NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767996129|ref|XP_011523643|]
View 

Fanconi anemia group J protein isoform X10 [Homo sapiens]

Protein Classification

DEAD_2 and P-loop containing Nucleoside Triphosphate Hydrolases domain-containing protein( domain architecture ID 13514383)

protein containing domains PRK08074, DEAD-like_helicase_N, DEAD_2, and P-loop containing Nucleoside Triphosphate Hydrolases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
248-415 1.01e-72

DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases that are seemingly ubiquitous - members include proteins of eukaryotic, bacterial and archaeal origin. RAD3 is involved in nucleotide excision repair, and forms part of the transcription factor TFIIH in yeast.


:

Pssm-ID: 399602 [Multi-domain]  Cd Length: 168  Bit Score: 231.77  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  248 FGTRTHKQIAQITRELRRTAY-SGVPMTILSSRDHTCVHPEVV---GNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQH 323
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYyKKIRGLILGSRKNLCINPEVLklkKGNLVNERCRELVKSKARGSCPFYNNLEDLLKLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  324 tlqtFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCAR 403
Cdd:pfam06733  81 ----DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCI 156
                         170
                  ....*....|..
gi 767996129  404 ESASYSVTEVQL 415
Cdd:pfam06733 157 ESASFSISRSQL 168
rad3 super family cl36704
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
245-648 1.55e-45

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00604:

Pssm-ID: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 172.59  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  245 KIYFGTRTHKQIAQITRELRRTAYSGVPMTI---------LSSRDHTCVHPEVVGNFN---RNEKCMELLDGKNGK---- 308
Cdd:TIGR00604  62 KIIYASRTHSQLEQATEELRKLMSYRTPRIGeespvsglsLASRKNLCLHPEVSKERQgkvVNGKCIKLTVSKIKEqrte 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  309 -----SCYFYHGVHKISDQHTLqtFQGmcKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDL 383
Cdd:TIGR00604 142 kpnveSCEFYENFDELREVEDL--LLS--EIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSI 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  384 NLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSmvnnnIRKKDHEPLRAVCCSLINWLEANAEYLVERDYES 463
Cdd:TIGR00604 218 ELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAE-----YFEKIEERKEVDARKLLDELQKLVEGLKQEDLLT 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  464 ACKIWSGNEMLLTLhkmgITTATFPILQG---HFSAVLQKEEKispiYGKEEAREVPVISASTQIMLKGLF---MVLDYL 537
Cdd:TIGR00604 293 DEDIFLANPVLPKE----VLPEAVPGNIRiaeIFLHKLSRYLE----YLKDALKVLGVVSELPDAFLEHLKektFIDRPL 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  538 FRQNSRFAD-----------DYkIAIQQTYSWtNQIDISDKNGLLvlpKNKKRSRQKTAVH-VLNFWCLNPAVAFSDING 605
Cdd:TIGR00604 365 RFCSERLSNllreleithpeDF-SALVLLFTF-ATLVLTYTNGFL---EGIEPYENKTVPNpILKFMCLDPSIALKPLFE 439
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 767996129  606 KVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQSVP 648
Cdd:TIGR00604 440 RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLT 482
PRK08074 super family cl35639
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
18-61 4.71e-05

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


The actual alignment was detected with superfamily member PRK08074:

Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 46.87  E-value: 4.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767996129  18 PYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLA-LLCSAL 61
Cdd:PRK08074 255 KYEKREGQQEMMKEVYTALRDSEHALIEAGTGTGKSLAyLLPAAY 299
 
Name Accession Description Interval E-value
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
248-415 1.01e-72

DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases that are seemingly ubiquitous - members include proteins of eukaryotic, bacterial and archaeal origin. RAD3 is involved in nucleotide excision repair, and forms part of the transcription factor TFIIH in yeast.


Pssm-ID: 399602 [Multi-domain]  Cd Length: 168  Bit Score: 231.77  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  248 FGTRTHKQIAQITRELRRTAY-SGVPMTILSSRDHTCVHPEVV---GNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQH 323
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYyKKIRGLILGSRKNLCINPEVLklkKGNLVNERCRELVKSKARGSCPFYNNLEDLLKLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  324 tlqtFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCAR 403
Cdd:pfam06733  81 ----DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCI 156
                         170
                  ....*....|..
gi 767996129  404 ESASYSVTEVQL 415
Cdd:pfam06733 157 ESASFSISRSQL 168
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
39-399 5.16e-54

DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi anemia group J protein (FACJ or FANCJ, also known as BRIP1) is a DNA helicase required for the maintenance of chromosomal stability. It plays a role in the repair of DNA double-strand breaks by homologous recombination dependent on its interaction with BRCA1. FANCJ belongs to the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350728 [Multi-domain]  Cd Length: 181  Bit Score: 182.93  E-value: 5.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  39 KQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGvsekaevqlscccachskdftnndmnqgtsrhfnypstppser 118
Cdd:cd17970    1 GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATSEG------------------------------------------- 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 119 ngtsstcqdspekttlaaklsakkqasiyrdenddfqvekkrirplettqqirkrhcfgtevhnldakvdsgktvklnsp 198
Cdd:cd17970      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 199 lekinsfspqkppghcsrcccstkqgnsqessntikKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSS 278
Cdd:cd17970   38 ------------------------------------SDGGGSGKIPKIIYASRTHSQLAQVVRELKRTAYKRPRMTILGS 81
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 279 RDHTCVHP--EVVGNFNRNEKCMELLDGKNgkscyfyhgvhkisdqhtlqtfqgmckawdieelvslgkklkacpyytar 356
Cdd:cd17970   82 RDHLCIHPviNKLSNQNANEACMALLSGKN-------------------------------------------------- 111
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767996129 357 eliqDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIE 399
Cdd:cd17970  112 ----EADLVFCPYNYLLDPNIRRSMGLNLKGSVVIFDEAHNIE 150
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
245-648 1.55e-45

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. 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: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 172.59  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  245 KIYFGTRTHKQIAQITRELRRTAYSGVPMTI---------LSSRDHTCVHPEVVGNFN---RNEKCMELLDGKNGK---- 308
Cdd:TIGR00604  62 KIIYASRTHSQLEQATEELRKLMSYRTPRIGeespvsglsLASRKNLCLHPEVSKERQgkvVNGKCIKLTVSKIKEqrte 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  309 -----SCYFYHGVHKISDQHTLqtFQGmcKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDL 383
Cdd:TIGR00604 142 kpnveSCEFYENFDELREVEDL--LLS--EIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSI 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  384 NLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSmvnnnIRKKDHEPLRAVCCSLINWLEANAEYLVERDYES 463
Cdd:TIGR00604 218 ELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAE-----YFEKIEERKEVDARKLLDELQKLVEGLKQEDLLT 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  464 ACKIWSGNEMLLTLhkmgITTATFPILQG---HFSAVLQKEEKispiYGKEEAREVPVISASTQIMLKGLF---MVLDYL 537
Cdd:TIGR00604 293 DEDIFLANPVLPKE----VLPEAVPGNIRiaeIFLHKLSRYLE----YLKDALKVLGVVSELPDAFLEHLKektFIDRPL 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  538 FRQNSRFAD-----------DYkIAIQQTYSWtNQIDISDKNGLLvlpKNKKRSRQKTAVH-VLNFWCLNPAVAFSDING 605
Cdd:TIGR00604 365 RFCSERLSNllreleithpeDF-SALVLLFTF-ATLVLTYTNGFL---EGIEPYENKTVPNpILKFMCLDPSIALKPLFE 439
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 767996129  606 KVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQSVP 648
Cdd:TIGR00604 440 RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLT 482
DEXDc2 smart00488
DEAD-like helicases superfamily;
15-427 1.99e-43

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 157.93  E-value: 1.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    15 IYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLsgkPADEGVSEKAEVQLscccachskd 94
Cdd:smart00488   3 FYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSF---PERIQKIKLIYLSR---------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    95 fTNNDMNQgtsrhfnypstppserngtsstcqdspekttlaaklsakkqasiyrdenddfqvekkrirpleTTQQIRKRH 174
Cdd:smart00488  70 -TVSEIEK---------------------------------------------------------------RLEELRKLM 85
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   175 CfgtevhnldakvdsgktvklnsplekinsfspqkppghcsrcccstkqgnsqessntikkdhtgkskiPKIYFGTRTHK 254
Cdd:smart00488  86 Q--------------------------------------------------------------------KVEYESDEESE 97
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   255 QIAQITRELRRTAYSGVPMtILSSRDHTCVHPEV-----VGNFNrNEKCMELLDGK---------NGKSCYFYHGVHKIS 320
Cdd:smart00488  98 KQAQLLHELGREKPKVLGL-SLTSRKNLCLNPEVrtlkqNGLVV-DEVCRSLTASKarkyryenpKVERCPFYENTEFLL 175
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   321 DQHTLQTfqgmcKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIED 400
Cdd:smart00488 176 VRDLLPA-----EVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELKDSIVIFDEAHNLDN 250
                          410       420
                   ....*....|....*....|....*..
gi 767996129   401 CARESASYSVTEVQLRFARDELDSMVN 427
Cdd:smart00488 251 VCISALSSELSRRSLERAHKNIKKYFE 277
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
350-628 9.10e-17

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 84.21  E-value: 9.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 350 CPYYTARELIQDADIIFCPYNYLLDAQIRESmDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELdsmvNNN 429
Cdd:COG1199  176 CPYELARRLAREADVVVVNHHLLFADLALGE-ELLPEDDVLIIDEAHNLPDRARDMFSAELSSRSLLRLLREL----RKL 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 430 IRKKDHEPLRAVCCSLINWLEANAEYLVERDyesackiwsgnEMLLTLHKMGITTATfpiLQGHFSAVLQKEEKISpiyg 509
Cdd:COG1199  251 GLRPGLKKLLDLLERLREALDDLFLALEEEE-----------ELRLALGELPDEPEE---LLEALDALRDALEALA---- 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 510 kEEAREVPVISAStqimLKGLFMVLDYLFRQNSRFADDYkiaiqqtyswtnqidiSDKNGLLVLPKNKKRSRqktavhvL 589
Cdd:COG1199  313 -EALEEELERLAE----LDALLERLEELLFALARFLRIA----------------EDEGYVRWLEREGGDVR-------L 364
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767996129 590 NFWCLNPAVAFSD-INGKVQTIVLTSGTLSPMKSFS---SELG 628
Cdd:COG1199  365 HAAPLDPADLLRElLFSRARSVVLTSATLSVGGPFDyfaRRLG 407
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
18-61 4.71e-05

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 46.87  E-value: 4.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767996129  18 PYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLA-LLCSAL 61
Cdd:PRK08074 255 KYEKREGQQEMMKEVYTALRDSEHALIEAGTGTGKSLAyLLPAAY 299
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
604-637 8.97e-05

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 42.80  E-value: 8.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767996129 604 NGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEA 637
Cdd:cd17915  105 NLDERSVIITSGTLSPLDIYSKILGIRNMLVLAV 138
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
43-63 7.73e-04

DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) encodes a protein of the conserved family of Iron-Sulfur (Fe-S) cluster DNA helicases and is thought to function in maintaining chromosome transmission fidelity and genome stability. Mutations in the Chl1 human homologs ChlR1/DDX11 and BACH1/BRIP1/FANCJ collectively result in Warsaw Breakage Syndrome, Fanconi anemia, cell aneuploidy and breast and ovarian cancers. DDX11 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350726  Cd Length: 134  Bit Score: 40.00  E-value: 7.73e-04
                         10        20
                 ....*....|....*....|.
gi 767996129  43 LLESPTGSGKSLALLCSALAW 63
Cdd:cd17968    5 IFESPTGTGKSLSLICGALTW 25
DEXDc smart00487
DEAD-like helicases superfamily;
13-72 1.64e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 40.17  E-value: 1.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    13 VKIYFPYKAYPSQLAMMNSILRGLnskQHCLLESPTGSGKSLALLCSALAWQQSLSGKPA 72
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRV 57
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
23-74 3.42e-03

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 40.47  E-value: 3.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767996129  23 PSQLAMMNSILRGlnskQHCLLESPTGSGKSLALLCSALA--WQQSLSGKPADE 74
Cdd:COG1201   27 PPQREAWPAIAAG----ESTLLIAPTGSGKTLAAFLPALDelARRPRPGELPDG 76
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
350-425 4.11e-03

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 40.20  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 350 CPYYTARELIQDADIIFCpyNY-LLDAqireSMDL-------NLKEQVVILDEAHNIEDCARESASYSVTevqLRFARDE 421
Cdd:PRK11747 208 CPFFKARREIDEADVVVA--NHdLVLA----DLELgggvvlpDPENLLYVLDEGHHLPDVARDHFAASAE---LKGTADW 278

                 ....
gi 767996129 422 LDSM 425
Cdd:PRK11747 279 LEKL 282
 
Name Accession Description Interval E-value
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
248-415 1.01e-72

DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases that are seemingly ubiquitous - members include proteins of eukaryotic, bacterial and archaeal origin. RAD3 is involved in nucleotide excision repair, and forms part of the transcription factor TFIIH in yeast.


Pssm-ID: 399602 [Multi-domain]  Cd Length: 168  Bit Score: 231.77  E-value: 1.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  248 FGTRTHKQIAQITRELRRTAY-SGVPMTILSSRDHTCVHPEVV---GNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQH 323
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYyKKIRGLILGSRKNLCINPEVLklkKGNLVNERCRELVKSKARGSCPFYNNLEDLLKLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  324 tlqtFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCAR 403
Cdd:pfam06733  81 ----DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCI 156
                         170
                  ....*....|..
gi 767996129  404 ESASYSVTEVQL 415
Cdd:pfam06733 157 ESASFSISRSQL 168
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
39-399 5.16e-54

DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi anemia group J protein (FACJ or FANCJ, also known as BRIP1) is a DNA helicase required for the maintenance of chromosomal stability. It plays a role in the repair of DNA double-strand breaks by homologous recombination dependent on its interaction with BRCA1. FANCJ belongs to the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350728 [Multi-domain]  Cd Length: 181  Bit Score: 182.93  E-value: 5.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  39 KQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGvsekaevqlscccachskdftnndmnqgtsrhfnypstppser 118
Cdd:cd17970    1 GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATSEG------------------------------------------- 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 119 ngtsstcqdspekttlaaklsakkqasiyrdenddfqvekkrirplettqqirkrhcfgtevhnldakvdsgktvklnsp 198
Cdd:cd17970      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 199 lekinsfspqkppghcsrcccstkqgnsqessntikKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSS 278
Cdd:cd17970   38 ------------------------------------SDGGGSGKIPKIIYASRTHSQLAQVVRELKRTAYKRPRMTILGS 81
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 279 RDHTCVHP--EVVGNFNRNEKCMELLDGKNgkscyfyhgvhkisdqhtlqtfqgmckawdieelvslgkklkacpyytar 356
Cdd:cd17970   82 RDHLCIHPviNKLSNQNANEACMALLSGKN-------------------------------------------------- 111
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767996129 357 eliqDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIE 399
Cdd:cd17970  112 ----EADLVFCPYNYLLDPNIRRSMGLNLKGSVVIFDEAHNIE 150
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
245-648 1.55e-45

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair as part of the TFIIH complex. 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: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 172.59  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  245 KIYFGTRTHKQIAQITRELRRTAYSGVPMTI---------LSSRDHTCVHPEVVGNFN---RNEKCMELLDGKNGK---- 308
Cdd:TIGR00604  62 KIIYASRTHSQLEQATEELRKLMSYRTPRIGeespvsglsLASRKNLCLHPEVSKERQgkvVNGKCIKLTVSKIKEqrte 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  309 -----SCYFYHGVHKISDQHTLqtFQGmcKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDL 383
Cdd:TIGR00604 142 kpnveSCEFYENFDELREVEDL--LLS--EIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSI 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  384 NLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSmvnnnIRKKDHEPLRAVCCSLINWLEANAEYLVERDYES 463
Cdd:TIGR00604 218 ELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAE-----YFEKIEERKEVDARKLLDELQKLVEGLKQEDLLT 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  464 ACKIWSGNEMLLTLhkmgITTATFPILQG---HFSAVLQKEEKispiYGKEEAREVPVISASTQIMLKGLF---MVLDYL 537
Cdd:TIGR00604 293 DEDIFLANPVLPKE----VLPEAVPGNIRiaeIFLHKLSRYLE----YLKDALKVLGVVSELPDAFLEHLKektFIDRPL 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129  538 FRQNSRFAD-----------DYkIAIQQTYSWtNQIDISDKNGLLvlpKNKKRSRQKTAVH-VLNFWCLNPAVAFSDING 605
Cdd:TIGR00604 365 RFCSERLSNllreleithpeDF-SALVLLFTF-ATLVLTYTNGFL---EGIEPYENKTVPNpILKFMCLDPSIALKPLFE 439
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 767996129  606 KVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQSVP 648
Cdd:TIGR00604 440 RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLT 482
DEXDc2 smart00488
DEAD-like helicases superfamily;
15-427 1.99e-43

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 157.93  E-value: 1.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    15 IYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLsgkPADEGVSEKAEVQLscccachskd 94
Cdd:smart00488   3 FYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSF---PERIQKIKLIYLSR---------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    95 fTNNDMNQgtsrhfnypstppserngtsstcqdspekttlaaklsakkqasiyrdenddfqvekkrirpleTTQQIRKRH 174
Cdd:smart00488  70 -TVSEIEK---------------------------------------------------------------RLEELRKLM 85
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   175 CfgtevhnldakvdsgktvklnsplekinsfspqkppghcsrcccstkqgnsqessntikkdhtgkskiPKIYFGTRTHK 254
Cdd:smart00488  86 Q--------------------------------------------------------------------KVEYESDEESE 97
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   255 QIAQITRELRRTAYSGVPMtILSSRDHTCVHPEV-----VGNFNrNEKCMELLDGK---------NGKSCYFYHGVHKIS 320
Cdd:smart00488  98 KQAQLLHELGREKPKVLGL-SLTSRKNLCLNPEVrtlkqNGLVV-DEVCRSLTASKarkyryenpKVERCPFYENTEFLL 175
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129   321 DQHTLQTfqgmcKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIED 400
Cdd:smart00488 176 VRDLLPA-----EVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELKDSIVIFDEAHNLDN 250
                          410       420
                   ....*....|....*....|....*..
gi 767996129   401 CARESASYSVTEVQLRFARDELDSMVN 427
Cdd:smart00488 251 VCISALSSELSRRSLERAHKNIKKYFE 277
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
242-399 1.98e-21

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 90.57  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 242 KIPKIYFGTRTHKQIAQITRELRRTAYS-GVPMTILSSRDhtcvhpevvgnfnrnekcmelldgkngkscyfyhgvhkis 320
Cdd:cd17915   30 HKTKVLYCSRTHSQIEQIIRELRKLLEKrKIRALALSSRD---------------------------------------- 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996129 321 dqhtlqtfqgmckawdieelvslgkklkacpyytareliqdADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIE 399
Cdd:cd17915   70 -----------------------------------------ADIVVLPYPYLLDARIREFIGIDLREQVVIIDEAHNLD 107
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
350-628 9.10e-17

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 84.21  E-value: 9.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 350 CPYYTARELIQDADIIFCPYNYLLDAQIRESmDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELdsmvNNN 429
Cdd:COG1199  176 CPYELARRLAREADVVVVNHHLLFADLALGE-ELLPEDDVLIIDEAHNLPDRARDMFSAELSSRSLLRLLREL----RKL 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 430 IRKKDHEPLRAVCCSLINWLEANAEYLVERDyesackiwsgnEMLLTLHKMGITTATfpiLQGHFSAVLQKEEKISpiyg 509
Cdd:COG1199  251 GLRPGLKKLLDLLERLREALDDLFLALEEEE-----------ELRLALGELPDEPEE---LLEALDALRDALEALA---- 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 510 kEEAREVPVISAStqimLKGLFMVLDYLFRQNSRFADDYkiaiqqtyswtnqidiSDKNGLLVLPKNKKRSRqktavhvL 589
Cdd:COG1199  313 -EALEEELERLAE----LDALLERLEELLFALARFLRIA----------------EDEGYVRWLEREGGDVR-------L 364
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 767996129 590 NFWCLNPAVAFSD-INGKVQTIVLTSGTLSPMKSFS---SELG 628
Cdd:COG1199  365 HAAPLDPADLLRElLFSRARSVVLTSATLSVGGPFDyfaRRLG 407
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
340-398 1.51e-05

DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) encodes a protein of the conserved family of Iron-Sulfur (Fe-S) cluster DNA helicases and is thought to function in maintaining chromosome transmission fidelity and genome stability. Mutations in the Chl1 human homologs ChlR1/DDX11 and BACH1/BRIP1/FANCJ collectively result in Warsaw Breakage Syndrome, Fanconi anemia, cell aneuploidy and breast and ovarian cancers. DDX11 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350726  Cd Length: 134  Bit Score: 45.00  E-value: 1.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767996129 340 LVSLGKKLKAcpyytareliqdADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNI 398
Cdd:cd17968   57 LVSLGSRQPA------------AQVVVLPYQMLLHAATRKASGIKLKDQVVIIDEAHNL 103
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
18-61 4.71e-05

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 46.87  E-value: 4.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767996129  18 PYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLA-LLCSAL 61
Cdd:PRK08074 255 KYEKREGQQEMMKEVYTALRDSEHALIEAGTGTGKSLAyLLPAAY 299
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
604-637 8.97e-05

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 42.80  E-value: 8.97e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767996129 604 NGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEA 637
Cdd:cd17915  105 NLDERSVIITSGTLSPLDIYSKILGIRNMLVLAV 138
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
43-63 7.73e-04

DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) encodes a protein of the conserved family of Iron-Sulfur (Fe-S) cluster DNA helicases and is thought to function in maintaining chromosome transmission fidelity and genome stability. Mutations in the Chl1 human homologs ChlR1/DDX11 and BACH1/BRIP1/FANCJ collectively result in Warsaw Breakage Syndrome, Fanconi anemia, cell aneuploidy and breast and ovarian cancers. DDX11 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350726  Cd Length: 134  Bit Score: 40.00  E-value: 7.73e-04
                         10        20
                 ....*....|....*....|.
gi 767996129  43 LLESPTGSGKSLALLCSALAW 63
Cdd:cd17968    5 IFESPTGTGKSLSLICGALTW 25
DEXDc smart00487
DEAD-like helicases superfamily;
13-72 1.64e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 40.17  E-value: 1.64e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129    13 VKIYFPYKAYPSQLAMMNSILRGLnskQHCLLESPTGSGKSLALLCSALAWQQSLSGKPA 72
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRV 57
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
34-65 1.92e-03

DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; TFIIH can be resolved biochemically into a seven subunit core complex containing XPD/Rad3, XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and p8/Tfb5 and a three subunit Cdk Activating Kinase (CAK) complex containing CDK7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3. XPD interacts directly with p44, which stimulates XPD helicase activity. XPD/Rad3 also interacts directly with the CAK via its MAT1/Tfb3 subunit inhibiting the helicase activity of XPD. XPD is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350727 [Multi-domain]  Cd Length: 157  Bit Score: 39.34  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767996129  34 RGLNSKQHCLLESPTGSGKSLALLCSALAWQQ 65
Cdd:cd17969    5 RTLDAKGHCVLEMPSGTGKTVSLLSLIVAYQK 36
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
23-74 3.42e-03

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


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 40.47  E-value: 3.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767996129  23 PSQLAMMNSILRGlnskQHCLLESPTGSGKSLALLCSALA--WQQSLSGKPADE 74
Cdd:COG1201   27 PPQREAWPAIAAG----ESTLLIAPTGSGKTLAAFLPALDelARRPRPGELPDG 76
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
350-425 4.11e-03

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 40.20  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996129 350 CPYYTARELIQDADIIFCpyNY-LLDAqireSMDL-------NLKEQVVILDEAHNIEDCARESASYSVTevqLRFARDE 421
Cdd:PRK11747 208 CPFFKARREIDEADVVVA--NHdLVLA----DLELgggvvlpDPENLLYVLDEGHHLPDVARDHFAASAE---LKGTADW 278

                 ....
gi 767996129 422 LDSM 425
Cdd:PRK11747 279 LEKL 282
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
362-399 4.84e-03

DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; TFIIH can be resolved biochemically into a seven subunit core complex containing XPD/Rad3, XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and p8/Tfb5 and a three subunit Cdk Activating Kinase (CAK) complex containing CDK7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3. XPD interacts directly with p44, which stimulates XPD helicase activity. XPD/Rad3 also interacts directly with the CAK via its MAT1/Tfb3 subunit inhibiting the helicase activity of XPD. XPD is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350727 [Multi-domain]  Cd Length: 157  Bit Score: 38.18  E-value: 4.84e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767996129 362 ADIIFCPYNYLLDAQIRESMDLNL-KEQVVILDEAHNIE 399
Cdd:cd17969   89 ANVVVYSYHYLLDPKIAELVSKELsKKSVVVFDEAHNID 127
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
16-58 8.89e-03

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 37.90  E-value: 8.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767996129  16 YFPYKAY-PSQLAMMNSILRGlnskQHCLLESPTGSGKSL-----ALLC 58
Cdd:cd17920    7 VFGYDEFrPGQLEAINAVLAG----RDVLVVMPTGGGKSLcyqlpALLL 51
 
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