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Conserved domains on  [gi|326886207|gb|AEA08750|]
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Moloney leukemia virus 10-like 1 [Mus musculus]

Protein Classification

DEXXQc_Mov10L1 and SF1_C_Upf1 domain-containing protein( domain architecture ID 13030947)

DEXXQc_Mov10L1 and SF1_C_Upf1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 798-1027 7.70e-157

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 468.00  E-value: 7.70e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  798 VLNENQKLAVRRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESKVPKPAA 877
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  878 MVRVNATCRFEETIIDAIKPYCRDGEDIWRASRFRIIITTCSSAGLFYQIGVRVGYFTHVFVDEAGQASEPECLIPLGLI 957
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  958 SDINGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMSRPAYLRDENAFGACGAYNPLLVTKLVKNYR 1027
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 1028-1218 2.87e-58

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 198.61  E-value: 2.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1028 SHSALLALPSRLFYHRELEVCADPKvvtSLLGWEKLPRKGFPLIFHGVRGNEAREGRSPSWFSPAEAVQVMRYCCLLars 1107
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVA---ARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1108 VSSQVSSKDIGVITPYRKQVEKIKILLRNV--DLTDIKVGSVEEFQGQEYLVIVISTVRSNEDRFEddryfLGFLSNSKR 1185
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 326886207 1186 FNVAITRPKALLIILGNPHVLVRDPCFGALLEY 1218
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
 
Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 798-1027 7.70e-157

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 468.00  E-value: 7.70e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  798 VLNENQKLAVRRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESKVPKPAA 877
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  878 MVRVNATCRFEETIIDAIKPYCRDGEDIWRASRFRIIITTCSSAGLFYQIGVRVGYFTHVFVDEAGQASEPECLIPLGLI 957
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  958 SDINGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMSRPAYLRDENAFGACGAYNPLLVTKLVKNYR 1027
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 1028-1218 2.87e-58

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 198.61  E-value: 2.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1028 SHSALLALPSRLFYHRELEVCADPKvvtSLLGWEKLPRKGFPLIFHGVRGNEAREGRSPSWFSPAEAVQVMRYCCLLars 1107
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVA---ARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1108 VSSQVSSKDIGVITPYRKQVEKIKILLRNV--DLTDIKVGSVEEFQGQEYLVIVISTVRSNEDRFEddryfLGFLSNSKR 1185
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 326886207 1186 FNVAITRPKALLIILGNPHVLVRDPCFGALLEY 1218
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
880-1218 4.29e-57

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 213.45  E-value: 4.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  880 RVNATCRFEETIIDAIKPYCRDGEDIWRA--SRFRIIITTCSSAGLFyqIGVRVGYFTHVFVDEAGQASEPECLIPLGLi 957
Cdd:COG1112   502 ELREAARLRRALRRELKKRRELRKLLWDAllELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR- 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  958 sdiNGQIVLAGDPMQLGPVIKSRLAMA---YGLNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNYRSHSALLA 1034
Cdd:COG1112   579 ---AKRVVLVGDPKQLPPVVFGEEAEEvaeEGLDESLLDRLLAR----------------LPERGVMLREHYRMHPEIIA 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1035 LPSRLFYHRELEVCADPKVvtsllgwEKLPRKGFPLIFHGVRGNEAREGRspSWFSPAEAVQVMRyccLLARSVSSQVSS 1114
Cdd:COG1112   640 FSNRLFYDGKLVPLPSPKA-------RRLADPDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDG 707

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1115 KDIGVITPYRKQVEKIKILLRN---VDLTDIKVGSVEEFQGQEYLVIVISTVRSNEdrfEDDRYFLGFLSNS-KRFNVAI 1190
Cdd:COG1112   708 ESIGVITPYRAQVALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGFLNGGpRRLNVAV 784

                         330       340       350
                  ....*....|....*....|....*....|.
gi 326886207 1191 TRPKALLIILGNPHVLVRDP---CFGALLEY 1218
Cdd:COG1112   785 SRARRKLIVVGSRELLDSDPstpALKRLLEY 815
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 987-1203 1.55e-52

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 182.75  E-value: 1.55e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   987 LNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNYRSHSALLALPSRLFYHRELEvCADPKVVTSLLGWEKLPRK 1066
Cdd:pfam13087    1 LDRSLFERLQEL----------------GPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1067 GFPLIFHGV-RGNEAREGRSPSWFSPAEAVQVMRYC-CLLARSVssqVSSKDIGVITPYRKQVEKIKILLRN--VDLTDI 1142
Cdd:pfam13087   64 LGPLVFIDVdGSEEEESDGGTSYSNEAEAELVVQLVeKLIKSGP---EEPSDIGVITPYRAQVRLIRKLLKRklGGKLEI 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326886207  1143 KVGSVEEFQGQEYLVIVISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIILGNP 1203
Cdd:pfam13087  141 EVNTVDGFQGREKDVIIFSCVRSNEKG------GIGFLSDPRRLNVALTRAKRGLIIVGNA 195
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 786-1225 1.84e-52

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 196.19  E-value: 1.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   786 IPKARDKEFFNPVLNENQKLAVRRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhyALPDSRILVCAPSNSAADLVCL 865
Cdd:TIGR00376  145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDNLLE 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   866 RLheskVPKPAAMVRVNATCRFEETI------------------------IDAI----------KPYCRDG---EDIWR- 907
Cdd:TIGR00376  220 RL----ALCDQKIVRLGHPARLLKSNkqhsldylienhpkyqivadirekIDELieernkktkpSPQKRRGlsdIKILRk 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   908 ---------------ASRFRIIITTCSSAGLF---YQIGVRVG----------------------YFTHVFVDEAGQASE 947
Cdd:TIGR00376  296 alkkreargieslkiASMAEWIETNKSIDRLLkllPESEERIMneilaesdatnsmagseilngqYFDVAVIDEASQAME 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   948 PECLIPLglisdINGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNY 1026
Cdd:TIGR00376  376 PSCLIPL-----LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQY 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1027 RSHSALLALPSRLFYHRELEvcADPKVVTSLLgwEKLPRK-----------GFPLIF---HGVRGNEAREGRSPSWFSPA 1092
Cdd:TIGR00376  433 RMNQKIMEFPSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPG 508

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1093 EAVQVMRYCCLLarsVSSQVSSKDIGVITPYRKQVEKIKILLRNvDLTDIKVGSVEEFQGQEYLVIVISTVRSNEDRfed 1172
Cdd:TIGR00376  509 EAELVSEIIQAL---VKMGVPANDIGVITPYDAQVDLLRQLLEH-RHIDIEVSSVDGFQGREKEVIIISFVRSNRKG--- 581

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 326886207  1173 dryFLGFLSNSKRFNVAITRPKALLIILGNPHVLVRDPCFGALLEYSVSNGVY 1225
Cdd:TIGR00376  582 ---EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEV 631
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 803-980 2.39e-24

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 103.58  E-value: 2.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   803 QKLAVRRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHY-----ALPDSRILVCAPSNSAADLVCLRLHESKVPKPAA 877
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   878 MVRVNAtcrfEETIIDAIKPYCRD-------------------------------------------------------- 901
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   902 -----------GEDIWRASRF---------RIIITTCSSAG---LFYQIGVRVgyfthVFVDEAGQASEPECLIPLglis 958
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225

                          250       260
                   ....*....|....*....|....
gi 326886207   959 dING--QIVLAGDPMQLGPVIKSR 980
Cdd:pfam13086  226 -LRGpkKVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 778-976 4.35e-10

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 63.84  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  778 AETMDEIQIPKARDKEF--FNPVLNENQKLAVRRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHYALPDsRILVCAP 855
Cdd:COG0507   102 RPALDEADVEAALAALEprAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  856 SNSAAdlvcLRLHESkvpkpaamVRVNATcrfeeTI---IdaikpYCRDGEDIWRASRFRIIittcSSAGLfyqigvrvg 932
Cdd:COG0507   177 TGKAA----KRLSES--------TGIEAR-----TIhrlL-----GLRPDSGRFRHNRDNPL----TPADL--------- 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 326886207  933 yfthVFVDEAGQASEP--ECLipLGLISDINGQIVLAGDPMQLGPV 976
Cdd:COG0507   222 ----LVVDEASMVDTRlmAAL--LEALPRAGARLILVGDPDQLPSV 261
DEXDc smart00487
DEAD-like helicases superfamily;
792-942 9.68e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 56.73  E-value: 9.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207    792 KEFFNPVLNENQKLAVRRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESK 871
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLG 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326886207    872 VPKPaamvrVNATCRFEETIIDAIKpycrdgeDIWRASRFRIIITTCSSA-GLFYQIGVRVGYFTHVFVDEA 942
Cdd:smart00487   79 PSLG-----LKVVGLYGGDSKREQL-------RKLESGKTDILVTTPGRLlDLLENDKLSLSNVDLVILDEA 138
 
Name Accession Description Interval E-value
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 798-1027 7.70e-157

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 468.00  E-value: 7.70e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  798 VLNENQKLAVRRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESKVPKPAA 877
Cdd:cd18078     1 DLNELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLHESKVLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  878 MVRVNATCRFEETIIDAIKPYCRDGEDIWRASRFRIIITTCSSAGLFYQIGVRVGYFTHVFVDEAGQASEPECLIPLGLI 957
Cdd:cd18078    81 MVRLNAVNRFESTVIDARKLYCRLGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  958 SDINGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMSRPAYLRDENAFGACGAYNPLLVTKLVKNYR 1027
Cdd:cd18078   161 SSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFGESGGYNPLLVTKLVDNYR 230
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 798-1027 1.66e-116

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 361.55  E-value: 1.66e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  798 VLNENQKLAVRRILSGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHeSKVPKPAA 877
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLL-NALVTKRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  878 MVRVNATCRFEETIIDAIKPYCRDGED-------IWRASRFRIIITTCSSAGLFYQIGVRVGYFTHVFVDEAGQASEPEC 950
Cdd:cd18038    80 ILRLNAPSRDRASVPPELLPYCNSKAEgtfrlpsLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEPEA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326886207  951 LIPLGLISDINGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMSRPAYLRDenafgacGAYNPLLVTKLVKNYR 1027
Cdd:cd18038   160 LIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD-------GEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 1028-1218 2.87e-58

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 198.61  E-value: 2.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1028 SHSALLALPSRLFYHRELEVCADPKvvtSLLGWEKLPRKGFPLIFHGVRGNEAREGRSPSWFSPAEAVQVMRYCCLLars 1107
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAGVSVA---ARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYL--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1108 VSSQVSSKDIGVITPYRKQVEKIKILLRNV--DLTDIKVGSVEEFQGQEYLVIVISTVRSNEDRFEddryfLGFLSNSKR 1185
Cdd:cd18808    75 LKSGVKPSSIGVITPYRAQVALIRELLRKRggLLEDVEVGTVDNFQGREKDVIILSLVRSNESGGS-----IGFLSDPRR 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 326886207 1186 FNVAITRPKALLIILGNPHVLVRDPCFGALLEY 1218
Cdd:cd18808   150 LNVALTRAKRGLIIVGNPDTLSKDPLWKKLLEY 182
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
880-1218 4.29e-57

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 213.45  E-value: 4.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  880 RVNATCRFEETIIDAIKPYCRDGEDIWRA--SRFRIIITTCSSAGLFyqIGVRVGYFTHVFVDEAGQASEPECLIPLGLi 957
Cdd:COG1112   502 ELREAARLRRALRRELKKRRELRKLLWDAllELAPVVGMTPASVARL--LPLGEGSFDLVIIDEASQATLAEALGALAR- 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  958 sdiNGQIVLAGDPMQLGPVIKSRLAMA---YGLNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNYRSHSALLA 1034
Cdd:COG1112   579 ---AKRVVLVGDPKQLPPVVFGEEAEEvaeEGLDESLLDRLLAR----------------LPERGVMLREHYRMHPEIIA 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1035 LPSRLFYHRELEVCADPKVvtsllgwEKLPRKGFPLIFHGVRGNEAREGRspSWFSPAEAVQVMRyccLLARSVSSQVSS 1114
Cdd:COG1112   640 FSNRLFYDGKLVPLPSPKA-------RRLADPDSPLVFIDVDGVYERRGG--SRTNPEEAEAVVE---LVRELLEDGPDG 707

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1115 KDIGVITPYRKQVEKIKILLRN---VDLTDIKVGSVEEFQGQEYLVIVISTVRSNEdrfEDDRYFLGFLSNS-KRFNVAI 1190
Cdd:COG1112   708 ESIGVITPYRAQVALIRELLREalgDGLEPVFVGTVDRFQGDERDVIIFSLVYSND---EDVPRNFGFLNGGpRRLNVAV 784

                         330       340       350
                  ....*....|....*....|....*....|.
gi 326886207 1191 TRPKALLIILGNPHVLVRDP---CFGALLEY 1218
Cdd:COG1112   785 SRARRKLIVVGSRELLDSDPstpALKRLLEY 815
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 987-1203 1.55e-52

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 182.75  E-value: 1.55e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   987 LNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNYRSHSALLALPSRLFYHRELEvCADPKVVTSLLGWEKLPRK 1066
Cdd:pfam13087    1 LDRSLFERLQEL----------------GPSAVVMLDTQYRMHPEIMEFPSKLFYGGKLK-DGPSVAERPLPDDFHLPDP 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1067 GFPLIFHGV-RGNEAREGRSPSWFSPAEAVQVMRYC-CLLARSVssqVSSKDIGVITPYRKQVEKIKILLRN--VDLTDI 1142
Cdd:pfam13087   64 LGPLVFIDVdGSEEEESDGGTSYSNEAEAELVVQLVeKLIKSGP---EEPSDIGVITPYRAQVRLIRKLLKRklGGKLEI 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326886207  1143 KVGSVEEFQGQEYLVIVISTVRSNEDRfeddryFLGFLSNSKRFNVAITRPKALLIILGNP 1203
Cdd:pfam13087  141 EVNTVDGFQGREKDVIIFSCVRSNEKG------GIGFLSDPRRLNVALTRAKRGLIIVGNA 195
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 786-1225 1.84e-52

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 196.19  E-value: 1.84e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   786 IPKARDKEFFNPVLNENQKLAVRRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVhyALPDSRILVCAPSNSAADLVCL 865
Cdd:TIGR00376  145 ASEIHDFQFFDPNLNESQKEAVLFALSSKDL---FLIHGPPGTGKTRTVVELIRQL--VKRGLRVLVTAPSNIAVDNLLE 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   866 RLheskVPKPAAMVRVNATCRFEETI------------------------IDAI----------KPYCRDG---EDIWR- 907
Cdd:TIGR00376  220 RL----ALCDQKIVRLGHPARLLKSNkqhsldylienhpkyqivadirekIDELieernkktkpSPQKRRGlsdIKILRk 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   908 ---------------ASRFRIIITTCSSAGLF---YQIGVRVG----------------------YFTHVFVDEAGQASE 947
Cdd:TIGR00376  296 alkkreargieslkiASMAEWIETNKSIDRLLkllPESEERIMneilaesdatnsmagseilngqYFDVAVIDEASQAME 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   948 PECLIPLglisdINGQ-IVLAGDPMQLGPVIKSRlaMAYGLNVSMLERLMSRpaylrdenafgacgayNPLLVTKLVKNY 1026
Cdd:TIGR00376  376 PSCLIPL-----LKARkLILAGDHKQLPPTILSH--DAEELSLTLFERLIKE----------------YPERSRTLNVQY 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1027 RSHSALLALPSRLFYHRELEvcADPKVVTSLLgwEKLPRK-----------GFPLIF---HGVRGNEAREGRSPSWFSPA 1092
Cdd:TIGR00376  433 RMNQKIMEFPSREFYNGKLT--AHESVANILL--RDLPKVeateseddletGIPLLFidtSGCELFELKEADSTSKYNPG 508

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  1093 EAVQVMRYCCLLarsVSSQVSSKDIGVITPYRKQVEKIKILLRNvDLTDIKVGSVEEFQGQEYLVIVISTVRSNEDRfed 1172
Cdd:TIGR00376  509 EAELVSEIIQAL---VKMGVPANDIGVITPYDAQVDLLRQLLEH-RHIDIEVSSVDGFQGREKEVIIISFVRSNRKG--- 581

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 326886207  1173 dryFLGFLSNSKRFNVAITRPKALLIILGNPHVLVRDPCFGALLEYSVSNGVY 1225
Cdd:TIGR00376  582 ---EVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWCKQHGEV 631
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 799-1003 8.12e-40

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 147.78  E-value: 8.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSgdcRPLPYILfGPPGTGKTVTIIEAVLQVHYALPdSRILVCAPSNSAADLVCLRLHES--KVpkpa 876
Cdd:cd18039     2 LNHSQVDAVKTALQ---RPLSLIQ-GPPGTGKTVTSATIVYHLVKQGN-GPVLVCAPSNVAVDQLTEKIHQTglKV---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  877 amVRVNATCRfeETIIDAIKPYC---------------------RDGEDIWRAS--RFR---------------IIITTC 918
Cdd:cd18039    73 --VRLCAKSR--EAVESPVSFLAlhnqvrnldsaeklellkllkLETGELSSADekRYRklkrkaerellrnadVICCTC 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  919 SSAGlfyqiGVRVG--YFTHVFVDEAGQASEPECLIPLglisdING--QIVLAGDPMQLGPVIKSRLAMAYGLNVSMLER 994
Cdd:cd18039   149 VGAG-----DPRLSkmKFRTVLIDEATQATEPECLIPL-----VHGakQVILVGDHCQLGPVVMCKKAAKAGLSQSLFER 218

                         250
                  ....*....|..
gi 326886207  995 LMS---RPAYLR 1003
Cdd:cd18039   219 LVQlgiRPIRLQ 230
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 799-1027 2.97e-38

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 141.59  E-value: 2.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSGdcRPLpYILFGPPGTGKTVTIIEAVLQVhyALPDSRILVCAPSNSAADLVCLRLHESKVPkpaaM 878
Cdd:cd18044     2 LNDSQKEAVKFALSQ--KDV-ALIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNLVERLVALKVK----V 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  879 VRVNATCRfeetIIDAIKPYCRDgediwRASRFRIIITTCSSAGLFyqiGVRVG-YFTHVFVDEAGQASEPECLIPLgli 957
Cdd:cd18044    73 VRIGHPAR----LLESVLDHSLD-----ALVAAQVVLATNTGAGSR---QLLPNeLFDVVVIDEAAQALEASCWIPL--- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326886207  958 sdING-QIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMSRpaylrdenafgacgaYNPLLVTKLVKNYR 1027
Cdd:cd18044   138 --LKArRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNL---------------YGESVVRMLTVQYR 191
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 799-995 3.92e-35

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 134.15  E-value: 3.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSGDCRPLPYILF-GPPGTGKTVTIIEAVLQVhYALPDSRILVCAPSNSAADLVC---LRLHESKVPK 874
Cdd:cd18077     2 LNAKQKEAVLAITTPLSIQLPPVLLiGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADLYIkeyLHPYVETGNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  875 PAAMVRVNATCRFEETIIDAIKPYC---RDG-------EDIWRAsrfRIIITTCSSAGLFYQIGVRVGYFTHVFVDEAGQ 944
Cdd:cd18077    81 RARPLRVYYRNRWVKTVHPVVQKYClidEHGtfrmptrEDVMRH---RVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQ 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 326886207  945 ASEPECLIPLGLISDiNGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERL 995
Cdd:cd18077   158 AMECEAIMPLALATK-STRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 799-997 1.10e-28

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 115.00  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSGDcrplPYI--LFGPPGTGKTVTIIEAVLQVHYALPDS-----------------------RILVC 853
Cdd:cd18042     1 LNESQLEAIASALQNS----PGItlIQGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  854 APSNSAADLVCLRLHESKVPKPAA------MVRVnATCRFEETIIDaikpycrdgediwRAsrfRIIITTCSSAG--LFY 925
Cdd:cd18042    77 APSNAAVDEIVLRLLSEGFLDGDGrsykpnVVRV-GRQELRASILN-------------EA---DIVCTTLSSSGsdLLE 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326886207  926 QIGVRvgyFTHVFVDEAGQASEPECLIPLGLISdinGQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERLMS 997
Cdd:cd18042   140 SLPRG---FDTVIIDEAAQAVELSTLIPLRLGC---KRLILVGDPKQLPATVFSKVAQKLGYDRSLFERLQL 205
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 799-995 3.29e-27

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 110.40  E-value: 3.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSgdCRPLPYILfGPPGTGKTVTIIEAVlQVHYALPDSrILVCAPSNSAADLVCLRLHESKVPkpaaM 878
Cdd:cd18041     2 LNKDQRQAIKKVLN--AKDYALIL-GMPGTGKTTTIAALV-RILVALGKS-VLLTSYTHSAVDNILLKLKKFGVN----F 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  879 VRVNATCR----FEETIIDAIKPYCRDGEDIWRA-SRFRIIITTCSSaglFYQIGVRVGYFTHVFVDEAGQASEPECLIP 953
Cdd:cd18041    73 LRLGRLKKihpdVQEFTLEAILKSCKSVEELESKyESVSVVATTCLG---INHPIFRRRTFDYCIVDEASQITLPICLGP 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 326886207  954 LGLISdingQIVLAGDPMQLGPVIKSRLAMAYGLNVSMLERL 995
Cdd:cd18041   150 LRLAK----KFVLVGDHYQLPPLVKSREARELGMDESLFKRL 187
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 798-995 1.22e-25

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 106.90  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  798 VLNENQKLAVRRIL---SGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYAlPDSRILVCAPSNSAADLVC---LRLHESK 871
Cdd:cd18076     1 AGNNKQQLAFNFIAgkpSEARFVPPLLIYGPFGTGKTFTLAMAALEVIRE-PGTKVLICTHTNSAADIYIreyFHPYVDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  872 VPKPAAMVRVNATCR-FEETIIDAIK-PYCRDGEDIWRA------SRFRIIITTCSSAglfYQIGVRVGYFTHVFVDEAG 943
Cdd:cd18076    80 GHPEARPLRIKATDRpNAITDPDTITyCCLTKDRQCFRLptrdelDFHNIVITTTAMA---FNLHVLSGFFTHIFIDEAA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 326886207  944 QASEPECLIPLGLISdINGQIVLAGDPMQLGPVIKSrLAMAYGLNVSMLERL 995
Cdd:cd18076   157 QMLECEALIPLSYAG-PKTRVVLAGDHMQMTPKLFS-VADYNRANHTLLNRL 206
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 821-1001 8.82e-25

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 100.39  E-value: 8.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  821 ILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVclrlheskvpkpaamvrvnatcrfeetiidaikpycr 900
Cdd:cd17934     3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVDNV------------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  901 dgediwrasrfriiittcssaglfyqigvrvgyfTHVFVDEAGQASEPECLIPLGLisdiNGQIVLAGDPMQLGPVIKSR 980
Cdd:cd17934    46 ----------------------------------DVVIIDEASQITEPELLIALIR----AKKVVLVGDPKQLPPVVQED 87

                         170       180
                  ....*....|....*....|.
gi 326886207  981 LAMAYGLNVSMLERLMSRPAY 1001
Cdd:cd17934    88 HAALLGLSFILSLLLLFRLLL 108
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 803-980 2.39e-24

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 103.58  E-value: 2.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   803 QKLAVRRILSgdcRPLPYILFGPPGTGKTVTIIEAVLQVHY-----ALPDSRILVCAPSNSAADLVCLRLHESKVPKPAA 877
Cdd:pfam13086    2 QREAIRSALS---SSHFTLIQGPPGTGKTTTIVELIRQLLSypatsAAAGPRILVCAPSNAAVDNILERLLRKGQKYGPK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   878 MVRVNAtcrfEETIIDAIKPYCRD-------------------------------------------------------- 901
Cdd:pfam13086   79 IVRIGH----PAAISEAVLPVSLDylvesklnneedaqivkdiskeleklakalrafekeiivekllksrnkdkskleqe 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   902 -----------GEDIWRASRF---------RIIITTCSSAG---LFYQIGVRVgyfthVFVDEAGQASEPECLIPLglis 958
Cdd:pfam13086  155 rrklrserkelRKELRRREQSlereildeaQIVCSTLSGAGsrlLSSLANFDV-----VIIDEAAQALEPSTLIPL---- 225

                          250       260
                   ....*....|....*....|....
gi 326886207   959 dING--QIVLAGDPMQLGPVIKSR 980
Cdd:pfam13086  226 -LRGpkKVVLVGDPKQLPPTVISK 248
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 799-995 2.41e-20

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 92.59  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILsgdCRPLpYILFGPPGTGKTVTII-----------EAVLQVHYALPDSRILVCAPSNSAADLVC--- 864
Cdd:cd18040     2 LNPSQNHAVRTAL---TKPF-TLIQGPPGTGKTVTGVhiaywfakqnrEIQSVSGEGDGGPCVLYCGPSNKSVDVVAell 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  865 --------LRLH-----ESKVPKPAAMVRVN-------------------------------ATCRFEETIIDAIKPYCR 900
Cdd:cd18040    78 lkvpglkiLRVYseqieTTEYPIPNEPRHPNkksereskpnselssitlhhrirqpsnphsqQIKAFEARFERTQEKITE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  901 DGED-----IWRASRFR-----IIITTCSSAGlfyqiGVRVGYFTHV---FVDEAGQASEPECLIPlgLISDING-QIVL 966
Cdd:cd18040   158 EDIKtykilIWEARFEEletvdVILCTCSEAA-----SQKMRTHANVkqcIVDECGMCTEPESLIP--IVSAPRAeQVVL 230

                         250       260
                  ....*....|....*....|....*....
gi 326886207  967 AGDPMQLGPVIKSRLAMAYGLNVSMLERL 995
Cdd:cd18040   231 IGDHKQLRPVVQNKEAQKLGLGRSLFERY 259
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 799-995 6.61e-15

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 74.12  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  799 LNENQKLAVRRILSgdcRPLPYILfGPPGTGKT---VTIIEAVLQVHYALPDSRILVCAPSNSAADlvclrlheskvpkp 875
Cdd:cd17936     2 LDPSQLEALKHALT---SELALIQ-GPPGTGKTflgVKLVRALLQNQDLSITGPILVVCYTNHALD-------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  876 aamvrvnatcRFEETIIDAIKpycrdgEDIWRASrFRIIITTCSSA----GLFYQIGVRVgyfthVFVDEAGQASEPE-- 949
Cdd:cd17936    64 ----------QFLEGLLDFGP------TKIVRLG-ARVIGMTTTGAakyrELLQALGPKV-----VIVEEAAEVLEAHil 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 326886207  950 -CLIPlglisDINgQIVLAGDPMQLGPVIKSRL--AMAYGLNVSMLERL 995
Cdd:cd17936   122 aALTP-----STE-HLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERL 164
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 800-985 1.74e-11

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 62.60  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  800 NENQKLAVRRILSGDCrplpYILFGPPGTGKTVTIieAVLQVHYALPDSRILVCAPSNSAADLVclrlheskvpkpaamv 879
Cdd:cd18043     1 DSSQEAAIISARNGKN----VVIQGPPGTGKSQTI--ANIIANALARGKRVLFVSEKKAALDVV---------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  880 rvnatcrfeetiidaikpycrdgediwrasRFRIIITTCSSAGLFYQIGvrVGYFTHVFVDEAGQASePECLIPLGLISD 959
Cdd:cd18043    59 ------------------------------RFPCWIMSPLSVSQYLPLN--RNLFDLVIFDEASQIP-IEEALPALFRGK 105

                         170       180
                  ....*....|....*....|....*.
gi 326886207  960 ingQIVLAGDPMQLGPVIksRLAMAY 985
Cdd:cd18043   106 ---QVVVVGDDKQLPPSI--LLREHY 126
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 807-995 1.65e-10

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 62.06  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  807 VRRILSGdCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESKVPKpAAMVRVNatcr 886
Cdd:cd17935    11 IEAIRSG-MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKIMALDIDE-RHLLRLG---- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  887 feetiidaikpycrDGEdiwrasrfRIIITTCSSAGLFYQIGVRVGY-FTHVFVDEAGQASEPECLIPLGLISDING--- 962
Cdd:cd17935    85 --------------HGA--------KIIAMTCTHAALKRGELVELGFkYDNILMEEAAQILEIETFIPLLLQNPEDGpnr 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 326886207  963 --QIVLAGDPMQLGPVIKSRLAMAYG-LNVSMLERL 995
Cdd:cd17935   143 lkRLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRL 178
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 778-976 4.35e-10

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 63.84  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  778 AETMDEIQIPKARDKEF--FNPVLNENQKLAVRRILSGdcRPLpYILFGPPGTGKTvTIIEAVLQVHYALPDsRILVCAP 855
Cdd:COG0507   102 RPALDEADVEAALAALEprAGITLSDEQREAVALALTT--RRV-SVLTGGAGTGKT-TTLRALLAALEALGL-RVALAAP 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  856 SNSAAdlvcLRLHESkvpkpaamVRVNATcrfeeTI---IdaikpYCRDGEDIWRASRFRIIittcSSAGLfyqigvrvg 932
Cdd:COG0507   177 TGKAA----KRLSES--------TGIEAR-----TIhrlL-----GLRPDSGRFRHNRDNPL----TPADL--------- 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 326886207  933 yfthVFVDEAGQASEP--ECLipLGLISDINGQIVLAGDPMQLGPV 976
Cdd:COG0507   222 ----LVVDEASMVDTRlmAAL--LEALPRAGARLILVGDPDQLPSV 261
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 799-976 4.50e-10

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 60.27  E-value: 4.50e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   799 LNENQKLAVRRILSGDCRPLpyILFGPPGTGKTvTIIEAVLQVHYALPdSRILVCAPSNSAADlvclRLHESkvpkpaam 878
Cdd:pfam13604    2 LNAEQAAAVRALLTSGDRVA--VLVGPAGTGKT-TALKALREAWEAAG-YRVIGLAPTGRAAK----VLGEE-------- 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   879 vrvnatcrfeetiidaikpycrdgediwrasrfrIIITTCSSAGLFYQIGVRVGYFTH--VFVDEAGQASEPECLIPLGL 956
Cdd:pfam13604   66 ----------------------------------LGIPADTIAKLLHRLGGRAGLDPGtlLIVDEAGMVGTRQMARLLKL 111

                          170       180
                   ....*....|....*....|
gi 326886207   957 ISDINGQIVLAGDPMQLGPV 976
Cdd:pfam13604  112 AEDAGARVILVGDPRQLPSV 131
DEXDc smart00487
DEAD-like helicases superfamily;
792-942 9.68e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 56.73  E-value: 9.68e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207    792 KEFFNPVLNENQKLAVRRILSGDCRplpYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNSAADLVCLRLHESK 871
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLG 78

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326886207    872 VPKPaamvrVNATCRFEETIIDAIKpycrdgeDIWRASRFRIIITTCSSA-GLFYQIGVRVGYFTHVFVDEA 942
Cdd:smart00487   79 PSLG-----LKVVGLYGGDSKREQL-------RKLESGKTDILVTTPGRLlDLLENDKLSLSNVDLVILDEA 138
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 824-997 1.45e-08

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. 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. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 54.03  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  824 GPPGTGKT---VTIIEAVLQVHYAlPDSRILVCAPSNSAADlvclrlheskvpkpaamvrvnatcrfeetiidaikpycr 900
Cdd:cd17914     6 GPPGTGKTrvlVKIVAALMQNKNG-EPGRILLVTPTNKAAA--------------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  901 dgediwrasRFRIIittcssaglfyqigvrvgyfthvFVDEAGQASEPECLIPLGLISDInGQIVLAGDPMQLGPVIKSR 980
Cdd:cd17914    46 ---------QLDNI-----------------------LVDEAAQILEPETSRLIDLALDQ-GRVILVGDHDQLGPVWRGA 92

                         170
                  ....*....|....*..
gi 326886207  981 LAMAYGLNVSMLERLMS 997
Cdd:cd17914    93 VLAKICNEQSLFTRLVR 109
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 803-976 2.83e-06

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 48.32  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  803 QKLAVRRILSGdcrplPYILF-GPPGTGKTvTIIEAVLQVhYALPDSRILVCAPSNSAADlvclRLHESkVPKPAAMVrv 881
Cdd:cd17933     2 QKAAVRLVLRN-----RVSVLtGGAGTGKT-TTLKALLAA-LEAEGKRVVLAAPTGKAAK----RLSES-TGIEASTI-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207  882 natCRFEETIIDAIKPYcrdgEDIWRASRFRIIIttcssaglfyqigvrvgyfthvfVDEAGQASepeclIPL--GLIS- 958
Cdd:cd17933    68 ---HRLLGINPGGGGFY----YNEENPLDADLLI-----------------------VDEASMVD-----TRLmaALLSa 112

                         170
                  ....*....|....*....
gi 326886207  959 -DINGQIVLAGDPMQLGPV 976
Cdd:cd17933   113 iPAGARLILVGDPDQLPSV 131
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 1116-1201 4.61e-05

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 43.19  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207 1116 DIGVITPYRKQVEKI-KILLRN----VDLTDIKVGSVEEFQGQEYLVIVISTVRSNEDrfeddryflgflsNSKRFNVAI 1190
Cdd:cd18786    12 KGVVLTPYHRDRAYLnQYLQGLsldeFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL-------------TPRRLYVAL 78

                          90
                  ....*....|.
gi 326886207 1191 TRPKALLIILG 1201
Cdd:cd18786    79 TRARKRLVIYD 89
AAA_19 pfam13245
AAA domain;
803-976 1.05e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 40.66  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   803 QKLAVRRILSGDcrplPYILFGPPGTGKT---VTIIEAVLQVHYAlpDSRILVCAPSNSAADlvclRLHEskvpkpaAMV 879
Cdd:pfam13245    1 QREAVRTALPSK----VVLLTGGPGTGKTttiRHIVALLVALGGV--SFPILLAAPTGRAAK----RLSE-------RTG 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326886207   880 RVNATC-RFEETIIDAIKPYCRDGEDIWRAsrfriiittcssaglfyqigvrvgyfTHVFVDEAGQASEPECLIPLGLIS 958
Cdd:pfam13245   64 LPASTIhRLLGFDDLEAGGFLRDEEEPLDG--------------------------DLLIVDEFSMVDLPLAYRLLKALP 117

                          170
                   ....*....|....*...
gi 326886207   959 DiNGQIVLAGDPMQLGPV 976
Cdd:pfam13245  118 D-GAQLLLVGDPDQLPSV 134
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 798-840 4.47e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 39.05  E-value: 4.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 326886207  798 VLNENQKLAVRRILSGDcRPLPYILFGPPGTGKTvTIIEAVLQ 840
Cdd:cd00009     1 VGQEEAIEALREALELP-PPKNLLLYGPPGTGKT-TLARAIAN 41
ResIII pfam04851
Type III restriction enzyme, res subunit;
796-858 5.48e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 39.19  E-value: 5.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 326886207   796 NPVLNENQKLAVRRIL-SGDCRPLPYILFGPPGTGKTVTIIEAVLQVHYALPDSRILVCAPSNS 858
Cdd:pfam04851    1 KLELRPYQIEAIENLLeSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD 64
 
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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