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Conserved domains on  [gi|568920270|ref|XP_006500703|]
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regulator of telomere elongation helicase 1 isoform X3 [Mus musculus]

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 ...
10-743 2.55e-142

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: 447.63  E-value: 2.55e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    10 TVDFPFQP-YPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVsslkiaervqgelfasrtlss 88
Cdd:TIGR00604    3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKPEVR--------------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    89 wgsaaaasgdsiecytdipKIIYASRTHSQLTQVIRELRNT--AYRP--------KVCVLGSREQLCIHPEVKKQ----E 154
Cdd:TIGR00604   62 -------------------KIIYASRTHSQLEQATEELRKLmsYRTPrigeespvSGLSLASRKNLCLHPEVSKErqgkV 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   155 SNHMQISLCRKK--------VASRSCHFYNNVEAKFLEQDLA-TPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMP 225
Cdd:TIGR00604  123 VNGKCIKLTVSKikeqrtekPNVESCEFYENFDELREVEDLLlSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   226 YNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRDVASGleiINQVLEEQARVTQQGELQQEFIVDTSS 305
Cdd:TIGR00604  203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRC---SKEIAEYFEKIEERKEVDARKLLDELQ 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   306 SGL-NMELEDIAKLKMILLR---LEEAIDAVQLPGDDRgvtKPGSYIFEL--FAEA-QITFQTKGCILESLDQIIQHLAG 378
Cdd:TIGR00604  280 KLVeGLKQEDLLTDEDIFLAnpvLPKEVLPEAVPGNIR---IAEIFLHKLsrYLEYlKDALKVLGVVSELPDAFLEHLKE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   379 RTGVF-TNTAGLQKLMDIIQIVFSVDPPEGSPGSLVglgISHSYKVHIHPETSHRRAAKRSDAWSTtasrkqGKVLSYWC 457
Cdd:TIGR00604  357 KTFIDrPLRFCSERLSNLLRELEITHPEDFSALVLL---FTFATLVLTYTNGFLEGIEPYENKTVP------NPILKFMC 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   458 FSPSQSMRELVCQgVRTLILTSGTLAPLSSFALEMQIPFPVCLENPHIIDKNQLWVGIVPRGPDGVQLSSAYDKRFSEEC 537
Cdd:TIGR00604  428 LDPSIALKPLFER-VRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPSL 506
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   538 LSSLGKALSNIARVVPHGLLVFFPSYPVMEKSLEFWQVQGLARKVEALKPLFVEPRNKGSFSEVIDAYYQQVASpaSNGA 617
Cdd:TIGR00604  507 VRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSE--GRGA 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   618 TFLAVCRGKASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFL-DEMRGRsgvggqclSGQEWYQQQASRAVNQAIG 696
Cdd:TIGR00604  585 VLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLrDQYPIR--------ENQDFYEFDAMRAVNQAIG 656
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*..
gi 568920270   697 RVIRHRHDYGAIFLCDHRFAYADARAQLPSWVRPYLKVYDNFGHVIR 743
Cdd:TIGR00604  657 RVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNGMAIS 703
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
877-976 1.25e-33

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: 125.08  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  877 KVRLVNHPEEPMAGTQAGRAKMFMVAVKQALSQANFDTFTQALQHYKSSDDFEALVASLTCLFAEdPKKHTLLKGFYQFV 956
Cdd:cd13932     1 KKSSVSASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFAE-PERHPLLRGFRRFV 79
                          90       100
                  ....*....|....*....|
gi 568920270  957 RPHHKQQFEDICFQLTGQRC 976
Cdd:cd13932    80 RPHHKKEFDERCKSLTGAGC 99
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
993-1081 4.03e-27

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: 106.20  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  993 VEKPGQPAVSDYLSDVHKALGSASCNQLTAALRAYKQDDDLDKVVAVVAALTTaKPEHLPLLQRFGMFVRRHHKPQFLQT 1072
Cdd:cd13932    12 GAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFA-EPERHPLLRGFRRFVRPHHKKEFDER 90

                  ....*....
gi 568920270 1073 CADLMGLPT 1081
Cdd:cd13932    91 CKSLTGAGC 99
COG2888 COG2888
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ...
1164-1205 4.47e-03

Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];


:

Pssm-ID: 442134 [Multi-domain]  Cd Length: 52  Bit Score: 36.63  E-value: 4.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920270 1164 VCPAC----ATEDTVLFQCPSCD---FYRCWACwKLQLQASRLCPACGA 1205
Cdd:COG2888     2 VCPSCgreiAPEGGVAFYCPNCGealIIRCPKC-RKQSNALYFCPKCGF 49
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
10-743 2.55e-142

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: 447.63  E-value: 2.55e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    10 TVDFPFQP-YPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVsslkiaervqgelfasrtlss 88
Cdd:TIGR00604    3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKPEVR--------------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    89 wgsaaaasgdsiecytdipKIIYASRTHSQLTQVIRELRNT--AYRP--------KVCVLGSREQLCIHPEVKKQ----E 154
Cdd:TIGR00604   62 -------------------KIIYASRTHSQLEQATEELRKLmsYRTPrigeespvSGLSLASRKNLCLHPEVSKErqgkV 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   155 SNHMQISLCRKK--------VASRSCHFYNNVEAKFLEQDLA-TPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMP 225
Cdd:TIGR00604  123 VNGKCIKLTVSKikeqrtekPNVESCEFYENFDELREVEDLLlSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   226 YNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRDVASGleiINQVLEEQARVTQQGELQQEFIVDTSS 305
Cdd:TIGR00604  203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRC---SKEIAEYFEKIEERKEVDARKLLDELQ 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   306 SGL-NMELEDIAKLKMILLR---LEEAIDAVQLPGDDRgvtKPGSYIFEL--FAEA-QITFQTKGCILESLDQIIQHLAG 378
Cdd:TIGR00604  280 KLVeGLKQEDLLTDEDIFLAnpvLPKEVLPEAVPGNIR---IAEIFLHKLsrYLEYlKDALKVLGVVSELPDAFLEHLKE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   379 RTGVF-TNTAGLQKLMDIIQIVFSVDPPEGSPGSLVglgISHSYKVHIHPETSHRRAAKRSDAWSTtasrkqGKVLSYWC 457
Cdd:TIGR00604  357 KTFIDrPLRFCSERLSNLLRELEITHPEDFSALVLL---FTFATLVLTYTNGFLEGIEPYENKTVP------NPILKFMC 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   458 FSPSQSMRELVCQgVRTLILTSGTLAPLSSFALEMQIPFPVCLENPHIIDKNQLWVGIVPRGPDGVQLSSAYDKRFSEEC 537
Cdd:TIGR00604  428 LDPSIALKPLFER-VRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPSL 506
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   538 LSSLGKALSNIARVVPHGLLVFFPSYPVMEKSLEFWQVQGLARKVEALKPLFVEPRNKGSFSEVIDAYYQQVASpaSNGA 617
Cdd:TIGR00604  507 VRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSE--GRGA 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   618 TFLAVCRGKASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFL-DEMRGRsgvggqclSGQEWYQQQASRAVNQAIG 696
Cdd:TIGR00604  585 VLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLrDQYPIR--------ENQDFYEFDAMRAVNQAIG 656
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*..
gi 568920270   697 RVIRHRHDYGAIFLCDHRFAYADARAQLPSWVRPYLKVYDNFGHVIR 743
Cdd:TIGR00604  657 RVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNGMAIS 703
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
111-272 3.14e-73

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: 240.63  E-value: 3.14e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   111 YASRTHSQLTQVIRELRNTAY--RPKVCVLGSREQLCIHPEVKKQESNHMQISLCRKKVASR---SCHFYNNV-EAKFLE 184
Cdd:pfam06733    1 YCSRTHSQLEQVVKELRRLPYykKIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKargSCPFYNNLeDLLKLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   185 QDLATPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESAS 264
Cdd:pfam06733   81 DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCIESAS 160

                   ....*...
gi 568920270   265 FDLTPRDV 272
Cdd:pfam06733  161 FSISRSQL 168
DEXDc2 smart00488
DEAD-like helicases superfamily;
9-285 3.88e-69

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 233.81  E-value: 3.88e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270      9 VTVDFPFQPYPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVSSLKIAERVQGELFASRTLSS 88
Cdd:smart00488    1 LLFYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIQKIKLIYLSRTVSEIEKRLEE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270     89 WGSAAAasgdsiecytdiPKIIYASRTHSQLTQVIRELRNTAYRPKVCVLGSREQLCIHPEVKKQESNH-MQISLCRKKV 167
Cdd:smart00488   81 LRKLMQ------------KVEYESDEESEKQAQLLHELGREKPKVLGLSLTSRKNLCLNPEVRTLKQNGlVVDEVCRSLT 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    168 ASR------------SCHFYNNVEAKFLEQDLATPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMPYNYLLDAKSR 235
Cdd:smart00488  149 ASKarkyryenpkveRCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIR 228
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 568920270    236 KAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRDVASGLEIINQVLEE 285
Cdd:smart00488  229 QALSIELKDSIVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFER 278
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
509-715 8.94e-63

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: 210.54  E-value: 8.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  509 NQLWVGIVPRGPDGVQLSSAYDKRFSEECLSSLGKALSNIARVVPHGLLVFFPSYPVMEkslefwqvqglarkvealkpl 588
Cdd:cd18788     1 DQVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYME--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  589 fveprnkgsfsEVIdayyqqvaspaSNGATFLAVCRGKASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFLDEMRG 668
Cdd:cd18788    60 -----------RVV-----------SRGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDLEYLRD 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568920270  669 RSGvggqcLSGQEWYQQQASRAVNQAIGRVIRHRHDYGAIFLCDHRF 715
Cdd:cd18788   118 KGL-----LTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
13-738 2.49e-45

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 174.34  E-value: 2.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   13 FP-FQPYPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLcstlawqqhlrdaVSSLKIAeRVQGElfasrtlsswgs 91
Cdd:COG1199    10 FPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYL-------------VPALLAA-RETGK------------ 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   92 aaaasgdsiecytdipKIIYASRTHSQLTQVI-REL----RNTAYRPKVCVLGSREQ-LCIHP--EVKKQESNHMQISLC 163
Cdd:COG1199    64 ----------------KVVISTATKALQEQLVeKDLpllrKALGLPLRVALLKGRSNyLCLRRleQALQEGDDLDDEELL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  164 RKKVASRSchfynnveAKFLEQDLATPILDIEDLVK----------NGSK---QKMCPYYLSRNMKQQADIIFMPYNYLL 230
Cdd:COG1199   128 LARILAWA--------SETWTGDRDELPLPEDDELWrqvtsdadncLGRRcpyYGVCPYELARRLAREADVVVVNHHLLF 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  231 DAKSRKAHSIDlKGTVVIFDEAHNVEKICEESASFDLTPRDVasgLEIINQVLEEQARvtqqgelqqefivdtsssglnm 310
Cdd:COG1199   200 ADLALGEELLP-EDDVLIIDEAHNLPDRARDMFSAELSSRSL---LRLLRELRKLGLR---------------------- 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  311 elEDIAKLKMILLRLEEAIDAvqlpgddrgvtkpgsyIFELFAEAQITFQTKGCILESLDQIIQHLAGrtgvftntagLQ 390
Cdd:COG1199   254 --PGLKKLLDLLERLREALDD----------------LFLALEEEEELRLALGELPDEPEELLEALDA----------LR 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  391 KLMDIIQIVFsvdppEGSPGSLVGLGISHSYKVHIHPETSHRRAAKRSDAWSTTASRKQGKV-LSYWCFSPSQSMRELVC 469
Cdd:COG1199   306 DALEALAEAL-----EEELERLAELDALLERLEELLFALARFLRIAEDEGYVRWLEREGGDVrLHAAPLDPADLLRELLF 380
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  470 QGVRTLILTSGTLAPLSSF------------ALEMQI--PFPvclenphiiDKNQLwVGIVPRGPdgvqlsSAYDKRfsE 535
Cdd:COG1199   381 SRARSVVLTSATLSVGGPFdyfarrlgldedARTLSLpsPFD---------YENQA-LLYVPRDL------PRPSDR--D 442
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  536 ECLSSLGKALSNIARVVPHGLLVFFPSYPVMEKSLEfwqvqGLARKVEalKPLFVEPRnkGSFSEVIDAYyqqvaspASN 615
Cdd:COG1199   443 GYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE-----LLRERLD--IPVLVQGD--GSREALLERF-------REG 506
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  616 GATFLaVCRGKASEGLDFSdmnG---RGVIVTGLPYPPRMDPRVVLKMQFLDEmRGRSGVggqclsgQEWYQQQASRAVN 692
Cdd:COG1199   507 GNSVL-VGTGSFWEGVDLP---GdalSLVIIVKLPFPPPDDPVLEARREALEA-RGGNGF-------MYAYLPPAVIKLK 574
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920270  693 QAIGRVIRHRHDYGAIFLCDHRFA---YADA-RAQLPSWVRPYLKVYDNF 738
Cdd:COG1199   575 QGAGRLIRSEEDRGVVVLLDRRLLtkrYGKRfLDSLPPFRRTRPEELRAF 624
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
877-976 1.25e-33

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: 125.08  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  877 KVRLVNHPEEPMAGTQAGRAKMFMVAVKQALSQANFDTFTQALQHYKSSDDFEALVASLTCLFAEdPKKHTLLKGFYQFV 956
Cdd:cd13932     1 KKSSVSASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFAE-PERHPLLRGFRRFV 79
                          90       100
                  ....*....|....*....|
gi 568920270  957 RPHHKQQFEDICFQLTGQRC 976
Cdd:cd13932    80 RPHHKKEFDERCKSLTGAGC 99
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
993-1081 4.03e-27

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: 106.20  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  993 VEKPGQPAVSDYLSDVHKALGSASCNQLTAALRAYKQDDDLDKVVAVVAALTTaKPEHLPLLQRFGMFVRRHHKPQFLQT 1072
Cdd:cd13932    12 GAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFA-EPERHPLLRGFRRFVRPHHKKEFDER 90

                  ....*....
gi 568920270 1073 CADLMGLPT 1081
Cdd:cd13932    91 CKSLTGAGC 99
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
473-714 3.02e-03

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 41.86  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  473 RTLILTSGTLA------------PLSSFA-LEMQIPFPVCLEnphiiDKNQLwvgIVPRgpDGVQLSSAYDKRFSEEcls 539
Cdd:PRK08074  673 KSVILTSATLTvngsfdyiierlGLEDFYpRTLQIPSPFSYE-----EQAKL---MIPT--DMPPIKDVPIEEYIEE--- 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  540 sLGKALSNIARVVPHGLLVFFPSYpvmekslefwqvqglarkvEALKPLFVEPRNKGSFSEvidayYQQVASPASNGA-- 617
Cdd:PRK08074  740 -VAAYIAKIAKATKGRMLVLFTSY-------------------EMLKKTYYNLKNEEELEG-----YVLLAQGVSSGSra 794
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  618 ----TFL----AVCRGKAS--EGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFLDEmRGRSgvggqclSGQEWYQQQA 687
Cdd:PRK08074  795 rltkQFQqfdkAILLGTSSfwEGIDIPGDELSCLVIVRLPFAPPDQPVMEAKSEWAKE-QGEN-------PFQELSLPQA 866
                         250       260
                  ....*....|....*....|....*..
gi 568920270  688 SRAVNQAIGRVIRHRHDYGAIFLCDHR 714
Cdd:PRK08074  867 VLRFKQGFGRLIRTETDRGTVFVLDRR 893
COG2888 COG2888
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ...
1164-1205 4.47e-03

Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];


Pssm-ID: 442134 [Multi-domain]  Cd Length: 52  Bit Score: 36.63  E-value: 4.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920270 1164 VCPAC----ATEDTVLFQCPSCD---FYRCWACwKLQLQASRLCPACGA 1205
Cdd:COG2888     2 VCPSCgreiAPEGGVAFYCPNCGealIIRCPKC-RKQSNALYFCPKCGF 49
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
10-743 2.55e-142

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: 447.63  E-value: 2.55e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    10 TVDFPFQP-YPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVsslkiaervqgelfasrtlss 88
Cdd:TIGR00604    3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKPEVR--------------------- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    89 wgsaaaasgdsiecytdipKIIYASRTHSQLTQVIRELRNT--AYRP--------KVCVLGSREQLCIHPEVKKQ----E 154
Cdd:TIGR00604   62 -------------------KIIYASRTHSQLEQATEELRKLmsYRTPrigeespvSGLSLASRKNLCLHPEVSKErqgkV 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   155 SNHMQISLCRKK--------VASRSCHFYNNVEAKFLEQDLA-TPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMP 225
Cdd:TIGR00604  123 VNGKCIKLTVSKikeqrtekPNVESCEFYENFDELREVEDLLlSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLP 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   226 YNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRDVASGleiINQVLEEQARVTQQGELQQEFIVDTSS 305
Cdd:TIGR00604  203 YQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSLSSNLSVRSLKRC---SKEIAEYFEKIEERKEVDARKLLDELQ 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   306 SGL-NMELEDIAKLKMILLR---LEEAIDAVQLPGDDRgvtKPGSYIFEL--FAEA-QITFQTKGCILESLDQIIQHLAG 378
Cdd:TIGR00604  280 KLVeGLKQEDLLTDEDIFLAnpvLPKEVLPEAVPGNIR---IAEIFLHKLsrYLEYlKDALKVLGVVSELPDAFLEHLKE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   379 RTGVF-TNTAGLQKLMDIIQIVFSVDPPEGSPGSLVglgISHSYKVHIHPETSHRRAAKRSDAWSTtasrkqGKVLSYWC 457
Cdd:TIGR00604  357 KTFIDrPLRFCSERLSNLLRELEITHPEDFSALVLL---FTFATLVLTYTNGFLEGIEPYENKTVP------NPILKFMC 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   458 FSPSQSMRELVCQgVRTLILTSGTLAPLSSFALEMQIPFPVCLENPHIIDKNQLWVGIVPRGPDGVQLSSAYDKRFSEEC 537
Cdd:TIGR00604  428 LDPSIALKPLFER-VRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHILKRENLLTLIVTRGSDQVPLSSTFEIRNDPSL 506
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   538 LSSLGKALSNIARVVPHGLLVFFPSYPVMEKSLEFWQVQGLARKVEALKPLFVEPRNKGSFSEVIDAYYQQVASpaSNGA 617
Cdd:TIGR00604  507 VRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKKLIFVETKDAQETSDALERYKQAVSE--GRGA 584
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   618 TFLAVCRGKASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFL-DEMRGRsgvggqclSGQEWYQQQASRAVNQAIG 696
Cdd:TIGR00604  585 VLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLrDQYPIR--------ENQDFYEFDAMRAVNQAIG 656
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*..
gi 568920270   697 RVIRHRHDYGAIFLCDHRFAYADARAQLPSWVRPYLKVYDNFGHVIR 743
Cdd:TIGR00604  657 RVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNGMAIS 703
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
111-272 3.14e-73

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: 240.63  E-value: 3.14e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   111 YASRTHSQLTQVIRELRNTAY--RPKVCVLGSREQLCIHPEVKKQESNHMQISLCRKKVASR---SCHFYNNV-EAKFLE 184
Cdd:pfam06733    1 YCSRTHSQLEQVVKELRRLPYykKIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKargSCPFYNNLeDLLKLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   185 QDLATPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESAS 264
Cdd:pfam06733   81 DLLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCIESAS 160

                   ....*...
gi 568920270   265 FDLTPRDV 272
Cdd:pfam06733  161 FSISRSQL 168
DEXDc2 smart00488
DEAD-like helicases superfamily;
9-285 3.88e-69

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 233.81  E-value: 3.88e-69
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270      9 VTVDFPFQPYPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVSSLKIAERVQGELFASRTLSS 88
Cdd:smart00488    1 LLFYFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIQKIKLIYLSRTVSEIEKRLEE 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270     89 WGSAAAasgdsiecytdiPKIIYASRTHSQLTQVIRELRNTAYRPKVCVLGSREQLCIHPEVKKQESNH-MQISLCRKKV 167
Cdd:smart00488   81 LRKLMQ------------KVEYESDEESEKQAQLLHELGREKPKVLGLSLTSRKNLCLNPEVRTLKQNGlVVDEVCRSLT 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    168 ASR------------SCHFYNNVEAKFLEQDLATPILDIEDLVKNGSKQKMCPYYLSRNMKQQADIIFMPYNYLLDAKSR 235
Cdd:smart00488  149 ASKarkyryenpkveRCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIR 228
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|
gi 568920270    236 KAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRDVASGLEIINQVLEE 285
Cdd:smart00488  229 QALSIELKDSIVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFER 278
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
509-715 8.94e-63

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: 210.54  E-value: 8.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  509 NQLWVGIVPRGPDGVQLSSAYDKRFSEECLSSLGKALSNIARVVPHGLLVFFPSYPVMEkslefwqvqglarkvealkpl 588
Cdd:cd18788     1 DQVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYME--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  589 fveprnkgsfsEVIdayyqqvaspaSNGATFLAVCRGKASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFLDEMRG 668
Cdd:cd18788    60 -----------RVV-----------SRGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDLEYLRD 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568920270  669 RSGvggqcLSGQEWYQQQASRAVNQAIGRVIRHRHDYGAIFLCDHRF 715
Cdd:cd18788   118 KGL-----LTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
35-256 2.33e-60

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: 204.50  E-value: 2.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   35 KVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVSSLKIAERVQGElfasrtlsswgsaaaasgdsiecytdIPKIIYASR 114
Cdd:cd17970     1 GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATSEGSDGGGSGK--------------------------IPKIIYASR 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  115 THSQLTQVIRELRNTAY-RPKVCVLGSREQLCIHPEVKKqesnhmqislcrkkvasrschfynnveakfleqdlatpild 193
Cdd:cd17970    55 THSQLAQVVRELKRTAYkRPRMTILGSRDHLCIHPVINK----------------------------------------- 93
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920270  194 iedlVKNGSKQKMCPYYLSRnmKQQADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNVE 256
Cdd:cd17970    94 ----LSNQNANEACMALLSG--KNEADLVFCPYNYLLDPNIRRSMGLNLKGSVVIFDEAHNIE 150
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
546-731 1.22e-56

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: 193.55  E-value: 1.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   546 SNIARVVPHGLLVFFPSYPVMEKSLEFWQVQGLARKvealKPLFVEPRNkGSFSEVIDAYYQqvaspASNGATFLAVCRG 625
Cdd:pfam13307    1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEKG----IEIFVQPGE-GSREKLLEEFKK-----KGKGAVLFGVCGG 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   626 KASEGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFLDEmRGRSGvggqclsGQEWYQQQASRAVNQAIGRVIRHRHDY 705
Cdd:pfam13307   71 SFSEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLDS-KGGNP-------FNEWYLPQAVRAVNQAIGRLIRHENDY 142
                          170       180
                   ....*....|....*....|....*.
gi 568920270   706 GAIFLCDHRFAYADARAQLPSWVRPY 731
Cdd:pfam13307  143 GAIVLLDSRFLTKRYGKLLPKWLPPG 168
HELICc2 smart00491
helicase superfamily c-terminal domain;
563-716 1.85e-47

helicase superfamily c-terminal domain;


Pssm-ID: 214694 [Multi-domain]  Cd Length: 142  Bit Score: 165.92  E-value: 1.85e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270    563 YPVMEKSLEFWQVQGLArkvEALKPLFVEPRNKGSFSEVIDAYyqqVASPASNGATFLAVCRGKASEGLDFSDMNGRGVI 642
Cdd:smart00491    1 YRYLEQVVEYWKENGIL---EINKPVFIEGKDSGETEELLEKY---SAACEARGALLLAVARGKVSEGIDFPDDLGRAVI 74
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568920270    643 VTGLPYPPRMDPRVVLKMQFLDEMrgrsgvgGQCLSGQEWYQQQASRAVNQAIGRVIRHRHDYGAIFLCDHRFA 716
Cdd:smart00491   75 IVGIPFPNPDSPILRARLEYLDEK-------GGIRPFDEVYLFDAMRALAQAIGRAIRHKNDYGVVVLLDKRYA 141
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
13-738 2.49e-45

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 174.34  E-value: 2.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   13 FP-FQPYPCQQEYMTKVLECLQKKVNGILESPTGTGKTLCLLcstlawqqhlrdaVSSLKIAeRVQGElfasrtlsswgs 91
Cdd:COG1199    10 FPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYL-------------VPALLAA-RETGK------------ 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   92 aaaasgdsiecytdipKIIYASRTHSQLTQVI-REL----RNTAYRPKVCVLGSREQ-LCIHP--EVKKQESNHMQISLC 163
Cdd:COG1199    64 ----------------KVVISTATKALQEQLVeKDLpllrKALGLPLRVALLKGRSNyLCLRRleQALQEGDDLDDEELL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  164 RKKVASRSchfynnveAKFLEQDLATPILDIEDLVK----------NGSK---QKMCPYYLSRNMKQQADIIFMPYNYLL 230
Cdd:COG1199   128 LARILAWA--------SETWTGDRDELPLPEDDELWrqvtsdadncLGRRcpyYGVCPYELARRLAREADVVVVNHHLLF 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  231 DAKSRKAHSIDlKGTVVIFDEAHNVEKICEESASFDLTPRDVasgLEIINQVLEEQARvtqqgelqqefivdtsssglnm 310
Cdd:COG1199   200 ADLALGEELLP-EDDVLIIDEAHNLPDRARDMFSAELSSRSL---LRLLRELRKLGLR---------------------- 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  311 elEDIAKLKMILLRLEEAIDAvqlpgddrgvtkpgsyIFELFAEAQITFQTKGCILESLDQIIQHLAGrtgvftntagLQ 390
Cdd:COG1199   254 --PGLKKLLDLLERLREALDD----------------LFLALEEEEELRLALGELPDEPEELLEALDA----------LR 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  391 KLMDIIQIVFsvdppEGSPGSLVGLGISHSYKVHIHPETSHRRAAKRSDAWSTTASRKQGKV-LSYWCFSPSQSMRELVC 469
Cdd:COG1199   306 DALEALAEAL-----EEELERLAELDALLERLEELLFALARFLRIAEDEGYVRWLEREGGDVrLHAAPLDPADLLRELLF 380
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  470 QGVRTLILTSGTLAPLSSF------------ALEMQI--PFPvclenphiiDKNQLwVGIVPRGPdgvqlsSAYDKRfsE 535
Cdd:COG1199   381 SRARSVVLTSATLSVGGPFdyfarrlgldedARTLSLpsPFD---------YENQA-LLYVPRDL------PRPSDR--D 442
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  536 ECLSSLGKALSNIARVVPHGLLVFFPSYPVMEKSLEfwqvqGLARKVEalKPLFVEPRnkGSFSEVIDAYyqqvaspASN 615
Cdd:COG1199   443 GYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE-----LLRERLD--IPVLVQGD--GSREALLERF-------REG 506
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  616 GATFLaVCRGKASEGLDFSdmnG---RGVIVTGLPYPPRMDPRVVLKMQFLDEmRGRSGVggqclsgQEWYQQQASRAVN 692
Cdd:COG1199   507 GNSVL-VGTGSFWEGVDLP---GdalSLVIIVKLPFPPPDDPVLEARREALEA-RGGNGF-------MYAYLPPAVIKLK 574
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|
gi 568920270  693 QAIGRVIRHRHDYGAIFLCDHRFA---YADA-RAQLPSWVRPYLKVYDNF 738
Cdd:COG1199   575 QGAGRLIRSEEDRGVVVLLDRRLLtkrYGKRfLDSLPPFRRTRPEELRAF 624
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
877-976 1.25e-33

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: 125.08  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  877 KVRLVNHPEEPMAGTQAGRAKMFMVAVKQALSQANFDTFTQALQHYKSSDDFEALVASLTCLFAEdPKKHTLLKGFYQFV 956
Cdd:cd13932     1 KKSSVSASSSSGAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFAE-PERHPLLRGFRRFV 79
                          90       100
                  ....*....|....*....|
gi 568920270  957 RPHHKQQFEDICFQLTGQRC 976
Cdd:cd13932    80 RPHHKKEFDERCKSLTGAGC 99
HN_RTEL1 cd13932
harmonin_N_like domain of regulator of telomere elongation helicase 1 (also known as RTEL); ...
993-1081 4.03e-27

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: 106.20  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  993 VEKPGQPAVSDYLSDVHKALGSASCNQLTAALRAYKQDDDLDKVVAVVAALTTaKPEHLPLLQRFGMFVRRHHKPQFLQT 1072
Cdd:cd13932    12 GAKPAPESASAFLREVKQKLSAAEYRQFSAALQAYKTGDDFEQLLAVLAELFA-EPERHPLLRGFRRFVRPHHKKEFDER 90

                  ....*....
gi 568920270 1073 CADLMGLPT 1081
Cdd:cd13932    91 CKSLTGAGC 99
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
38-271 3.22e-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: 93.65  E-value: 3.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   38 GILESPTGTGKTLCLLCSTLAWQQHLRdavsslkiaervqgelfasrtlsswgsaaaasgdsiecytdIPKIIYASRTHS 117
Cdd:cd17915     4 VALESPTGSGKTLSLLCSALSYQREFH-----------------------------------------KTKVLYCSRTHS 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  118 QLTQVIRELRNTAYRPKV--CVLGSREqlcihpevkkqesnhmqislcrkkvasrschfynnveakfleqdlatpildie 195
Cdd:cd17915    43 QIEQIIRELRKLLEKRKIraLALSSRD----------------------------------------------------- 69
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568920270  196 dlvkngskqkmcpyylsrnmkqqADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNVEKICEESASFDLTPRD 271
Cdd:cd17915    70 -----------------------ADIVVLPYPYLLDARIREFIGIDLREQVVIIDEAHNLDERSVIITSGTLSPLD 122
harmonin_N_like cd07347
N-terminal protein-binding module of harmonin and similar domains, also known as HHD (harmonin ...
895-968 1.87e-15

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: 72.23  E-value: 1.87e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568920270  895 RAKMFMVAVKQALSQANFDTFTQALQHYKSSDDFEALVASLTCLFAEdPKKHTLLKGFYQFVRPHHKQQFEDIC 968
Cdd:cd07347     4 LARLFSEQADQLLTDQERAYVTQALSEYRKGRSVEALVADLFPVLDT-PAKLSLLQGLRSLIPPKDQQRFDELV 76
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
471-502 2.22e-10

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: 61.21  E-value: 2.22e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568920270  471 GVRTLILTSGTLAPLSSFALEMQIPFPVCLEN 502
Cdd:cd17970   150 EVRTIILTSGTLSPLDSFASELGTKFPIRLEN 181
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
38-259 2.51e-10

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: 59.64  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   38 GILESPTGTGKTLCLLCSTLAWqqhlrdavsslkiaervqgelfasrtlsswgsaaaasgdsiecytdIPKIIYASRTHS 117
Cdd:cd17968     4 GIFESPTGTGKSLSLICGALTW----------------------------------------------LTKIYYCSRTHS 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  118 QLTQVIRELRNTAYRPKVcvlgsreqlcihpevkkqesnhmqislcrkkvasrschfynnveakfleqdlatpildieDL 197
Cdd:cd17968    38 QLAQFVHEVQKSPFGKDV------------------------------------------------------------RL 57
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568920270  198 VKNGSKQKmcpyylsrnmkqQADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNVekIC 259
Cdd:cd17968    58 VSLGSRQP------------AAQVVVLPYQMLLHAATRKASGIKLKDQVVIIDEAHNL--IC 105
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
31-256 1.05e-05

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: 47.04  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270   31 CLQKKVNGILESPTGTGKTLCLLCSTLAWQQHLRDAVSslkiaervqgelfasrtlsswgsaaaasgdsiecytdipKII 110
Cdd:cd17969     6 TLDAKGHCVLEMPSGTGKTVSLLSLIVAYQKAYPLEVT---------------------------------------KLI 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  111 YASRTHSQLTQVIRELRNTAyrpkvcvlgsreqlcihpevkkqesnhmqislcrkkvasrschfynnveaKFLEQDLatp 190
Cdd:cd17969    47 YCSRTVPEIEKVVEELRKLM--------------------------------------------------DYYEKQT--- 73
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568920270  191 ildiedlvknGSKQKMCPYYLSRnmkQQADIIFMPYNYLLDAKSRKAHSIDL-KGTVVIFDEAHNVE 256
Cdd:cd17969    74 ----------GEKPNFLGLALSS---RHANVVVYSYHYLLDPKIAELVSKELsKKSVVVFDEAHNID 127
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
208-255 1.28e-03

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 40.46  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568920270  208 PYYLSRNMKQQADIIFMPYNYLLDAKSRKAHSIDLKGTVVIFDEAHNV 255
Cdd:cd00046    69 AEEREKNKLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHAL 116
PRK08074 PRK08074
bifunctional ATP-dependent DNA helicase/DNA polymerase III subunit epsilon; Validated
473-714 3.02e-03

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


Pssm-ID: 236148 [Multi-domain]  Cd Length: 928  Bit Score: 41.86  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  473 RTLILTSGTLA------------PLSSFA-LEMQIPFPVCLEnphiiDKNQLwvgIVPRgpDGVQLSSAYDKRFSEEcls 539
Cdd:PRK08074  673 KSVILTSATLTvngsfdyiierlGLEDFYpRTLQIPSPFSYE-----EQAKL---MIPT--DMPPIKDVPIEEYIEE--- 739
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  540 sLGKALSNIARVVPHGLLVFFPSYpvmekslefwqvqglarkvEALKPLFVEPRNKGSFSEvidayYQQVASPASNGA-- 617
Cdd:PRK08074  740 -VAAYIAKIAKATKGRMLVLFTSY-------------------EMLKKTYYNLKNEEELEG-----YVLLAQGVSSGSra 794
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920270  618 ----TFL----AVCRGKAS--EGLDFSDMNGRGVIVTGLPYPPRMDPRVVLKMQFLDEmRGRSgvggqclSGQEWYQQQA 687
Cdd:PRK08074  795 rltkQFQqfdkAILLGTSSfwEGIDIPGDELSCLVIVRLPFAPPDQPVMEAKSEWAKE-QGEN-------PFQELSLPQA 866
                         250       260
                  ....*....|....*....|....*..
gi 568920270  688 SRAVNQAIGRVIRHRHDYGAIFLCDHR 714
Cdd:PRK08074  867 VLRFKQGFGRLIRTETDRGTVFVLDRR 893
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
10-53 3.57e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 41.55  E-value: 3.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568920270   10 TVDFPFQPYPCQQEYMTKVLECLQKKVN-GILESPTGTGKTLCLL 53
Cdd:COG1061    74 ASGTSFELRPYQQEALEALLAALERGGGrGLVVAPTGTGKTVLAL 118
COG2888 COG2888
Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 ...
1164-1205 4.47e-03

Predicted RNA-binding protein involved in translation, contains Zn-ribbon domain, DUF1610 family [General function prediction only];


Pssm-ID: 442134 [Multi-domain]  Cd Length: 52  Bit Score: 36.63  E-value: 4.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568920270 1164 VCPAC----ATEDTVLFQCPSCD---FYRCWACwKLQLQASRLCPACGA 1205
Cdd:COG2888     2 VCPSCgreiAPEGGVAFYCPNCGealIIRCPKC-RKQSNALYFCPKCGF 49
DEXDc smart00487
DEAD-like helicases superfamily;
13-53 6.36e-03

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 39.40  E-value: 6.36e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 568920270     13 FPFQPYPCQQEYMTKVLECLQkkvNGILESPTGTGKTLCLL 53
Cdd:smart00487    5 GFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAAL 42
ResIII pfam04851
Type III restriction enzyme, res subunit;
15-86 9.57e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.42  E-value: 9.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568920270    15 FQPYPCQQEYMTKVLEC-LQKKVNGILESPTGTGKTLCllcstlawqqhlrdavsSLKIAERVQGELFASRTL 86
Cdd:pfam04851    2 LELRPYQIEAIENLLESiKNGQKRGLIVMATGSGKTLT-----------------AAKLIARLFKKGPIKKVL 57
 
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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