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Conserved domains on  [gi|51338772|sp|P34689|]
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RecName: Full=ATP-dependent RNA helicase glh-1; AltName: Full=Germline helicase 1

Protein Classification

PTZ00368 and SrmB domain-containing protein( domain architecture ID 13283651)

PTZ00368 and SrmB domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
342-713 1.55e-135

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


:

Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 407.23  E-value: 1.55e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnlNTAGEGGcyPRC 421
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL------DPSRPRA--PQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGlaVGYNKgQIE---KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGG--VSIGR-QIRalkRGVDIVVATPGRLLDLIERGALDLSGVETLVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 499 DEADRMIDaMGFGTDIETIVnyDSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKCVLQEFERCER 578
Cdd:COG0513 152 DEADRMLD-MGFIEDIERIL--KLLPKE--RQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 579 SEKKDKLLELLgidiDSYTTEKsaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:COG0513 226 RDKLELLRRLL----RDEDPER--------AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:COG0513 294 VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD 348
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
160-278 3.31e-27

universal minicircle sequence binding protein (UMSBP); Provisional


The actual alignment was detected with superfamily member PTZ00368:

Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 107.59  E-value: 3.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  160 CFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTggfgggagfgnnggndgfggdggfgggeer 239
Cdd:PTZ00368  55 CYNCGKTGHLSRECPEAPPGSGPRSCYNCGQTGHISRECPNRAKGGAARR------------------------------ 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 51338772  240 gpmKCFNCKGEGHRSAECPEPP------RGCFNCGEQGHRSNECP 278
Cdd:PTZ00368 105 ---ACYNCGGEGHISRDCPNAGkrpggdKTCYNCGQTGHLSRDCP 146
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
342-713 1.55e-135

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 407.23  E-value: 1.55e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnlNTAGEGGcyPRC 421
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL------DPSRPRA--PQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGlaVGYNKgQIE---KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGG--VSIGR-QIRalkRGVDIVVATPGRLLDLIERGALDLSGVETLVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 499 DEADRMIDaMGFGTDIETIVnyDSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKCVLQEFERCER 578
Cdd:COG0513 152 DEADRMLD-MGFIEDIERIL--KLLPKE--RQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 579 SEKKDKLLELLgidiDSYTTEKsaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:COG0513 226 RDKLELLRRLL----RDEDPER--------AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:COG0513 294 VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD 348
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
342-563 1.98e-116

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: 350.25  E-value: 1.98e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDN-NLNTAGEGGCYPR 420
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGpPSVGRGRRKAYPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 421 CIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDE 500
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51338772 501 ADRMIDaMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIG 563
Cdd:cd17967 161 ADRMLD-MGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
343-734 1.18e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 302.49  E-value: 1.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMtrliddNNLNTAgeggcYPRC- 421
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL------QKLDVK-----RFRVq 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  422 -IILTPTRELADQIYNEGRKFAyQTMMEIKPVY--GGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:PRK11776  75 aLVLCPTRELADQVAKEIRRLA-RFIPNIKVLTlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDaMGFGTDIETIVnyDSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKcVLQEFERCER 578
Cdd:PRK11776 154 DEADRMLD-MGFQDAIDAII--RQAPAR--RQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDLPA-IEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  579 SEKKDKLLELLGididSYTTEKsaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:PRK11776 227 DERLPALQRLLL----HHQPES--------CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCS 294
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772  659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDcslLSELVGVLADAQQIVPDW 734
Cdd:PRK11776 295 VLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE---EMQRANAIEDYLGRKLNW 367
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
365-544 8.88e-49

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: 169.35  E-value: 8.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   365 TPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcYPRCIILTPTRELADQIYNEGRKFAYQ 444
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN---------GPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   445 TMMEIKPVYGGLAVGYNKGQIeKGATIIVGTVGRIKHFCEEgTIKLDKCRFFVLDEADRMIDaMGFGTDIETIVNydSMP 524
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLD-MGFGPDLEEILR--RLP 146
                         170       180
                  ....*....|....*....|
gi 51338772   525 rkENRQTLMFSATFPDSVQE 544
Cdd:pfam00270 147 --KKRQILLLSATLPRNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
359-561 3.27e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 158.04  E-value: 3.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772    359 AGYSKTTPIQQYALPLVHQGY-DIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcyPRCIILTPTRELADQIYNE 437
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG----------GRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772    438 GRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGAT-IIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIET 516
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 51338772    517 IVNYdsmpRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAIDK 561
Cdd:smart00487 153 LLKL----LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
160-278 3.31e-27

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 107.59  E-value: 3.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  160 CFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTggfgggagfgnnggndgfggdggfgggeer 239
Cdd:PTZ00368  55 CYNCGKTGHLSRECPEAPPGSGPRSCYNCGQTGHISRECPNRAKGGAARR------------------------------ 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 51338772  240 gpmKCFNCKGEGHRSAECPEPP------RGCFNCGEQGHRSNECP 278
Cdd:PTZ00368 105 ---ACYNCGGEGHISRDCPNAGkrpggdKTCYNCGQTGHLSRDCP 146
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
156-282 3.07e-13

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 68.72  E-value: 3.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 156 RNNNCFNCQQPGHRSSDCPEprkerepRVCYNCQQPGHTSRECTEerkpregrtggfgggagfgnnggndgfggdggfgg 235
Cdd:COG5082  59 ENPVCFNCGQNGHLRRDCPH-------SICYNCSWDGHRSNHCPK----------------------------------- 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51338772 236 geergPMKCFNCKGEGHRSAECPEPPRG---CFNCGEQGHRSNECPNPAK 282
Cdd:COG5082  97 -----PKKCYNCGETGHLSRDCNPSKDQqksCFDCNSTRHSSEDCPSIWK 141
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
183-200 4.04e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 4.04e-04
                          10
                  ....*....|....*...
gi 51338772   183 RVCYNCQQPGHTSRECTE 200
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
263-279 3.05e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 3.05e-03
                           10
                   ....*....|....*..
gi 51338772    263 GCFNCGEQGHRSNECPN 279
Cdd:smart00343   1 KCYNCGKEGHIARDCPS 17
 
Name Accession Description Interval E-value
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
342-713 1.55e-135

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 407.23  E-value: 1.55e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnlNTAGEGGcyPRC 421
Cdd:COG0513   3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRL------DPSRPRA--PQA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGlaVGYNKgQIE---KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:COG0513  75 LILAPTRELALQVAEELRKLAKYLGLRVATVYGG--VSIGR-QIRalkRGVDIVVATPGRLLDLIERGALDLSGVETLVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 499 DEADRMIDaMGFGTDIETIVnyDSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKCVLQEFERCER 578
Cdd:COG0513 152 DEADRMLD-MGFIEDIERIL--KLLPKE--RQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYLVDK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 579 SEKKDKLLELLgidiDSYTTEKsaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:COG0513 226 RDKLELLRRLL----RDEDPER--------AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIR 293
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:COG0513 294 VLVATDVAARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPD 348
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
342-563 1.98e-116

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: 350.25  E-value: 1.98e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDN-NLNTAGEGGCYPR 420
Cdd:cd17967   1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGpPSVGRGRRKAYPS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 421 CIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDE 500
Cdd:cd17967  81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51338772 501 ADRMIDaMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIG 563
Cdd:cd17967 161 ADRMLD-MGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
296-563 4.96e-106

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: 325.00  E-value: 4.96e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 296 YVPVE--DNMEDVFnmQKISEGLMFNKFFDAEVKLTSSEKTvgiKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALP 373
Cdd:cd18052   1 YIPPPppEDEDEIF--ATIQTGINFDKYDEIPVEVTGRNPP---PAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 374 LVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMmeIKPV- 452
Cdd:cd18052  76 IILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTC--IRPVv 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 453 -YGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIETIVNYDSMPRKENRQT 531
Cdd:cd18052 154 vYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLD-MGFGPEIRKLVSEPGMPSKEDRQT 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 51338772 532 LMFSATFPDSVQEAARAFLRENYVMIAIDKIG 563
Cdd:cd18052 233 LMFSATFPEEIQRLAAEFLKEDYLFLTVGRVG 264
PRK11776 PRK11776
ATP-dependent RNA helicase DbpA; Provisional
343-734 1.18e-94

ATP-dependent RNA helicase DbpA; Provisional


Pssm-ID: 236977 [Multi-domain]  Cd Length: 460  Bit Score: 302.49  E-value: 1.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMtrliddNNLNTAgeggcYPRC- 421
Cdd:PRK11776   6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLL------QKLDVK-----RFRVq 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  422 -IILTPTRELADQIYNEGRKFAyQTMMEIKPVY--GGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:PRK11776  75 aLVLCPTRELADQVAKEIRRLA-RFIPNIKVLTlcGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDaMGFGTDIETIVnyDSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKcVLQEFERCER 578
Cdd:PRK11776 154 DEADRMLD-MGFQDAIDAII--RQAPAR--RQTLLFSATYPEGIAAISQRFQR-DPVEVKVESTHDLPA-IEQRFYEVSP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  579 SEKKDKLLELLGididSYTTEKsaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:PRK11776 227 DERLPALQRLLL----HHQPES--------CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCS 294
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772  659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDcslLSELVGVLADAQQIVPDW 734
Cdd:PRK11776 295 VLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE---EMQRANAIEDYLGRKLNW 367
PTZ00110 PTZ00110
helicase; Provisional
338-757 1.09e-90

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 294.76  E-value: 1.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  338 KPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNtAGEGgc 417
Cdd:PTZ00110 127 KPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLR-YGDG-- 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  418 yPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFV 497
Cdd:PTZ00110 204 -PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLV 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  498 LDEADRMIDaMGFGTDIETIVnydSMPRKEnRQTLMFSATFPDSVQEAARAFLRENYVMIAIDKIG-AANKCVLQEFERC 576
Cdd:PTZ00110 283 LDEADRMLD-MGFEPQIRKIV---SQIRPD-RQTLMWSATWPKEVQSLARDLCKEEPVHVNVGSLDlTACHNIKQEVFVV 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  577 ERSEKKDKLLELLG-IDIDsytteksaevyTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNG 655
Cdd:PTZ00110 358 EEHEKRGKLKMLLQrIMRD-----------GDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTG 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  656 SKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED-CSLLSELVGVLADAQQIVPDW 734
Cdd:PTZ00110 427 KSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDkYRLARDLVKVLREAKQPVPPE 506
                        410       420       430
                 ....*....|....*....|....*....|.
gi 51338772  735 MQ--------GAAGGNYGASGFGSSVPTQVP 757
Cdd:PTZ00110 507 LEklsnersnGTERRRWGGYGRFSNNVNNIP 537
DEADc_DDX3 cd18051
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ...
318-564 5.24e-82

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: 261.51  E-value: 5.24e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 318 FNKFFDAEVKLTSSEktvGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLL 397
Cdd:cd18051   1 FDKYEDIPVEATGEN---CPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 398 PIMTRLIDD----NNLNTAGEGG---CYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGAT 470
Cdd:cd18051  78 PILSQIYEQgpgeSLPSESGYYGrrkQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 471 IIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFL 550
Cdd:cd18051 158 LLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLD-MGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL 236
                       250
                ....*....|....
gi 51338772 551 rENYVMIAIDKIGA 564
Cdd:cd18051 237 -DNYIFLAVGRVGS 249
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
341-710 1.29e-81

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 267.19  E-value: 1.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  341 KTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDdnnlntageggcYP- 419
Cdd:PRK11192   1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLD------------FPr 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  420 ------RCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGyNKGQI-EKGATIIVGTVGRIKHFCEEGtiKLDk 492
Cdd:PRK11192  69 rksgppRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYM-NHAEVfSENQDIVVATPGRLLQYIKEE--NFD- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  493 CR---FFVLDEADRMIDaMGFGTDIETIVNyDSMPRKenrQTLMFSATFP-DSVQEAARAFLRENyVMIAIDKIGAANKC 568
Cdd:PRK11192 145 CRaveTLILDEADRMLD-MGFAQDIETIAA-ETRWRK---QTLLFSATLEgDAVQDFAERLLNDP-VEVEAEPSRRERKK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  569 VLQEFERCERSEKKDKLLE-LLgididsytteKSAEVytKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSE 647
Cdd:PRK11192 219 IHQWYYRADDLEHKTALLChLL----------KQPEV--TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNE 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51338772  648 ALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFI 710
Cdd:PRK11192 287 AIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLV 349
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
352-557 9.12e-72

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: 232.72  E-value: 9.12e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 352 MQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGeggcyPRCIILTPTRELA 431
Cdd:cd00268   1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRG-----PQALVLAPTRELA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 432 DQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFG 511
Cdd:cd00268  76 MQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLD-MGFE 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 51338772 512 TDIETIVNYdsMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMI 557
Cdd:cd00268 155 EDVEKILSA--LPKD--RQTLLFSATLPEEVKELAKKFLK-NPVRI 195
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
356-713 7.63e-70

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 236.63  E-value: 7.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  356 VAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNnlnTAGEGGCYPRCIILTPTRELADQIY 435
Cdd:PRK10590  16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQ---PHAKGRRPVRALILTPTRELAAQIG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  436 NEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIE 515
Cdd:PRK10590  93 ENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLD-MGFIHDIR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  516 TIVNydSMPRKenRQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKCVLQEFERCERSEKKDKLLELLGidids 595
Cdd:PRK10590 172 RVLA--KLPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG----- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  596 ytteksaEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGV 675
Cdd:PRK10590 242 -------KGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEEL 314
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 51338772  676 DHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:PRK10590 315 PHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVD 352
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
343-713 1.71e-69

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 236.35  E-value: 1.71e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnLNTAGEGGCY---P 419
Cdd:PRK01297  89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQL-----LQTPPPKERYmgeP 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  420 RCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIE-KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:PRK01297 164 RALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVL 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDaMGFGTDIETIVNYDsmPRKENRQTLMFSATFPDSVQEAARAFLRENyVMIAIDKIGAANKCVLQEFERCER 578
Cdd:PRK01297 244 DEADRMLD-MGFIPQVRQIIRQT--PRKEERQTLLFSATFTDDVMNLAKQWTTDP-AIVEIEPENVASDTVEQHVYAVAG 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  579 SEKKDKLLELLgididsytTEKSAEvytkKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:PRK01297 320 SDKYKLLYNLV--------TQNPWE----RVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIR 387
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772  659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:PRK01297 388 VLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGED 442
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
339-732 3.03e-69

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 236.61  E-value: 3.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  339 PCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGcy 418
Cdd:PLN00206 119 PILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSEQRN-- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  419 PRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:PLN00206 197 PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVL 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDAmGFGTDIETIVNYDSMPrkenrQTLMFSATFPDSVQEAARAFLReNYVMIAIDKIGAANKCVLQEFERCER 578
Cdd:PLN00206 277 DEVDCMLER-GFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPNKAVKQLAIWVET 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  579 SEKKDKLLELLgididsytteKSAEVYTKKTMVFVSQRAMADTLA-SILSSAQVPAITIHGAREQRERSEALRQFRNGSK 657
Cdd:PLN00206 350 KQKKQKLFDIL----------KSKQHFKPPAVVFVSSRLGADLLAnAITVVTGLKALSIHGEKSMKERREVMKSFLVGEV 419
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772  658 PVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFIS-EDCSLLSELVGVLADAQQIVP 732
Cdd:PLN00206 420 PVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNeEDRNLFPELVALLKSSGAAIP 495
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
342-712 5.41e-68

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 234.84  E-value: 5.41e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLntAGEGGCYPRC 421
Cdd:PRK04537  10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPAL--ADRKPEDPRA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGlaVGYNKGQ--IEKGATIIVGTVGR-IKHFCEEGTIKLDKCRFFVL 498
Cdd:PRK04537  88 LILAPTRELAIQIHKDAVKFGADLGLRFALVYGG--VDYDKQRelLQQGVDVIIATPGRlIDYVKQHKVVSLHACEICVL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDaMGFGTDIETIVNydSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIA-IDKIGAANkcVLQEFERCE 577
Cdd:PRK04537 166 DEADRMFD-LGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVeTETITAAR--VRQRIYFPA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  578 RSEKKDKLLELLGididsyTTEKSaevytkKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSK 657
Cdd:PRK04537 241 DEEKQTLLLGLLS------RSEGA------RTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQL 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772  658 PVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISE 712
Cdd:PRK04537 309 EILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE 363
PRK04837 PRK04837
ATP-dependent RNA helicase RhlB; Provisional
341-713 2.79e-65

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235314 [Multi-domain]  Cd Length: 423  Bit Score: 223.31  E-value: 2.79e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  341 KTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIddNNLNTAGEGGCYPR 420
Cdd:PRK04837   8 QKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLL--SHPAPEDRKVNQPR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  421 CIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGlaVGYNK--GQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL 498
Cdd:PRK04837  86 ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGG--DGYDKqlKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  499 DEADRMIDaMGFGTDIETIvnYDSMPRKENRQTLMFSATFPDSVQEAarAFLREN---YVMIAID-KIGaanKCVLQEFE 574
Cdd:PRK04837 164 DEADRMFD-LGFIKDIRWL--FRRMPPANQRLNMLFSATLSYRVREL--AFEHMNnpeYVEVEPEqKTG---HRIKEELF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  575 RCERSEKKDKLLELLgididsytteksAEVYTKKTMVFVSQRAMADTLASILSS--AQVPAITihGAREQRERSEALRQF 652
Cdd:PRK04837 236 YPSNEEKMRLLQTLI------------EEEWPDRAIIFANTKHRCEEIWGHLAAdgHRVGLLT--GDVAQKKRLRILEEF 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51338772  653 RNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:PRK04837 302 TRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
569-710 2.62e-55

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: 185.79  E-value: 2.62e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 569 VLQEFERCERSEKKDKLLELLGIDIDsytteksaevyTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEA 648
Cdd:cd18787   1 IKQLYVVVEEEEKKLLLLLLLLEKLK-----------PGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERA 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51338772 649 LRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFI 710
Cdd:cd18787  70 LKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
342-710 5.78e-52

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 191.60  E-value: 5.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMtrliddNNLNTAGEGgcyPRC 421
Cdd:PRK11634   7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL------HNLDPELKA---PQI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  422 IILTPTRELADQIYNEGRKFAyQTMMEIKPV--YGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLD 499
Cdd:PRK11634  78 LVLAPTRELAVQVAEAMTDFS-KHMRGVNVValYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  500 EADRMIdAMGFGTDIETIVNydSMPrkENRQTLMFSATFPDSVQEAARAFLRENYvMIAIDKIGAANKCVLQEFERCERS 579
Cdd:PRK11634 157 EADEML-RMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQ-EVRIQSSVTTRPDISQSYWTVWGM 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  580 EKKDKLLELL-GIDIDSytteksaevytkkTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP 658
Cdd:PRK11634 231 RKNEALVRFLeAEDFDA-------------AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLD 297
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51338772  659 VLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFI 710
Cdd:PRK11634 298 ILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
PTZ00424 PTZ00424
helicase 45; Provisional
342-713 5.05e-51

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 183.49  E-value: 5.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLidDNNLNTAgeggcypRC 421
Cdd:PTZ00424  29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI--DYDLNAC-------QA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEA 501
Cdd:PTZ00424 100 LILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  502 DRMIdAMGFGTDIETIvnYDSMPrkENRQTLMFSATFPDSVQEAARAFLRENYVMIAidkigaankcvlqefercerseK 581
Cdd:PTZ00424 180 DEML-SRGFKGQIYDV--FKKLP--PDVQVALFSATMPNEILELTTKFMRDPKRILV----------------------K 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  582 KDKL-LE-----LLGIDIDSYTTEKSAEVYTKKTMV----FVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQ 651
Cdd:PTZ00424 233 KDELtLEgirqfYVAVEKEEWKFDTLCDLYETLTITqaiiYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMRE 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51338772  652 FRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:PTZ00424 313 FRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPD 374
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
338-551 3.01e-49

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: 172.56  E-value: 3.01e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 338 KPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPiMTRLIDDNNLNTAGEGgc 417
Cdd:cd17953   9 KPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLP-MFRHIKDQRPVKPGEG-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 418 yPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGR-IKHFCEEG--TIKLDKCR 494
Cdd:cd17953  86 -PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRmIDILTANNgrVTNLRRVT 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 51338772 495 FFVLDEADRMIDaMGFGTDIETIVNydsmPRKENRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17953 165 YVVLDEADRMFD-MGFEPQIMKIVN----NIRPDRQTVLFSATFPRKVEALARKVLH 216
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
354-559 7.88e-49

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: 170.46  E-value: 7.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntagEGGcyPRCIILTPTRELADQ 433
Cdd:cd17957   3 NNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRK-----KKG--LRALILAPTRELASQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 434 IYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIE-KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGT 512
Cdd:cd17957  76 IYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFE-PGFRE 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 51338772 513 DIETIVNYDSMPRKenrQTLMFSATFPDSVQEAARAFLReNYVMIAI 559
Cdd:cd17957 155 QTDEILAACTNPNL---QRSLFSATIPSEVEELARSVMK-DPIRIIV 197
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
365-544 8.88e-49

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: 169.35  E-value: 8.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   365 TPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcYPRCIILTPTRELADQIYNEGRKFAYQ 444
Cdd:pfam00270   1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDN---------GPQALVLAPTRELAEQIYEELKKLGKG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   445 TMMEIKPVYGGLAVGYNKGQIeKGATIIVGTVGRIKHFCEEgTIKLDKCRFFVLDEADRMIDaMGFGTDIETIVNydSMP 524
Cdd:pfam00270  72 LGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLD-MGFGPDLEEILR--RLP 146
                         170       180
                  ....*....|....*....|
gi 51338772   525 rkENRQTLMFSATFPDSVQE 544
Cdd:pfam00270 147 --KKRQILLLSATLPRNLED 164
DEADc_DDX5_DDX17 cd17966
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ...
354-552 3.49e-48

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: 168.70  E-value: 3.49e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRlIDDNNLNTAGEGgcyPRCIILTPTRELADQ 433
Cdd:cd17966   3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVH-INAQPPLERGDG---PIVLVLAPTRELAQQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 434 IYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTD 513
Cdd:cd17966  79 IQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLD-MGFEPQ 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51338772 514 IETIVNydsmPRKENRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17966 158 IRKIVD----QIRPDRQTLMWSATWPKEVRRLAEDFLKD 192
DEADc_DDX42 cd17952
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ...
356-550 6.17e-48

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: 167.98  E-value: 6.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 356 VAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLnTAGEGgcyPRCIILTPTRELADQIY 435
Cdd:cd17952   5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQREL-EKGEG---PIAVIVAPTRELAQQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 436 NEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIE 515
Cdd:cd17952  81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFD-MGFEYQVR 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 51338772 516 TIVNYdsmpRKENRQTLMFSATFPDSVQEAARAFL 550
Cdd:cd17952 160 SIVGH----VRPDRQTLLFSATFKKKIEQLARDIL 190
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
354-551 2.49e-46

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: 163.58  E-value: 2.49e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnLNTAGEGGcYPRCIILTPTRELADQ 433
Cdd:cd17947   3 RALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL-----LYRPKKKA-ATRVLVLVPTRELAMQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 434 IYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGR-IKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGT 512
Cdd:cd17947  77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRlIDHLRNSPSFDLDSIEILVLDEADRMLE-EGFAD 155
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51338772 513 DIETIVNYdsMPRkeNRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17947 156 ELKEILRL--CPR--TRQTMLFSATMTDEVKDLAKLSLN 190
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
360-552 7.90e-45

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 160.18  E-value: 7.90e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 360 GYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLN--TAGEGgcyPRCIILTPTRELADQIYNE 437
Cdd:cd17945   9 GYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeeTKDDG---PYALILAPTRELAQQIEEE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 438 GRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIETI 517
Cdd:cd17945  86 TQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMID-MGFEPQVTKI 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 51338772 518 VnyDSMP------------------RKENRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17945 165 L--DAMPvsnkkpdteeaeklaasgKHRYRQTMMFTATMPPAVEKIAKGYLRR 215
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
342-557 1.26e-44

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: 159.39  E-value: 1.26e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLidDNNLNTAGeggcyPRC 421
Cdd:cd17959   2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--KAHSPTVG-----ARA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 422 IILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEA 501
Cdd:cd17959  75 LILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEA 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772 502 DRMIDaMGFGTDIETIVNydSMPrkENRQTLMFSATFPDSVQEAARAFLREnYVMI 557
Cdd:cd17959 155 DRLFE-MGFAEQLHEILS--RLP--ENRQTLLFSATLPKLLVEFAKAGLNE-PVLI 204
DEXDc smart00487
DEAD-like helicases superfamily;
359-561 3.27e-44

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 158.04  E-value: 3.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772    359 AGYSKTTPIQQYALPLVHQGY-DIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcyPRCIILTPTRELADQIYNE 437
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRGKG----------GRVLVLVPTRELAEQWAEE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772    438 GRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGAT-IIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTDIET 516
Cdd:smart00487  74 LKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTdILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD-GGFGDQLEK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 51338772    517 IVNYdsmpRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAIDK 561
Cdd:smart00487 153 LLKL----LPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
348-557 2.55e-43

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: 155.82  E-value: 2.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 348 LTETMQKNVAHAGYSKTTPIQQYAL-PLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEggcyPRCIILTP 426
Cdd:cd17964   1 LDPSLLKALTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSG----VSALIISP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 427 TRELADQIYNEGRKF-AYQTMMEIKPVYGGLAVGYNKGQIEK-GATIIVGTVGRIK-HFCEEGTIK-LDKCRFFVLDEAD 502
Cdd:cd17964  77 TRELALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIdHLENPGVAKaFTDLDYLVLDEAD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 503 RMIDaMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMI 557
Cdd:cd17964 157 RLLD-MGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
DEADc_DDX5 cd18049
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ...
330-559 8.21e-43

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: 155.17  E-value: 8.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 330 SSEKTV----GIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRlID 405
Cdd:cd18049   9 SKEITVrghnCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVH-IN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 406 DNNLNTAGEGgcyPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEE 485
Cdd:cd18049  88 HQPFLERGDG---PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEA 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51338772 486 GTIKLDKCRFFVLDEADRMIDaMGFGTDIETIVnyDSMprKENRQTLMFSATFPDSVQEAARAFLREnYVMIAI 559
Cdd:cd18049 165 GKTNLRRCTYLVLDEADRMLD-MGFEPQIRKIV--DQI--RPDRQTLMWSATWPKEVRQLAEDFLKD-YIHINI 232
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
342-551 1.23e-42

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 153.63  E-value: 1.23e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 342 TFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDnnlntageggcyPR- 420
Cdd:cd17954   1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLEN------------PQr 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 421 --CIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGT-IKLDKCRFFV 497
Cdd:cd17954  69 ffALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLV 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 51338772 498 LDEADRMIDaMGFGTDIETIVnyDSMPRkeNRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17954 149 MDEADRLLN-MDFEPEIDKIL--KVIPR--ERTTYLFSATMTTKVAKLQRASLK 197
DEADc_DDX10 cd17941
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ...
353-552 3.22e-42

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: 152.06  E-value: 3.22e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 353 QKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGgcyprCIILTPTRELAD 432
Cdd:cd17941   2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEDGLG-----ALIISPTRELAM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 433 QIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEkGATIIVGTVGRI-KHFCEEGTIKLDKCRFFVLDEADRMIDaMGFG 511
Cdd:cd17941  77 QIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLlQHMDETPGFDTSNLQMLVLDEADRILD-MGFK 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 51338772 512 TDIETIVNYdsMPRKenRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17941 155 ETLDAIVEN--LPKS--RQTLLFSATQTKSVKDLARLSLKN 191
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
352-552 6.29e-42

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: 151.46  E-value: 6.29e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 352 MQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGgcyPRCIILTPTRELA 431
Cdd:cd17958   1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPIPREQRNG---PGVLVLTPTRELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 432 DQIYNEGRKFAYQTMMEIkPVYGGlavGYNKGQIE---KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaM 508
Cdd:cd17958  78 LQIEAECSKYSYKGLKSV-CVYGG---GNRNEQIEdlsKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLD-M 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 51338772 509 GFGTDIETIVnYDSMPrkeNRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17958 153 GFEPQIRKIL-LDIRP---DRQTIMTSATWPDGVRRLAQSYLKD 192
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
343-550 5.43e-41

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: 148.91  E-value: 5.43e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntagegGCYprCI 422
Cdd:cd17955   1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPY-------GIF--AL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIK-HF--CEEGTIKLDKCRFFVLD 499
Cdd:cd17955  72 VLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLAdHLrsSDDTTKVLSRVKFLVLD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 51338772 500 EADRMIDAmGFGTDIETIVNydSMPRKenRQTLMFSATFPDSVQEAARAFL 550
Cdd:cd17955 152 EADRLLTG-SFEDDLATILS--ALPPK--RQTLLFSATLTDALKALKELFG 197
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
356-551 1.02e-40

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: 148.11  E-value: 1.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 356 VAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDnnlnTAGEGGCYPRCIILTPTRELADQIY 435
Cdd:cd17960   5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKR----KANLKKGQVGALIISPTRELATQIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 436 NEGRKFAYQTMMEIKP--VYGGLAVGYNKGQI-EKGATIIVGTVGRIKHFCEEGTIKLDKCRF--FVLDEADRMIDaMGF 510
Cdd:cd17960  81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADKVKVKSLevLVLDEADRLLD-LGF 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 51338772 511 GTDIETIVNYdsMPRkeNRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17960 160 EADLNRILSK--LPK--QRRTGLFSATQTDAVEELIKAGLR 196
DEADc_DDX17 cd18050
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ...
338-559 1.24e-40

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: 150.16  E-value: 1.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 338 KPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnNLNTAGEGGC 417
Cdd:cd18050  59 KPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI----NHQPYLERGD 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 418 YPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFV 497
Cdd:cd18050 135 GPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLV 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51338772 498 LDEADRMIDaMGFGTDIETIVnyDSMprKENRQTLMFSATFPDSVQEAARAFLREnYVMIAI 559
Cdd:cd18050 215 LDEADRMLD-MGFEPQIRKIV--DQI--RPDRQTLMWSATWPKEVRQLAEDFLRD-YVQINI 270
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
360-557 5.48e-40

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: 146.58  E-value: 5.48e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 360 GYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGgcyPRCIILTPTRELADQIYNEGR 439
Cdd:cd17949  10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDG---TLALVLVPTRELALQIYEVLE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 440 KFayqtmmeIKP----VYGGLAVGYN----KGQIEKGATIIVGTVGRI-KHFCEEGTIKLDKCRFFVLDEADRMIDaMGF 510
Cdd:cd17949  87 KL-------LKPfhwiVPGYLIGGEKrkseKARLRKGVNILIATPGRLlDHLKNTQSFDVSNLRWLVLDEADRLLD-MGF 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772 511 GTDIETIVNY-DSMPRKEN--------RQTLMFSATFPDSVQEAARAFLReNYVMI 557
Cdd:cd17949 159 EKDITKILELlDDKRSKAGgekskpsrRQTVLVSATLTDGVKRLAGLSLK-DPVYI 213
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
352-538 2.27e-39

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: 145.46  E-value: 2.27e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 352 MQKNVAHAGYSKTTPIQQYALPL-VHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGCYPRCIILTPTREL 430
Cdd:cd17946   1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILERLLSQKSSNGVGGKQKPLRALILTPTREL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 431 ADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEG---TIKLDKCRFFVLDEADRMIDA 507
Cdd:cd17946  81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 51338772 508 MGFgTDIETI---VNYDSMPRKENRQTLMFSATF 538
Cdd:cd17946 161 GHF-AELEKIlelLNKDRAGKKRKRQTFVFSATL 193
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
343-554 2.68e-39

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: 143.98  E-value: 2.68e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRlIDDNNLNTAGeggcyprcI 422
Cdd:cd17940   1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEK-IDPKKDVIQA--------L 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEAD 502
Cdd:cd17940  72 ILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEAD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 51338772 503 RMIDaMGFGTDIETIVNYdsMPRkeNRQTLMFSATFPDSVQEAARAFLRENY 554
Cdd:cd17940 152 KLLS-QDFQPIIEKILNF--LPK--ERQILLFSATFPLTVKNFMDRHMHNPY 198
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
343-537 5.54e-39

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: 143.23  E-value: 5.54e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnlntageggcypRCI 422
Cdd:cd17938   1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV----------------VAL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNEGRKFA-YQTMMEIKP--VYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLD 499
Cdd:cd17938  65 ILEPSRELAEQTYNCIENFKkYLDNPKLRValLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51338772 500 EADRMIDAmgfgTDIETIVN-YDSMPRKENR----QTLMFSAT 537
Cdd:cd17938 145 EADRLLSQ----GNLETINRiYNRIPKITSDgkrlQVIVCSAT 183
DEADc_DDX19_DDX25 cd17963
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ...
354-549 6.52e-39

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: 142.71  E-value: 6.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKTTPIQQYALPLVHQGYD--IMACAQTGSGKTAAFLLPIMTRLidDNNLNtageggcYPRCIILTPTRELA 431
Cdd:cd17963   7 KGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRV--DPTLK-------SPQALCLAPTRELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 432 DQIYNEGRKFAYQTMMEIkpvygGLAVGYNKGQIEKGAT--IIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDAMG 509
Cdd:cd17963  78 RQIGEVVEKMGKFTGVKV-----ALAVPGNDVPRGKKITaqIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTQG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 51338772 510 FGTDIETIVNYdsMPRkeNRQTLMFSATFPDSVQEAARAF 549
Cdd:cd17963 153 HGDQSIRIKRM--LPR--NCQILLFSATFPDSVRKFAEKI 188
DEADc_DDX41 cd17951
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ...
360-550 2.42e-38

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: 141.71  E-value: 2.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 360 GYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLP-IMTRLIDDNNLN-TAGEGgcyPRCIILTPTRELADQIYNE 437
Cdd:cd17951   9 GIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEQEKKLPfIKGEG---PYGLIVCPSRELARQTHEV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 438 GRKFAYQTMMEIKP------VYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFG 511
Cdd:cd17951  86 IEYYCKALQEGGYPqlrcllCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID-MGFE 164
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51338772 512 TDIETIVNYdsmpRKENRQTLMFSATFPDSVQEAARAFL 550
Cdd:cd17951 165 EDIRTIFSY----FKGQRQTLLFSATMPKKIQNFAKSAL 199
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
354-557 2.16e-34

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: 130.35  E-value: 2.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGgcyPRCIILTPTRELADQ 433
Cdd:cd17944   3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRA---PKVLVLAPTRELANQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 434 IYNEGRKFAYQtmMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTD 513
Cdd:cd17944  80 VTKDFKDITRK--LSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLD-MGFAEQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 51338772 514 IETI--VNYDSMPrKENRQTLMFSATFPDSVQEAARAFLRENYVMI 557
Cdd:cd17944 157 VEEIlsVSYKKDS-EDNPQTLLFSATCPDWVYNVAKKYMKSQYEQV 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
580-701 5.41e-34

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: 125.79  E-value: 5.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   580 EKKDKLLELLgididsytteksAEVYTKKTMVFVSQRAMADtLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPV 659
Cdd:pfam00271   1 EKLEALLELL------------KKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 51338772   660 LIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVG 701
Cdd:pfam00271  68 LVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
353-551 5.89e-33

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: 126.16  E-value: 5.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 353 QKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlNTAGEGGcyPRCIILTPTRELAD 432
Cdd:cd17961   6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKA-ESGEEQG--TRALILVPTRELAQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 433 QIYNEGRKFAYQTMMEIKPV--YGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKL-DKCRFFVLDEADrMIDAMG 509
Cdd:cd17961  83 QVSKVLEQLTAYCRKDVRVVnlSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEAD-LVLSYG 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 51338772 510 FGTDIETIVnyDSMPRkeNRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17961 162 YEEDLKSLL--SYLPK--NYQTFLMSATLSEDVEALKKLVLH 199
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
348-551 1.03e-32

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: 125.54  E-value: 1.03e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 348 LTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMtrliddNNLNTAgEGGCypRCIILTPT 427
Cdd:cd17950   9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTL------QQLEPV-DGQV--SVLVICHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 428 RELADQIYNEGRKFA-YQTMMEIKPVYGGLAVGYNKGQIE-KGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMI 505
Cdd:cd17950  80 RELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKnKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKML 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 51338772 506 DAMGFGTDIETIvnYDSMPRKenRQTLMFSATFPDSVQEAARAFLR 551
Cdd:cd17950 160 EQLDMRRDVQEI--FRATPHD--KQVMMFSATLSKEIRPVCKKFMQ 201
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
359-552 4.68e-32

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: 123.14  E-value: 4.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 359 AGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnNLNTAGeggcyPRCIILTPTRELADQIYNEG 438
Cdd:cd17943   8 AGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----DLERRH-----PQVLILAPTREIAVQIHDVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 439 RKFAyQTMMEIKPVY--GGLAVGYNKGQIeKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDAmGFGTDIET 516
Cdd:cd17943  79 KKIG-KKLEGLKCEVfiGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEG-SFQKDVNW 155
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 51338772 517 IvnYDSMPrkENRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17943 156 I--FSSLP--KNKQVIAFSATYPKNLDNLLARYMRK 187
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
355-552 7.42e-32

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: 122.66  E-value: 7.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 355 NVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcYPRCIILTPTRELADQI 434
Cdd:cd17962   4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHR---------NPSALILTPTRELAVQI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 435 YNEGRKFAYQTM-MEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDaMGFGTD 513
Cdd:cd17962  75 EDQAKELMKGLPpMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLK-MGFQQQ 153
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 51338772 514 IETIvnYDSMPRkeNRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17962 154 VLDI--LENISH--DHQTILVSATIPRGIEQLAGQLLQN 188
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
353-552 5.92e-31

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: 120.16  E-value: 5.92e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 353 QKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGgcyprCIILTPTRELAD 432
Cdd:cd17942   2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTG-----VIIISPTRELAL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 433 QIYNEGR---KFAYQTmmeikpvYGGLAVGYNKGQ----IEKGATIIVGTVGR-IKHFCEEGTIKLDKCRFFVLDEADRM 504
Cdd:cd17942  77 QIYGVAKellKYHSQT-------FGIVIGGANRKAeaekLGKGVNILVATPGRlLDHLQNTKGFLYKNLQCLIIDEADRI 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 51338772 505 IDAmGFGTDIETIVNYdsMPRKenRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17942 150 LEI-GFEEEMRQIIKL--LPKR--RQTMLFSATQTRKVEDLARISLKK 192
HELICc smart00490
helicase superfamily c-terminal domain;
620-701 6.77e-31

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 115.77  E-value: 6.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772    620 DTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGR 699
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80

                   ..
gi 51338772    700 VG 701
Cdd:smart00490  81 AG 82
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
345-552 1.88e-30

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: 118.97  E-value: 1.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 345 EANLTETMQKNVAHAGYSKTTPIQQYA-LPLVhQGYDIMACAQTGSGKTAAFLLPIMTRLidDNNLNTageggcyPRCII 423
Cdd:cd17939   1 DMGLSEDLLRGIYAYGFEKPSAIQQRAiVPII-KGRDVIAQAQSGTGKTATFSIGALQRI--DTTVRE-------TQALV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 424 LTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADR 503
Cdd:cd17939  71 LAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADE 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 51338772 504 MIDAmGFGTDIETIVNYdsMPRKEnrQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd17939 151 MLSR-GFKDQIYDIFQF--LPPET--QVVLFSATMPHEVLEVTKKFMRD 194
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
343-552 5.42e-30

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: 117.55  E-value: 5.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLidDNNLNTageggcyPRCI 422
Cdd:cd18046   1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI--DTSLKA-------TQAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEAD 502
Cdd:cd18046  72 VLAPTRELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEAD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 51338772 503 RMIdAMGFGTDIETIvnYDSMPrkENRQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd18046 152 EML-SRGFKDQIYDI--FQKLP--PDTQVVLLSATMPNDVLEVTTKFMRD 196
DEADc_DDX25 cd18048
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ...
326-542 1.19e-27

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: 111.65  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 326 VKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALP--LVHQGYDIMACAQTGSGKTAAFLLPIMTRl 403
Cdd:cd18048   3 VEVLQRDPTSPLFSVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPmmLADPPQNLIAQSQSGTGKTAAFVLAMLSR- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 404 IDDNNLntageggcYPRCIILTPTRELADQ---IYNEGRKFAyqtmMEIKPVYGGLAVGYNKG-QIEkgATIIVGTVGRI 479
Cdd:cd18048  82 VDALKL--------YPQCLCLSPTFELALQtgkVVEEMGKFC----VGIQVIYAIRGNRPGKGtDIE--AQIVIGTPGTV 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51338772 480 KHFC-EEGTIKLDKCRFFVLDEADRMIDAMGFGTdiETIVNYDSMPRkeNRQTLMFSATFPDSV 542
Cdd:cd18048 148 LDWCfKLRLIDVTNISVFVLDEADVMINVQGHSD--HSVRVKRSMPK--ECQMLLFSATFEDSV 207
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
160-278 3.31e-27

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 107.59  E-value: 3.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  160 CFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTggfgggagfgnnggndgfggdggfgggeer 239
Cdd:PTZ00368  55 CYNCGKTGHLSRECPEAPPGSGPRSCYNCGQTGHISRECPNRAKGGAARR------------------------------ 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 51338772  240 gpmKCFNCKGEGHRSAECPEPP------RGCFNCGEQGHRSNECP 278
Cdd:PTZ00368 105 ---ACYNCGGEGHISRDCPNAGkrpggdKTCYNCGQTGHLSRDCP 146
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
348-544 1.07e-25

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 106.30  E-value: 1.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 348 LTETMQKNvahaGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGcyPRCIILTPT 427
Cdd:cd17948   1 LVEILQRQ----GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPFNA--PRGLVITPS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 428 RELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMID- 506
Cdd:cd17948  75 RELAEQIGSVAQSLTEGLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDd 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 51338772 507 -------------AMGFGTDIETIVNYdsmprkENRQTLMFSATFPDSVQE 544
Cdd:cd17948 155 sfneklshflrrfPLASRRSENTDGLD------PGTQLVLVSATMPSGVGE 199
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
158-297 6.56e-25

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 101.04  E-value: 6.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  158 NNCFNCQQPGHRSSDCPEPRK--EREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDggfgg 235
Cdd:PTZ00368   1 MVCYRCGGVGHQSRECPNSAPagAAKARPCYKCGEPGHLSRECPSAPGGRGERSCYNCGKTGHLSRECPEAPPGS----- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51338772  236 geerGPMKCFNCKGEGHRSAECPEPPRG------CFNCGEQGHRSNECPNPAKPregveGEGPKATYV 297
Cdd:PTZ00368  76 ----GPRSCYNCGQTGHISRECPNRAKGgaarraCYNCGGEGHISRDCPNAGKR-----PGGDKTCYN 134
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
352-508 2.41e-20

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: 90.77  E-value: 2.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 352 MQKNVAHAGYSKTTPIQQYALPLVHQGY---------DIMACAQTGSGKTAAFLLPIMTRLiddnnlntAGEGGCYPRCI 422
Cdd:cd17956   1 LLKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQAL--------SKRVVPRLRAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNE----------------GRKFAYQTMMEIKPVYGGLAvgynkgqiEKGATIIVGTVGRI-KHFCEE 485
Cdd:cd17956  73 IVVPTKELVQQVYKVfeslckgtglkvvslsGQKSFKKEQKLLLVDTSGRY--------LSRVDILVATPGRLvDHLNST 144
                       170       180
                ....*....|....*....|...
gi 51338772 486 GTIKLDKCRFFVLDEADRMIDAM 508
Cdd:cd17956 145 PGFTLKHLRFLVIDEADRLLNQS 167
DEADc_EIF4AIII_DDX48 cd18045
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ...
343-552 6.55e-20

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: 88.68  E-value: 6.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 343 FAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTrlIDDNNLNTageggcyPRCI 422
Cdd:cd18045   1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ--CLDIQVRE-------TQAL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 423 ILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEAD 502
Cdd:cd18045  72 ILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEAD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 51338772 503 RMIDaMGFGTDIETIVNYdsMPRKEnrQTLMFSATFPDSVQEAARAFLRE 552
Cdd:cd18045 152 EMLN-KGFKEQIYDVYRY--LPPAT--QVVLVSATLPQDILEMTNKFMTD 196
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
545-713 1.24e-18

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 90.56  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 545 AARAFLRENYVMIAIDKIGAANkcvlqefercERSEKKDKLLEL----LGIDIDSytteksaevytkKTMVFVSQRAMAD 620
Cdd:COG1111 310 ASKRLVSDPRFRKAMRLAEEAD----------IEHPKLSKLREIlkeqLGTNPDS------------RIIVFTQYRDTAE 367
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 621 TLASILSSAQVPAITIHG--ARE------QRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYD-MPDNIdDYI 691
Cdd:COG1111 368 MIVEFLSEPGIKAGRFVGqaSKEgdkgltQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEI-RSI 446
                       170       180
                ....*....|....*....|..
gi 51338772 692 HRIGRTGRvGNSGRATSFISED 713
Cdd:COG1111 447 QRKGRTGR-KREGRVVVLIAKG 467
DEADc_DDX19 cd18047
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ...
341-546 1.66e-17

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: 81.69  E-value: 1.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 341 KTFAEANLTETMQKNVAHAGYSKTTPIQQYALP--LVHQGYDIMACAQTGSGKTAAFLLPIMTRLiddnnlntagEGGC- 417
Cdd:cd18047   1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPlmLAEPPQNLIAQSQSGTGKTAAFVLAMLSQV----------EPANk 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 418 YPRCIILTPTRELADQIyneGRkfAYQTMMEIKPVYgGLAVGYNKGQIEKGA----TIIVGTVGRIKHFC-EEGTIKLDK 492
Cdd:cd18047  71 YPQCLCLSPTYELALQT---GK--VIEQMGKFYPEL-KLAYAVRGNKLERGQkiseQIVIGTPGTVLDWCsKLKFIDPKK 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 51338772 493 CRFFVLDEADRMIDAMGFGTdiETIVNYDSMPRkeNRQTLMFSATFPDSVQEAA 546
Cdd:cd18047 145 IKVFVLDEADVMIATQGHQD--QSIRIQRMLPR--NCQMLLFSATFEDSVWKFA 194
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
367-679 3.52e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 85.46  E-value: 3.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 367 IQQYALPLVHQGYDIMACAQTGSGKTAAFLLpIMTRLIDDnnlntageggcyPRCIILTPTRELADQIYNEGRKFayqtm 446
Cdd:COG1061  89 LEALLAALERGGGRGLVVAPTGTGKTVLALA-LAAELLRG------------KRVLVLVPRRELLEQWAEELRRF----- 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 447 mEIKPVYGGlavgynkGQIEKGATIIVGTVGRIKHFCEEGTIKlDKCRFFVLDEADRMIdAMGFgtdiETIVNYDSMPRK 526
Cdd:COG1061 151 -LGDPLAGG-------GKKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAG-APSY----RRILEAFPAAYR 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 527 enrqtLMFSAT------------------FPDSVQEAARA-FLRE-NYVMIAIDkigaankcvLQEfERCERSEKKDKLL 586
Cdd:COG1061 217 -----LGLTATpfrsdgreillflfdgivYEYSLKEAIEDgYLAPpEYYGIRVD---------LTD-ERAEYDALSERLR 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 587 ELLGID----IDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIA 662
Cdd:COG1061 282 EALAADaerkDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVT 361
                       330
                ....*....|....*..
gi 51338772 663 TAVAERGLDIKGVDHVI 679
Cdd:COG1061 362 VDVLNEGVDVPRLDVAI 378
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
354-506 4.37e-17

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: 81.65  E-value: 4.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 354 KNVAHAGYSKT------TPIQQYALPLVHQGYDI----------------MACAQTGSGKTAAFLLPIM---------TR 402
Cdd:cd17965  15 IKEILKGSNKTdeeikpSPIQTLAIKKLLKTLMRkvtkqtsneepklevfLLAAETGSGKTLAYLAPLLdylkrqeqePF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 403 LIDDNNLNTAGEGGcYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQ--IEKGATIIVGTVGRIK 480
Cdd:cd17965  95 EEAEEEYESAKDTG-RPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQlaFKGRIDILVTTPGKLA 173
                       170       180
                ....*....|....*....|....*.
gi 51338772 481 HFCEEGTIKLDKCRFFVLDEADRMID 506
Cdd:cd17965 174 SLAKSRPKILSRVTHLVVDEADTLFD 199
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
578-703 1.37e-16

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: 77.25  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 578 RSEKKDKLLELLgidIDSYTTEKSAevytkKTMVFVSQRAMADTLASILSSAQV------PAITI-HGAR--------EQ 642
Cdd:cd18802   5 VIPKLQKLIEIL---REYFPKTPDF-----RGIIFVERRATAVVLSRLLKEHPStlafirCGFLIgRGNSsqrkrslmTQ 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51338772 643 RERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRtGRVGNS 703
Cdd:cd18802  77 RKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPNS 136
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
581-705 8.17e-15

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: 72.00  E-value: 8.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 581 KKDKLLELLgIDIDsyttEKSAEVYTKKTMVFVSQRAMADTLASILSS--AQVPAITIHG--------AREQRERSEALR 650
Cdd:cd18801  10 KLEKLEEIV-KEHF----KKKQEGSDTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGqasgksskGMSQKEQKEVIE 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 651 QFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRvGNSGR 705
Cdd:cd18801  85 QFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGR 138
PRK13766 PRK13766
Hef nuclease; Provisional
581-713 1.46e-14

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 77.61  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  581 KKDKLLEL----LGIDIDSytteksaevytkKTMVFVSQRAMADTLASILSSAQVPAITIHG--ARE------QRERSEA 648
Cdd:PRK13766 348 KLEKLREIvkeqLGKNPDS------------RIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGqaSKDgdkgmsQKEQIEI 415
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51338772  649 LRQFRNGSKPVLIATAVAERGLDIKGVDHVINYD-MPDNIdDYIHRIGRTGRvGNSGRATSFISED 713
Cdd:PRK13766 416 LDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGR-QEEGRVVVLIAKG 479
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
371-704 1.38e-13

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: 74.49  E-value: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 371 ALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcyPRCIILTPTRELA-DQiYNEGRKFAYQTMMEI 449
Cdd:COG1205  64 AIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG----------ATALYLYPTKALArDQ-LRRLRELAEALGLGV 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 450 KP-VYGGLAVGYNKGQIEKGATIIVGT-----VG------RIKHFceegtikLDKCRFFVLDEA---------------D 502
Cdd:COG1205 133 RVaTYDGDTPPEERRWIREHPDIVLTNpdmlhYGllphhtRWARF-------FRNLRYVVIDEAhtyrgvfgshvanvlR 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 503 RMIDAMGFgtdietivnYDSMPrkenrQTLMFSATFPDSVQEAARAFLREnyvMIAIDKIGAA---------NKCVLQEF 573
Cdd:COG1205 206 RLRRICRH---------YGSDP-----QFILASATIGNPAEHAERLTGRP---VTVVDEDGSPrgertfvlwNPPLVDDG 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 574 ERceRS---EKKDKLLELLGIDIdsytteksaevytkKTMVFVSQRAMADTLASILSSA-----QVPAITIH-GAREQRE 644
Cdd:COG1205 269 IR--RSalaEAARLLADLVREGL--------------RTLVFTRSRRGAELLARYARRAlrepdLADRVAAYrAGYLPEE 332
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 645 RSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSG 704
Cdd:COG1205 333 RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDS 392
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
156-282 3.07e-13

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 68.72  E-value: 3.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 156 RNNNCFNCQQPGHRSSDCPEprkerepRVCYNCQQPGHTSRECTEerkpregrtggfgggagfgnnggndgfggdggfgg 235
Cdd:COG5082  59 ENPVCFNCGQNGHLRRDCPH-------SICYNCSWDGHRSNHCPK----------------------------------- 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 51338772 236 geergPMKCFNCKGEGHRSAECPEPPRG---CFNCGEQGHRSNECPNPAK 282
Cdd:COG5082  97 -----PKKCYNCGETGHLSRDCNPSKDQqksCFDCNSTRHSSEDCPSIWK 141
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
160-284 6.91e-13

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 67.95  E-value: 6.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 160 CFNCQQPGHRSSDCPEPRKereprvCYNCQQPGHTSRECTEERkpregrtggfgggagfgnnggndgfggdggfgggeeR 239
Cdd:COG5082  81 CYNCSWDGHRSNHCPKPKK------CYNCGETGHLSRDCNPSK------------------------------------D 118
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51338772 240 GPMKCFNCKGEGHRSAECPEPPRG--------------CFNCGEQGHRSNECPNPAKPR 284
Cdd:COG5082 119 QQKSCFDCNSTRHSSEDCPSIWKHyvlnngdghpikkfCYSCGSAGHFGDDCKEPRSSR 177
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
569-700 8.56e-13

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 71.79  E-value: 8.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 569 VLQEFER-CERSEKKDKLLELLgididsytTEKSAEvyTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSE 647
Cdd:COG0553 521 LLEEGAElSGRSAKLEALLELL--------EELLAE--GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDE 590
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51338772 648 ALRQFRNGSKP--VLIAT-AVAErGLDIKGVDHVINYDMPDNID------DYIHRIGRTGRV 700
Cdd:COG0553 591 LVDRFQEGPEApvFLISLkAGGE-GLNLTAADHVIHYDLWWNPAveeqaiDRAHRIGQTRDV 651
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
160-201 5.23e-12

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 64.06  E-value: 5.23e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 51338772  160 CFNCQQPGHRSSDCPEPRKE-REPRVCYNCQQPGHTSRECTEE 201
Cdd:PTZ00368 106 CYNCGGEGHISRDCPNAGKRpGGDKTCYNCGQTGHLSRDCPDK 148
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
606-695 1.12e-11

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: 62.88  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 606 TKKTMVFvSQ-RAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKP--VLIATAVAERGLDIKGVDHVINYD 682
Cdd:cd18793  27 GEKVLIF-SQfTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAANRVILYD 105
                        90
                ....*....|....*....
gi 51338772 683 MPDN--ID----DYIHRIG 695
Cdd:cd18793 106 PWWNpaVEeqaiDRAHRIG 124
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
607-699 6.96e-11

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: 61.13  E-value: 6.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 607 KKTMVFVSQRAMADTLASIL---SSAQVPAITI---HG--AREQRERSEAlrQFRNGSKPVLIATAVAERGLDIKGVDHV 678
Cdd:cd18796  39 KSTLVFTNTRSQAERLAQRLrelCPDRVPPDFIalhHGslSRELREEVEA--ALKRGDLKVVVATSSLELGIDIGDVDLV 116
                        90       100
                ....*....|....*....|.
gi 51338772 679 INYDMPDNIDDYIHRIGRTGR 699
Cdd:cd18796 117 IQIGSPKSVARLLQRLGRSGH 137
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
572-713 1.65e-10

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 64.01  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 572 EFERCERSEKKDKLLELL-------GIdidsytteksaeVYTkktmvfvSQRAMADTLASILSSAQVPAITIHGAREQRE 644
Cdd:COG0514 208 EVVPKPPDDKLAQLLDFLkehpggsGI------------VYC-------LSRKKVEELAEWLREAGIRAAAYHAGLDAEE 268
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51338772 645 RSEALRQFRNGSKPVLIATaVAeRGLdikGVDH-----VINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISED 713
Cdd:COG0514 269 REANQDRFLRDEVDVIVAT-IA-FGM---GIDKpdvrfVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
608-699 3.15e-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: 56.94  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 608 KTMVFVSQRAMADTLASILSsaqvpaitihgareqrersealrqfrngskpVLIATAVAERGLDIKGVDHVINYDMPDNI 687
Cdd:cd18785   5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
                        90
                ....*....|..
gi 51338772 688 DDYIHRIGRTGR 699
Cdd:cd18785  54 ASYIQRVGRAGR 65
PRK13767 PRK13767
ATP-dependent helicase; Provisional
361-435 8.87e-09

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 59.13  E-value: 8.87e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51338772  361 YSKTTPIQQYALPLVHQGYDIMACAQTGSGKT-AAFLLPI--MTRLIDDNNLntagEGGCYprCIILTPTRELADQIY 435
Cdd:PRK13767  30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIdeLFRLGREGEL----EDKVY--CLYVSPLRALNNDIH 101
AIR1 COG5082
Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational ...
176-285 1.15e-08

Arginine methyltransferase-interacting protein, contains RING Zn-finger [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion];


Pssm-ID: 227414 [Multi-domain]  Cd Length: 190  Bit Score: 55.63  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 176 PRKEREPRVCYNCQQPGHTSRECTEErkpregrtggfgggagfgnnggndgfggdggfgggeergpmKCFNCKGEGHRSA 255
Cdd:COG5082  54 SAIREENPVCFNCGQNGHLRRDCPHS-----------------------------------------ICYNCSWDGHRSN 92
                        90       100       110
                ....*....|....*....|....*....|.
gi 51338772 256 ECPEPpRGCFNCGEQGHRSNEC-PNPAKPRE 285
Cdd:COG5082  93 HCPKP-KKCYNCGETGHLSRDCnPSKDQQKS 122
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
609-701 1.33e-08

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: 54.14  E-value: 1.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 609 TMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNID 688
Cdd:cd18794  33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
                        90
                ....*....|...
gi 51338772 689 DYIHRIGRTGRVG 701
Cdd:cd18794 113 SYYQESGRAGRDG 125
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
378-537 5.06e-08

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: 52.79  E-value: 5.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 378 GYDIMACAQTGSGKTAAFLLPImtrlidDNNLNTAGeggcyPRCIILTPTRELADQIYNEGRKFaYQTMMEIKPVYGGLA 457
Cdd:cd00046   1 GENVLITAPTGSGKTLAALLAA------LLLLLKKG-----KKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 458 VGYNKGQIEKGATIIVGTVGRIKHFCE-EGTIKLDKCRFFVLDEADRMIDAmGFGTDIETIVNYDSMpRKENRQTLMfSA 536
Cdd:cd00046  69 AEEREKNKLGDADIIIATPDMLLNLLLrEDRLFLKDLKLIIVDEAHALLID-SRGALILDLAVRKAG-LKNAQVILL-SA 145

                .
gi 51338772 537 T 537
Cdd:cd00046 146 T 146
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
608-703 4.63e-07

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 49.95  E-value: 4.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 608 KTMVFVSQRAMADTLA----SILSSAQVPAITIHGAR-----EQRERSEalRQFRNGSKPVLIATAVAERGLDIKGVDHV 678
Cdd:cd18797  37 KTIVFCRSRKLAELLLrylkARLVEEGPLASKVASYRagylaEDRREIE--AELFNGELLGVVATNALELGIDIGGLDAV 114
                        90       100
                ....*....|....*....|....*
gi 51338772 679 INYDMPDNIDDYIHRIGRTGRVGNS 703
Cdd:cd18797 115 VLAGYPGSLASLWQQAGRAGRRGKD 139
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
385-672 5.85e-07

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 52.78  E-value: 5.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 385 AQTGSGKT-AAFLlpIMTRLIDDNNLntageggcyPRCIILTPTRELADQIYNEGRKFAYQTMMEIkpvyGGLAVGYNKG 463
Cdd:COG1203 154 APTGGGKTeAALL--FALRLAAKHGG---------RRIIYALPFTSIINQTYDRLRDLFGEDVLLH----HSLADLDLLE 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 464 QIEKGAT---------------IIVGTV--------GRIKHFCeegtikldkCRFF-------VLDEAD----------- 502
Cdd:COG1203 219 EEEEYESearwlkllkelwdapVVVTTIdqlfeslfSNRKGQE---------RRLHnlansviILDEVQayppymlalll 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 503 RMIDAMG-FGTdieTIVnydsmprkenrqtLMfSATFPDsvqeAARAFLRENYVMIAIDKIGAANKCVLQEFERCERSEK 581
Cdd:COG1203 290 RLLEWLKnLGG---SVI-------------LM-TATLPP----LLREELLEAYELIPDEPEELPEYFRAFVRKRVELKEG 348
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 582 KDKLLELLGIDIDSYTTEKSA--EVYTKKTMvfvsqRAMADTLASILssAQVPAITIHGA-----REQRERsEALRQFRN 654
Cdd:COG1203 349 PLSDEELAELILEALHKGKSVlvIVNTVKDA-----QELYEALKEKL--PDEEVYLLHSRfcpadRSEIEK-EIKERLER 420
                       330
                ....*....|....*...
gi 51338772 655 GSKPVLIATAVAERGLDI 672
Cdd:COG1203 421 GKPCILVSTQVVEAGVDI 438
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
380-537 1.18e-06

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: 49.34  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 380 DIMACAQTGSGKTAAFLLPIMtrLIDDNNLNTAgeggcyprciILTPTRELADQIYNEGRKFAYQtmMEIKPVYGGlavg 459
Cdd:cd17918  38 DRLLSGDVGSGKTLVALGAAL--LAYKNGKQVA----------ILVPTEILAHQHYEEARKFLPF--INVELVTGG---- 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51338772 460 yNKGQIEKGATIIVGTVGRIkhFCEEGTIKLDkcrFFVLDEADRmidamgFGTdietiVNYDSMPRKENRQTLMFSAT 537
Cdd:cd17918 100 -TKAQILSGISLLVGTHALL--HLDVKFKNLD---LVIVDEQHR------FGV-----AQREALYNLGATHFLEATAT 160
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
385-701 1.50e-06

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


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 50.89  E-value: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 385 AQTGSGKTAAFLLpIMTRLIDDNNLNtageggcypRCIILTPTRELADQIYNEGR-------------KFAYQTMMEIKP 451
Cdd:cd09639   6 APTGYGKTEAALL-WALHSLKSQKAD---------RVIIALPTRATINAMYRRAKeafgetglyhssiLSSRIKEMGDSE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 452 VYGGLAVGYNKGQIEKGATIIvgTVGRIKHFCEEGTiKLDKCRFF----------VLDEADRMID-AMGFgtdIETIVny 520
Cdd:cd09639  76 EFEHLFPLYIHSNDTLFLDPI--TVCTIDQVLKSVF-GEFGHYEFtlasiansllIFDEVHFYDEyTLAL---ILAVL-- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 521 dsMPRKENRQTLM-FSATFPDsvqeaaraFLRENY--VMIAIDKIGAANKCVLQEFERCERSEKKDKLLELLGIdIDSYT 597
Cdd:cd09639 148 --EVLKDNDVPILlMSATLPK--------FLKEYAekIGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERL-LEFIK 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 598 TEKSAEVY--TKKTMVFVSQRAMADtlasilsSAQVPAITIHG--AREQRERSEA--LRQFRNGSKPVLIATAVAERGLD 671
Cdd:cd09639 217 KGGSVAIIvnTVDRAQEFYQQLKEK-------GPEEEIMLIHSrfTEKDRAKKEAelLLEFKKSEKFVIVATQVIEASLD 289
                       330       340       350
                ....*....|....*....|....*....|
gi 51338772 672 IKgVDHVINYDMPdnIDDYIHRIGRTGRVG 701
Cdd:cd09639 290 IS-VDVMITELAP--IDSLIQRLGRLHRYG 316
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
368-433 1.57e-06

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 49.12  E-value: 1.57e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51338772 368 QQY-ALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcyPRCIILTPTRELA-DQ 433
Cdd:cd17923   4 HQAeAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPG----------SRALYLYPTKALAqDQ 61
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
365-431 2.14e-06

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 51.26  E-value: 2.14e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51338772 365 TPIQQYALPLVHQGYDIMACAQTGSGKT-AAFlLPIMTRLIDDNNLNTAGEGgcyPRCIILTPTRELA 431
Cdd:COG1201  26 TPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDG---LRVLYISPLKALA 89
ResIII pfam04851
Type III restriction enzyme, res subunit;
376-540 2.49e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.05  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   376 HQGYDIMAcaqTGSGKTAafllpIMTRLIDdnNLNTAGEggcYPRCIILTPTRELADQIYNEGRKFAyqtmmEIKPVYGG 455
Cdd:pfam04851  24 KRGLIVMA---TGSGKTL-----TAAKLIA--RLFKKGP---IKKVLFLVPRKDLLEQALEEFKKFL-----PNYVEIGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772   456 LAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVL--DEADRMIDAMgfgtdIETIVNYDSMPRKenrqtLM 533
Cdd:pfam04851  86 IISGDKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHRSGASS-----YRNILEYFKPAFL-----LG 155

                  ....*..
gi 51338772   534 FSATFPD 540
Cdd:pfam04851 156 LTATPER 162
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
365-551 2.50e-06

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: 48.41  E-value: 2.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 365 TPIQQYAL-PLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNlntageggcypRCIILTPTRELADQIYNEGRKFAY 443
Cdd:cd17921   3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGG-----------KAVYIAPTRALVNQKEADLRERFG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 444 QTMMEIKPVYGGlaVGYNKGQIEKgATIIVGTvgrIKHF----CEEGTIKLDKCRFFVLDEADRMIDAMGfGTDIETIVN 519
Cdd:cd17921  72 PLGKNVGLLTGD--PSVNKLLLAE-ADILVAT---PEKLdlllRNGGERLIQDVRLVVVDEAHLIGDGER-GVVLELLLS 144
                       170       180       190
                ....*....|....*....|....*....|...
gi 51338772 520 YdsMPRKE-NRQTLMFSATFPDsvqeaARAFLR 551
Cdd:cd17921 145 R--LLRINkNARFVGLSATLPN-----AEDLAE 170
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
376-538 2.65e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 44.60  E-value: 2.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 376 HQGYDIMAcaqTGSGKTAafllpIMTRLIddnnlntageggCY---PRCIILTPTRELADQIYNEGRKFAYQTMMeikpv 452
Cdd:cd17926  19 RRGILVLP---TGSGKTL-----TALALI------------AYlkeLRTLIVVPTDALLDQWKERFEDFLGDSSI----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 453 yGGLAVGYNKGQIekGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRmIDAMGFGtdiETIVNYDSMPRkenrqtL 532
Cdd:cd17926  74 -GLIGGGKKKDFD--DANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHH-LPAKTFS---EILKELNAKYR------L 140

                ....*.
gi 51338772 533 MFSATF 538
Cdd:cd17926 141 GLTATP 146
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
603-679 3.68e-05

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 43.70  E-value: 3.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 603 EVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERS-EALRQFRNGSKPVLIATAV---AErGLDIKGVDHV 678
Cdd:cd18799   3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELKPPILVTVdllTT-GVDIPEVDNV 81

                .
gi 51338772 679 I 679
Cdd:cd18799  82 V 82
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
570-699 5.55e-05

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


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 44.08  E-value: 5.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 570 LQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKK--TMVFVSQRAMADTLASILSsaqvpAITIHGA---REQRE 644
Cdd:cd18795   5 LEEYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGkpVLVFCSSRKECEKTAKDLA-----GIAFHHAgltREDRE 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51338772 645 RSEALrqFRNGSKPVLIATAVAERGLD-------IKGVDHVINYDMPD-NIDDYIHRIGRTGR 699
Cdd:cd18795  80 LVEEL--FREGLIKVLVATSTLAAGVNlpartviIKGTQRYDGKGYRElSPLEYLQMIGRAGR 140
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
183-200 4.04e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.89  E-value: 4.04e-04
                          10
                  ....*....|....*...
gi 51338772   183 RVCYNCQQPGHTSRECTE 200
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
158-175 5.81e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.51  E-value: 5.81e-04
                          10
                  ....*....|....*...
gi 51338772   158 NNCFNCQQPGHRSSDCPE 175
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
608-672 6.53e-04

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


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 40.70  E-value: 6.53e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51338772 608 KTMVFVSQRAMADTLASILssaQVPAITihGAREQRERSEALRQFRNGSKPVLIATAVAERGLDI 672
Cdd:cd18789  51 KIIVFTDNVEALYRYAKRL---LKPFIT--GETPQSEREEILQNFREGEYNTLVVSKVGDEGIDL 110
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
262-279 7.20e-04

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 37.51  E-value: 7.20e-04
                          10
                  ....*....|....*...
gi 51338772   262 RGCFNCGEQGHRSNECPN 279
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
378-436 7.23e-04

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: 41.03  E-value: 7.23e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51338772 378 GYDIMACAQTGSGKTAAFLLPIMTRLIDDNnlntaGEGGcypRCIILTPTRELADQIYN 436
Cdd:cd17922   1 GRNVLIAAPTGSGKTEAAFLPALSSLADEP-----EKGV---QVLYISPLKALINDQER 51
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
378-539 8.03e-04

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


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 41.17  E-value: 8.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 378 GYDIMACAQTGSGKTaafLLPIMTRliddnnLNTAGEGGcypRCIILTPTRELADQIYNEgrkFAYQTMMEIKPvygGLA 457
Cdd:cd18028  17 GENLLISIPTASGKT---LIAEMAM------VNTLLEGG---KALYLVPLRALASEKYEE---FKKLEEIGLKV---GIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 458 VG-YN-KGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEAdRMIDAMGFGTDIETIVNYDSMPRKeNRQTLMFS 535
Cdd:cd18028  79 TGdYDeDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEI-HLISDEERGPTLESIVARLRRLNP-NTQIIGLS 156

                ....
gi 51338772 536 ATFP 539
Cdd:cd18028 157 ATIG 160
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
367-441 8.34e-04

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: 41.57  E-value: 8.34e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51338772 367 IQQYALP-LVHQGYDIMACAQTGSGKTAAFLLPiMTRLIDDNNLNTAGEggcyPRCIILTPTRELADQIYNEGR-KF 441
Cdd:cd18023   5 IQSEVFPdLLYSDKNFVVSAPTGSGKTVLFELA-ILRLLKERNPLPWGN----RKVVYIAPIKALCSEKYDDWKeKF 76
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
380-501 1.04e-03

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: 41.10  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772 380 DIMACAQTGSGKTaafLLPIM--TRLIDDNNLNTAGEggcyPRCIILTPTRELADQIYNEGRKfayQTMMEIKPVYGGLA 457
Cdd:cd18034  18 NTIVVLPTGSGKT---LIAVMliKEMGELNRKEKNPK----KRAVFLVPTVPLVAQQAEAIRS---HTDLKVGEYSGEMG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 51338772 458 VGYNKGQIEKGA----TIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEA 501
Cdd:cd18034  88 VDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
secA PRK12898
preprotein translocase subunit SecA; Reviewed
611-722 2.23e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237253 [Multi-domain]  Cd Length: 656  Bit Score: 41.53  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  611 VFVSQRAMADT--LASILSSAQVPAITIHGAREQRER---SEALRQFRngskpVLIATAVAERGLDIK--------GVDH 677
Cdd:PRK12898 476 VLVGTRSVAASerLSALLREAGLPHQVLNAKQDAEEAaivARAGQRGR-----ITVATNMAGRGTDIKlepgvaarGGLH 550
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 51338772  678 VINYDMPDN--IDDYIhrIGRTGRVGNSGRATSFISEDCSLLSELVG 722
Cdd:PRK12898 551 VILTERHDSarIDRQL--AGRCGRQGDPGSYEAILSLEDDLLQSFLG 595
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
607-701 3.00e-03

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 40.85  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51338772  607 KKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDN 686
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRN 316
                         90
                 ....*....|....*
gi 51338772  687 IDDYIHRIGRTGRVG 701
Cdd:PRK11057 317 IESYYQETGRAGRDG 331
ZnF_C2HC smart00343
zinc finger;
263-279 3.05e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 3.05e-03
                           10
                   ....*....|....*..
gi 51338772    263 GCFNCGEQGHRSNECPN 279
Cdd:smart00343   1 KCYNCGKEGHIARDCPS 17
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
610-676 3.24e-03

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


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 40.63  E-value: 3.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51338772 610 MVFVSQRAMADTLASILSsAQVPAITIHG--ArEQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVD 676
Cdd:COG4098 323 LIFVPTIELLEQLVALLQ-KLFPEERIAGvhA-EDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
ZnF_C2HC smart00343
zinc finger;
243-259 4.05e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.11  E-value: 4.05e-03
                           10
                   ....*....|....*..
gi 51338772    243 KCFNCKGEGHRSAECPE 259
Cdd:smart00343   1 KCYNCGKEGHIARDCPS 17
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
242-259 5.11e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 34.81  E-value: 5.11e-03
                          10
                  ....*....|....*...
gi 51338772   242 MKCFNCKGEGHRSAECPE 259
Cdd:pfam00098   1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
160-175 5.43e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 34.73  E-value: 5.43e-03
                           10
                   ....*....|....*.
gi 51338772    160 CFNCQQPGHRSSDCPE 175
Cdd:smart00343   2 CYNCGKEGHIARDCPS 17
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
381-442 7.34e-03

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


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 38.43  E-value: 7.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51338772 381 IMACAQTGSGKTAAFLLPImtrliddnnLNTAGEGGCyPRCIILTPTRELADQIYNEGRKFA 442
Cdd:cd17930   4 VILEAPTGSGKTEAALLWA---------LKLAARGGK-RRIIYALPTRATINQMYERIREIL 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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