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Conserved domains on  [gi|442615242|ref|NP_001259262|]
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regulator of telomere elongation helicase 1, isoform B [Drosophila melanogaster]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13514309)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to human ATP-dependent DNA helicase DDX11

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad3 super family cl36704
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
10-742 5.45e-140

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: 435.30  E-value: 5.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   10 PVHFPFEP-YPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRtRQSEHQKqmvkmekadfsglgggapg 88
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQ-EKPEVRK------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   89 gdlselaktmgrannwgvpkVIYASRTHSQLTQAMRELKRTAYA---------NMRSVVLGSRDQLCIHPEVMREQGNSN 159
Cdd:TIGR00604  63 --------------------IIYASRTHSQLEQATEELRKLMSYrtprigeesPVSGLSLASRKNLCLHPEVSKERQGKV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  160 KTNMCKLRVHSK------------TCSFQMRVESRKDHPDLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMP 227
Cdd:TIGR00604 123 VNGKCIKLTVSKikeqrtekpnveSCEFYENFDELREVEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  228 YNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQD--MAGDEPKDFT 305
Cdd:TIGR00604 203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDarKLLDELQKLV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  306 L---DDLTLLKEMLLELEKAIDAIVVDNAVDGTTFPASMMYELL---GKANFTYGNVATIVSLLDKLVQYLLVASQQMSI 379
Cdd:TIGR00604 283 EglkQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRIAEIFLHKLsryLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  380 RKGGTFTLLSDLL-TIVFANKEDVMSKV-YASFKVHVLVEESKQGHGKQQGAKQqggwlgkgtiaAATGLskvakIINFW 457
Cdd:TIGR00604 363 PLRFCSERLSNLLrELEITHPEDFSALVlLFTFATLVLTYTNGFLEGIEPYENK-----------TVPNP-----ILKFM 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  458 CFNPGFGMEQLLNtQVRSVILTSGTLAPLKPLIAELAIPVAQHLENPHIVDQSQVYVKIIGTGPDRQQLISNYANRDNPK 537
Cdd:TIGR00604 427 CLDPSIALKPLFE-RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPS 505
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  538 YISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASGLWADISCKKPIFLEPRSKDQFTSTMEEFYQAIRDSKGAV 617
Cdd:TIGR00604 506 LVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSEGRGAV 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  618 FMAVCRGKVSEGLDFADRNGRAVIITGLPFPplkdpkVILKRRYLEANRTRE--NQLLSGQEWYNLDATRAVNQAIGRVI 695
Cdd:TIGR00604 586 LLSVAGGKVSEGIDFCDDLGRAVIMVGIPYE------YTESRILLARLEFLRdqYPIRENQDFYEFDAMRAVNQAIGRVI 659
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 442615242  696 RHRNDYGAILLCDSRFKDASQVQQLSKWIRGHLGDRPQcspFGPIVR 742
Cdd:TIGR00604 660 RHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDL---NGMAIS 703
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
896-985 5.46e-22

harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin.


:

Pssm-ID: 259826 [Multi-domain]  Cd Length: 99  Bit Score: 91.57  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 896 EPSSSQAKEAPEERAAFLRELRSLVTQDQFRRFGKALLEYKNGTyeSFQALMAILLDVLSAPKVRYMLVGMRKYLKNEHK 975
Cdd:cd13932    7 ASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGD--DFEQLLAVLAELFAEPERHPLLRGFRRFVRPHHK 84
                         90
                 ....*....|
gi 442615242 976 DEFDRRVGNL 985
Cdd:cd13932   85 KEFDERCKSL 94
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
10-742 5.45e-140

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: 435.30  E-value: 5.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   10 PVHFPFEP-YPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRtRQSEHQKqmvkmekadfsglgggapg 88
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQ-EKPEVRK------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   89 gdlselaktmgrannwgvpkVIYASRTHSQLTQAMRELKRTAYA---------NMRSVVLGSRDQLCIHPEVMREQGNSN 159
Cdd:TIGR00604  63 --------------------IIYASRTHSQLEQATEELRKLMSYrtprigeesPVSGLSLASRKNLCLHPEVSKERQGKV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  160 KTNMCKLRVHSK------------TCSFQMRVESRKDHPDLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMP 227
Cdd:TIGR00604 123 VNGKCIKLTVSKikeqrtekpnveSCEFYENFDELREVEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  228 YNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQD--MAGDEPKDFT 305
Cdd:TIGR00604 203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDarKLLDELQKLV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  306 L---DDLTLLKEMLLELEKAIDAIVVDNAVDGTTFPASMMYELL---GKANFTYGNVATIVSLLDKLVQYLLVASQQMSI 379
Cdd:TIGR00604 283 EglkQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRIAEIFLHKLsryLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  380 RKGGTFTLLSDLL-TIVFANKEDVMSKV-YASFKVHVLVEESKQGHGKQQGAKQqggwlgkgtiaAATGLskvakIINFW 457
Cdd:TIGR00604 363 PLRFCSERLSNLLrELEITHPEDFSALVlLFTFATLVLTYTNGFLEGIEPYENK-----------TVPNP-----ILKFM 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  458 CFNPGFGMEQLLNtQVRSVILTSGTLAPLKPLIAELAIPVAQHLENPHIVDQSQVYVKIIGTGPDRQQLISNYANRDNPK 537
Cdd:TIGR00604 427 CLDPSIALKPLFE-RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPS 505
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  538 YISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASGLWADISCKKPIFLEPRSKDQFTSTMEEFYQAIRDSKGAV 617
Cdd:TIGR00604 506 LVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSEGRGAV 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  618 FMAVCRGKVSEGLDFADRNGRAVIITGLPFPplkdpkVILKRRYLEANRTRE--NQLLSGQEWYNLDATRAVNQAIGRVI 695
Cdd:TIGR00604 586 LLSVAGGKVSEGIDFCDDLGRAVIMVGIPYE------YTESRILLARLEFLRdqYPIRENQDFYEFDAMRAVNQAIGRVI 659
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 442615242  696 RHRNDYGAILLCDSRFKDASQVQQLSKWIRGHLGDRPQcspFGPIVR 742
Cdd:TIGR00604 660 RHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDL---NGMAIS 703
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
111-274 1.37e-78

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: 253.34  E-value: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  111 YASRTHSQLTQAMRELKRTAYA-NMRSVVLGSRDQLCIHPEVMREQGNSNKTNMCKLRVHSK---TCSFQMRVESRKDHP 186
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYkKIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKargSCPFYNNLEDLLKLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  187 DLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESAS 266
Cdd:pfam06733  81 DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCIESAS 160

                  ....*...
gi 442615242  267 VQIKSSDV 274
Cdd:pfam06733 161 FSISRSQL 168
DEXDc2 smart00488
DEAD-like helicases superfamily;
9-292 5.18e-70

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 234.58  E-value: 5.18e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242     9 IPVHFPFEPYPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRtRQSEHQKQMVKMEKADFsglgggapg 88
Cdd:smart00488   1 LLFYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLR-SFPERIQKIKLIYLSRT--------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242    89 gdLSELAKTMGRANNWGVPKVIYASRTHSQLTQAMRELKRTAYANmRSVVLGSRDQLCIHPEVMREQGNSNKTN------ 162
Cdd:smart00488  71 --VSEIEKRLEELRKLMQKVEYESDEESEKQAQLLHELGREKPKV-LGLSLTSRKNLCLNPEVRTLKQNGLVVDevcrsl 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   163 ----MCKLRVHS---KTCSFQMRVESRKDHPDLRgPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPK 235
Cdd:smart00488 148 taskARKYRYENpkvERCPFYENTEFLLVRDLLP-AEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPK 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442615242   236 ARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDvthIMQVFASGE 292
Cdd:smart00488 227 IRQALSIELKDSIVIFDEAHNLDNVCISALSSELSRRSLERAHKN---IKKYFERIE 280
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
510-711 8.13e-67

C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. 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: 350175 [Multi-domain]  Cd Length: 159  Bit Score: 220.94  E-value: 8.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 510 SQVYVKIIGTGPDRQQLISNYANRDNPKYISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVdawqasglwadisckkpi 589
Cdd:cd18788    1 DQVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVV------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 590 fleprskdqftstmeefyqairdSKGAVFMAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANRTRE 669
Cdd:cd18788   63 -----------------------SRGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDLEYLRDKG 119
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 442615242 670 nqLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILLCDSRF 711
Cdd:cd18788  120 --LLTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
12-752 1.59e-53

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 198.23  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  12 HFP-FEPYPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRTRQSehqkqmvkmekadfsglgggapggd 90
Cdd:COG1199    9 AFPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAARETGK------------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  91 lselaktmgrannwgvpKVIYASRTHSQLTQAMRE----LKRTAYANMRSVVL-GSRDQLCIHP--EVMREQGNSNKTNM 163
Cdd:COG1199   64 -----------------KVVISTATKALQEQLVEKdlplLRKALGLPLRVALLkGRSNYLCLRRleQALQEGDDLDDEEL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 164 CKLRVHSktcsFQMRVESRkDHPDLRGPTIMDIEDLVKV------GQR---LKICPYFASRELVPQADITFMPYNYLLDP 234
Cdd:COG1199  127 LLARILA----WASETWTG-DRDELPLPEDDELWRQVTSdadnclGRRcpyYGVCPYELARRLAREADVVVVNHHLLFAD 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 235 KARKaNKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQDMAGDepkdftlddltllke 314
Cdd:COG1199  202 LALG-EELLPEDDVLIIDEAHNLPDRARDMFSAELSSRSLLRLLRELRKLGLRPGLKKLLDLLER--------------- 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 315 mllelekaidaivVDNAVDGTTFPASMMYELLGKANFTYGNVATIVSLLDKLVQYLLVASQQMSirkggTFTLLSDLLTI 394
Cdd:COG1199  266 -------------LREALDDLFLALEEEEELRLALGELPDEPEELLEALDALRDALEALAEALE-----EELERLAELDA 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 395 VFANKEDVMSKVYasfkvHVLVEESKQGHGKqqgakqqggWL---GKGTIAAATGLSkVAKIInfwcfnpgfgmEQLLNT 471
Cdd:COG1199  328 LLERLEELLFALA-----RFLRIAEDEGYVR---------WLereGGDVRLHAAPLD-PADLL-----------RELLFS 381
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 472 QVRSVILTSGTLAPLKP---LIAELAIPvaqhlENPHIVD---------QSQVYVkiigtgPDRqqlISNYANRDNpkYI 539
Cdd:COG1199  382 RARSVVLTSATLSVGGPfdyFARRLGLD-----EDARTLSlpspfdyenQALLYV------PRD---LPRPSDRDG--YL 445
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 540 SSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASglwadisCKKPIFLEPR-SKDQFtstMEEFyqaiRDSKGAVf 618
Cdd:COG1199  446 EAIAEAIAELLEASGGNTLVLFTSYRALEQVAELLRER-------LDIPVLVQGDgSREAL---LERF----REGGNSV- 510
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 619 mAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANrtrenqllSGQEWYNLDATRAVN---QAIGRVI 695
Cdd:COG1199  511 -LVGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPVLEARREALEAR--------GGNGFMYAYLPPAVIklkQGAGRLI 581
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442615242 696 RHRNDYGAILLCDSRFKDASQVQQLSKWIrghlgdrpqcsPFGPIVR--ELRQFFKNAE 752
Cdd:COG1199  582 RSEEDRGVVVLLDRRLLTKRYGKRFLDSL-----------PPFRRTRpeELRAFLERLD 629
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
896-985 5.46e-22

harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin.


Pssm-ID: 259826 [Multi-domain]  Cd Length: 99  Bit Score: 91.57  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 896 EPSSSQAKEAPEERAAFLRELRSLVTQDQFRRFGKALLEYKNGTyeSFQALMAILLDVLSAPKVRYMLVGMRKYLKNEHK 975
Cdd:cd13932    7 ASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGD--DFEQLLAVLAELFAEPERHPLLRGFRRFVRPHHK 84
                         90
                 ....*....|
gi 442615242 976 DEFDRRVGNL 985
Cdd:cd13932   85 KEFDERCKSL 94
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
474-715 5.35e-09

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 60.35  E-value: 5.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 474 RSVILTSGTLA---PLKPLIAELAI----PVAQHLENP-HIVDQSQVYVkiigtgPDRQQLISNyanRDNPKYISSLGQT 545
Cdd:PRK08074 673 KSVILTSATLTvngSFDYIIERLGLedfyPRTLQIPSPfSYEEQAKLMI------PTDMPPIKD---VPIEEYIEEVAAY 743
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 546 ILNVARIVPDGLLVFFPSYPMLNKCVDAWQasglwaDISCKKPIFL-----EPRSKDQFTSTMEEFYQAIrdskgaVFma 620
Cdd:PRK08074 744 IAKIAKATKGRMLVLFTSYEMLKKTYYNLK------NEEELEGYVLlaqgvSSGSRARLTKQFQQFDKAI------LL-- 809
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 621 vcrGKVS--EGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANrtrenqllSGQEWYNLDATRAV---NQAIGRVI 695
Cdd:PRK08074 810 ---GTSSfwEGIDIPGDELSCLVIVRLPFAPPDQPVMEAKSEWAKEQ--------GENPFQELSLPQAVlrfKQGFGRLI 878
                        250       260
                 ....*....|....*....|
gi 442615242 696 RHRNDYGAILLCDSRFKDAS 715
Cdd:PRK08074 879 RTETDRGTVFVLDRRLTTTS 898
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
10-742 5.45e-140

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: 435.30  E-value: 5.45e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   10 PVHFPFEP-YPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRtRQSEHQKqmvkmekadfsglgggapg 88
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQ-EKPEVRK------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   89 gdlselaktmgrannwgvpkVIYASRTHSQLTQAMRELKRTAYA---------NMRSVVLGSRDQLCIHPEVMREQGNSN 159
Cdd:TIGR00604  63 --------------------IIYASRTHSQLEQATEELRKLMSYrtprigeesPVSGLSLASRKNLCLHPEVSKERQGKV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  160 KTNMCKLRVHSK------------TCSFQMRVESRKDHPDLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMP 227
Cdd:TIGR00604 123 VNGKCIKLTVSKikeqrtekpnveSCEFYENFDELREVEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  228 YNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQD--MAGDEPKDFT 305
Cdd:TIGR00604 203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDarKLLDELQKLV 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  306 L---DDLTLLKEMLLELEKAIDAIVVDNAVDGTTFPASMMYELL---GKANFTYGNVATIVSLLDKLVQYLLVASQQMSI 379
Cdd:TIGR00604 283 EglkQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRIAEIFLHKLsryLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  380 RKGGTFTLLSDLL-TIVFANKEDVMSKV-YASFKVHVLVEESKQGHGKQQGAKQqggwlgkgtiaAATGLskvakIINFW 457
Cdd:TIGR00604 363 PLRFCSERLSNLLrELEITHPEDFSALVlLFTFATLVLTYTNGFLEGIEPYENK-----------TVPNP-----ILKFM 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  458 CFNPGFGMEQLLNtQVRSVILTSGTLAPLKPLIAELAIPVAQHLENPHIVDQSQVYVKIIGTGPDRQQLISNYANRDNPK 537
Cdd:TIGR00604 427 CLDPSIALKPLFE-RVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPS 505
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  538 YISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASGLWADISCKKPIFLEPRSKDQFTSTMEEFYQAIRDSKGAV 617
Cdd:TIGR00604 506 LVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSEGRGAV 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  618 FMAVCRGKVSEGLDFADRNGRAVIITGLPFPplkdpkVILKRRYLEANRTRE--NQLLSGQEWYNLDATRAVNQAIGRVI 695
Cdd:TIGR00604 586 LLSVAGGKVSEGIDFCDDLGRAVIMVGIPYE------YTESRILLARLEFLRdqYPIRENQDFYEFDAMRAVNQAIGRVI 659
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 442615242  696 RHRNDYGAILLCDSRFKDASQVQQLSKWIRGHLGDRPQcspFGPIVR 742
Cdd:TIGR00604 660 RHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDL---NGMAIS 703
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
111-274 1.37e-78

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: 253.34  E-value: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  111 YASRTHSQLTQAMRELKRTAYA-NMRSVVLGSRDQLCIHPEVMREQGNSNKTNMCKLRVHSK---TCSFQMRVESRKDHP 186
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYkKIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKargSCPFYNNLEDLLKLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  187 DLRGPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIEKICEESAS 266
Cdd:pfam06733  81 DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCIESAS 160

                  ....*...
gi 442615242  267 VQIKSSDV 274
Cdd:pfam06733 161 FSISRSQL 168
DEXDc2 smart00488
DEAD-like helicases superfamily;
9-292 5.18e-70

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 234.58  E-value: 5.18e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242     9 IPVHFPFEPYPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRtRQSEHQKQMVKMEKADFsglgggapg 88
Cdd:smart00488   1 LLFYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLR-SFPERIQKIKLIYLSRT--------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242    89 gdLSELAKTMGRANNWGVPKVIYASRTHSQLTQAMRELKRTAYANmRSVVLGSRDQLCIHPEVMREQGNSNKTN------ 162
Cdd:smart00488  71 --VSEIEKRLEELRKLMQKVEYESDEESEKQAQLLHELGREKPKV-LGLSLTSRKNLCLNPEVRTLKQNGLVVDevcrsl 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   163 ----MCKLRVHS---KTCSFQMRVESRKDHPDLRgPTIMDIEDLVKVGQRLKICPYFASRELVPQADITFMPYNYLLDPK 235
Cdd:smart00488 148 taskARKYRYENpkvERCPFYENTEFLLVRDLLP-AEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPK 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 442615242   236 ARKANKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDvthIMQVFASGE 292
Cdd:smart00488 227 IRQALSIELKDSIVIFDEAHNLDNVCISALSSELSRRSLERAHKN---IKKYFERIE 280
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
510-711 8.13e-67

C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. 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: 350175 [Multi-domain]  Cd Length: 159  Bit Score: 220.94  E-value: 8.13e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 510 SQVYVKIIGTGPDRQQLISNYANRDNPKYISSLGQTILNVARIVPDGLLVFFPSYPMLNKCVdawqasglwadisckkpi 589
Cdd:cd18788    1 DQVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVV------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 590 fleprskdqftstmeefyqairdSKGAVFMAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANRTRE 669
Cdd:cd18788   63 -----------------------SRGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDLEYLRDKG 119
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 442615242 670 nqLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILLCDSRF 711
Cdd:cd18788  120 --LLTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
547-725 6.41e-65

Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.


Pssm-ID: 463840 [Multi-domain]  Cd Length: 168  Bit Score: 215.89  E-value: 6.41e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  547 LNVARIVPDGLLVFFPSYPMLNKCVDAWQASGLWAdiscKKPIFLEPRSKDqFTSTMEEFYQAirdSKGAVFMAVCRGKV 626
Cdd:pfam13307   1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEK----GIEIFVQPGEGS-REKLLEEFKKK---GKGAVLFGVCGGSF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  627 SEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEanrtrENQLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILL 706
Cdd:pfam13307  73 SEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLD-----SKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVL 147
                         170
                  ....*....|....*....
gi 442615242  707 CDSRFKDASQVQQLSKWIR 725
Cdd:pfam13307 148 LDSRFLTKRYGKLLPKWLP 166
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
35-258 1.61e-55

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: 190.25  E-value: 1.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  35 GTNGVLESPTGTGKTLSLLCSSLAWirtrqSEHQKQMVKMEKADFSGLGggapggdlselaktmgrannwGVPKVIYASR 114
Cdd:cd17970    1 GQNALLESPTGTGKTLSLLCSTLAW-----RQSLKGKATSEGSDGGGSG---------------------KIPKIIYASR 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 115 THSQLTQAMRELKRTAYANMRSVVLGSRDQLCIHPeVMREQGNSNKTNMCklrvhsktcsfqmrvesrkdhpdlrgptim 194
Cdd:cd17970   55 THSQLAQVVRELKRTAYKRPRMTILGSRDHLCIHP-VINKLSNQNANEAC------------------------------ 103
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442615242 195 diedlvkvgqrlkiCPYFASRElvpQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIE 258
Cdd:cd17970  104 --------------MALLSGKN---EADLVFCPYNYLLDPNIRRSMGLNLKGSVVIFDEAHNIE 150
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
12-752 1.59e-53

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 198.23  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  12 HFP-FEPYPVQRAYMEKVIHCLRDGTNGVLESPTGTGKTLSLLCSSLAWIRTRQSehqkqmvkmekadfsglgggapggd 90
Cdd:COG1199    9 AFPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLVPALLAARETGK------------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  91 lselaktmgrannwgvpKVIYASRTHSQLTQAMRE----LKRTAYANMRSVVL-GSRDQLCIHP--EVMREQGNSNKTNM 163
Cdd:COG1199   64 -----------------KVVISTATKALQEQLVEKdlplLRKALGLPLRVALLkGRSNYLCLRRleQALQEGDDLDDEEL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 164 CKLRVHSktcsFQMRVESRkDHPDLRGPTIMDIEDLVKV------GQR---LKICPYFASRELVPQADITFMPYNYLLDP 234
Cdd:COG1199  127 LLARILA----WASETWTG-DRDELPLPEDDELWRQVTSdadnclGRRcpyYGVCPYELARRLAREADVVVVNHHLLFAD 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 235 KARKaNKIELGNTIVILDEAHNIEKICEESASVQIKSSDVAMAIEDVTHIMQVFASGESQDMAGDepkdftlddltllke 314
Cdd:COG1199  202 LALG-EELLPEDDVLIIDEAHNLPDRARDMFSAELSSRSLLRLLRELRKLGLRPGLKKLLDLLER--------------- 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 315 mllelekaidaivVDNAVDGTTFPASMMYELLGKANFTYGNVATIVSLLDKLVQYLLVASQQMSirkggTFTLLSDLLTI 394
Cdd:COG1199  266 -------------LREALDDLFLALEEEEELRLALGELPDEPEELLEALDALRDALEALAEALE-----EELERLAELDA 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 395 VFANKEDVMSKVYasfkvHVLVEESKQGHGKqqgakqqggWL---GKGTIAAATGLSkVAKIInfwcfnpgfgmEQLLNT 471
Cdd:COG1199  328 LLERLEELLFALA-----RFLRIAEDEGYVR---------WLereGGDVRLHAAPLD-PADLL-----------RELLFS 381
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 472 QVRSVILTSGTLAPLKP---LIAELAIPvaqhlENPHIVD---------QSQVYVkiigtgPDRqqlISNYANRDNpkYI 539
Cdd:COG1199  382 RARSVVLTSATLSVGGPfdyFARRLGLD-----EDARTLSlpspfdyenQALLYV------PRD---LPRPSDRDG--YL 445
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 540 SSLGQTILNVARIVPDGLLVFFPSYPMLNKCVDAWQASglwadisCKKPIFLEPR-SKDQFtstMEEFyqaiRDSKGAVf 618
Cdd:COG1199  446 EAIAEAIAELLEASGGNTLVLFTSYRALEQVAELLRER-------LDIPVLVQGDgSREAL---LERF----REGGNSV- 510
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 619 mAVCRGKVSEGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANrtrenqllSGQEWYNLDATRAVN---QAIGRVI 695
Cdd:COG1199  511 -LVGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPVLEARREALEAR--------GGNGFMYAYLPPAVIklkQGAGRLI 581
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442615242 696 RHRNDYGAILLCDSRFKDASQVQQLSKWIrghlgdrpqcsPFGPIVR--ELRQFFKNAE 752
Cdd:COG1199  582 RSEEDRGVVVLLDRRLLTKRYGKRFLDSL-----------PPFRRTRpeELRAFLERLD 629
HELICc2 smart00491
helicase superfamily c-terminal domain;
564-713 2.67e-43

helicase superfamily c-terminal domain;


Pssm-ID: 214694 [Multi-domain]  Cd Length: 142  Bit Score: 153.97  E-value: 2.67e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   564 YPMLNKCVDAWQASGLwadISCKKPIFLEPRSKDQFTSTMEEFYQAIrDSKGAVFMAVCRGKVSEGLDFADRNGRAVIIT 643
Cdd:smart00491   1 YRYLEQVVEYWKENGI---LEINKPVFIEGKDSGETEELLEKYSAAC-EARGALLLAVARGKVSEGIDFPDDLGRAVIIV 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242   644 GLPFPPLKDPKVILKRRYLEanrtRENQLLSGQEWYNLDATRAVNQAIGRVIRHRNDYGAILLCDSRFKD 713
Cdd:smart00491  77 GIPFPNPDSPILRARLEYLD----EKGGIRPFDEVYLFDAMRALAQAIGRAIRHKNDYGVVVLLDKRYAR 142
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
38-258 2.13e-22

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: 94.03  E-value: 2.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  38 GVLESPTGTGKTLSLLCSSLAWirtrQSEHQKqmvkmekadfsglgggapggdlselaktmgrannwgvPKVIYASRTHS 117
Cdd:cd17915    4 VALESPTGSGKTLSLLCSALSY----QREFHK-------------------------------------TKVLYCSRTHS 42
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 118 QLTQAMRELKRTAYA-NMRSVVLGSRDqlcihpevmreqgnsnktnmcklrvhsktcsfqmrvesrkdhpdlrgptimdi 196
Cdd:cd17915   43 QIEQIIRELRKLLEKrKIRALALSSRD----------------------------------------------------- 69
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442615242 197 edlvkvgqrlkicpyfasrelvpqADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIE 258
Cdd:cd17915   70 ------------------------ADIVVLPYPYLLDARIREFIGIDLREQVVIIDEAHNLD 107
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
896-985 5.46e-22

harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); Mouse Rtel is an essential protein required for the maintenance of both telomeric and genomic stability. RTEL1 appears to maintain genome stability by suppressing homologous recombination (HR). In vitro, purified human and insect RTEL1 have been shown to promote the disassembly of D loop recombination intermediates, in a reaction dependent upon ATP hydrolysis. Human RTEL1 is implicated in the etiology of Dyskeratosis congenital (DC, is an inherited bone marrow failure and cancer predisposition syndrome). Point mutations in its helicase domains, and truncations which result in loss of its C-terminus have been discovered in DC families. RTEL1 is also a candidate gene influencing glioma susceptibility. The C-terminal domain of RTEL1, represented here, appears similar to the N-terminal domain of the scaffolding protein harmonin.


Pssm-ID: 259826 [Multi-domain]  Cd Length: 99  Bit Score: 91.57  E-value: 5.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 896 EPSSSQAKEAPEERAAFLRELRSLVTQDQFRRFGKALLEYKNGTyeSFQALMAILLDVLSAPKVRYMLVGMRKYLKNEHK 975
Cdd:cd13932    7 ASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGD--DFEQLLAVLAELFAEPERHPLLRGFRRFVRPHHK 84
                         90
                 ....*....|
gi 442615242 976 DEFDRRVGNL 985
Cdd:cd13932   85 KEFDERCKSL 94
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
35-261 5.16e-12

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: 64.26  E-value: 5.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  35 GTNGVLESPTGTGKTLSLLCSSLAWIrtrqsehqkqmvkmekadfsglgggapggdlselaktmgrannwgvPKVIYASR 114
Cdd:cd17968    1 GKVGIFESPTGTGKSLSLICGALTWL----------------------------------------------TKIYYCSR 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 115 THSQLTQAMRELKRTAYA-NMRSVVLGSRDqlcihpevmreqgnsnktnmcklrvhsktcsfqmrvesrkdhpdlrgpti 193
Cdd:cd17968   35 THSQLAQFVHEVQKSPFGkDVRLVSLGSRQ-------------------------------------------------- 64
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615242 194 mdiedlvkvgqrlkicpyfasrelvPQADITFMPYNYLLDPKARKANKIELGNTIVILDEAHNIekIC 261
Cdd:cd17968   65 -------------------------PAAQVVVLPYQMLLHAATRKASGIKLKDQVVIIDEAHNL--IC 105
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
474-715 5.35e-09

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 60.35  E-value: 5.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 474 RSVILTSGTLA---PLKPLIAELAI----PVAQHLENP-HIVDQSQVYVkiigtgPDRQQLISNyanRDNPKYISSLGQT 545
Cdd:PRK08074 673 KSVILTSATLTvngSFDYIIERLGLedfyPRTLQIPSPfSYEEQAKLMI------PTDMPPIKD---VPIEEYIEEVAAY 743
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 546 ILNVARIVPDGLLVFFPSYPMLNKCVDAWQasglwaDISCKKPIFL-----EPRSKDQFTSTMEEFYQAIrdskgaVFma 620
Cdd:PRK08074 744 IAKIAKATKGRMLVLFTSYEMLKKTYYNLK------NEEELEGYVLlaqgvSSGSRARLTKQFQQFDKAI------LL-- 809
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 621 vcrGKVS--EGLDFADRNGRAVIITGLPFPPLKDPKVILKRRYLEANrtrenqllSGQEWYNLDATRAV---NQAIGRVI 695
Cdd:PRK08074 810 ---GTSSfwEGIDIPGDELSCLVIVRLPFAPPDQPVMEAKSEWAKEQ--------GENPFQELSLPQAVlrfKQGFGRLI 878
                        250       260
                 ....*....|....*....|
gi 442615242 696 RHRNDYGAILLCDSRFKDAS 715
Cdd:PRK08074 879 RTETDRGTVFVLDRRLTTTS 898
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
470-503 1.26e-05

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: 46.96  E-value: 1.26e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 442615242 470 NTQVRSVILTSGTLAPLKPLIAELAIPVAQHLEN 503
Cdd:cd17970  148 NIEVRTIILTSGTLSPLDSFASELGTKFPIRLEN 181
harmonin_N_like cd07347
N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin ...
905-982 2.01e-05

N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin homology domain); This domain is found in harmonin, and similar proteins such as delphilin, and whirlin. These are postsynaptic density-95/discs-large/ZO-1 (PDZ) domain-containing scaffold proteins. Harmonin and whirlin are organizers of the Usher protein network of the inner ear and the retina, delphilin is found at the cerebellar parallel fiber-Purkinje cell synapses. This domain is also found in CCM2 (also called malcavernin; C7orf22/chromosome 7 open reading frame 22; OSM). CCM2 along with CCM1 and CCM3 constitutes a set of proteins which when mutated are responsible for cerebral cavernous malformations, an autosomal dominant neurovascular disease characterized by cerebral hemorrhages and vascular malformations in the central nervous system. CCM2 plays many functional roles. CCM2 functions as a scaffold involved in small GTPase Rac-dependent p38 mitogen-activated protein kinase (MAPK) activation when the cell is under hyperosmotic stress. It associates with CCM1 in the signaling cascades that regulate vascular integrity and participates in HEG1 (the transmembrane receptor heart of glass 1) mediated endothelial cell junctions. CCM proteins also inhibit the activation of small GTPase RhoA and its downstream effector Rho kinase (ROCK) to limit vascular permeability. CCM2 mediates TrkA-dependent cell death via its N-terminal PTB domain in pediatric neuroblastic tumours; the C-terminal domain of malcavernin represented here has also been refered to as the Karet domain. Harmonin contains a single copy of this domain at its N-terminus which binds specifically to a short internal peptide fragment of the cadherin 23 cytoplasmic domain (a component of the Usher protein network). Whirlin contains two copies of this domain; the first of these has been assayed for interaction with the cytoplasmic domain of cadherin 23 and no interaction could be detected.


Pssm-ID: 259818  Cd Length: 78  Bit Score: 43.73  E-value: 2.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615242 905 APEERAAFLRELRSLVTQDQFRRFGKALLEYKNGtyESFQALMAILLDVLSAPKVRYMLVGMRKYLKNEHKDEFDRRV 982
Cdd:cd07347    1 RRELARLFSEQADQLLTDQERAYVTQALSEYRKG--RSVEALVADLFPVLDTPAKLSLLQGLRSLIPPKDQQRFDELV 76
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
31-258 9.53e-04

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: 40.88  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242  31 CLRDGTNGVLESPTGTGKTLSLLCSSLAWIRTRQSEhqkqmvkmekadfsglgggapggdlselaktmgrannwgVPKVI 110
Cdd:cd17969    6 TLDAKGHCVLEMPSGTGKTVSLLSLIVAYQKAYPLE---------------------------------------VTKLI 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 111 YASRTHSQLTQAMRELKR-TAYanmrsvvlgsrdqlcihpevmREQGNSNKTNMCKLRVHSKtcsfqmrvesrkdhpdlr 189
Cdd:cd17969   47 YCSRTVPEIEKVVEELRKlMDY---------------------YEKQTGEKPNFLGLALSSR------------------ 87
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615242 190 gptimdiedlvkvgqrlkicpyfasrelvpQADITFMPYNYLLDPKARKANKIELG-NTIVILDEAHNIE 258
Cdd:cd17969   88 ------------------------------HANVVVYSYHYLLDPKIAELVSKELSkKSVVVFDEAHNID 127
DEXDc smart00487
DEAD-like helicases superfamily;
9-53 9.96e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 41.32  E-value: 9.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 442615242     9 IPVHFPFEPYPVQRAYMEKVIHCLRDGtngVLESPTGTGKTLSLL 53
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV---ILAAPTGSGKTLAAL 42
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
13-50 4.09e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 40.78  E-value: 4.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 442615242  13 FPFEPYPVQRAYMEKVIHCL-RDGTNGVLESPTGTGKTL 50
Cdd:COG1061   77 TSFELRPYQQEALEALLAALeRGGGRGLVVAPTGTGKTV 115
 
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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