NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568971938|ref|XP_006532424|]
View 

ATP-dependent DNA helicase Q5 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RecQ5 pfam06959
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ...
 320-508 1.38e-108

RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.


:

Pssm-ID: 399738  Cd Length: 202  Bit Score: 326.83  E-value: 1.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  320 KSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDED 399
Cdd:pfam06959   1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  400 RSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGS--AKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRS 477
Cdd:pfam06959  81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSsvAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568971938  478 EDASPSCGDV------PGKCT-QEVGAQGHLVAVFQTE 508
Cdd:pfam06959 161 EGASPSCEGVqgppmaPEKCTgEEDGAQGHLAAPPQTE 198
RecQ super family cl33925
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
1-143 5.99e-43

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


The actual alignment was detected with superfamily member COG0514:

Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 161.85  E-value: 5.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938   1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEK 80
Cdd:COG0514  277 LRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERK 356

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971938  81 RgnkpSDKATLlafDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPaaiTKKLDALE 143
Cdd:COG0514  357 R----VERAKL---DAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGP---PETFDGTE 409
 
Name Accession Description Interval E-value
RecQ5 pfam06959
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ...
 320-508 1.38e-108

RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.


Pssm-ID: 399738  Cd Length: 202  Bit Score: 326.83  E-value: 1.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  320 KSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDED 399
Cdd:pfam06959   1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  400 RSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGS--AKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRS 477
Cdd:pfam06959  81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSsvAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568971938  478 EDASPSCGDV------PGKCT-QEVGAQGHLVAVFQTE 508
Cdd:pfam06959 161 EGASPSCEGVqgppmaPEKCTgEEDGAQGHLAAPPQTE 198
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
1-143 5.99e-43

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 161.85  E-value: 5.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938   1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEK 80
Cdd:COG0514  277 LRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERK 356

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971938  81 RgnkpSDKATLlafDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPaaiTKKLDALE 143
Cdd:COG0514  357 R----VERAKL---DAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGP---PETFDGTE 409
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 1-58 1.05e-32

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: 122.70  E-value: 1.05e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971938   1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 58
Cdd:cd18794   77 LRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
 1-141 6.58e-30

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


Pssm-ID: 273594 [Multi-domain]  Cd Length: 591  Bit Score: 125.19  E-value: 6.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938    1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkELAKLQEK 80
Cdd:TIGR01389 271 LYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDD 348

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971938   81 RGNKPSDKatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYC-QNPAAITKKLDA 141
Cdd:TIGR01389 349 YKQIEREK-----LRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNClDPPKSYDATVEA 405
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 7-143 5.33e-21

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 97.48  E-value: 5.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938   7 VIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KELAKLQEKRG 82
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIER 365

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971938  83 NKpsdkatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPAaitKKLDALE 143
Cdd:PRK11057 366 HK---------LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP---KQYDGLE 414
DpdF NF041063
protein DpdF;
2-65 6.13e-15

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 78.80  E-value: 6.13e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971938   2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 65
Cdd:NF041063 426 ENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
HELICc smart00490
helicase superfamily c-terminal domain;
2-49 3.46e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 53.75  E-value: 3.46e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568971938     2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDG 49
Cdd:smart00490  35 NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
RecQ_Zn_bind pfam16124
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
 60-129 5.77e-08

RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.


Pssm-ID: 465031 [Multi-domain]  Cd Length: 66  Bit Score: 49.98  E-value: 5.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971938   60 RNDRDQVSFLIRKELAKLQEKRGNkpsdkatLLAFDALVTFCE-EVGCRHAAIAKYFGDA--PPACaKGCDYC 129
Cdd:pfam16124   1 YQDVVRLRFLIEQSEADEERKEVE-------LQKLQAMVAYCEnTTDCRRKQLLRYFGEEfdSEPC-GNCDNC 65
 
Name Accession Description Interval E-value
RecQ5 pfam06959
RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately ...
 320-508 1.38e-108

RecQ helicase protein-like 5 (RecQ5); This family represents a conserved region approximately 200 residues long within eukaryotic RecQ helicase protein-like 5 (RecQ5). The RecQ helicases have been implicated in DNA repair and recombination, and RecQ5 may have an important role in DNA metabolism.


Pssm-ID: 399738  Cd Length: 202  Bit Score: 326.83  E-value: 1.38e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  320 KSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDED 399
Cdd:pfam06959   1 KSCSAQAEPPEPTEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMEKTRAQEQAPQPVQGGEQEPPSQPCGLQDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938  400 RSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGS--AKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRS 477
Cdd:pfam06959  81 RSEPLPGPRGEAPGSSAHCGGPSPEKKAKGSSGGSsvAKARASKKQQLLATAALKDSQNITRFFCQRAESPPPLASAPRA 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568971938  478 EDASPSCGDV------PGKCT-QEVGAQGHLVAVFQTE 508
Cdd:pfam06959 161 EGASPSCEGVqgppmaPEKCTgEEDGAQGHLAAPPQTE 198
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
1-143 5.99e-43

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 161.85  E-value: 5.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938   1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEK 80
Cdd:COG0514  277 LRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIEQSPPDEERK 356

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971938  81 RgnkpSDKATLlafDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPaaiTKKLDALE 143
Cdd:COG0514  357 R----VERAKL---DAMLAYAETTGCRRQFLLRYFGEELAEPCGNCDNCLGP---PETFDGTE 409
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 1-58 1.05e-32

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: 122.70  E-value: 1.05e-32
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568971938   1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYY 58
Cdd:cd18794   77 LRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
recQ TIGR01389
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ...
 1-141 6.58e-30

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


Pssm-ID: 273594 [Multi-domain]  Cd Length: 591  Bit Score: 125.19  E-value: 6.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938    1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIrkELAKLQEK 80
Cdd:TIGR01389 271 LYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDGLPAEAILLYSPADIALLKRRI--EQSEADDD 348

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971938   81 RGNKPSDKatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYC-QNPAAITKKLDA 141
Cdd:TIGR01389 349 YKQIEREK-----LRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNClDPPKSYDATVEA 405
recQ_fam TIGR00614
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ...
 1-129 9.63e-28

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


Pssm-ID: 129701 [Multi-domain]  Cd Length: 470  Bit Score: 117.18  E-value: 9.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938    1 MEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqvSFLIRKELakLQEK 80
Cdd:TIGR00614 273 QRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECHLFYAPAD----MNRLRRLL--MEEP 346

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568971938   81 RGNKPSDKATLLafdALVTFCEEVG-CRHAAIAKYFGD---APPACAKGCDYC 129
Cdd:TIGR00614 347 DGNFRTYKLKLY---EMMEYCLNSStCRRLILLSYFGEkgfNKSFCIMGTEKC 396
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
 7-143 5.33e-21

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 97.48  E-value: 5.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938   7 VIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDrdqVSFLIR----KELAKLQEKRG 82
Cdd:PRK11057 289 IVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPAD---MAWLRRcleeKPAGQQQDIER 365

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971938  83 NKpsdkatllaFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPAaitKKLDALE 143
Cdd:PRK11057 366 HK---------LNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNCDICLDPP---KQYDGLE 414
PLN03137 PLN03137
ATP-dependent DNA helicase; Q4-like; Provisional
 2-138 2.92e-19

ATP-dependent DNA helicase; Q4-like; Provisional


Pssm-ID: 215597 [Multi-domain]  Cd Length: 1195  Bit Score: 92.65  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971938    2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRK-ELAKLQEK 80
Cdd:PLN03137  728 KDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSDYIRVKHMISQgGVEQSPMA 807

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971938   81 RG-NKPSDKATLLAFDA-----LVTFCE-EVGCRHAAIAKYFGDAPPA--CAKGCDYCQNPAAITKK 138
Cdd:PLN03137  808 MGyNRMASSGRILETNTenllrMVSYCEnEVDCRRFLQLVHFGEKFDStnCKKTCDNCSSSKSLIDK 874
DpdF NF041063
protein DpdF;
2-65 6.13e-15

protein DpdF;


Pssm-ID: 468990 [Multi-domain]  Cd Length: 813  Bit Score: 78.80  E-value: 6.13e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568971938   2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQ 65
Cdd:NF041063 426 ENELDIVVATSAFGLGMDKSDVRTVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDLDI 489
HELICc smart00490
helicase superfamily c-terminal domain;
2-49 3.46e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 53.75  E-value: 3.46e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568971938     2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDG 49
Cdd:smart00490  35 NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
RecQ_Zn_bind pfam16124
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
 60-129 5.77e-08

RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.


Pssm-ID: 465031 [Multi-domain]  Cd Length: 66  Bit Score: 49.98  E-value: 5.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971938   60 RNDRDQVSFLIRKELAKLQEKRGNkpsdkatLLAFDALVTFCE-EVGCRHAAIAKYFGDA--PPACaKGCDYC 129
Cdd:pfam16124   1 YQDVVRLRFLIEQSEADEERKEVE-------LQKLQAMVAYCEnTTDCRRKQLLRYFGEEfdSEPC-GNCDNC 65
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 2-49 7.27e-07

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: 47.98  E-value: 7.27e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568971938    2 EEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDG 49
Cdd:pfam00271  62 KGKIDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 7-50 7.80e-06

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: 44.23  E-value: 7.80e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568971938   7 VIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGK 50
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
 8-52 1.16e-05

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: 45.71  E-value: 1.16e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568971938   8 IVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPS 52
Cdd:cd18797   96 VVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDS 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH