRKQTMLFSATLEgDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEhKTKLLV 240
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 241 NLLQQPEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHV 320
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 321 FNFDMPRTADTYLHRIGRTGRAGKKGTAISLVEAHDHLLLgkigRYIEEPLKARVidelrPTTRAPSEKLTGkpsKKVLA 400
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLL----RNIERTMKLTI-----PEVELPNAELLG---KRRLE 385
                        410
                 ....*....|.
gi 555017726 401 KRAQKKKDEKE 411
Cdd:PRK11634 386 KFAAKVQQQLE 396
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
20-211 3.05e-82

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: 251.59  E-value: 3.05e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHAREL 99
Cdd:cd00268    6 KKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd00268   86 GKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKILSALP 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd00268  166 KDRQTLLFSATLP-EEVKELAKKFLKNPVRIE 196
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
20-384 2.87e-79

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 253.30  E-value: 2.87e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKS---GPPRILILTPTRELAMQVADHA 96
Cdd:PRK01297 103 HDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGEPRALIIAPTRELVVQIAKDA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  97 RELAKHTHLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIA 175
Cdd:PRK01297 183 AALTKYTGLNVMTFVGGMDFDKQLKQLEARFcDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQII 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 176 GET--RWRKQTMLFSATLEGDAIkDFAERLLEEPVEVSANPSTRERKKIHQWYYrADDIEHKTKLLVNLLQQPEATRAIV 253
Cdd:PRK01297 263 RQTprKEERQTLLFSATFTDDVM-NLAKQWTTDPAIVEIEPENVASDTVEQHVY-AVAGSDKYKLLYNLVTQNPWERVMV 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 254 FVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYL 333
Cdd:PRK01297 341 FANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYV 420
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 555017726 334 HRIGRTGRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARV--IDELRPTTR 384
Cdd:PRK01297 421 HRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMppAELLKPVPR 473
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
21-388 2.25e-77

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 247.80  E-value: 2.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSG--PPRILILTPTRELAMQVADHARE 98
Cdd:PRK10590  18 EQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrPVRALILTPTRELAAQIGENVRD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  99 LAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGET 178
Cdd:PRK10590  98 YSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRVLAKL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 179 RWRKQTMLFSATLEgDAIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDiEHKTKLLVNLLQQPEATRAIVFVRKR 258
Cdd:PRK10590 178 PAKRQNLLFSATFS-DDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDK-KRKRELLSQMIGKGNWQQVLVFTRTK 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 259 ERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGR 338
Cdd:PRK10590 256 HGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPEDYVHRIGR 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 555017726 339 TGRAGKKGTAISLVEAHDHLLLGKIGRYIEEPLKARVIDELRPTTRAPSE 388
Cdd:PRK10590 336 TGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAE 385
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
1-437 2.20e-76

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 248.71  E-value: 2.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   1 MTVTTFSELELDENLLEALQDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFP---RKKSGPP 77
Cdd:PRK04537   6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPalaDRKPEDP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  78 RILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKE-ENFDCRAVETLIL 156
Cdd:PRK04537  86 RALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 157 DEADRMLDMGFAQDIETIAGET--RWRKQTMLFSATLEGDAIkDFAERLLEEP----VEVSANPSTRERKKIhqwYYRAD 230
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVL-ELAYEHMNEPeklvVETETITAARVRQRI---YFPAD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 231 DieHKTKLLVNLLQQPEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAAR 310
Cdd:PRK04537 242 E--EKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 311 GIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKGTAISLVEAHDHLLLGKIGRYIE-----EPLKARVIDELRPTTRA 385
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEqkipvEPVTAELLTPLPRPPRV 399
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555017726 386 PSEKLTG------------KPSKKVLAKRAQKKKDEKEKPRVKKRHRDTKNIGKRRKPSAAGTP 437
Cdd:PRK04537 400 PVEGEEAddeagdsvgtifREAREQRAAEEQRRGGGRSGPGGGSRSGSVGGGGRRDGAGADGKP 463
PTZ00110 PTZ00110
helicase; Provisional
23-350 4.36e-64

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 215.41  E-value: 4.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHARELAK 101
Cdd:PTZ00110 149 GFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDgPIVLVLAPTRELAEQIREQCNKFGA 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 102 HTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWR 181
Cdd:PTZ00110 229 SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPD 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 182 KQTMLFSATLEGDAIKDFAERLLEEPVEVSANPST-RERKKIHQWYYRADDIEHKTKLLVnLLQQ--PEATRAIVFVRKR 258
Cdd:PTZ00110 309 RQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKM-LLQRimRDGDKILIFVETK 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 259 ERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGR 338
Cdd:PTZ00110 388 KGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGR 467
                        330
                 ....*....|..
gi 555017726 339 TGRAGKKGTAIS 350
Cdd:PTZ00110 468 TGRAGAKGASYT 479
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
222-352 6.50e-59

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: 189.26  E-value: 6.50e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 222 IHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNV 301
Cdd:cd18787    1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 555017726 302 LIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKGTAISLV 352
Cdd:cd18787   81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PTZ00424 PTZ00424
helicase 45; Provisional
23-369 3.08e-57

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 193.89  E-value: 3.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQhLLDFPRKKSgppRILILTPTRELAMQVADHARELAKH 102
Cdd:PTZ00424  47 GFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLNAC---QALILAPTRELAQQIQKVVLALGDY 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 THLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRK 182
Cdd:PTZ00424 123 LKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 183 QTMLFSATLEGDaIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRERVH 262
Cdd:PTZ00424 203 QVALFSATMPNE-ILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTITQAIIYCNTRRKVD 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 263 ELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRA 342
Cdd:PTZ00424 282 YLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRF 361
                        330       340       350
                 ....*....|....*....|....*....|.
gi 555017726 343 GKKGTAISLVEAHDHLLLGKIGRY----IEE 369
Cdd:PTZ00424 362 GRKGVAINFVTPDDIEQLKEIERHyntqIEE 392
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
20-211 5.36e-56

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: 184.00  E-value: 5.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGpPRILILTPTRELAMQVADHAREL 99
Cdd:cd17947    6 SSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAA-TRVLVLVPTRELAMQCFSVLQQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEE-NFDCRAVETLILDEADRMLDMGFAQDIETIAGET 178
Cdd:cd17947   85 AQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKEILRLC 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 179 RWRKQTMLFSATLeGDAIKDFAERLLEEPVEVS 211
Cdd:cd17947  165 PRTRQTMLFSATM-TDEVKDLAKLSLNKPVRVF 196
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
23-359 9.31e-51

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 179.21  E-value: 9.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSG---PPRILILTPTRELAMQVADHAREL 99
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSeqrNPLAMVLTPTRELCVQVEDQAKVL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAgETR 179
Cdd:PLN00206 220 GKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIF-QAL 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVSANPSTRERKKIHQ---WYyradDIEHKTKLLVNLLQQPEATR--AIVF 254
Cdd:PLN00206 299 SQPQVLLFSATVS-PEVEKFASSLAKDIILISIGNPNRPNKAVKQlaiWV----ETKQKKQKLFDILKSKQHFKppAVVF 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 255 VRKRERVHELANWLREA-GINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYL 333
Cdd:PLN00206 374 VSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYI 453
                        330       340
                 ....*....|....*....|....*.
gi 555017726 334 HRIGRTGRAGKKGTAISLVEAHDHLL 359
Cdd:PLN00206 454 HQIGRASRMGEKGTAIVFVNEEDRNL 479
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
39-191 9.69e-50

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 166.65  E-value: 9.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   39 LDGRDILGSAPTGTGKTAAYLLPALQHLldfpRKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMN 118
Cdd:pfam00270  12 LEGRDVLVQAPTGSGKTLAFLLPALEAL----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKE 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555017726  119 HAEVFsENQDIVVATTGRLLQYIKEENFdCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATL 191
Cdd:pfam00270  88 QLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
22-208 2.01e-48

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: 164.40  E-value: 2.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  22 KGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDfpRKKSGPPRILILTPTRELAMQVADHARELAK 101
Cdd:cd17959   19 KGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVGARALILSPTRELALQTLKVTKELGK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 102 HTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWR 181
Cdd:cd17959   97 FTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLPEN 176
                        170       180
                 ....*....|....*....|....*..
gi 555017726 182 KQTMLFSATLEgDAIKDFAERLLEEPV 208
Cdd:cd17959  177 RQTLLFSATLP-KLLVEFAKAGLNEPV 202
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
20-213 1.24e-47

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: 162.07  E-value: 1.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLdfpRKKSGPPR---ILILTPTRELAMQVADHA 96
Cdd:cd17941    6 KEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY---RERWTPEDglgALIISPTRELAMQIFEVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  97 RELAKHTHLDIATITGGVAYMNHAEVFSEnQDIVVATTGRLLQYIKEE-NFDCRAVETLILDEADRMLDMGFAQDIETIA 175
Cdd:cd17941   83 RKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDAIV 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 555017726 176 GETRWRKQTMLFSATLEGDaIKDFAERLLEEPVEVSAN 213
Cdd:cd17941  162 ENLPKSRQTLLFSATQTKS-VKDLARLSLKNPEYISVH 198
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
23-191 2.77e-47

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: 161.89  E-value: 2.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFP------RKKSGPPRILILTPTRELAMQVADHA 96
Cdd:cd17967   19 GYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrGRRKAYPSALILAPTRELAIQIYEEA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  97 RELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIA- 175
Cdd:cd17967   99 RKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEADRMLDMGFEPQIRKIVe 178
                        170       180
                 ....*....|....*....|..
gi 555017726 176 ------GETRwrkQTMLFSATL 191
Cdd:cd17967  179 hpdmppKGER---QTLMFSATF 197
DEXDc smart00487
DEAD-like helicases superfamily;
42-223 2.71e-45

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 156.11  E-value: 2.71e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726    42 RDILGSAPTGTGKTAAYLLPALQHLldfprKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAY-MNHA 120
Cdd:smart00487  25 RDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKrEQLR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   121 EVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATLEGDaIKDFA 200
Cdd:smart00487 100 KLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSATPPEE-IENLL 178
                          170       180
                   ....*....|....*....|...
gi 555017726   201 ERLLEEPVEVSANPSTRERKKIH 223
Cdd:smart00487 179 ELFLNDPVFIDVGFTPLEPIEQF 201
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
40-200 1.72e-44

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: 154.28  E-value: 1.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  40 DGRDILGSAPTGTGKTAAYLLPALQHLL-DFPRKKSGPPRILILTPTRELAMQVADHARELAKHTH-LDIATITGGVAYM 117
Cdd:cd17964   31 TGDDVLARAKTGTGKTLAFLLPAIQSLLnTKPAGRRSGVSALIISPTRELALQIAAEAKKLLQGLRkLRVQSAVGGTSRR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 118 -NHAEVFSENQDIVVATTGRLLQYIKEENF--DCRAVETLILDEADRMLDMGFAQDIETI------AGETRWrkQTMLFS 188
Cdd:cd17964  111 aELNRLRRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDMGFRPDLEQIlrhlpeKNADPR--QTLLFS 188
                        170
                 ....*....|..
gi 555017726 189 ATLEgDAIKDFA 200
Cdd:cd17964  189 ATVP-DEVQQIA 199
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
23-191 2.81e-44

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: 153.63  E-value: 2.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRkksgPPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd17954   19 GWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ----RFFALVLAPTRELAQQISEQFEALGSS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 THLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDCRAVETLILDEADRMLDMGFAQDIETIAGETRWR 181
Cdd:cd17954   95 IGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLLNMDFEPEIDKILKVIPRE 174
                        170
                 ....*....|
gi 555017726 182 KQTMLFSATL 191
Cdd:cd17954  175 RTTYLFSATM 184
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
20-194 1.28e-43

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: 152.78  E-value: 1.28e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPAL-DGRDILGSAPTGTGKTAAYLLPALQHLLD-----FPRKKSGPPRILILTPTRELAMQVA 93
Cdd:cd17946    6 ADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSqkssnGVGGKQKPLRALILTPTRELAVQVK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  94 DHARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDC--RAVETLILDEADRMLDMGFAQD 170
Cdd:cd17946   86 DHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNeHLAnlKSLRFLVLDEADRMLEKGHFAE 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 171 IETI--------AGETRWRkQTMLFSATLEGD 194
Cdd:cd17946  166 LEKIlellnkdrAGKKRKR-QTFVFSATLTLD 196
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
23-211 4.15e-43

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: 150.45  E-value: 4.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPrkkSGpPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd17955   18 GIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP---YG-IFALVLTPTRELAYQIAEQFRALGAP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 THLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIK---EENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd17955   94 LGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSALP 173
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd17955  174 PKRQTLLFSATLT-DALKALKELFGNKPFFWE 204
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
21-211 6.58e-43

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: 149.83  E-value: 6.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHAREL 99
Cdd:cd17966    7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDgPIVLVLAPTRELAQQIQQEANKF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd17966   87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIR 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEGDaIKDFAERLLEEPVEVS 211
Cdd:cd17966  167 PDRQTLMWSATWPKE-VRRLAEDFLKDYIQVN 197
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
23-211 1.35e-41

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: 146.41  E-value: 1.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHARELAK 101
Cdd:cd17952    9 EYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEgPIAVIVAPTRELAQQIYLEAKKFGK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 102 HTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWR 181
Cdd:cd17952   89 AYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIVGHVRPD 168
                        170       180       190
                 ....*....|....*....|....*....|
gi 555017726 182 KQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd17952  169 RQTLLFSATFK-KKIEQLARDILSDPIRVV 197
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
21-211 2.78e-41

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: 145.42  E-value: 2.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDfPRKKSGpPRILILTPTRELAMQVADHARELA 100
Cdd:cd17957    7 ESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKG-LRALILAPTRELASQIYRELLKLS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KHTHLDIATITGG-VAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI-AGET 178
Cdd:cd17957   85 KGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEIlAACT 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 179 RWRKQTMLFSATLeGDAIKDFAERLLEEPVEVS 211
Cdd:cd17957  165 NPNLQRSLFSATI-PSEVEELARSVMKDPIRII 196
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
23-211 5.21e-40

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: 142.84  E-value: 5.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFP----RKKSGPPRILILTPTRELAMQVADHARE 98
Cdd:cd17945    9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldeETKDDGPYALILAPTRELAQQIEEETQK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  99 LAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI---- 174
Cdd:cd17945   89 FAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKIldam 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 555017726 175 ----------------AGETRWRKQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd17945  169 pvsnkkpdteeaeklaASGKHRYRQTMMFTATMP-PAVEKIAKGYLRRPVVVT 220
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
20-194 1.99e-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: 140.80  E-value: 1.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP--PRILILTPTRELAMQVADHAR 97
Cdd:cd17961   10 AKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqgTRALILVPTRELAQQVSKVLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  98 ELAKHT--HLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDCRAVETLILDEADRMLDMGFAQDIETI 174
Cdd:cd17961   90 QLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLSYGYEEDLKSL 169
                        170       180
                 ....*....|....*....|
gi 555017726 175 AGETRWRKQTMLFSATLEGD 194
Cdd:cd17961  170 LSYLPKNYQTFLMSATLSED 189
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
23-206 5.75e-39

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: 141.26  E-value: 5.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSG-----PPRILILTPTRELAMQVADHAR 97
Cdd:cd18052   62 GYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfsevqEPQALIVAPTRELANQIFLEAR 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  98 ELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGE 177
Cdd:cd18052  142 KFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSE 221
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 178 TRW----RKQTMLFSATLEgDAIKDFAERLLEE 206
Cdd:cd18052  222 PGMpskeDRQTLMFSATFP-EEIQRLAAEFLKE 253
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
20-210 1.07e-38

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: 139.43  E-value: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHARE 98
Cdd:cd17953   28 KKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEgPIGLIMAPTRELALQIYVECKK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  99 LAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN---FDCRAVETLILDEADRMLDMGFAQDIETIA 175
Cdd:cd17953  108 FSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEADRMFDMGFEPQIMKIV 187
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 555017726 176 GETRWRKQTMLFSATLEgDAIKDFAERLLEEPVEV 210
Cdd:cd17953  188 NNIRPDRQTVLFSATFP-RKVEALARKVLHKPIEI 221
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
23-210 1.18e-37

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: 135.67  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLL--DFPRKKSGPPRILILTPTRELAMQVADharELA 100
Cdd:cd17958    9 GFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREQRNGPGVLVLTPTRELALQIEA---ECS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KHTH--LDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGET 178
Cdd:cd17958   86 KYSYkgLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDI 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 179 RWRKQTMLFSATLEgDAIKDFAERLLEEPVEV 210
Cdd:cd17958  166 RPDRQTIMTSATWP-DGVRRLAQSYLKDPMIV 196
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
23-190 3.26e-37

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: 134.80  E-value: 3.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQ--HLLDF-PRKKSGpprILILTPTRELAMQVADHAREL 99
Cdd:cd17942    9 GFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllYKLKFkPRNGTG---VIIISPTRELALQIYGVAKEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIK-EENFDCRAVETLILDEADRMLDMGFAQDIETIAGET 178
Cdd:cd17942   86 LKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLL 165
                        170
                 ....*....|..
gi 555017726 179 RWRKQTMLFSAT 190
Cdd:cd17942  166 PKRRQTMLFSAT 177
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
23-211 5.07e-37

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: 134.64  E-value: 5.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRK---KSGpPRILILTPTRELAMQVADHAREL 99
Cdd:cd17949   10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrSDG-TLALVLVPTRELALQIYEVLEKL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTH-LDIATITGGvaymnhaevfsENQD-----------IVVATTGRLLQYIKE-ENFDCRAVETLILDEADRMLDMG 166
Cdd:cd17949   89 LKPFHwIVPGYLIGG-----------EKRKsekarlrkgvnILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 555017726 167 FAQDIETIAGETRW-------------RKQTMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd17949  158 FEKDITKILELLDDkrskaggekskpsRRQTVLVSATLT-DGVKRLAGLSLKDPVYID 214
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
21-210 1.06e-36

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: 133.19  E-value: 1.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLldfpRKKSGPPRILILTPTRELAMQVADHARELA 100
Cdd:cd17940   16 EKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI----DPKKDVIQALILVPTRELALQTSQVCKELG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRW 180
Cdd:cd17940   92 KHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPK 171
                        170       180       190
                 ....*....|....*....|....*....|
gi 555017726 181 RKQTMLFSATLEGDaIKDFAERLLEEPVEV 210
Cdd:cd17940  172 ERQILLFSATFPLT-VKNFMDRHMHNPYEI 200
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
20-211 1.41e-36

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: 133.09  E-value: 1.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDfPRKKSGPPRI--LILTPTRELAMQVADHAR 97
Cdd:cd17960    6 AELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK-RKANLKKGQVgaLIISPTRELATQIYEVLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  98 ELAKH--THLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYI--KEENFDCRAVETLILDEADRMLDMGFAQDIE 172
Cdd:cd17960   85 SFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNGpNILVGTPGRLEELLsrKADKVKVKSLEVLVLDEADRLLDLGFEADLN 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 555017726 173 TIAGetRWRKQ--TMLFSATLEgDAIKDFAERLLEEPVEVS 211
Cdd:cd17960  165 RILS--KLPKQrrTGLFSATQT-DAVEELIKAGLRNPVRVV 202
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
20-210 1.34e-35

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: 130.54  E-value: 1.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLD----FPRKKSGPPRILILTPTRELAMQVADH 95
Cdd:cd17951    6 KKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEqekkLPFIKGEGPYGLIVCPSRELARQTHEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  96 ARELAKHTH------LDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQ 169
Cdd:cd17951   86 IEYYCKALQeggypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMGFEE 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 555017726 170 DIETIAGETRWRKQTMLFSATLEgDAIKDFAERLLEEPVEV 210
Cdd:cd17951  166 DIRTIFSYFKGQRQTLLFSATMP-KKIQNFAKSALVKPVTV 205
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
23-211 3.62e-35

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: 129.21  E-value: 3.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKksgpPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd17962    9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----PSALILTPTRELAVQIEDQAKELMKG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 T-HLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWR 181
Cdd:cd17962   85 LpPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 555017726 182 KQTMLFSATLEGdAIKDFAERLLEEPVEVS 211
Cdd:cd17962  165 HQTILVSATIPR-GIEQLAGQLLQNPVRIT 193
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
22-211 7.16e-34

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: 127.05  E-value: 7.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  22 KGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHARELA 100
Cdd:cd18049   42 QNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDgPICLVLAPTRELAQQVQQVAAEYG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRW 180
Cdd:cd18049  122 RACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 201
                        170       180       190
                 ....*....|....*....|....*....|.
gi 555017726 181 RKQTMLFSATLEGDaIKDFAERLLEEPVEVS 211
Cdd:cd18049  202 DRQTLMWSATWPKE-VRQLAEDFLKDYIHIN 231
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
21-211 2.10e-33

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 [Multi-domain]  Cd Length: 271  Bit Score: 126.66  E-value: 2.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP-PRILILTPTRELAMQVADHAREL 99
Cdd:cd18050   79 DQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDgPICLVLAPTRELAQQVQQVADDY 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd18050  159 GKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR 238
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEGDaIKDFAERLLEEPVEVS 211
Cdd:cd18050  239 PDRQTLMWSATWPKE-VRQLAEDFLRDYVQIN 269
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
20-210 1.03e-32

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: 122.81  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLldfprkksgppRILILTPTRELAMQVADHAREL 99
Cdd:cd17938   15 EELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-----------VALILEPSRELAEQTYNCIENF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 100 AKHTH---LDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI-- 174
Cdd:cd17938   84 KKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIyn 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 555017726 175 ----AGETRWRKQTMLFSATLEGDAIKDFAERLLEEPVEV 210
Cdd:cd17938  164 ripkITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWV 203
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
41-197 1.53e-32

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: 123.13  E-value: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  41 GRDILGSAPTGTGKTAAYLLPALQHLLDFPRkksgpPRI--LILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMN 118
Cdd:cd17956   36 PGDLCVSAPTGSGKTLAYVLPIVQALSKRVV-----PRLraLIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFKK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 119 --------HAEVFSENQDIVVATTGRLLQYIKE-ENFDCRAVETLILDEADRMLDMGFAQDIETIAGET----------- 178
Cdd:cd17956  111 eqklllvdTSGRYLSRVDILVATPGRLVDHLNStPGFTLKHLRFLVIDEADRLLNQSFQDWLETVMKALgrptapdlgsf 190
                        170       180
                 ....*....|....*....|....*...
gi 555017726 179 -------RWRK--QTMLFSATLEGDAIK 197
Cdd:cd17956  191 gdanlleRSVRplQKLLFSATLTRDPEK 218
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
22-210 2.19e-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: 121.66  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  22 KGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLlDFPRKKsgpPRILILTPTRELAMQVADHARELAK 101
Cdd:cd17939   15 YGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-DTTVRE---TQALVLAPTRELAQQIQKVVKALGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 102 HTHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI----AGE 177
Cdd:cd17939   91 YMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIfqflPPE 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 178 TrwrkQTMLFSATLEGDAIKdFAERLLEEPVEV 210
Cdd:cd17939  171 T----QVVLFSATMPHEVLE-VTKKFMRDPVRI 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
235-343 2.96e-32

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 118.47  E-value: 2.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  235 KTKLLVNLLQQPEATRAIVFVRKRERVhELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDI 314
Cdd:pfam00271   2 KLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100
                  ....*....|....*....|....*....
gi 555017726  315 PDVSHVFNFDMPRTADTYLHRIGRTGRAG 343
Cdd:pfam00271  81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
40-190 1.28e-30

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: 117.26  E-value: 1.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  40 DGRDILGSAPTGTGKTAAYLLPALQHLL--DFPRKKSGPPRILILTPTRELAMQVADHARELAKHthLDIATITGGVAYM 117
Cdd:cd17944   26 SGKDLIAQARTGTGKTFSFAIPLIEKLQedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRK--LSVACFYGGTPYQ 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555017726 118 NHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGEtRWRK------QTMLFSAT 190
Cdd:cd17944  104 QQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV-SYKKdsednpQTLLFSAT 181
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
42-210 2.50e-29

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: 113.44  E-value: 2.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  42 RDILGSAPTGTGKTAAYLLPALQHLlDfPRKKSgpPRILILTPTRELAMQVADHARELAKHTHLDIA-TITGGVAYMNha 120
Cdd:cd17963   34 ENLIAQSQSGTGKTAAFVLAMLSRV-D-PTLKS--PQALCLAPTRELARQIGEVVEKMGKFTGVKVAlAVPGNDVPRG-- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 121 EVFSENqdIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDM-GFAQDIETIAGETRWRKQTMLFSATLEgDAIKDF 199
Cdd:cd17963  108 KKITAQ--IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRIKRMLPRNCQILLFSATFP-DSVRKF 184
                        170
                 ....*....|.
gi 555017726 200 AERLLEEPVEV 210
Cdd:cd17963  185 AEKIAPNANTI 195
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
21-211 3.03e-29

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: 113.13  E-value: 3.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLldfpRKKSGPPRILILTPTRELAMQVADHARELA 100
Cdd:cd17943    7 AAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----DLERRHPQVLILAPTREIAVQIHDVFKKIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KH-THLDIATITGGVAYMNHAEVFSENQdIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETR 179
Cdd:cd17943   83 KKlEGLKCEVFIGGTPVKEDKKKLKGCH-IAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLP 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 555017726 180 WRKQTMLFSATLEGDAIKDFAeRLLEEPVEVS 211
Cdd:cd17943  162 KNKQVIAFSATYPKNLDNLLA-RYMRKPVLVR 192
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
23-210 9.11e-29

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: 112.18  E-value: 9.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQhLLDFPRKKsgpPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd18045   18 GFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDIQVRE---TQALILSPTRELAVQIQKVLLALGDY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 THLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRK 182
Cdd:cd18045   94 MNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDVYRYLPPAT 173
                        170       180
                 ....*....|....*....|....*...
gi 555017726 183 QTMLFSATLEGDaIKDFAERLLEEPVEV 210
Cdd:cd18045  174 QVVLVSATLPQD-ILEMTNKFMTDPIRI 200
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
21-210 6.38e-28

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: 109.74  E-value: 6.38e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSgpprILILTPTRELAMQVADHARELA 100
Cdd:cd17950   19 DCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS----VLVICHTRELAFQISNEYERFS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KH-THLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYIKEENFDCRAVETLILDEADRML-DMGFAQDIETIAGE 177
Cdd:cd17950   95 KYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQLDMRRDVQEIFRA 174
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 178 TRWRKQTMLFSATLEGDaIKDFAERLLEEPVEV 210
Cdd:cd17950  175 TPHDKQVMMFSATLSKE-IRPVCKKFMQDPLEI 206
HELICc smart00490
helicase superfamily c-terminal domain;
263-343 7.60e-27

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 102.68  E-value: 7.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726   263 ELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRA 342
Cdd:smart00490   2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                   .
gi 555017726   343 G 343
Cdd:smart00490  82 G 82
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
24-190 2.21e-26

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: 106.66  E-value: 2.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  24 FTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLdfprkKSGP-----------------PRILILTPTR 86
Cdd:cd18051   41 YTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY-----EQGPgeslpsesgyygrrkqyPLALVLAPTR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  87 ELAMQVADHARELAKHTHLDIATITGGvaymnhAEVFSENQDI------VVATTGRLLQYIKEENFDCRAVETLILDEAD 160
Cdd:cd18051  116 ELASQIYDEARKFAYRSRVRPCVVYGG------ADIGQQMRDLergchlLVATPGRLVDMLERGKIGLDYCKYLVLDEAD 189
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 555017726 161 RMLDMGFAQDIETI--------AGEtrwrKQTMLFSAT 190
Cdd:cd18051  190 RMLDMGFEPQIRRIveqdtmppTGE----RQTLMFSAT 223
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
20-174 1.44e-25

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: 103.99  E-value: 1.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  20 QDKGFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGP---PRILILTPTRELAMQVADHA 96
Cdd:cd17948    6 QRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnaPRGLVITPSRELAEQIGSVA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  97 RELAKHTHLDIATITGG--VAYMNHAEvFSENqDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETI 174
Cdd:cd17948   86 QSLTEGLGLKVKVITGGrtKRQIRNPH-FEEV-DILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHF 163
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
23-210 1.64e-23

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: 97.52  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDGRDILGSAPTGTGKTAAYLLPALQHlLDFPRKKsgpPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd18046   18 GFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQ-IDTSLKA---TQALVLAPTRELAQQIQKVVMALGDY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 103 THLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRK 182
Cdd:cd18046   94 MGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPDT 173
                        170       180
                 ....*....|....*....|....*...
gi 555017726 183 QTMLFSATLEGDAIkDFAERLLEEPVEV 210
Cdd:cd18046  174 QVVLLSATMPNDVL-EVTTKFMRDPIRI 200
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
40-357 3.94e-20

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 92.78  E-value: 3.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  40 DGRDILGSAPTGTGKTAAyllpalqhLLDFPRKKSGPPRILILTPTRELAMQVADHARElakhtHLDIATITGGVaymnh 119
Cdd:COG1061   99 GGGRGLVVAPTGTGKTVL--------ALALAAELLRGKRVLVLVPRRELLEQWAEELRR-----FLGDPLAGGGK----- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 120 aevFSENQDIVVATTGRLLQYIKEENFDcRAVETLILDEADRMLDMGFAQDIETIAGETRwrkqtMLFSATLE---GDAI 196
Cdd:COG1061  161 ---KDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAFPAAYR-----LGLTATPFrsdGREI 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 197 KDF----------AERLLEE---------PVEVSANPSTRERKKIHQWYYR--ADDIEHKTKLLVNLLQQ-PEATRAIVF 254
Cdd:COG1061  232 LLFlfdgivyeysLKEAIEDgylappeyyGIRVDLTDERAEYDALSERLREalAADAERKDKILRELLREhPDDRKTLVF 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 255 VRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLH 334
Cdd:COG1061  312 CSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQ 391
                        330       340
                 ....*....|....*....|...
gi 555017726 335 RIGRTGRAGKKGTAISLVEAHDH 357
Cdd:COG1061  392 RLGRGLRPAPGKEDALVYDFVGN 414
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
48-190 8.26e-19

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: 82.84  E-value: 8.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  48 APTGTGKTAAYLLPALQHLLDFprkksgPPRILILTPTRELAMQVADHARELAKHtHLDIATITGGVAYMNHAEVFSENQ 127
Cdd:cd00046    8 APTGSGKTLAALLAALLLLLKK------GKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKLGDA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555017726 128 DIVVATTGRLLQYIKEENFDC-RAVETLILDEADRMLDMGFAQDIETIAGETRWRK--QTMLFSAT 190
Cdd:cd00046   81 DIIIATPDMLLNLLLREDRLFlKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnaQVILLSAT 146
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
48-191 3.26e-18

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: 83.97  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  48 APTGTGKTAAYLLPALQHLLDF-------------PRKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATI--TG 112
Cdd:cd17965   68 AETGSGKTLAYLAPLLDYLKRQeqepfeeaeeeyeSAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFssGF 147
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555017726 113 GVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLFSATL 191
Cdd:cd17965  148 GPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATI 226
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
39-356 7.36e-18

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 86.04  E-value: 7.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRkksgpPRILILTPTRELAmqvAD---HARELAKHTHLDI--ATITGG 113
Cdd:COG1205   69 RAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-----ATALYLYPTKALA---RDqlrRLRELAEALGLGVrvATYDGD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 114 VAYMNHAEVFsENQDIVVAT-----TGRLLQYIKEENFdCRAVETLILDEA---------------DRMLDmgfaqdiet 173
Cdd:COG1205  141 TPPEERRWIR-EHPDIVLTNpdmlhYGLLPHHTRWARF-FRNLRYVVIDEAhtyrgvfgshvanvlRRLRR--------- 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 174 IAGETRWRKQTMLFSATLeGDAiKDFAERLLEEPVE-VSANPSTRERKKI-------HQWYYRADDIEHKTKLLVNLLQQ 245
Cdd:COG1205  210 ICRHYGSDPQFILASATI-GNP-AEHAERLTGRPVTvVDEDGSPRGERTFvlwnpplVDDGIRRSALAEAARLLADLVRE 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 246 peATRAIVFVRKRERVHELANWLREAGINTcwLEGEMVQA--------KRNEAIKRLTDGRVNVLIATDVAARGIDIPDV 317
Cdd:COG1205  288 --GLRTLVFTRSRRGAELLARYARRALREP--DLADRVAAyragylpeERREIERGLRSGELLGVVSTNALELGIDIGGL 363
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 555017726 318 SHVFNFDMPRTADTYLHRIGRTGRAGKKGTAIsLVEAHD 356
Cdd:COG1205  364 DAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD 401
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
233-342 9.78e-18

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: 79.56  E-value: 9.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 233 EHKTKLLVNLLQ----QPEATRAIVFVRKRERVHELANWLRE---------------AGINTCWLEGEMVQAKRNEAIKR 293
Cdd:cd18802    6 IPKLQKLIEILReyfpKTPDFRGIIFVERRATAVVLSRLLKEhpstlafircgfligRGNSSQRKRSLMTQRKQKETLDK 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 555017726 294 LTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRtGRA 342
Cdd:cd18802   86 FRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
194-345 2.27e-15

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 78.62  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 194 DAIKDFAERLLEEPVEVSANPSTR---ERKKIHQWYYRAD--DIEH-KTKLLVNLLQQPEAT----RAIVFVRKRERVHE 263
Cdd:COG1111  289 EALLRYLERLEEEARSSGGSKASKrlvSDPRFRKAMRLAEeaDIEHpKLSKLREILKEQLGTnpdsRIIVFTQYRDTAEM 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 264 LANWLREAGINTCWLEGE--------MVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHR 335
Cdd:COG1111  369 IVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQR 448
                        170
                 ....*....|
gi 555017726 336 IGRTGRAGKK 345
Cdd:COG1111  449 KGRTGRKREG 458
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
39-356 1.04e-13

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 72.87  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALqhLLDfprkksGPprILILTPTreLA-M--QVaDHARELakhthldiatitgGV- 114
Cdd:COG0514   30 LAGRDALVVMPTGGGKSLCYQLPAL--LLP------GL--TLVVSPL--IAlMkdQV-DALRAA-------------GIr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 115 -AYMNHAEVFSENQDIV------------VA----TTGRLLQYIKEENFDCRAVetlilDEA--------D-----RMLD 164
Cdd:COG0514   84 aAFLNSSLSAEERREVLralragelkllyVAperlLNPRFLELLRRLKISLFAI-----DEAhcisqwghDfrpdyRRLG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 165 MgFAQDIETIagetrwrkQTMLFSATLEGDAIKDFAERL-LEEPVEVSANPstrERKKIHqwyYRADDIEHKTKL--LVN 241
Cdd:COG0514  159 E-LRERLPNV--------PVLALTATATPRVRADIAEQLgLEDPRVFVGSF---DRPNLR---LEVVPKPPDDKLaqLLD 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 242 LLQQPEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATdVA-ARGIDIPDVSHV 320
Cdd:COG0514  224 FLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFV 302
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 555017726 321 FNFDMPRTADTYLHRIGRTGRAGKKGTAISLVEAHD 356
Cdd:COG0514  303 IHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
PRK13766 PRK13766
Hef nuclease; Provisional
194-431 5.92e-13

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 71.06  E-value: 5.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 194 DAIKDFAERLLEEPVEVSANPSTR---ERKKIHQWYYRAD--DIEH-KTKLLVNLLQQP----EATRAIVFVRKRERVHE 263
Cdd:PRK13766 301 EALRRYLERLREEARSSGGSKASKrlvEDPRFRKAVRKAKelDIEHpKLEKLREIVKEQlgknPDSRIIVFTQYRDTAEK 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 264 LANWLREAGINTCWLEGE--------MVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHR 335
Cdd:PRK13766 381 IVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQR 460
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 336 IGRTGRaGKKGTAISLV------EAHDHlllgkIGRYIE-------EPLKARVIDELRPTTRAPSEKLTGKPSKKVLAKR 402
Cdd:PRK13766 461 KGRTGR-QEEGRVVVLIakgtrdEAYYW-----SSRRKEkkmkeelKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDF 534
                        250       260
                 ....*....|....*....|....*....
gi 555017726 403 AQKKKDEKEKPRVKKRHRDTKNIGKRRKP 431
Cdd:PRK13766 535 VKSKGKEEEEEEEKEEKDKETEEDEPEGP 563
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
21-207 8.50e-13

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: 67.05  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  21 DKGFTRPTAIQAAAIPPAL--DGRDILGSAPTGTGKTAAYLLPALQHlLDFPRKKSgppRILILTPTRELAMQVADHARE 98
Cdd:cd18047   18 AMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYP---QCLCLSPTYELALQTGKVIEQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  99 LAK-HTHLDIATITGGVAYMNHAEVfseNQDIVVATTGRLLQY-IKEENFDCRAVETLILDEADRMLDMGFAQDiETIAG 176
Cdd:cd18047   94 MGKfYPELKLAYAVRGNKLERGQKI---SEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEADVMIATQGHQD-QSIRI 169
                        170       180       190
                 ....*....|....*....|....*....|...
gi 555017726 177 ETRWRK--QTMLFSATLEgDAIKDFAERLLEEP 207
Cdd:cd18047  170 QRMLPRncQMLLFSATFE-DSVWKFAQKVVPDP 201
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
23-207 8.61e-13

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: 67.74  E-value: 8.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  23 GFTRPTAIQAAAIPPALDG--RDILGSAPTGTGKTAAYLLPALQHLldfpRKKSGPPRILILTPTRELAMQVADHARELA 100
Cdd:cd18048   37 GFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV----DALKLYPQCLCLSPTFELALQTGKVVEEMG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 101 KHThLDIATITGGVAYMNHAEVFSENQdIVVATTGRLLQY-IKEENFDCRAVETLILDEADRMLDM-GFAQDIETIAGET 178
Cdd:cd18048  113 KFC-VGIQVIYAIRGNRPGKGTDIEAQ-IVIGTPGTVLDWcFKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRSM 190
                        170       180
                 ....*....|....*....|....*....
gi 555017726 179 RWRKQTMLFSATLEgDAIKDFAERLLEEP 207
Cdd:cd18048  191 PKECQMLLFSATFE-DSVWAFAERIVPDP 218
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
287-346 8.05e-12

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 60.80  E-value: 8.05e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 287 RNEAIKRLTDgRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKG 346
Cdd:cd18785   12 SIEHAEEIAS-SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
217-341 2.81e-11

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: 61.22  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 217 RERKKIHQwyyradDIEHKTKLLVNLLQQPEA---TRAIVFVRKRERVHELANWLRE--AGINTCWLEGE--------MV 283
Cdd:cd18801    2 RKVEKIHP------KLEKLEEIVKEHFKKKQEgsdTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGQasgksskgMS 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 555017726 284 QAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGR 341
Cdd:cd18801   76 QKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
219-349 1.99e-10

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 58.37  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 219 RKKIHQWYYRADDIEHKTKLLVNLLQQPEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGR 298
Cdd:cd18794    1 RPNLFYSVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 555017726 299 VNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKGTAI 349
Cdd:cd18794   81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECI 131
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
48-345 4.21e-09

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: 57.82  E-value: 4.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  48 APTGTGKTAAYLLPALQHLldfprKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMN-HAEVFSEN 126
Cdd:cd09639    6 APTGYGKTEAALLWALHSL-----KSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMgDSEEFEHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 127 QDIVVATTGRLLQY-IKEENFDCRAVE------------------TLILDEADRMLD---MGFAQDIETIAgetRWRKQT 184
Cdd:cd09639   81 FPLYIHSNDTLFLDpITVCTIDQVLKSvfgefghyeftlasiansLLIFDEVHFYDEytlALILAVLEVLK---DNDVPI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 185 MLFSATLEgDAIKDFAERLleEPVEvsaNPSTRERKKIHQWYY--RADDIEHKTKLLVNLLQQ-PEATRAIVFVRKRERV 261
Cdd:cd09639  158 LLMSATLP-KFLKEYAEKI--GYVE---ENEPLDLKPNERAPFikIESDKVGEISSLERLLEFiKKGGSVAIIVNTVDRA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 262 HELANWLREAG--INTCWLEGEMVQA----KRNEAIKRLTDGRVNVLIATDVAARGIDIpdvshvfNFDM----PRTADT 331
Cdd:cd09639  232 QEFYQQLKEKGpeEEIMLIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDI-------SVDVmiteLAPIDS 304
                        330
                 ....*....|....
gi 555017726 332 YLHRIGRTGRAGKK 345
Cdd:cd09639  305 LIQRLGRLHRYGEK 318
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
39-203 4.88e-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: 4.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKksgpprILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMN 118
Cdd:cd17921   15 LSGDSVLVSAPTSSGKTLIAELAILRALATSGGK------AVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 119 HAEvfsENQDIVVATTGRLLQYI-KEENFDCRAVETLILDEADRMLDMGFAQDIETIAGETRWRKQTMLF---SATLeGD 194
Cdd:cd17921   89 LLL---AEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKNARFvglSATL-PN 164

                 ....*....
gi 555017726 195 AiKDFAERL 203
Cdd:cd17921  165 A-EDLAEWL 172
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
42-159 7.83e-09

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: 55.35  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  42 RDILGSAPTGTGKT--AAYLLPALQHLLDfpRKKSGPPRILILTPTRELAMQVADHARElakHTHLDIATITGG-VAYMN 118
Cdd:cd18034   17 RNTIVVLPTGSGKTliAVMLIKEMGELNR--KEKNPKKRAVFLVPTVPLVAQQAEAIRS---HTDLKVGEYSGEmGVDKW 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 555017726 119 HAEVFSE---NQDIVVATTGRLLQYIKEENFDCRAVETLILDEA 159
Cdd:cd18034   92 TKERWKEeleKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
39-356 2.33e-08

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 56.06  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLldfprKKSGppRILILTPTRELAMQVADHARELAKHTHLDIATITGgvAYMN 118
Cdd:COG1204   36 LEGKNLVVSAPTASGKTLIAELAILKAL-----LNGG--KALYIVPLRALASEKYREFKRDFEELGIKVGVSTG--DYDS 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 119 HAEVFSENqDIVVATTGRLLQYIKEENFDCRAVETLILDEA------DRmldmGFaqDIETIAgeTRWRK-----QTMLF 187
Cdd:COG1204  107 DDEWLGRY-DILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GP--TLEVLL--ARLRRlnpeaQIVAL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 188 SATLEGdaIKDFAERLLEEPVEVSANPSTRERKKIHQWYYRADDIEHKTKL-LVNLLQQ--PEATRAIVFVRKR------ 258
Cdd:COG1204  178 SATIGN--AEEIAEWLDAELVKSDWRPVPLNEGVLYDGVLRFDDGSRRSKDpTLALALDllEEGGQVLVFVSSRrdaesl 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 259 -----------------ERVHELANWLREAG--INTCWLEGEMVQ-------AKRNEAIKRL-----TDGRVNVLIATDV 307
Cdd:COG1204  256 akkladelkrrltpeerEELEELAEELLEVSeeTHTNEKLADCLEkgvafhhAGLPSELRRLvedafREGLIKVLVATPT 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 555017726 308 AARGIDIPdVSHVF------NFDMPRTADTYLHRIGRTGRAGK--KGTAISLVEAHD 356
Cdd:COG1204  336 LAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGYdpYGEAILVAKSSD 391
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
40-112 4.86e-08

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: 52.59  E-value: 4.86e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 555017726  40 DGRDILGSAPTGTGKTAAYLLPALQHLLDFPRkksgpPRILILTPTRELAMQVADHARELAKHTHLDI--ATITG 112
Cdd:cd17923   14 AGRSVVVTTGTASGKSLCYQLPILEALLRDPG-----SRALYLYPTKALAQDQLRSLRELLEQLGLGIrvATYDG 83
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
235-339 5.58e-08

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 55.23  E-value: 5.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 235 KTKLLVNLLQQPEAT--RAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDG---RVnVLIATDVAA 309
Cdd:COG0553  534 KLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpeaPV-FLISLKAGG 612
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 555017726 310 RGIDIPDVSHVFNFDMP-----------RtadtyLHRIGRT 339
Cdd:COG0553  613 EGLNLTAADHVIHYDLWwnpaveeqaidR-----AHRIGQT 648
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
235-337 9.89e-08

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 50.55  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 235 KTKLLVNLLQQ--PEATRAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRL-TDGRVNV-LIATDVAAR 310
Cdd:cd18793   12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGGV 91
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 555017726 311 GIDIPDVSHVFNFDMP-----------RtadtyLHRIG 337
Cdd:cd18793   92 GLNLTAANRVILYDPWwnpaveeqaidR-----AHRIG 124
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
41-107 2.56e-07

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: 50.27  E-value: 2.56e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555017726  41 GRDILGSAPTGTGKTAAYLLPALQHLLDFPRKksgPPRILILTPTRELAMQVADHARELAKHTHLDI 107
Cdd:cd17922    1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK---GVQVLYISPLKALINDQERRLEEPLDEIDLEI 64
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
226-353 2.92e-07

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 50.38  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 226 YYRADDIEHKTKLLVNLLqqpeATRAIVFVRK---RERVHELANWLREAGINTcwlegEMVQAKRNEAIKRLTDGRVNVL 302
Cdd:cd18798    6 YIEDSDSLEKLLELVKKL----GDGGLIFVSIdygKEYAEELKEFLERHGIKA-----ELALSSTEKNLEKFEEGEIDVL 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726 303 IAT----DVAARGIDIPDVSH--VFnFDMPrtADTYLHRIGRTGR--AG--KKGTAISLVE 353
Cdd:cd18798   77 IGVasyyGVLVRGIDLPERIKyaIF-YGVP--VTTYIQASGRTSRlyAGglTKGLSVVLVD 134
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
42-162 3.72e-07

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: 50.11  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  42 RDILGSAPTGTGKTAAYLLPALQHLldfprkkSGPPRILILTPTRELAMQVADHARELAKHTHldIATITGGVaymnhAE 121
Cdd:cd17918   37 MDRLLSGDVGSGKTLVALGAALLAY-------KNGKQVAILVPTEILAHQHYEEARKFLPFIN--VELVTGGT-----KA 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 555017726 122 VFSENQDIVVATTGRLLQYIKEENFDcraveTLILDEADRM 162
Cdd:cd17918  103 QILSGISLLVGTHALLHLDVKFKNLD-----LVIVDEQHRF 138
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
205-346 4.94e-07

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 49.17  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 205 EEPVEVSANPSTRERKKIHqwyyraddIEHKTKL--LVNLLQQPEAT-RAIVFVRKRERVHELANWLREAGINtcwleGE 281
Cdd:cd18789   11 EFYREYLGLGAHRKRRLLA--------AMNPNKLraLEELLKRHEQGdKIIVFTDNVEALYRYAKRLLKPFIT-----GE 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726 282 MVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPD------VSHVFNfdmprTADTYLHRIGRTGRAGKKG 346
Cdd:cd18789   78 TPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEanvaiqISGHGG-----SRRQEAQRLGRILRPKKGG 143
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
40-112 6.80e-07

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 51.46  E-value: 6.80e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555017726  40 DGRDILGSAPTGTGKTAAYLLPALQHLLDfpRKKsgppRILILTPTRELAMQVADHA-RELAKHTHLDI--ATITG 112
Cdd:COG1199   32 EGRHLLIEAGTGTGKTLAYLVPALLAARE--TGK----KVVISTATKALQEQLVEKDlPLLRKALGLPLrvALLKG 101
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
252-344 7.20e-07

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 48.41  E-value: 7.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 252 IVFVRKRERVHELANWLREAGINTCWLE------GEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDM 325
Cdd:cd18796   42 LVFTNTRSQAERLAQRLRELCPDRVPPDfialhhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS 121
                         90
                 ....*....|....*....
gi 555017726 326 PRTADTYLHRIGRTGRAGK 344
Cdd:cd18796  122 PKSVARLLQRLGRSGHRPG 140
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
39-356 2.06e-06

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 50.10  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALqhLLDfprkksgpPRILILTPTRELaMQvaDHARELAKHthldiatitgGVA--Y 116
Cdd:PRK11057  38 LSGRDCLVVMPTGGGKSLCYQIPAL--VLD--------GLTLVVSPLISL-MK--DQVDQLLAN----------GVAaaC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 117 MNHAEVFSENQDIVVAT-TGRL-LQYIKEE-----NFDCRAVET----LILDEADRMLDMGFAQDIETIA-GETRWRKQT 184
Cdd:PRK11057  95 LNSTQTREQQLEVMAGCrTGQIkLLYIAPErlmmdNFLEHLAHWnpalLAVDEAHCISQWGHDFRPEYAAlGQLRQRFPT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 185 ---MLFSATLEGDAIKDFAERL-LEEPVEvsaNPSTRERKKIhqwyyRADDIE-HK-TKLLVNLLQQPEATRAIVFVRKR 258
Cdd:PRK11057 175 lpfMALTATADDTTRQDIVRLLgLNDPLI---QISSFDRPNI-----RYTLVEkFKpLDQLMRYVQEQRGKSGIIYCNSR 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 259 ERVHELANWLREAGINTCWLEGEMVQAKRN---EAIKRltdGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADTYLHR 335
Cdd:PRK11057 247 AKVEDTAARLQSRGISAAAYHAGLDNDVRAdvqEAFQR---DDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQE 323
                        330       340
                 ....*....|....*....|.
gi 555017726 336 IGRTGRAGKKGTAISLVEAHD 356
Cdd:PRK11057 324 TGRAGRDGLPAEAMLFYDPAD 344
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
250-317 2.31e-06

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 46.40  E-value: 2.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726 250 RAIVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRN-EAIKRLTDG--RVNVLIATDVAARGIDIPDV 317
Cdd:cd18799    8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGelKPPILVTVDLLTTGVDIPEV 78
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
39-99 4.15e-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: 49.09  E-value: 4.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726   39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAmqvADHAREL 99
Cdd:TIGR04121  26 LEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYITPLRALA---VDIARNL 83
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
252-349 6.21e-06

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 48.74  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  252 IVFVRKRERVHELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFDMPRTADT 331
Cdd:PLN03137  684 IIYCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEG 763
                          90
                  ....*....|....*...
gi 555017726  332 YLHRIGRTGRAGKKGTAI 349
Cdd:PLN03137  764 YHQECGRAGRDGQRSSCV 781
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
48-161 1.31e-05

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: 45.58  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  48 APTGTGKTAAYLLPALQHLldfpRKKSGppRILILTPTRELAMQVADHARELAkHTHLDIATITGGVAYMNHAEVFSENQ 127
Cdd:cd18035   23 LPTGLGKTIIAILVAADRL----TKKGG--KVLILAPSRPLVEQHAENLKRVL-NIPDKITSLTGEVKPEERAERWDASK 95
                         90       100       110
                 ....*....|....*....|....*....|....
gi 555017726 128 dIVVATTGRLLQYIKEENFDCRAVETLILDEADR 161
Cdd:cd18035   96 -IIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
42-161 2.16e-05

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 44.47  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  42 RDILGSAPTGTGKT--AAYLLPALQhlldfprKKSGPPRILILTPTRELAMQVADHARElakhtHLDIATItgGVAYMNH 119
Cdd:cd18032   21 RRALLVMATGTGKTytAAFLIKRLL-------EANRKKRILFLAHREELLEQAERSFKE-----VLPDGSF--GNLKGGK 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 555017726 120 AEVFSEnqDIVVATTGRLLQYIKEENFDCRAVETLILDEADR 161
Cdd:cd18032   87 KKPDDA--RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
39-161 3.66e-05

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


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 44.35  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGppRILILTPTRELAMQvadHARELAKHTH---LDIATITGGVA 115
Cdd:cd17927   15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG--KVVFLANKVPLVEQ---QKEVFRKHFErpgYKVTGLSGDTS 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 555017726 116 YMNHAEVFSENQDIVVATTGRLLQYIKE------ENFDCravetLILDEADR 161
Cdd:cd17927   90 ENVSVEQIVESSDVIIVTPQILVNDLKSgtivslSDFSL-----LVFDECHN 136
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
48-102 4.44e-05

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


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 44.20  E-value: 4.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 555017726  48 APTGTGKTAAYLLPALQHlldfpRKKSGPPRILILTPTRELAMQVADHARELAKH 102
Cdd:cd17930    8 APTGSGKTEAALLWALKL-----AARGGKRRIIYALPTRATINQMYERIREILGR 57
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
47-208 7.66e-05

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 43.09  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  47 SAPTGTGKTAAYLLPALQHLLDFPRkksgppRILILTPtRELAMQVAdhARELAKhthLDIATITGGVAYMNHAE-VFSE 125
Cdd:cd17990   23 EAPPGAGKTTRVPLALLAELWIAGG------KIIVLEP-RRVAARAA--ARRLAT---LLGEAPGETVGYRVRGEsRVGR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 126 NQDIVVATTGRLLQYIkEENFDCRAVETLILDEA-DRML--DMGFAQDIEtIAGETRWRKQTMLFSATLEGDAikdFAER 202
Cdd:cd17990   91 RTRVEVVTEGVLLRRL-QRDPELSGVGAVILDEFhERSLdaDLALALLLE-VQQLLRDDLRLLAMSATLDGDG---LAAL 165

                 ....*.
gi 555017726 203 LLEEPV 208
Cdd:cd17990  166 LPEAPV 171
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
39-89 8.29e-05

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 45.09  E-value: 8.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILIL--TPTRELA 89
Cdd:COG1201   37 AAGESTLLIAPTGSGKTLAAFLPALDELARRPRPGELPDGLRVLyiSPLKALA 89
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
47-159 8.42e-05

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 42.83  E-value: 8.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  47 SAPTGTGKTAayLLPalQHLLDFPRKKSGPPRILILTPTRELAMQVADH-ARELAkhthldiATITGGVAYMNHAE-VFS 124
Cdd:cd17917    7 VGETGSGKTT--QVP--QFLLEDGLAKGGKGRIVCTQPRRIAAISVAERvAEERG-------EKLGEEVGYQIRFEsKTS 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 555017726 125 ENQDIVVATTGRLLQYIkEENFDCRAVETLILDEA 159
Cdd:cd17917   76 SKTRIKFCTDGILLREL-LSDPLLSGYSHVILDEA 109
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
48-314 1.56e-04

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 43.92  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  48 APTGTGKTAAYLLPALQHlldfpRKKSGPPRILILTPTRELAMQVADHARE-----LAKHTHL-DIATITGGVAYMNHAE 121
Cdd:COG1203  154 APTGGGKTEAALLFALRL-----AAKHGGRRIIYALPFTSIINQTYDRLRDlfgedVLLHHSLaDLDLLEEEEEYESEAR 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 122 VFSE-----NQDIVVATTGRLLQ-YIKEENFDCR-------AVetLILDEADrMLDMGFAQDIETIageTRWRKQ----T 184
Cdd:COG1203  229 WLKLlkelwDAPVVVTTIDQLFEsLFSNRKGQERrlhnlanSV--IILDEVQ-AYPPYMLALLLRL---LEWLKNlggsV 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 185 MLFSATL---EGDAIKDFAERLLEEPVEVSANPSTRERKKIHqwyYRADDIEHKT--KLLVNLLQQPEatRAIVFVRKRE 259
Cdd:COG1203  303 ILMTATLpplLREELLEAYELIPDEPEELPEYFRAFVRKRVE---LKEGPLSDEElaELILEALHKGK--SVLVIVNTVK 377
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726 260 RVHELANWLREAG--INTCWLEGEMVQAKRNEAIK----RLTDGRVNVLIATDVAARGIDI 314
Cdd:COG1203  378 DAQELYEALKEKLpdEEVYLLHSRFCPADRSEIEKeikeRLERGKPCILVSTQVVEAGVDI 438
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
263-341 2.16e-04

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 41.85  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 263 ELANWLREAGINTCWLEGEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSHVFNFD-----MPRTADTYLHRIG 337
Cdd:cd18790   42 DLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETSLIQTIG 121

                 ....
gi 555017726 338 RTGR 341
Cdd:cd18790  122 RAAR 125
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
280-358 3.40e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 40.79  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 280 GEMVQAKRNEAIKRLTDGRVNVLIATDVAARGIDIPDVSH--VFNFDMPRTADTYLHRiGRTGRAGKKGTAISLVEAHDH 357
Cdd:cd18810   59 GQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTiiIERADKFGLAQLYQLR-GRVGRSKERAYAYFLYPDQKK 137

                 .
gi 555017726 358 L 358
Cdd:cd18810  138 L 138
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
47-159 4.39e-04

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: 40.37  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  47 SAPTGTGKT--AAYLLPALqhlldfprkksGPPRILILTPTRELAMQVADHARELAKHTHLDIatITGGvaymnhAEVFS 124
Cdd:cd17926   24 VLPTGSGKTltALALIAYL-----------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGL--IGGG------KKKDF 84
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 555017726 125 ENQDIVVATTGRLLQYIKEENFDCRAVETLILDEA 159
Cdd:cd17926   85 DDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
47-133 1.12e-03

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


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 40.03  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  47 SAPTGTGKTAAYLLPALQHLLDFPRKKSGPPRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMNHAEVFseN 126
Cdd:cd18023   23 SAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEMDDTFEIQ--D 100

                 ....*..
gi 555017726 127 QDIVVAT 133
Cdd:cd18023  101 ADIILTT 107
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
41-158 1.26e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 39.80  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  41 GRDILGSAPTGTGKTAAYLLPALQHLLDFPRKKSGppRILILTPTRELAMQVADHARELAKHTHLDIATITGGVAYMNHA 120
Cdd:cd18073   17 GKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG--KVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAENVPV 94
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 555017726 121 EVFSENQDIVVATTGRLLQYIKEENFDCRAVETLIL-DE 158
Cdd:cd18073   95 EQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIfDE 133
PRK07246 PRK07246
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
48-117 1.28e-03

bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated


Pssm-ID: 180905 [Multi-domain]  Cd Length: 820  Bit Score: 41.21  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726  48 APTGTGKTAAYLLPALQhlldfprkKSGPPRILILTPTRELAMQV-ADHARELAKHTHLDIATITGGVAYM 117
Cdd:PRK07246 271 AQTGIGKTYGYLLPLLA--------QSDQRQIIVSVPTKILQDQImAEEVKAIQEVFHIDCHSLKGPQNYL 333
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
39-63 3.51e-03

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: 38.67  E-value: 3.51e-03
                         10        20
                 ....*....|....*....|....*
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPAL 63
Cdd:cd17920   25 LAGRDVLVVMPTGGGKSLCYQLPAL 49
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
237-349 5.59e-03

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 37.24  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726 237 KLLVNLLQQpeATRAIVFVRKRERVHELANWLREAGINTCWLEGEmVQAKR-------NEAIKR-LTDGRVNVLIATDVA 308
Cdd:cd18797   26 RLFADLVRA--GVKTIVFCRSRKLAELLLRYLKARLVEEGPLASK-VASYRagylaedRREIEAeLFNGELLGVVATNAL 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 555017726 309 ARGIDIPDVSHVFNFDMPRTADTYLHRIGRTGRAGKKGTAI 349
Cdd:cd18797  103 ELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
39-133 6.79e-03

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 37.84  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555017726  39 LDGRDILGSAPTGTGKTAAYLLPALQHLLDFPrKKSGPPRILILTPTRELAMQvadHARELAKHTH--LDIATITGGVAY 116
Cdd:cd18036   15 LRGKNTIICAPTGSGKTRVAVYICRHHLEKRR-SAGEKGRVVVLVNKVPLVEQ---QLEKFFKYFRkgYKVTGLSGDSSH 90
                         90
                 ....*....|....*..
gi 555017726 117 MNHAEVFSENQDIVVAT 133
Cdd:cd18036   91 KVSFGQIVKASDVIICT 107
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
47-107 9.57e-03

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.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 37.31  E-value: 9.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555017726  47 SAPTGTGKTAAYLLPALqhlldFPRKKSGppRILILTPTRELAMQVADHARELAKHTHLDI 107
Cdd:cd17924   38 IAPTGVGKTTFGLATSL-----YLASKGK--RSYLIFPTKSLVKQAYERLSKYAEKAGVEV 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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