|
Name |
Accession |
Description |
Interval |
E-value |
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
338-548 |
8.67e-114 |
|
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: 348.42 E-value: 8.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLLSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGVLALVIVPTRELVMQT 417
Cdd:cd17949 2 VSHLKSKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDGTLALVLVPTRELALQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 418 YELIQKLVKPYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERD 497
Cdd:cd17949 82 YEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18859659 498 VKQLVEAIDKQRAEC--EDKELPQLQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd17949 162 ITKILELLDDKRSKAggEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
329-780 |
1.72e-105 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 334.42 E-value: 1.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 329 STLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRiqrkdGVLALVIV 408
Cdd:COG0513 5 ADLGLSPPLLKALAEL-GYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPR-----APQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 409 PTRELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTAsFKLTKLQFLILDEADR 488
Cdd:COG0513 79 PTRELALQVAEELRKLAK-YLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGA-LDLSGVETLVLDEADR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 489 LLELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYIdnsdeaasaalkskdgyqket 568
Cdd:COG0513 157 MLDMGFIEDIERILKLLPKER-----------QTLLFSATMPPEIRKLAKRYLKNPVRI--------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 569 ieallevddglgeyqeDVTGVLSIPENLQLSYVVVPPKLRLVALSSLLAKEvdaspKQFKAIVFMSTTEMVnfhhDMLNE 648
Cdd:COG0513 205 ----------------EVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE-----DPERAIVFCNTKRGA----DRLAE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 649 ALTRRvldeedeqekgdsdddgdipllqGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQY 728
Cdd:COG0513 260 KLQKR-----------------------GISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINY 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 18859659 729 TPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLEKK-RIRIQQGDM 780
Cdd:COG0513 317 DLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLiGQKIEEEEL 369
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
338-548 |
7.88e-69 |
|
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: 227.71 E-value: 7.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQqpRIQRKDGVLALVIVPTRELVMQT 417
Cdd:cd00268 2 LKALKKL-GFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPE--PKKKGRGPQALVLAPTRELAMQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 418 YELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFKLTKLQFLILDEADRLLELGYERD 497
Cdd:cd00268 79 AEVARKLGK-GTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDL-IERGKLDLSNVKYLVLDEADRMLDMGFEED 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18859659 498 VKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd00268 157 VEKILSALPKDR-----------QTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
349-548 |
6.60e-58 |
|
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: 197.58 E-value: 6.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQqpRIQRKDGVLALVIVPTRELVMQTYELIQKLVKpY 428
Cdd:cd17942 12 KMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKL--KFKPRNGTGVIIISPTRELALQIYGVAKELLK-Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 429 TWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQ 508
Cdd:cd17942 89 HSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIKLLPKR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18859659 509 RaecedkelpqlQRMLLSATLTSQVQQLAGLTLKN-PLYID 548
Cdd:cd17942 169 R-----------QTMLFSATQTRKVEDLARISLKKkPLYVG 198
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
348-547 |
1.06e-56 |
|
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: 194.05 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 348 RELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQqpRIQRKDGVLALVIVPTRELVMQTYELIQKLVKp 427
Cdd:cd17941 11 IKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRE--RWTPEDGLGALIISPTRELAMQIFEVLRKVGK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 428 YTWIVPGSLLGGESRKSEKARLrKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDK 507
Cdd:cd17941 88 YHSFSAGLIIGGKDVKEEKERI-NRMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18859659 508 QRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17941 167 SR-----------QTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
345-548 |
1.60e-54 |
|
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: 187.85 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 345 LSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdGVLALVIVPTRELVMQTYELIQKL 424
Cdd:cd17947 8 LGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKA---ATRVLVLVPTRELAMQCFSVLQQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 425 VKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEA 504
Cdd:cd17947 85 AQ-FTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18859659 505 IDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd17947 164 CPRTR-----------QTMLFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
329-769 |
2.56e-54 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 196.18 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 329 STLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIV 408
Cdd:PRK11776 7 STLPLPPALLANLNEL-GYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQ------ALVLC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 409 PTRELVMQTYELIQKL------VKPYTwivpgsLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFKLTKLQFLI 482
Cdd:PRK11776 80 PTRELADQVAKEIRRLarfipnIKVLT------LCGGVPMGPQIDSLEHGAHIIVGTPGRILDH-LRKGTLDLDALNTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 483 LDEADRLLELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYIdnsdeaasaalKSKD 562
Cdd:PRK11776 153 LDEADRMLDMGFQDAIDAIIRQAPARR-----------QTLLFSATYPEGIAAISQRFQRDPVEV-----------KVES 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 563 GYQKETIEallevddglgeyqedvtgvlsipenlQLSYVVVPPKlRLVALSSLLAKEVDASpkqfkAIVFMSTTEMVnfh 642
Cdd:PRK11776 211 THDLPAIE--------------------------QRFYEVSPDE-RLPALQRLLLHHQPES-----CVVFCNTKKEC--- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 643 hDMLNEALTRrvldeedeqekgdsdddgdipllQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDI 722
Cdd:PRK11776 256 -QEVADALNA-----------------------QGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18859659 723 KLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLE 769
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIE 358
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
345-547 |
9.18e-52 |
|
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: 180.46 E-value: 9.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 345 LSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDgVLALVIVPTRELVMQTYELIQKL 424
Cdd:cd17960 8 LGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKKGQ-VGALIISPTRELATQIYEVLQSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 425 VKPYTWIVPGSLL--GGESRKSEKARLRKGINILIGTPGRLVDHLLHTAS-FKLTKLQFLILDEADRLLELGYERDVKQL 501
Cdd:cd17960 87 LEHHLPKLKCQLLigGTNVEEDVKKFKRNGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLGFEADLNRI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18859659 502 VEAIDKQRaecedkelpqlqRM-LLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17960 167 LSKLPKQR------------RTgLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
351-536 |
1.87e-51 |
|
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: 177.82 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKqqpriqRKDGVLALVIVPTRELVMQTYELIQKLVKpYTW 430
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK------LDNGPQALVLAPTRELAEQIYEELKKLGK-GLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPGSLLGGESRKSEKARLrKGINILIGTPGRLVDHLLHTASFKltKLQFLILDEADRLLELGYERDVKQLVEAIDKQRa 510
Cdd:pfam00270 74 LKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKR- 149
|
170 180
....*....|....*....|....*.
gi 18859659 511 ecedkelpqlQRMLLSATLTSQVQQL 536
Cdd:pfam00270 150 ----------QILLLSATLPRNLEDL 165
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
348-548 |
1.46e-50 |
|
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: 177.39 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 348 RELTSVQQKTIPEVLQ-GKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDgVLALVIVPTRELVMQTYELIQKLVK 426
Cdd:cd17964 15 ETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG-VSALIISPTRELALQIAAEAKKLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 427 PYTWIVPGSLLGGESRKSEKARLRK-GINILIGTPGRLVDHLLHTASFK-LTKLQFLILDEADRLLELGYERDVKQLVEA 504
Cdd:cd17964 94 GLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRLLDMGFRPDLEQILRH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18859659 505 IDKQRAEcedkelpQLQRMLLSATLTSQVQQLAGLTL-KNPLYID 548
Cdd:cd17964 174 LPEKNAD-------PRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
338-548 |
6.15e-48 |
|
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: 170.51 E-value: 6.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLlSIRELTSVQQKTIPEVLQG---------KDVLVRSQTGSGKTLAYALPLVELLQKQQ-PRIQrkdgvlALVI 407
Cdd:cd17956 2 LKNLQNN-GITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVvPRLR------ALIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 408 VPTRELVMQTYELIQKLVKPYTWIVpGSLLGGESRKSEKARLRKG--------INILIGTPGRLVDHLLHTASFKLTKLQ 479
Cdd:cd17956 75 VPTKELVQQVYKVFESLCKGTGLKV-VSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859659 480 FLILDEADRLLELGYERDVKQLVEAIDKQRAECEDKEL---------PQLQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd17956 154 FLVIDEADRLLNQSFQDWLETVMKALGRPTAPDLGSFGdanllersvRPLQKLLFSATLTRDPEKLSSLKLHRPRLFT 231
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
331-547 |
7.17e-48 |
|
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: 169.42 E-value: 7.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVE-LLQKQQPriqrkdgVLALVIVP 409
Cdd:cd17954 5 LGVCEELCEACEKL-GWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQaLLENPQR-------FFALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 410 TRELVMQTYELIQKLvkpytwivpGS--------LLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFL 481
Cdd:cd17954 77 TRELAQQISEQFEAL---------GSsiglksavLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859659 482 ILDEADRLLELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17954 148 VMDEADRLLNMDFEPEIDKILKVIPRER-----------TTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
351-754 |
1.67e-47 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 175.90 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELL------QKQQPRIqrkdgvlaLVIVPTRELVMQTYELIQKL 424
Cdd:PRK11192 25 TAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprrKSGPPRI--------LILTPTRELAMQVADQAREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 425 VKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVea 504
Cdd:PRK11192 97 AK-HTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQY-IKEENFDCRAVETLILDEADRMLDMGFAQDIETIA-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 505 idkqrAECEDKElpqlQRMLLSATLTSQ-VQQLAGLTLKNPLYIDnsdeaASAALKSKdgyqKETIEALLEVDDglgeyq 583
Cdd:PRK11192 173 -----AETRWRK----QTLLFSATLEGDaVQDFAERLLNDPVEVE-----AEPSRRER----KKIHQWYYRADD------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 584 edvtgvlsipenlqlsyvvVPPKLRLvaLSSLLaKEVDASpkqfKAIVFMSTTEMVNfhhdMLNEALTRRvldeedeqek 663
Cdd:PRK11192 229 -------------------LEHKTAL--LCHLL-KQPEVT----RSIVFVRTRERVH----ELAGWLRKA---------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 664 gdsdddgdipllqGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGR 743
Cdd:PRK11192 269 -------------GINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGR 335
|
410
....*....|.
gi 18859659 744 TARAGRKGRAV 754
Cdd:PRK11192 336 TGRAGRKGTAI 346
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
331-547 |
9.11e-47 |
|
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: 166.25 E-value: 9.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLqkqqpriqRKD--GVLALVIV 408
Cdd:cd17955 4 LGLSSWLVKQCASL-GIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRL--------SEDpyGIFALVLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 409 PTRELVMQTYELIQKLVKPY----TWIVpgsllGGESRKSEKARLRKGINILIGTPGRLVDHLLH--TASFKLTKLQFLI 482
Cdd:cd17955 75 PTRELAYQIAEQFRALGAPLglrcCVIV-----GGMDMVKQALELSKRPHIVVATPGRLADHLRSsdDTTKVLSRVKFLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 483 LDEADRLLELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17955 150 LDEADRLLTGSFEDDLATILSALPPKR-----------QTLLFSATLTDALKALKELFGNKPFFW 203
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
351-544 |
1.91e-46 |
|
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: 165.45 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLVKPYTW 430
Cdd:cd17961 18 TLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQGTRALILVPTRELAQQVSKVLEQLTAYCRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPG-SLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEaidkqr 509
Cdd:cd17961 98 DVRVvNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLKSLLS------ 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 18859659 510 aecedkELPQ-LQRMLLSATLTSQVQQLAGLTLKNP 544
Cdd:cd17961 172 ------YLPKnYQTFLMSATLSEDVEALKKLVLHNP 201
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
347-770 |
3.15e-46 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 174.96 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 347 IRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALP-LVELLqkQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLV 425
Cdd:PTZ00110 150 FTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHIN--AQPLLRYGDGPIVLVLAPTRELAEQIREQCNKFG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 426 KPYTwIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAI 505
Cdd:PTZ00110 228 ASSK-IRNTVAYGGVPKRGQIYALRRGVEILIACPGRLID-FLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 506 DkqraecedkelPQLQRMLLSATLTSQVQQLA-GLTLKNPLYIDnsdeAASAALKSKDGYQKETIeaLLEvddglgEYQe 584
Cdd:PTZ00110 306 R-----------PDRQTLMWSATWPKEVQSLArDLCKEEPVHVN----VGSLDLTACHNIKQEVF--VVE------EHE- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 585 dvtgvlsipenlqlsyvvvppklRLVALSSLLAKEVDASPkqfKAIVFMSTTEMVNFhhdmlneaLTRRVldeedeqekg 664
Cdd:PTZ00110 362 -----------------------KRGKLKMLLQRIMRDGD---KILIFVETKKGADF--------LTKEL---------- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 665 dsdddgdipLLQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRT 744
Cdd:PTZ00110 398 ---------RLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRT 468
|
410 420
....*....|....*....|....*.
gi 18859659 745 ARAGRKGRAVLFLTPSEAQFVRHLEK 770
Cdd:PTZ00110 469 GRAGAKGASYTFLTPDKYRLARDLVK 494
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
330-770 |
7.45e-46 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 171.53 E-value: 7.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 330 TLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGVLALVIVP 409
Cdd:PRK10590 5 SLGLSPDILRAVAEQ-GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGRRPVRALILTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 410 TRELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRL 489
Cdd:PRK10590 84 TRELAAQIGENVRDYSK-YLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 490 LELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYIdnsdEAASAALKSkdgyqketi 569
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKR-----------QNLLFSATFSDDIKALAEKLLHNPLEI----EVARRNTAS--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 570 eallevddglgeyqEDVTgvlsipenlqlSYVVVPPKLRLVALSSLLAKEVDASpkqfKAIVFMSTTEMVNFHHDMLNEa 649
Cdd:PRK10590 218 --------------EQVT-----------QHVHFVDKKRKRELLSQMIGKGNWQ----QVLVFTRTKHGANHLAEQLNK- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 650 ltrrvldeedeqekgdsdddgdipllQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYT 729
Cdd:PRK10590 268 --------------------------DGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYE 321
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18859659 730 PPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLEK 770
Cdd:PRK10590 322 LPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEK 362
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
329-547 |
1.82e-45 |
|
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: 163.04 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 329 STLGLHPHAVKNLEdLLSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLV-ELLQKQQPRIQRKDGV---LA 404
Cdd:cd17967 3 EEAGLRELLLENIK-RAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIIsKLLEDGPPSVGRGRRKaypSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 405 LVIVPTRELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILD 484
Cdd:cd17967 82 LILAPTRELAIQIYEEARKFSY-RSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVD-FIERGRISLSSIKFLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859659 485 EADRLLELGYERDVKQLVEaiDKQRAECEDKelpqlQRMLLSATLTSQVQQLAGLTLKNplYI 547
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVE--HPDMPPKGER-----QTLMFSATFPREIQRLAADFLKN--YI 213
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
596-757 |
2.22e-44 |
|
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: 156.51 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 596 LQLSYVVVPPKLRLVALSSLLAKEvdasPKQFKAIVFMSTTEMVNFHHDMLNEAltrrvldeedeqekgdsdddgdipll 675
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEK----LKPGKAIIFVNTKKRVDRLAELLEEL-------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 676 qGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVL 755
Cdd:cd18787 51 -GIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAIT 129
|
..
gi 18859659 756 FL 757
Cdd:cd18787 130 FV 131
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
319-756 |
2.67e-43 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 163.22 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 319 KETIFTGSKISTLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYalpLV----ELLQKQQP 394
Cdd:PRK04837 1 SKTHLTEQKFSDFALHPQVVEALEKK-GFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAF---LTatfhYLLSHPAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 395 RIQRKDGVLALVIVPTRELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFK 474
Cdd:PRK04837 77 EDRKVNQPRALIMAPTRELAVQIHADAEPLAQ-ATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDY-AKQNHIN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 475 LTKLQFLILDEADRLLELGYERDVKQLVeaidkQRAECEDKELpqlqRMLLSATLTSQVQQLAGLTLKNPLYIDNSDEaa 554
Cdd:PRK04837 155 LGAIQVVVLDEADRMFDLGFIKDIRWLF-----RRMPPANQRL----NMLFSATLSYRVRELAFEHMNNPEYVEVEPE-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 555 saalkskdgyQKetieallevddglgeyqedvTGVlSIPEnlQLSYVVVPPKLRLvaLSSLLAKEvdaSPKqfKAIVFMS 634
Cdd:PRK04837 224 ----------QK--------------------TGH-RIKE--ELFYPSNEEKMRL--LQTLIEEE---WPD--RAIIFAN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 635 TTEMVNFHHDMLnEALTRRVldeedeqekgdsdddgdipllqGLrffkLHGSMTQTERQGVFRGFRDCASCVLLATDVVG 714
Cdd:PRK04837 264 TKHRCEEIWGHL-AADGHRV----------------------GL----LTGDVAQKKRLRILEEFTRGDLDILVATDVAA 316
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 18859659 715 RGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLF 756
Cdd:PRK04837 317 RGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
331-547 |
3.40e-43 |
|
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: 155.93 E-value: 3.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIqrkdGVLALVIVPT 410
Cdd:cd17959 6 MGLSPPLLRAIKKK-GYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTV----GARALILSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 411 RELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVdHLLHTASFKLTKLQFLILDEADRLL 490
Cdd:cd17959 81 RELALQTLKVTKELGK-FTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLL-HLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18859659 491 ELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17959 159 EMGFAEQLHEILSRLPENR-----------QTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
347-553 |
3.43e-43 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 155.73 E-value: 3.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 347 IRELTSVQQKTIPEVLQG-KDVLVRSQTGSGKTLAYALPLVELLQKQqpriqrkDGVLALVIVPTRELVMQTYELIQKLV 425
Cdd:smart00487 6 FEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRG-------KGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 426 kPYTWIVPGSLLGGESRKSEKARLRKG-INILIGTPGRLVDHLLHTaSFKLTKLQFLILDEADRLLELGYERDVKQLVEA 504
Cdd:smart00487 79 -PSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLEND-KLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18859659 505 IDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYIDNSDEA 553
Cdd:smart00487 157 LPKNV-----------QLLLLSATPPEEIENLLELFLNDPVFIDVGFTP 194
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
349-547 |
4.28e-43 |
|
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: 156.33 E-value: 4.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRK--DGVLALVIVPTRELVMQTYELIQKLVK 426
Cdd:cd17945 12 EPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDEETkdDGPYALILAPTRELAQQIEEETQKFAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 427 PYTWIVPgSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTAsFKLTKLQFLILDEADRLLELGYERDVKQLVEAID 506
Cdd:cd17945 92 PLGIRVV-SIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRL-LVLNQCTYVVLDEADRMIDMGFEPQVTKILDAMP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18859659 507 KQRAECEDKELPQL---------QRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17945 170 VSNKKPDTEEAEKLaasgkhryrQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
331-770 |
3.45e-42 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 164.25 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQK--QQPRIqrkdgvlaLVIV 408
Cdd:PRK11634 11 LGLKAPILEALNDL-GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPelKAPQI--------LVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 409 PTRELVMQTYELIQKLVKPYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFKLTKLQFLILDEADR 488
Cdd:PRK11634 82 PTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDH-LKRGTLDLSKLSGLVLDEADE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 489 LLELGYERDVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPlyidnsdeaasaalkskdgyQKET 568
Cdd:PRK11634 161 MLRMGFIEDVETIMAQIPEGH-----------QTALFSATMPEAIRRITRRFMKEP--------------------QEVR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 569 IeallevddglgeyQEDVTGVLSIPEnlqlSYVVVPPKLRLVALSSLL-AKEVDAspkqfkAIVFMSTTEMVNfhhdMLN 647
Cdd:PRK11634 210 I-------------QSSVTTRPDISQ----SYWTVWGMRKNEALVRFLeAEDFDA------AIIFVRTKNATL----EVA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 648 EALTRrvldeedeqekgdsdddgdipllQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQ 727
Cdd:PRK11634 263 EALER-----------------------NGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVN 319
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 18859659 728 YTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLEK 770
Cdd:PRK11634 320 YDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIER 362
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
254-771 |
2.73e-41 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 158.54 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 254 SDEEPDESSAQSPGQEKEPKQTAKKPPKAEETSSTNRFRTKKiglfdqSDVEALKQLGQRAVKP---------VKETIFT 324
Cdd:PRK01297 12 GEAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAAPRA------EKPKKDKPRRERKPKPaslwkledfVVEPQEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 325 GSKISTLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDG-VL 403
Cdd:PRK01297 86 KTRFHDFNLAPELMHAIHDL-GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKERYMGePR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 404 ALVIVPTRELVMQTYELIQKLVKpYTWIVPGSLLGGESRKSEKARLR-KGINILIGTPGRLVDhLLHTASFKLTKLQFLI 482
Cdd:PRK01297 165 ALIIAPTRELVVQIAKDAAALTK-YTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLD-FNQRGEVHLDMVEVMV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 483 LDEADRLLELGYERDVKQLVeaidKQRAECEDKelpqlQRMLLSATLTSQVQQLAGLTLKNPLYIDNSDEAASAalkskd 562
Cdd:PRK01297 243 LDEADRMLDMGFIPQVRQII----RQTPRKEER-----QTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVAS------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 563 gyqkETIEallevddglgeyqedvtgvlsipenlQLSYVVV-PPKLRLvaLSSLLAKEvdaspKQFKAIVFMSTTEMVNf 641
Cdd:PRK01297 308 ----DTVE--------------------------QHVYAVAgSDKYKL--LYNLVTQN-----PWERVMVFANRKDEVR- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 642 hhdMLNEALTRrvldeedeqekgdsdddgdipllQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPD 721
Cdd:PRK01297 350 ---RIEERLVK-----------------------DGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 18859659 722 IKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLEKK 771
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEEL 453
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
338-547 |
2.98e-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: 150.05 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQqpriQRKDGVLALVIVPTRELVMQT 417
Cdd:cd17957 2 LNNLEES-GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP----RKKKGLRALILAPTRELASQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 418 YELIQKLVKPYT-WIVpgsLL--GGESRKSEKARLRKGINILIGTPGRLVdHLLHTASFKLTKLQFLILDEADRLLELGY 494
Cdd:cd17957 77 YRELLKLSKGTGlRIV---LLskSLEAKAKDGPKSITKYDILVSTPLRLV-FLLKQGPIDLSSVEYLVLDEADKLFEPGF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18859659 495 ERDVKQLVEAidkqraeCEDkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17957 153 REQTDEILAA-------CTN---PNLQRSLFSATIPSEVEELARSVMKDPIRI 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
329-757 |
7.00e-39 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 152.63 E-value: 7.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 329 STLGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVE---LLQKQQPRIQRKDgvLAL 405
Cdd:PLN00206 124 SSCGLPPKLLLNLETA-GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQRNP--LAM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 406 VIVPTRELVMQTYELIQKLVK--PY-TWIVpgslLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLI 482
Cdd:PLN00206 201 VLTPTRELCVQVEDQAKVLGKglPFkTALV----VGGDAMPQQLYRIQQGVELIVGTPGRLID-LLSKHDIELDNVSVLV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 483 LDEADRLLELGYERDVKQLVEAidkqraecedkeLPQLQRMLLSATLTSQVQQLAGLTLKNPLYID-NSDEAASAALKsk 561
Cdd:PLN00206 276 LDEVDCMLERGFRDQVMQIFQA------------LSQPQVLLFSATVSPEVEKFASSLAKDIILISiGNPNRPNKAVK-- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 562 dgyqketieallevddglgeyqedvtgvlsipenlQLSyVVVPPKLRLVALSSLLAKEVDASPkqfKAIVFMSTtemvNF 641
Cdd:PLN00206 342 -----------------------------------QLA-IWVETKQKKQKLFDILKSKQHFKP---PAVVFVSS----RL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 642 HHDMLNEALTrrvldeedeqekgdsdddgdipLLQGLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPD 721
Cdd:PLN00206 379 GADLLANAIT----------------------VVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
410 420 430
....*....|....*....|....*....|....*.
gi 18859659 722 IKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFL 757
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFV 472
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
331-548 |
1.18e-38 |
|
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: 142.85 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDL---LSirelTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELlqkqqpriqrkdgVLALVI 407
Cdd:cd17938 4 LGVMPELIKAVEELdwlLP----TDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-------------VVALIL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 408 VPTRELVMQTYELIQKLVKPYT--WIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDE 485
Cdd:cd17938 67 EPSRELAEQTYNCIENFKKYLDnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLED-LIKTGKLDLSSVRFFVLDE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859659 486 ADRLLELGYERDVKQLVEAIDKQRAECEdkelpQLQRMLLSATLTS-QVQQLAGLTLKNPLYID 548
Cdd:cd17938 146 ADRLLSQGNLETINRIYNRIPKITSDGK-----RLQVIVCSATLHSfEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
351-547 |
1.39e-38 |
|
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: 142.51 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALP-LVELlqKQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLVKPyT 429
Cdd:cd17966 14 TAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaIVHI--NAQPPLERGDGPIVLVLAPTRELAQQIQQEANKFGGS-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 430 WIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQR 509
Cdd:cd17966 91 RLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLID-FLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 18859659 510 aecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17966 170 -----------QTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
279-542 |
1.85e-37 |
|
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: 141.64 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 279 PPKAEETSSTnrFRTKKIGL-FDQSDVEALKQLGQRAVKPVKEtiFTgskisTLGLHPHAVKNLeDLLSIRELTSVQQKT 357
Cdd:cd18052 4 PPPPEDEDEI--FATIQTGInFDKYDEIPVEVTGRNPPPAILT--FE-----EANLCETLLKNI-RKAGYEKPTPVQKYA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 358 IPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGV---LALVIVPTRELVMQTYELIQKLVKPyTWIVPG 434
Cdd:cd18052 74 IPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVqepQALIVAPTRELANQIFLEARKFSYG-TCIRPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 435 SLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQRAEced 514
Cdd:cd18052 153 VVYGGVSVGHQIRQIEKGCHILVATPGRLLD-FIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKE--- 228
|
250 260
....*....|....*....|....*...
gi 18859659 515 kelpQLQRMLLSATLTSQVQQLAGLTLK 542
Cdd:cd18052 229 ----DRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
351-547 |
3.46e-37 |
|
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: 138.32 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALP-LVELLqkQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLVKPYT 429
Cdd:cd17952 14 TPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPmLVHIM--DQRELEKGEGPIAVIVAPTRELAQQIYLEAKKFGKAYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 430 wIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLHTASfKLTKLQFLILDEADRLLELGYERDVKQLVEAIDkqr 509
Cdd:cd17952 92 -LRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKAT-NLQRVTYLVLDEADRMFDMGFEYQVRSIVGHVR--- 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 18859659 510 aecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17952 167 --------PDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
342-547 |
1.19e-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: 137.04 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 342 EDLLSIREL-----TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIVPTRELVMQ 416
Cdd:cd17940 9 ELLMGIFEKgfekpSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQ------ALILVPTRELALQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 417 TYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYER 496
Cdd:cd17940 83 TSQVCKELGK-HMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQDFQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18859659 497 DVKQLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17940 161 IIEKILNFLPKER-----------QILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
316-547 |
1.21e-36 |
|
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: 137.89 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 316 KPVKetiftgsKISTLGLhPHAVKNLEDLLSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPr 395
Cdd:cd17953 9 KPIQ-------KWSQCGL-SEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 396 IQRKDGVLALVIVPTRELVMQTYELIQKLVKPYTWIVPgSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKL 475
Cdd:cd17953 80 VKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVV-CVYGGSGISEQIAELKRGAEIVVCTPGRMID-ILTANNGRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 476 TKLQ---FLILDEADRLLELGYERDVKQLVEAIDkqraecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17953 158 TNLRrvtYVVLDEADRMFDMGFEPQIMKIVNNIR-----------PDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
351-530 |
1.74e-36 |
|
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: 137.76 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPE-VLQGKDVLVRSQTGSGKTLAYALPLVELL---QKQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLVK 426
Cdd:cd17946 14 TPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLlsqKSSNGVGGKQKPLRALILTPTRELAVQVKDHLKAIAK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 427 pYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHL----LHTASFKltKLQFLILDEADRLLELGYERDVKQLV 502
Cdd:cd17946 94 -YTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIqegnEHLANLK--SLRFLVLDEADRMLEKGHFAELEKIL 170
|
170 180
....*....|....*....|....*...
gi 18859659 503 EAIDKQRAEcedkELPQLQRMLLSATLT 530
Cdd:cd17946 171 ELLNKDRAG----KKRKRQTFVFSATLT 194
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
347-548 |
2.29e-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: 133.62 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 347 IRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPR--IQRKDGVLALVIVPTRELVMQTYELIQKL 424
Cdd:cd17951 10 IKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKlpFIKGEGPYGLIVCPSRELARQTHEVIEYY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 425 VKP-----YTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVK 499
Cdd:cd17951 90 CKAlqeggYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMD-MLNKKKINLDICRYLCLDEADRMIDMGFEEDIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18859659 500 QLVEAIDKQRaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd17951 169 TIFSYFKGQR-----------QTLLFSATMPKKIQNFAKSALVKPVTVN 206
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
351-770 |
1.23e-34 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 137.27 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYAlplVELLQKQQPRIQrkdGVLALVIVPTRELVMQtyelIQKLVKP--- 427
Cdd:PTZ00424 52 SAIQQRGIKPILDGYDTIGQAQSGTGKTATFV---IAALQLIDYDLN---ACQALILAPTRELAQQ----IQKVVLAlgd 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 428 YTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVeaidk 507
Cdd:PTZ00424 122 YLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYD-MIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVF----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 508 qraecedKELPQ-LQRMLLSATLTSQVQQLAGLTLKNPLYI-DNSDEAASAALKS------KDGYQKETIEALLEVddgl 579
Cdd:PTZ00424 196 -------KKLPPdVQVALFSATMPNEILELTTKFMRDPKRIlVKKDELTLEGIRQfyvaveKEEWKFDTLCDLYET---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 580 geyqedvtgvLSIPEnlqlsyvvvppklrlvalssllakevdaspkqfkAIVFMSTTEMVnfhhDMLNEALTRRVLDEEd 659
Cdd:PTZ00424 265 ----------LTITQ----------------------------------AIIYCNTRRKV----DYLTKKMHERDFTVS- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 660 eqekgdsdddgdipllqglrffKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVH 739
Cdd:PTZ00424 296 ----------------------CMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIH 353
|
410 420 430
....*....|....*....|....*....|.
gi 18859659 740 RVGRTARAGRKGRAVLFLTPSEAQFVRHLEK 770
Cdd:PTZ00424 354 RIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
316-803 |
1.49e-33 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 137.39 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 316 KPVKETIFtgskiSTLGLHPHAVKNLEDLLSIReLTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPR 395
Cdd:PRK04537 4 KPLTDLTF-----SSFDLHPALLAGLESAGFTR-CTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 396 IQRK-DGVLALVIVPTRELVMQTYELIQKLvkpytwivpGSLLG--------GESRKSEKARLRKGINILIGTPGRLVDH 466
Cdd:PRK04537 78 ADRKpEDPRALILAPTRELAIQIHKDAVKF---------GADLGlrfalvygGVDYDKQRELLQQGVDVIIATPGRLIDY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 467 LLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQRAEcedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLY 546
Cdd:PRK04537 149 VKQHKVVSLHACEICVLDEADRMFDLGFIKDIRFLLRRMPERGTR---------QTLLFSATLSHRVLELAYEHMNEPEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 547 IDNSDEAASAALKSKDGY---QKETIEALLevddglgeyqedvtGVLSIPENLqlsyvvvppklrlvalssllakevdas 623
Cdd:PRK04537 220 LVVETETITAARVRQRIYfpaDEEKQTLLL--------------GLLSRSEGA--------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 624 pkqfKAIVFMSTTEMVNfhhdmlneaLTRRVLDEedeqekgdsdddgdipllQGLRFFKLHGSMTQTERQGVFRGFRDCA 703
Cdd:PRK04537 259 ----RTMVFVNTKAFVE---------RVARTLER------------------HGYRVGVLSGDVPQKKRESLLNRFQKGQ 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 704 SCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQFVRHLEKK-RIRIQQGDMYA 782
Cdd:PRK04537 308 LEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYiEQKIPVEPVTA 387
|
490 500
....*....|....*....|.
gi 18859659 783 YLQTLLPKDDEARTVQEAASN 803
Cdd:PRK04537 388 ELLTPLPRPPRVPVEGEEADD 408
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
351-547 |
7.45e-32 |
|
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: 123.34 E-value: 7.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALP-LVELLQKQQPRIQRkDGVLALVIVPTRELVMQTYELIQKLVkpYT 429
Cdd:cd17958 14 SPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREQR-NGPGVLVLTPTRELALQIEAECSKYS--YK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 430 WIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDkqr 509
Cdd:cd17958 91 GLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIR--- 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 18859659 510 aecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17958 167 --------PDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
339-548 |
1.05e-31 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 123.97 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 339 KNLEDLLSIR---ELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQkQQPRIQRKDGVLALVIVPTRELVM 415
Cdd:cd18049 33 ANVMDVIARQnftEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPFLERGDGPICLVLAPTRELAQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 416 QtyelIQKLVKPY---TWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLEL 492
Cdd:cd18049 112 Q----VQQVAAEYgraCRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID-FLEAGKTNLRRCTYLVLDEADRMLDM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18859659 493 GYERDVKQLVEAIDkqraecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd18049 187 GFEPQIRKIVDQIR-----------PDRQTLMWSATWPKEVRQLAEDFLKDYIHIN 231
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
348-537 |
2.04e-29 |
|
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: 118.57 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 348 RELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQkQQPRIQRKDGVLALVIVPTRELVMQtyelIQKLVKP 427
Cdd:cd18050 83 KEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN-HQPYLERGDGPICLVLAPTRELAQQ----VQQVADD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 428 Y---TWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEA 504
Cdd:cd18050 158 YgksSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLID-FLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQ 236
|
170 180 190
....*....|....*....|....*....|...
gi 18859659 505 IDkqraecedkelPQLQRMLLSATLTSQVQQLA 537
Cdd:cd18050 237 IR-----------PDRQTLMWSATWPKEVRQLA 258
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
351-547 |
3.01e-29 |
|
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: 117.45 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQP----------RIQRKDGVLALVIVPTRELVMQTYEL 420
Cdd:cd18051 45 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQGPgeslpsesgyYGRRKQYPLALVLAPTRELASQIYDE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 421 IQKLVkpYTWIV-PGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVK 499
Cdd:cd18051 125 ARKFA--YRSRVrPCVVYGGADIGQQMRDLERGCHLLVATPGRLVD-MLERGKIGLDYCKYLVLDEADRMLDMGFEPQIR 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18859659 500 QLVEaidkqraecEDKELP--QLQRMLLSATLTSQVQQLAGLTLKNplYI 547
Cdd:cd18051 202 RIVE---------QDTMPPtgERQTLMFSATFPKEIQMLARDFLDN--YI 240
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
350-537 |
4.03e-29 |
|
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: 115.33 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 350 LTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGVLALVIVPTRELVMQTYELIQKLVKPYT 429
Cdd:cd17944 13 LFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRAPKVLVLAPTRELANQVTKDFKDITRKLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 430 wivPGSLLGGESRKSEKARLRKGINILIGTPGRLVDHlLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAidKQR 509
Cdd:cd17944 93 ---VACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDH-LQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV--SYK 166
|
170 180
....*....|....*....|....*...
gi 18859659 510 AECEDKElpqlQRMLLSATLTSQVQQLA 537
Cdd:cd17944 167 KDSEDNP----QTLLFSATCPDWVYNVA 190
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
351-548 |
7.46e-28 |
|
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: 111.65 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIVPTRELVMQTYELIQKLVKpYTW 430
Cdd:cd17939 21 SAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQ------ALVLAPTRELAQQIQKVVKALGD-YMG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDkqra 510
Cdd:cd17939 94 VKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFD-MLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLP---- 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 18859659 511 ecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYID 548
Cdd:cd17939 169 -------PETQVVLFSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
351-547 |
9.41e-28 |
|
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: 111.10 E-value: 9.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVE--LLQKQQPriqrkdgvLALVIVPTRELVMQTYELIQKLVKPY 428
Cdd:cd17962 14 TPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIrcLTEHRNP--------SALILTPTRELAVQIEDQAKELMKGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 429 TWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQ 508
Cdd:cd17962 86 PPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLD-ILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 18859659 509 RaecedkelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17962 165 H-----------QTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
338-536 |
1.66e-27 |
|
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: 111.69 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVE-LLQKQQPRIQRKDGVLALVIVPTRELVMQ 416
Cdd:cd17948 2 VEILQRQ-GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrLLRYKLLAEGPFNAPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 417 TYELIQKLVKpYTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYER 496
Cdd:cd17948 81 IGSVAQSLTE-GLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18859659 497 DVKQLVE--AIDKQRAECEDKELPQLQRMLLSATLTSQVQQL 536
Cdd:cd17948 159 KLSHFLRrfPLASRRSENTDGLDPGTQLVLVSATMPSGVGEV 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
351-509 |
5.63e-27 |
|
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: 108.89 E-value: 5.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIVPTRELVMQTYELIQKLVKPYTW 430
Cdd:cd17943 14 SPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQ------VLILAPTREIAVQIHDVFKKIGKKLEG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859659 431 IVPGSLLGGESRKSEKARLrKGINILIGTPGRLVdHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVEAIDKQR 509
Cdd:cd17943 88 LKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNK 164
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
614-748 |
1.81e-24 |
|
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: 98.82 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 614 SLLAKEVDASPKQfKAIVFMSTTEMVNFHHdmlnealtrrvldeedeqekgdsdddgdIPLLQGLRFFKLHGSMTQTERQ 693
Cdd:pfam00271 4 EALLELLKKERGG-KVLIFSQTKKTLEAEL----------------------------LLEKEGIKVARLHGDLSQEERE 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 694 GVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAG 748
Cdd:pfam00271 55 EILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
364-528 |
2.81e-23 |
|
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: 96.70 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 364 GKDVLVRSQTGSGKTLAYALPLVELLQKQQPRiqrkdgvlALVIVPTRELVMQTYELIQKLvkpYTWIVPGSLLGGESRK 443
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKKGKK--------VLVLVPTKALALQTAERLREL---FGPGIRVAVLVGGSSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 444 SEKARLRKG-INILIGTPGRLVDHLLHTASFKLTKLQFLILDEADRLleLGYERDVKQLVEAIDKqraecedKELPQLQR 522
Cdd:cd00046 70 EEREKNKLGdADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHAL--LIDSRGALILDLAVRK-------AGLKNAQV 140
|
....*.
gi 18859659 523 MLLSAT 528
Cdd:cd00046 141 ILLSAT 146
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
351-547 |
3.21e-23 |
|
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: 98.57 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIVPTRELVMQTYELIQKLVKPYTW 430
Cdd:cd17950 26 SEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS------VLVICHTRELAFQISNEYERFSKYMPN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPGSLLGGESRKSEKARLR-KGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLE-LGYERDVKQLVeaidkq 508
Cdd:cd17950 100 VKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILA-LVREKKLKLSHVKHFVLDECDKMLEqLDMRRDVQEIF------ 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 18859659 509 RAECEDKelpqlQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17950 173 RATPHDK-----QVMMFSATLSKEIRPVCKKFMQDPLEI 206
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
353-547 |
3.92e-23 |
|
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: 98.03 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 353 VQQKTIPEVLQG--KDVLVRSQTGSGKTLAYALplvELLQKQQPRIQRKDgvlALVIVPTRELVMQTYELIQKLVKpYTW 430
Cdd:cd17963 20 IQETALPLILSDppENLIAQSQSGTGKTAAFVL---AMLSRVDPTLKSPQ---ALCLAPTRELARQIGEVVEKMGK-FTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPGSLLggesrKSEKARLRKGIN--ILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLEL-GYERDVKQLVEAIDk 507
Cdd:cd17963 93 VKVALAV-----PGNDVPRGKKITaqIVIGTPGTVLD-WLKKRQLDLKKIKILVLDEADVMLDTqGHGDQSIRIKRMLP- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18859659 508 qraecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd17963 166 ----------RNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
677-748 |
8.89e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.05 E-value: 8.89e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859659 677 GLRFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAG 748
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
351-547 |
2.26e-22 |
|
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: 96.00 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIVPTRELVMQTYELIQKLVKpYTW 430
Cdd:cd18045 23 SAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQ------ALILSPTRELAVQIQKVLLALGD-YMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 IVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYerdvKQLVEAIDKQRA 510
Cdd:cd18045 96 VQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFD-MIRRRSLRTRHIKMLVLDEADEMLNKGF----KEQIYDVYRYLP 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 18859659 511 ecedkelPQLQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd18045 171 -------PATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
351-547 |
5.49e-22 |
|
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: 94.82 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYAlplVELLQKQQPRIQrkdGVLALVIVPTRELVMQtyelIQKLVKP--- 427
Cdd:cd18046 23 SAIQQRAIMPCIKGYDVIAQAQSGTGKTATFS---ISILQQIDTSLK---ATQALVLAPTRELAQQ----IQKVVMAlgd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 428 YTWIVPGSLLGGESRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEADRLLELGYERDVKQLVeaidk 507
Cdd:cd18046 93 YMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFD-MINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDIF----- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18859659 508 qraecedKELPQ-LQRMLLSATLTSQVQQLAGLTLKNPLYI 547
Cdd:cd18046 167 -------QKLPPdTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DUF4217 |
pfam13959 |
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many ... |
805-865 |
2.80e-18 |
|
Domain of unknown function (DUF4217); This short domain is found at the C-terminus of many helicase proteins.
Pssm-ID: 464056 [Multi-domain] Cd Length: 59 Bit Score: 79.36 E-value: 2.80e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859659 805 QHKFQTLLEDDRELHDKSCKAFVSWMKFYSTFPkeLKPIFNVRIAHMGHFAKSFALKEAPS 865
Cdd:pfam13959 1 QLQLEKLVLKDRELKELAQKAFVSYVRAYSKHL--AKSIFNVKKLDLGHLAKSFGLLRAPK 59
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
290-756 |
1.32e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.22 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 290 RFRTKKIGLFDQSDVEALKQLGQRAVKPVKETIFTgskisTLGLHPH---AVKNLEDLLSIReltsvqqktipevlqGKD 366
Cdd:COG1061 43 KEGTREDGRRLPEEDTERELAEAEALEAGDEASGT-----SFELRPYqqeALEALLAALERG---------------GGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 367 VLVRSQTGSGKTLAYALPLVELLQKQQpriqrkdgvlALVIVPTRELVMQTYELIQKlvkpytwIVPGSLLGGESRKSEK 446
Cdd:COG1061 103 GLVVAPTGTGKTVLALALAAELLRGKR----------VLVLVPRRELLEQWAEELRR-------FLGDPLAGGGKKDSDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 447 arlrkgiNILIGTpgrlVDHLLHTASFKLTKLQF--LILDEADRLLELGYERdvkqLVEAIDKQRaecedkelpqlqRML 524
Cdd:COG1061 166 -------PITVAT----YQSLARRAHLDELGDRFglVIIDEAHHAGAPSYRR----ILEAFPAAY------------RLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 525 LSAT------LTSQVQQLAGLTLKNPLyidnsDEAAsaalksKDGYQKETIeaLLEVDDGLGEYQEDVTgvlSIPENLQL 598
Cdd:COG1061 219 LTATpfrsdgREILLFLFDGIVYEYSL-----KEAI------EDGYLAPPE--YYGIRVDLTDERAEYD---ALSERLRE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 599 SYVVVPPKLRLValsslLAKEVDASPKQFKAIVFMSTTEMVNFHHDMLNEAltrrvldeedeqekgdsdddgdipllqGL 678
Cdd:COG1061 283 ALAADAERKDKI-----LRELLREHPDDRKTLVFCSSVDHAEALAELLNEA---------------------------GI 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859659 679 RFFKLHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTAR-AGRKGRAVLF 756
Cdd:COG1061 331 RAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRpAPGKEDALVY 409
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
318-491 |
1.62e-14 |
|
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: 74.34 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 318 VKETIFTGSKISTLGLHPHAVKNLedllSIRELT-----SVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQ 392
Cdd:cd17965 14 IIKEILKGSNKTDEEIKPSPIQTL----AIKKLLktlmrKVTKQTSNEEPKLEVFLLAAETGSGKTLAYLAPLLDYLKRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 393 QPRIQRKDG-----------VLALVIVPTRELVMQTYELIQKLVKPYTW-IVPGSLLGGESRKSEKARLRKGINILIGTP 460
Cdd:cd17965 90 EQEPFEEAEeeyesakdtgrPRSVILVPTHELVEQVYSVLKKLSHTVKLgIKTFSSGFGPSYQRLQLAFKGRIDILVTTP 169
|
170 180 190
....*....|....*....|....*....|.
gi 18859659 461 GRLVDhLLHTASFKLTKLQFLILDEADRLLE 491
Cdd:cd17965 170 GKLAS-LAKSRPKILSRVTHLVVDEADTLFD 199
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
332-769 |
9.92e-12 |
|
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: 69.09 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 332 GLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVEllqkqqpRIQRKDGVLALVIVPT- 410
Cdd:COG1205 40 WLPPELRAALKKR-GIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLE-------ALLEDPGATALYLYPTk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 411 -------RELVmqtyELIQKL---VKPYTWIvpgsllgGESRKSEKARLRKGINILIGTPgrlvdHLLHT---------A 471
Cdd:COG1205 112 alardqlRRLR----ELAEALglgVRVATYD-------GDTPPEERRWIREHPDIVLTNP-----DMLHYgllphhtrwA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 472 SFkLTKLQFLILDEA---------------DRLlelgyerdvKQLVEAIDKQraecedkelPQLqrMLLSATltsqvqql 536
Cdd:COG1205 176 RF-FRNLRYVVIDEAhtyrgvfgshvanvlRRL---------RRICRHYGSD---------PQF--ILASAT-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 537 agltlknplyIDNSDEAAsaalkskdgyqketiEALLEVD----DGLGEYQEDVTGVLSIPEnlqlsyvVVPPKLRLVAL 612
Cdd:COG1205 227 ----------IGNPAEHA---------------ERLTGRPvtvvDEDGSPRGERTFVLWNPP-------LVDDGIRRSAL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 613 S---SLLAKEVDAspkQFKAIVFMSTTEMVnfhhdmlnEALTRRVLDEEDEQEKGDSdddgdiplLQGLRffklhGSMTQ 689
Cdd:COG1205 275 AeaaRLLADLVRE---GLRTLVFTRSRRGA--------ELLARYARRALREPDLADR--------VAAYR-----AGYLP 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 690 TERQGVFRGFRDcascvllatdvvGR------------GIDVPDIKLVVQYTPPQTTADFVHRVGrtaRAGRKGR-AVLF 756
Cdd:COG1205 331 EERREIERGLRS------------GEllgvvstnalelGIDIGGLDAVVLAGYPGTRASFWQQAG---RAGRRGQdSLVV 395
|
490
....*....|....*..
gi 18859659 757 LTPSEAQ----FVRHLE 769
Cdd:COG1205 396 LVAGDDPldqyYVRHPE 412
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
331-544 |
2.24e-10 |
|
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: 61.27 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 331 LGLHPHAVKNLEDLlSIRELTSVQQKTIPEVLQG--KDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgvlALVIV 408
Cdd:cd18047 6 LRLKPQLLQGVYAM-GFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQ------CLCLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 409 PTRELVMQTYELIQKLVKPYTWIVPGSLLGGEsRKSEKARLRKgiNILIGTPGRLVDHLLHTASFKLTKLQFLILDEADR 488
Cdd:cd18047 79 PTYELALQTGKVIEQMGKFYPELKLAYAVRGN-KLERGQKISE--QIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18859659 489 LLELGYERDvkqlvEAIDKQRAecedkeLPQ-LQRMLLSATLTSQVQQLAGLTLKNP 544
Cdd:cd18047 156 MIATQGHQD-----QSIRIQRM------LPRnCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
706-756 |
4.98e-10 |
|
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: 56.56 E-value: 4.98e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18859659 706 VLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAG-RKGRAVLF 756
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
337-544 |
1.87e-09 |
|
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: 58.88 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 337 AVKNLEDLLSIREL------------TSVQQKTIPEVLQG--KDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQrkdgv 402
Cdd:cd18048 16 SVKSFEELHLKEELlrgiyamgfnrpSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQ----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 403 lALVIVPTRELVMQTYELIQKLVKPYTWIVPGSLLGGeSRKSEKARLRKgiNILIGTPGRLVDHLLHTASFKLTKLQFLI 482
Cdd:cd18048 91 -CLCLSPTFELALQTGKVVEEMGKFCVGIQVIYAIRG-NRPGKGTDIEA--QIVIGTPGTVLDWCFKLRLIDVTNISVFV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859659 483 LDEADRLLELGYERDvkqlvEAIDKQRAecedkeLPQLQRMLL-SATLTSQVQQLAGLTLKNP 544
Cdd:cd18048 167 LDEADVMINVQGHSD-----HSVRVKRS------MPKECQMLLfSATFEDSVWAFAERIVPDP 218
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
364-529 |
4.51e-09 |
|
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: 56.44 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 364 GKDVLVRSQTGSGKTLAYALPLVELLQKQQPriqrkDGVLALVIVPTRELVMQTYELIQklvKPYTWIVPGSLLG---GE 440
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE-----KGVQVLYISPLKALINDQERRLE---EPLDEIDLEIPVAvrhGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 441 SRKSEKARLRKGI-NILIGTPGRLvdHLLHT---ASFKLTKLQFLILDEADRLleLGYERDV--KQLVEAIDKQRAeced 514
Cdd:cd17922 73 TSQSEKAKQLKNPpGILITTPESL--ELLLVnkkLRELFAGLRYVVVDEIHAL--LGSKRGVqlELLLERLRKLTG---- 144
|
170
....*....|....*
gi 18859659 515 kelPQLQRMLLSATL 529
Cdd:cd17922 145 ---RPLRRIGLSATL 156
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
327-549 |
5.50e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.91 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 327 KISTLGLHphAVKNLEDLLSIRELTSVQQKTIP-EVLQGKDVLVRSQTGSGKTLAYALPLVELLQKqqpriqrkdGVLAL 405
Cdd:COG1204 2 KVAELPLE--KVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKALLN---------GGKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 406 VIVPTRELVMQTY-ELIQKL----VKPYtwIVPGsllggeSRKSEKARLRKGiNILIGTPGRLvDHLL-HTASFkLTKLQ 479
Cdd:COG1204 71 YIVPLRALASEKYrEFKRDFeelgIKVG--VSTG------DYDSDDEWLGRY-DILVATPEKL-DSLLrNGPSW-LRDVD 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859659 480 FLILDEA------DR--LLELgyerdvkqlveAIDKQRAECedkelPQLQRMLLSATLtSQVQQLAGLtLKNPLYIDN 549
Cdd:COG1204 140 LVVVDEAhliddeSRgpTLEV-----------LLARLRRLN-----PEAQIVALSATI-GNAEEIAEW-LDAELVKSD 199
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
352-550 |
7.01e-09 |
|
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: 56.77 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 352 SVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELlqkqqpriqrkDGVlALVIVPTRELVM-QTYELIQKLVKPYTW 430
Cdd:cd17920 15 PGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLL-----------DGV-TLVVSPLISLMQdQVDRLQQLGIRAAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 431 ivpGSLLGGESRKSEKARLRKG-INILIGTPGRLV-----DHLLHTASFKLtkLQFLILDEADRLLELGYE-R-DVKQLV 502
Cdd:cd17920 83 ---NSTLSPEEKREVLLRIKNGqYKLLYVTPERLLspdflELLQRLPERKR--LALIVVDEAHCVSQWGHDfRpDYLRLG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18859659 503 EAIDkqraecedkELPQLQRMLLSATLTSQVQQ--LAGLTLKNPLYIDNS 550
Cdd:cd17920 158 RLRR---------ALPGVPILALTATATPEVREdiLKRLGLRNPVIFRAS 198
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
354-486 |
1.48e-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: 55.28 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 354 QQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVEllqkqqpRIQRKDGVLALVIVPTRELVM-QTYELIQKLVKPYTWIV 432
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILE-------ALLRDPGSRALYLYPTKALAQdQLRSLRELLEQLGLGIR 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18859659 433 PGSLLGGESRKSEKARLRKGINILIGTPGRLvDHLL---HTASFK-LTKLQFLILDEA 486
Cdd:cd17923 78 VATYDGDTPREERRAIIRNPPRILLTNPDML-HYALlphHDRWARfLRNLRYVVLDEA 134
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
348-756 |
1.74e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 58.58 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 348 RELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALP-LVELLQKQQPRiQRKDGVLALVIVPTRELvmqTYELIQKLVK 426
Cdd:COG1201 23 GAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPaLDELARRPRPG-ELPDGLRVLYISPLKAL---ANDIERNLRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 427 PYTWIvpGSLLGG-------ESR-----KSEKARLRKGI-NILIGTPGRLvdHLLHT---ASFKLTKLQFLILDE----A 486
Cdd:COG1201 99 PLEEI--GEAAGLplpeirvGVRtgdtpASERQRQRRRPpHILITTPESL--ALLLTspdARELLRGVRTVIVDEihalA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 487 D--R--LLELGYERdVKQLVEAidkqraecedkelpQLQRMLLSATLT--SQVQQ-LAGLTLKNPLYIDNSDEAASAALK 559
Cdd:COG1201 175 GskRgvHLALSLER-LRALAPR--------------PLQRIGLSATVGplEEVARfLVGYEDPRPVTIVDAGAGKKPDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 560 SKDgyQKETIEALLEVDDGLGEYQEDvtgvlsipenlqlsyvvvppklRLVALssllakeVDASpkqfKA-IVFMST--- 635
Cdd:COG1201 240 VLV--PVEDLIERFPWAGHLWPHLYP----------------------RVLDL-------IEAH----RTtLVFTNTrsq 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 636 TEMVnFHHdmLNEALtrrvldeedeqekgdsdddGDIPLLQGLRffklHGSMTQTERQGVFRGFRDCASCVLLAT---DV 712
Cdd:COG1201 285 AERL-FQR--LNELN-------------------PEDALPIAAH----HGSLSREQRLEVEEALKAGELRAVVATsslEL 338
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 18859659 713 vgrGIDVPDIKLVVQYTPPQTTADFVHRVGRtA--RAGRKGRAVLF 756
Cdd:COG1201 339 ---GIDIGDVDLVIQVGSPKSVARLLQRIGR-AghRVGEVSKGRLV 380
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
349-496 |
4.23e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 53.44 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQG-----KDVLVRSQTGSGKTLAYALpLVELLQKQQPrIQRkdgvlALVIVPTRELVMQTYELIQK 423
Cdd:pfam04851 3 ELRPYQIEAIENLLESikngqKRGLIVMATGSGKTLTAAK-LIARLFKKGP-IKK-----VLFLVPRKDLLEQALEEFKK 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 424 LVKPYTWIvpGSLLGGESRKSEkarlRKGINILIGTPGRLVDHlLHTASFKLTKLQF--LILDEADRLLELGYER 496
Cdd:pfam04851 76 FLPNYVEI--GEIISGDKKDES----VDDNKIVVTTIQSLYKA-LELASLELLPDFFdvIIIDEAHRSGASSYRN 143
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
684-757 |
1.32e-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: 51.88 E-value: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859659 684 HGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARagRKGRAVLFL 757
Cdd:cd18796 75 HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH--RPGAASKGR 146
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
349-548 |
1.57e-07 |
|
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: 52.26 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEV-LQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIqrkdgvlaLVIVPTRELVMQTYELIQKLVKP 427
Cdd:cd17921 1 LLNPIQREALRALyLSGDSVLVSAPTSSGKTLIAELAILRALATSGGKA--------VYIAPTRALVNQKEADLRERFGP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 428 YTwIVPGSLLGGESRKSEKARLRkgiNILIGTPGRLVDHLLHTASFKLTKLQFLILDEAdRLLELGyERDVKqLVEAIDK 507
Cdd:cd17921 73 LG-KNVGLLTGDPSVNKLLLAEA---DILVATPEKLDLLLRNGGERLIQDVRLVVVDEA-HLIGDG-ERGVV-LELLLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18859659 508 QRAECedkelPQLQRMLLSATLtSQVQQLAG-LTLKNPLYID 548
Cdd:cd17921 146 LLRIN-----KNARFVGLSATL-PNAEDLAEwLGVEDLIRFD 181
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
687-747 |
2.11e-07 |
|
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: 51.05 E-value: 2.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859659 687 MTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRtARA 747
Cdd:cd18802 74 MTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
687-757 |
2.20e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 51.20 E-value: 2.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859659 687 MTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARaGRKGRAVLFL 757
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
605-758 |
3.57e-07 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 54.35 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 605 PKLRLVAlsSLLAKEVDASPKQfKAIVFMS---TTEMVnfhHDMLNEAL--TRRVLdeedeqekGDSDDDGDipllQGlr 679
Cdd:COG1111 335 PKLSKLR--EILKEQLGTNPDS-RIIVFTQyrdTAEMI---VEFLSEPGikAGRFV--------GQASKEGD----KG-- 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859659 680 ffklhgsMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARaGRKGRAVLFLT 758
Cdd:COG1111 395 -------LTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIA 465
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
338-486 |
4.02e-07 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 51.49 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 338 VKNLEDLLSIRELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPlVELLQKQQPRIqrkdgvlALVIVPTRELVMQT 417
Cdd:cd18018 1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLP-ALLLRRRGPGL-------TLVVSPLIALMKDQ 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 418 YELIQKLVKPYTWIvpgSLLGGESRKSEKARLRKG-INILIGTPGRLVdhllhTASFKLTKLQ-----FLILDEA 486
Cdd:cd18018 73 VDALPRAIKAAALN---SSLTREERRRILEKLRAGeVKILYVSPERLV-----NESFRELLRQtppisLLVVDEA 139
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
365-486 |
5.99e-07 |
|
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: 51.11 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 365 KDVLVRSQTGSGKTLAYALPLVELLQkqQPRIQRKDGVLALVIVPTRELVMQTYELIQK----LVKPYTwivpGSLLGGE 440
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAVMLIKEMGE--LNRKEKNPKKRAVFLVPTVPLVAQQAEAIRShtdlKVGEYS----GEMGVDK 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 18859659 441 SRKSEKARLRKGINILIGTPGRLVDhLLHTASFKLTKLQFLILDEA 486
Cdd:cd18034 91 WTKERWKEELEKYDVLVMTAQILLD-ALRHGFLSLSDINLLIFDEC 135
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
349-485 |
6.45e-07 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 53.35 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKDGVLALVIVPTREL-------VMQTYELI 421
Cdd:PRK13767 32 TFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGELEDKVYCLYVSPLRALnndihrnLEEPLTEI 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 422 QKLVKPYTWIVPG---SLLGGESRKSEKAR-LRKGINILIGTPGRLVDhLLHTASF--KLTKLQFLILDE 485
Cdd:PRK13767 112 REIAKERGEELPEirvAIRTGDTSSYEKQKmLKKPPHILITTPESLAI-LLNSPKFreKLRTVKWVIVDE 180
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
605-758 |
1.49e-06 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 52.18 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 605 PKLRLVAlsSLLAKEVDASPKQfKAIVFMSTTEMVnfhhdmlnEALTRRVLDEEDEQEK--GDSDDDGDipllQGlrffk 682
Cdd:PRK13766 347 PKLEKLR--EIVKEQLGKNPDS-RIIVFTQYRDTA--------EKIVDLLEKEGIKAVRfvGQASKDGD----KG----- 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859659 683 lhgsMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARaGRKGRAVLFLT 758
Cdd:PRK13766 407 ----MSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVVVLIA 477
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
373-501 |
1.53e-06 |
|
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: 48.84 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 373 TGSGKTLAyALPLVELLQKQqpRIqrkdgvlaLVIVPTRELVMQTYELIQKlvkpYTWIVPGSLLGGESRKSEkarlrKG 452
Cdd:cd17926 27 TGSGKTLT-ALALIAYLKEL--RT--------LIVVPTDALLDQWKERFED----FLGDSSIGLIGGGKKKDF-----DD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18859659 453 INILIGTPgRLVDHLLHTASFKLTKLQFLILDEADRLLELGYERDVKQL 501
Cdd:cd17926 87 ANVVVATY-QSLSNLAEEEKDLFDQFGLLIVDEAHHLPAKTFSEILKEL 134
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
362-488 |
2.02e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 46.66 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 362 LQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIQRKdgvlALVIVPTRELVMQTYELIQKLVKPYTWIVpGSLLGGES 441
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGK----VVFLANKVPLVEQQKEVFRKHFERPGYKV-TGLSGDTS 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18859659 442 RKSEKARLRKGINILIGTPGRLVDHLLHTASFKLTKLQFLILDEADR 488
Cdd:cd17927 90 ENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
349-490 |
2.52e-05 |
|
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: 46.17 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQGKDVLVRSQTGSGKT---LAYALPLVELLQKqqpriqrkdgvlALVIVPTRELVMQTYELIQKLV 425
Cdd:cd17924 17 PPWGAQRTWAKRLLRGKSFAIIAPTGVGKTtfgLATSLYLASKGKR------------SYLIFPTKSLVKQAYERLSKYA 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859659 426 KPYTwiVPGSLL--GGESRKSEKARLRKGI-----NILIGTPGRLVDH--LLHTASFkltklQFLILDEADRLL 490
Cdd:cd17924 85 EKAG--VEVKILvyHSRLKKKEKEELLEKIekgdfDILVTTNQFLSKNfdLLSNKKF-----DFVFVDDVDAVL 151
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
684-756 |
2.93e-05 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 44.51 E-value: 2.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859659 684 HGSMTQTERQGVFRGF-RDCASCVLlATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLF 756
Cdd:cd18794 61 HAGLEPSDRRDVQRKWlRDKIQVIV-ATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
354-544 |
3.92e-05 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 45.97 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 354 QQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELlqkqqpriqrkDGVlALVIVPTRELVMqtyELIQKLVkpyTWIVP 433
Cdd:cd18016 22 QLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVS-----------PGV-TVVISPLRSLIV---DQVQKLT---SLDIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 434 GSLLGGESRKSEKAR----LRKG---INILIGTP------GRLVDHLLHTASFKLtkLQFLILDEADRLLELGYerDVKQ 500
Cdd:cd18016 84 ATYLTGDKTDAEATKiylqLSKKdpiIKLLYVTPekisasNRLISTLENLYERKL--LARFVIDEAHCVSQWGH--DFRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18859659 501 lveaiDKQRAECEDKELPQLQRMLLSATLTSQVQQ--LAGLTLKNP 544
Cdd:cd18016 160 -----DYKRLNMLRQKFPSVPMMALTATATPRVQKdiLNQLKMLRP 200
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
353-488 |
5.25e-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: 44.81 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 353 VQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQQPRIqrkdgvlaLVIVPTRELVMQTYELIQKLVKPYTWIV 432
Cdd:cd18035 5 LYQVLIAAVALNGNTLIVLPTGLGKTIIAILVAADRLTKKGGKV--------LILAPSRPLVEQHAENLKRVLNIPDKIT 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18859659 433 PgslLGGESRKSEKARLRKGINILIGTPgRLVDHLLHTASFKLTKLQFLILDEADR 488
Cdd:cd18035 77 S---LTGEVKPEERAERWDASKIIVATP-QVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
349-488 |
1.17e-04 |
|
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: 43.94 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQG------KDVLVRSQTGSGKTLAYALPLVELLqkqqpriqrKDGVLALVIVPTRELVMQTYELIQ 422
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY---------KNGKQVAILVPTEILAHQHYEEAR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859659 423 KLVKPytwiVPGSLLGGESRKSEKArlrkGINILIGTPGrlvdhLLHTASfKLTKLQFLILDEADR 488
Cdd:cd17918 86 KFLPF----INVELVTGGTKAQILS----GISLLVGTHA-----LLHLDV-KFKNLDLVIVDEQHR 137
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
684-786 |
1.23e-04 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 45.90 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 684 HGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQ 763
Cdd:COG0514 261 HAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVA 340
|
90 100 110
....*....|....*....|....*....|..
gi 18859659 764 FVRHL--------EKKRIRIQ-QGDMYAYLQT 786
Cdd:COG0514 341 IQRFFieqsppdeERKRVERAkLDAMLAYAET 372
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
601-742 |
2.13e-04 |
|
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: 42.08 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 601 VVVPPKLRlvALSSLLAKEVDaspKQFKAIVFMSTTEMVnfhhDMLNEALTRRvldeedeqekgdsdddgdipllqGLRF 680
Cdd:cd18793 7 EVVSGKLE--ALLELLEELRE---PGEKVLIFSQFTDTL----DILEEALRER-----------------------GIKY 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 681 FKLHGSMTQTERQGVFRGFRDCASC--VLLATDVVGRGIDVPDIKLVVQYTPPQTTA------DFVHRVG 742
Cdd:cd18793 55 LRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYDPWWNPAveeqaiDRAHRIG 124
|
|
| SEEEED |
pfam14797 |
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly ... |
211-305 |
3.01e-04 |
|
Serine-rich region of AP3B1, clathrin-adaptor complex; This short low-complexity, highly serine-rich region lies on clathrin-adaptor complex 3 beta-1 subunit proteins, between family Adaptin_N, pfam01602 and a C-terminal domain, AP3B1_C,pfam14796.
Pssm-ID: 434218 [Multi-domain] Cd Length: 111 Bit Score: 41.07 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 211 DEEDAKNNSGGGSPRVKPSSAVKESKKSSDIEDSGESgeesaTSDEEPDESsaqspGQEKEPKQTAKKPPKA-EETSSTN 289
Cdd:pfam14797 10 EEEEDSSDSSSDSESESGSESEEEGKEGSSSEDSSED-----SSSEQESES-----GSESEKKRTAKRNSKAkGKSDSED 79
|
90
....*....|....*..
gi 18859659 290 RFR-TKKIGLFDQSDVE 305
Cdd:pfam14797 80 GEKkNEKSKTSDSSDTE 96
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
677-777 |
4.30e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 43.93 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 677 GLRFFKLHGSMTQTERQGVFRGF-RDCASCVLlATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVL 755
Cdd:PRK11057 260 GISAAAYHAGLDNDVRADVQEAFqRDDLQIVV-ATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAML 338
|
90 100
....*....|....*....|...
gi 18859659 756 FLTPSEAQFVRH-LEKKRIRIQQ 777
Cdd:PRK11057 339 FYDPADMAWLRRcLEEKPAGQQQ 361
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
351-547 |
4.83e-04 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 42.46 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 351 TSVQQKTIPEVLQGK-DVLVRSQTGSGKTLAYALPlvELLQKQqpriqrkdgvLALVIVPTRELVMQTYELIQKLVkpyt 429
Cdd:cd18014 15 SPLQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLP--ALLAKG----------ITIVISPLIALIQDQVDHLKTLK---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 430 wiVPGSLLGGESRKSEKARL-------RKGINILIGTP--------GRLVDHLLHTasfklTKLQFLILDEADRLLELGY 494
Cdd:cd18014 79 --IRVDSLNSKLSAQERKRIiadleseKPQTKFLYITPemaatssfQPLLSSLVSR-----NLLSYLVVDEAHCVSQWGH 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 495 ERDVKQLVEAIDKQRAecedKELPQLqrmLLSATLTSQVQQ--LAGLTLKNPLYI 547
Cdd:cd18014 152 DFRPDYLRLGALRSRY----GHVPWV---ALTATATPQVQEdiFAQLRLKKPVAI 199
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
10-262 |
7.86e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.50 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 10 TVKSSARKNQQSPALSVKKRAQKSQDFDFQFNVDKPKVKaivVRRRAPPSKVEPTNSSVPNTTKSPTPSVSSSKSAISTL 89
Cdd:PTZ00108 1162 TKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKR---VDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKS 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 90 SASPKANASNDDLMFNVSPTKPPVKSVLGDDFMLNVTTKPVVAQKAKPKITRAERLGKKQ--RQGKPLTKLSEEQITRAL 167
Cdd:PTZ00108 1239 SVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGgsKPSSPTKKKVKKRLEGSL 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 168 KSNKKPKNPNQLPTPgdlfraqleeerrqkrreegggDQEASADEEDAKNNSgggSPRVKPSSAVKESKKSSDiEDSGES 247
Cdd:PTZ00108 1319 AALKKKKKSEKKTAR----------------------KKKSKTRVKQASASQ---SSRLLRRPRKKKSDSSSE-DDDDSE 1372
|
250
....*....|....*
gi 18859659 248 GEESATSDEEPDESS 262
Cdd:PTZ00108 1373 VDDSEDEDDEDDEDD 1387
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
349-488 |
1.24e-03 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 41.36 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEV-------------LQGkDVlvrsqtGSGKTLAYALPLVELLQkqqpriqrkDGVLALVIVPTRELVM 415
Cdd:cd17992 45 ELTGAQKRVIDEIlrdlasekpmnrlLQG-DV------GSGKTVVAALAMLAAVE---------NGYQVALMAPTEILAE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859659 416 QTYELIQKLVKPYTwiVPGSLLGGESRKSEK----ARLRKG-INILIGTpgrlvdHLLHTASFKLTKLQFLILDEADR 488
Cdd:cd17992 109 QHYDSLKKLLEPLG--IRVALLTGSTKAKEKreilEKIASGeIDIVIGT------HALIQEDVEFHNLGLVIIDEQHR 178
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
684-778 |
1.54e-03 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 42.58 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 684 HGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVHRVGRTARAGRKGRAVLFLTPSEAQ 763
Cdd:PLN03137 711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYI 790
|
90
....*....|....*
gi 18859659 764 FVRHLekkrirIQQG 778
Cdd:PLN03137 791 RVKHM------ISQG 799
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
327-470 |
2.24e-03 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 41.80 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 327 KISTLGLHPhavkNLEDLLSIR--ELTSVQQKTIPE-VLQGKDVLVRSQTGSGKTLAYALPLVellqkqqPRIQRKDGVL 403
Cdd:COG1202 189 PVDDLDLPP----ELKDLLEGRgeELLPVQSLAVENgLLEGKDQLVVSATATGKTLIGELAGI-------KNALEGKGKM 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 404 aLVIVPTRELVMQTYEliqKLVKPYTWIVPGSLLGGESRKSEKARlRKGIN--ILIGT-PGrlVDHLLHT 470
Cdd:COG1202 258 -LFLVPLVALANQKYE---DFKDRYGDGLDVSIRVGASRIRDDGT-RFDPNadIIVGTyEG--IDHALRT 320
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
683-743 |
3.35e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.25 E-value: 3.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 683 LHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIKLVVQYTPPQTTADFVH----RVGR 743
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHqlrgRVGR 131
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
351-418 |
5.48e-03 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 39.26 E-value: 5.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859659 351 TSVQQKTIPEVLQG-KDVLVRSQTGSGKTLAYALPLVELLQKQQPriQRKDGVLALVIVPTRELVMQTY 418
Cdd:cd18023 3 NRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNP--LPWGNRKVVYIAPIKALCSEKY 69
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
349-554 |
7.03e-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: 39.00 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 349 ELTSVQQKTIPEVLQGKDVLVRSQTGSGKTLAYALPLVELLQKQqpRIQRKDGVLAlVIVPTRELVMQTYELIQKLVKPY 428
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKR--RSAGEKGRVV-VLVNKVPLVEQQLEKFFKYFRKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 429 TWIVpgSLLGGESRKSEKARLRKGINILIGTPGRLVDHLLH---TASFKLTKLQFLILDeadrllelgyerdvkqlveai 505
Cdd:cd18036 79 YKVT--GLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSgreEERVYLSDFSLLIFD--------------------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18859659 506 dkqraECE--DKELP--QLQRMLLSATLTSQVQ--QLAGLTLKNPLYIDNSDEAA 554
Cdd:cd18036 136 -----ECHhtQKEHPynKIMRMYLDKKLSSQGPlpQILGLTASPGVGGARSFEEA 185
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
683-777 |
7.98e-03 |
|
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: 38.09 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 683 LHGSMTQTERQGVFRGFRDCASCVLLATDVVGRGIDVPDIK-LVVQYTPPQTTADFVHRVGRTARAGRKGRAvLFLTPSE 761
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANtIIIERADKFGLAQLYQLRGRVGRSKERAYA-YFLYPDQ 135
|
90
....*....|....*.
gi 18859659 762 AQFVRHLEKKRIRIQQ 777
Cdd:cd18810 136 KKLTEDALKRLEAIQE 151
|
|
| CobT2 |
COG4547 |
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ... |
205-301 |
8.26e-03 |
|
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 443611 [Multi-domain] Cd Length: 608 Bit Score: 39.78 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 205 DQEASADEEDAKNNSGGGSPrvkpSSAVKESKKSSDIEDSGESGEESATSDEEPDESSAQSPGQEKEPKQTAKKPPKAEE 284
Cdd:COG4547 226 SGEQEEDEEDGEDEDEESDE----GAEAEDAEASGDDAEEGESEAAEAESDEMAEEAEGEDSEEPGEPWRPNAPPPDDPA 301
|
90
....*....|....*..
gi 18859659 285 TSSTNRFRTKkiglFDQ 301
Cdd:COG4547 302 DPDYKVFTTA----FDE 314
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
203-288 |
8.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.57 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859659 203 GGDQEASADEEDAKNNSGGGSPRVKPSSAVKESKKSSD---------IEDSGESGEESATSDEEPDESS-AQSPGQEKEP 272
Cdd:PHA03169 138 PSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPeepepptsePEPDSPGPPQSETPTSSPPPQSpPDEPGEPQSP 217
|
90
....*....|....*..
gi 18859659 273 K-QTAKKPPKAEETSST 288
Cdd:PHA03169 218 TpQQAPSPNTQQAVEHE 234
|
|
| |
