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Conserved domains on  [gi|2058508|gb|AAB62732|]
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RepB [Dictyostelium discoideum]

Protein Classification

rad25 family protein( domain architecture ID 11489419)

rad25 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
65-794 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription 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: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1352.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     65 DYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITV 144
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    145 LGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTG----FI 220
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGskedFI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    221 INKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNsdQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFR 300
Cdd:TIGR00603 161 INKPGFTGGASAGQLEANQGESAVPKDIADFYELEEEEEDEDEE--TATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    301 NDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQF 380
Cdd:TIGR00603 239 NDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    381 KLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTV 460
Cdd:TIGR00603 319 KMWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTI 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    461 TKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQgKKKLLYTM 540
Cdd:TIGR00603 399 VQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR-KRMLLYVM 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    541 NPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSID 620
Cdd:TIGR00603 478 NPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSID 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    621 IPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDG-LYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGI 699
Cdd:TIGR00603 558 LPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAeEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGM 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    700 DQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAP 779
Cdd:TIGR00603 638 DNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKP 717
                         730
                  ....*....|....*
gi 2058508    780 AIYKSIPTQHALFKQ 794
Cdd:TIGR00603 718 AIKKSKKEVHPLFKK 732
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
65-794 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription 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: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1352.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     65 DYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITV 144
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    145 LGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTG----FI 220
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGskedFI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    221 INKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNsdQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFR 300
Cdd:TIGR00603 161 INKPGFTGGASAGQLEANQGESAVPKDIADFYELEEEEEDEDEE--TATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    301 NDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQF 380
Cdd:TIGR00603 239 NDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    381 KLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTV 460
Cdd:TIGR00603 319 KMWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTI 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    461 TKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQgKKKLLYTM 540
Cdd:TIGR00603 399 VQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR-KRMLLYVM 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    541 NPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSID 620
Cdd:TIGR00603 478 NPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSID 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    621 IPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDG-LYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGI 699
Cdd:TIGR00603 558 LPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAeEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGM 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    700 DQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAP 779
Cdd:TIGR00603 638 DNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKP 717
                         730
                  ....*....|....*
gi 2058508    780 AIYKSIPTQHALFKQ 794
Cdd:TIGR00603 718 AIKKSKKEVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
499-744 1.25e-169

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 489.03  E-value: 1.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    499 LQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQgKKKLLYTMNPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKG 578
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSR-KKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    579 LGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKS-DGL 657
Cdd:pfam16203  80 LNKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSnDEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    658 YNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGIDQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDF 737
Cdd:pfam16203 160 FNAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDL 239

                  ....*..
gi 2058508    738 DDITRGA 744
Cdd:pfam16203 240 GKDRKGG 246
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
310-479 3.34e-108

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 327.72  E-value: 3.34e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  310 IDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQFKLWSNIEER 389
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  390 QISKFTSDNKEKISNvAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGL 469
Cdd:cd18029  81 QIGRFTSDKKEIFPE-AGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGL 159
                       170
                ....*....|
gi 2058508  470 TATLLREDEK 479
Cdd:cd18029 160 TATLVREDDK 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
311-748 1.26e-56

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 203.72  E-value: 1.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  311 DLKPTTMI--RPYQEKSLSKMFGNGRA--RSGIIVLPCGAGKSLSGITAACTV--KKSILVLCTSAVSVEQWKYQFKLWS 384
Cdd:COG1061  72 DEASGTSFelRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRFL 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  385 NIEERqiskftSDNKEKISnvAGVTITTYtmvafggrRSAESLKIMNEITNReWGLVLLDEVHVVPAAMFRKVLTVTKAH 464
Cdd:COG1061 152 GDPLA------GGGKKDSD--APITVATY--------QSLARRAHLDELGDR-FGLVIIDEAHHAGAPSYRRILEAFPAA 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  465 CKLGLTATLLREDEKIQDLNFLIGpKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFyKEYLINDSQGKKKLLyTMNPNK 544
Cdd:COG1061 215 YRLGLTATPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEYDALSERLREALA-ADAERK 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  545 FRACEYLIRFHEqRGDKIIVFSDNVYALQKYAKGLGR-----YFIYGPTSGHERMSILSKFQHDpTVRTIFISKVGDTSI 619
Cdd:COG1061 292 DKILRELLREHP-DDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFRDG-ELRILVTVDVLNEGV 369
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  620 DIPEATVIIQVSSHyGSRRQEAQRLGRILRPKPKSDglyNAFFYSLVSKDTQEMYYSTKRQQFLIdqGYSFKVISELPGI 699
Cdd:COG1061 370 DVPRLDVAILLRPT-GSPREFIQRLGRGLRPAPGKE---DALVYDFVGNDVPVLEELAKDLRDLA--GYRVEFLDEEESE 443
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 2058508  700 DQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSK 748
Cdd:COG1061 444 ELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALA 492
DEXDc smart00487
DEAD-like helicases superfamily;
319-485 1.52e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.47  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     319 RPYQEKSLSKMFGNGRarSGIIVLPCGAGKSLSGITAA-----CTVKKSILVLCTSAVSVEQWKYQFKLW-SNIEERQIS 392
Cdd:smart00487  10 RPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgPSLGLKVVG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     393 KFTSDNKEK-----ISNVAGVTITTYTMVAfggrrsaeSLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLT-----VTK 462
Cdd:smart00487  88 LYGGDSKREqlrklESGKTDILVTTPGRLL--------DLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEkllklLPK 159
                          170       180
                   ....*....|....*....|...
gi 2058508     463 AHCKLGLTATLLREDEKIQDLNF 485
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFL 182
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
65-794 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription 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: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1352.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     65 DYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITV 144
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    145 LGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTG----FI 220
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGskedFI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    221 INKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNsdQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFR 300
Cdd:TIGR00603 161 INKPGFTGGASAGQLEANQGESAVPKDIADFYELEEEEEDEDEE--TATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    301 NDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQF 380
Cdd:TIGR00603 239 NDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    381 KLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTV 460
Cdd:TIGR00603 319 KMWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTI 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    461 TKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQgKKKLLYTM 540
Cdd:TIGR00603 399 VQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR-KRMLLYVM 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    541 NPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSID 620
Cdd:TIGR00603 478 NPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSID 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    621 IPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDG-LYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGI 699
Cdd:TIGR00603 558 LPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAeEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGM 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    700 DQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAP 779
Cdd:TIGR00603 638 DNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKP 717
                         730
                  ....*....|....*
gi 2058508    780 AIYKSIPTQHALFKQ 794
Cdd:TIGR00603 718 AIKKSKKEVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
499-744 1.25e-169

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 489.03  E-value: 1.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    499 LQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQgKKKLLYTMNPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKG 578
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSR-KKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    579 LGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKS-DGL 657
Cdd:pfam16203  80 LNKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSnDEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    658 YNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGIDQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDF 737
Cdd:pfam16203 160 FNAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDL 239

                  ....*..
gi 2058508    738 DDITRGA 744
Cdd:pfam16203 240 GKDRKGG 246
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
310-479 3.34e-108

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 327.72  E-value: 3.34e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  310 IDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQFKLWSNIEER 389
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  390 QISKFTSDNKEKISNvAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGL 469
Cdd:cd18029  81 QIGRFTSDKKEIFPE-AGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGL 159
                       170
                ....*....|
gi 2058508  470 TATLLREDEK 479
Cdd:cd18029 160 TATLVREDDK 169
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
510-666 4.35e-87

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 272.20  E-value: 4.35e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  510 CSEVWCPMTAEFYKEYLINDSQGKKKLLYTMNPNKFRACEYLIRFHEQrGDKIIVFSDNVYALQKYAKGLGRYFIYGPTS 589
Cdd:cd18789   1 CAEIRCPMTPEFYREYLGLGAHRKRRLLAAMNPNKLRALEELLKRHEQ-GDKIIVFTDNVEALYRYAKRLLKPFITGETP 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2058508  590 GHERMSILSKFQHDPtVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPksDGLYNAFFYSLV 666
Cdd:cd18789  80 QSEREEILQNFREGE-YNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPKK--GGGKNAFFYSLV 153
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
311-748 1.26e-56

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 203.72  E-value: 1.26e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  311 DLKPTTMI--RPYQEKSLSKMFGNGRA--RSGIIVLPCGAGKSLSGITAACTV--KKSILVLCTSAVSVEQWKYQFKLWS 384
Cdd:COG1061  72 DEASGTSFelRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRFL 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  385 NIEERqiskftSDNKEKISnvAGVTITTYtmvafggrRSAESLKIMNEITNReWGLVLLDEVHVVPAAMFRKVLTVTKAH 464
Cdd:COG1061 152 GDPLA------GGGKKDSD--APITVATY--------QSLARRAHLDELGDR-FGLVIIDEAHHAGAPSYRRILEAFPAA 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  465 CKLGLTATLLREDEKIQDLNFLIGpKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFyKEYLINDSQGKKKLLyTMNPNK 544
Cdd:COG1061 215 YRLGLTATPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEYDALSERLREALA-ADAERK 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  545 FRACEYLIRFHEqRGDKIIVFSDNVYALQKYAKGLGR-----YFIYGPTSGHERMSILSKFQHDpTVRTIFISKVGDTSI 619
Cdd:COG1061 292 DKILRELLREHP-DDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFRDG-ELRILVTVDVLNEGV 369
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  620 DIPEATVIIQVSSHyGSRRQEAQRLGRILRPKPKSDglyNAFFYSLVSKDTQEMYYSTKRQQFLIdqGYSFKVISELPGI 699
Cdd:COG1061 370 DVPRLDVAILLRPT-GSPREFIQRLGRGLRPAPGKE---DALVYDFVGNDVPVLEELAKDLRDLA--GYRVEFLDEEESE 443
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 2058508  700 DQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSK 748
Cdd:COG1061 444 ELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALA 492
Helicase_C_3 pfam13625
Helicase conserved C-terminal domain; This domain family is found in a wide variety of ...
81-204 6.91e-39

Helicase conserved C-terminal domain; This domain family is found in a wide variety of helicases and helicase-related proteins.


Pssm-ID: 463939 [Multi-domain]  Cd Length: 121  Bit Score: 139.94  E-value: 6.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     81 IWVCPDGHIFLETfsAIYKQASDFLVAIAEPVCRpQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQF 160
Cdd:pfam13625   1 LIVQADLTILLPG--PLAPEARDFLAAFAELESR-GHAHTYRLTPLSLRRALDAGLTAEDILDFLERHSKYPVPQALEYL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2058508    161 VRQCTQSYGKVKLVLqKNKYFVESAYPEVLEFLLKDSSIATARI 204
Cdd:pfam13625  78 IRDVARRHGRLRLGL-GASSYLRSDDPAVLAELLADPRIAPLGL 120
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
319-473 9.54e-31

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 117.79  E-value: 9.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  319 RPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKK-SILVLCTSAVSVEQWKYQFKLWSNIeeRQISKFTSD 397
Cdd:cd17926   2 RPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGD--SSIGLIGGG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2058508  398 NKEKIsNVAGVTITTYTMVAfggrRSAESLKIMNEitnrEWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGLTATL 473
Cdd:cd17926  80 KKKDF-DDANVVVATYQSLS----NLAEEEKDLFD----QFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
DEXDc smart00487
DEAD-like helicases superfamily;
319-485 1.52e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.47  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     319 RPYQEKSLSKMFGNGRarSGIIVLPCGAGKSLSGITAA-----CTVKKSILVLCTSAVSVEQWKYQFKLW-SNIEERQIS 392
Cdd:smart00487  10 RPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLgPSLGLKVVG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508     393 KFTSDNKEK-----ISNVAGVTITTYTMVAfggrrsaeSLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLT-----VTK 462
Cdd:smart00487  88 LYGGDSKREqlrklESGKTDILVTTPGRLL--------DLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEkllklLPK 159
                          170       180
                   ....*....|....*....|...
gi 2058508     463 AHCKLGLTATLLREDEKIQDLNF 485
Cdd:smart00487 160 NVQLLLLSATPPEEIENLLELFL 182
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
294-649 6.33e-16

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 82.20  E-value: 6.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  294 LEEYDFRNDTVNPNLNIDLkpttmiRPYQEKSLSKMFGNGRARSGII----VlpcGAGKSLSGITAACTVK-----KSIL 364
Cdd:COG0553 224 LRRLREALESLPAGLKATL------RPYQLEGAAWLLFLRRLGLGGLladdM---GLGKTIQALALLLELKerglaRPVL 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  365 VLCTSAVsVEQWkyqfklwsnieERQISKFT----------SDNKEKISNV---AGVTITTYTMVafggRRSAESLKimn 431
Cdd:COG0553 295 IVAPTSL-VGNW-----------QRELAKFApglrvlvldgTRERAKGANPfedADLVITSYGLL----RRDIELLA--- 355
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  432 eitNREWGLVLLDEVHVV---PAAMFRKVLTVtKAHCKLGLTAT-----------LLR---------------------- 475
Cdd:COG0553 356 ---AVDWDLVILDEAQHIknpATKRAKAVRAL-KARHRLALTGTpvenrleelwsLLDflnpgllgslkafrerfarpie 431
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  476 --EDEKIQDLNFLIGPKLyeanwLDLQK---AGFLANVSCSEVWCPMT---AEFYKEYL------INDSQGKKKLL---- 537
Cdd:COG0553 432 kgDEEALERLRRLLRPFL-----LRRTKedvLKDLPEKTEETLYVELTpeqRALYEAVLeylrreLEGAEGIRRRGlila 506
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  538 ---------------------YTMNPNKFRACEYLIRFHEQRGDKIIVFS---DNVYALQKY--AKGLGRYFIYGPTSGH 591
Cdd:COG0553 507 altrlrqicshpallleegaeLSGRSAKLEALLELLEELLAEGEKVLVFSqftDTLDLLEERleERGIEYAYLHGGTSAE 586
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058508  592 ERMSILSKFQHDPTVRTIFIS-KVGDTSIDIPEA-TVIiqvssHYG-----SRrqEAQRLGRILR 649
Cdd:COG0553 587 ERDELVDRFQEGPEAPVFLISlKAGGEGLNLTAAdHVI-----HYDlwwnpAV--EEQAIDRAHR 644
ResIII pfam04851
Type III restriction enzyme, res subunit;
318-475 1.57e-14

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 71.93  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    318 IRPYQE---KSLSKMFGNGRARsGIIVLPCGAGKSLsgiTAACTV--------KKSILVLCTSAVSVEQWKYQFKLWSNI 386
Cdd:pfam04851   4 LRPYQIeaiENLLESIKNGQKR-GLIVMATGSGKTL---TAAKLIarlfkkgpIKKVLFLVPRKDLLEQALEEFKKFLPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    387 EERQISKFTSDNKEKISNVAGVTITTYTMVafggrrSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCK 466
Cdd:pfam04851  80 YVEIGEIISGDKKDESVDDNKIVVTTIQSL------YKALELASLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFL 153

                  ....*....
gi 2058508    467 LGLTATLLR 475
Cdd:pfam04851 154 LGLTATPER 162
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
356-477 2.02e-10

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 62.01  E-value: 2.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  356 ACTVKKSILVLCTSAVsVEQWKYQFKLWSNIEerqISKFTSDNKEKISNV---AG---VTITTYTMVafggRRSAESLki 429
Cdd:cd18005  66 ASSAKKPVLIVAPLSV-LYNWKDELDTWGHFE---VGVYHGSRKDDELEGrlkAGrleVVVTTYDTL----RRCIDSL-- 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2058508  430 mNEItnrEWGLVLLDEVHVV--PAAMFRKVLTVTKAHCKLGLTATLLRED 477
Cdd:cd18005 136 -NSI---NWSAVIADEAHRIknPKSKLTQAMKELKCKVRIGLTGTLLQNN 181
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
543-651 5.14e-10

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 57.22  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    543 NKFRACEYLIRFHeqRGDKIIVFSDNVYALQ-KYAKGLGRY---FIYGPTSGHERMSILSKFQhDPTVRTIFISKVGDTS 618
Cdd:pfam00271   1 EKLEALLELLKKE--RGGKVLIFSQTKKTLEaELLLEKEGIkvaRLHGDLSQEEREEILEDFR-KGKIDVLVATDVAERG 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2058508    619 IDIPEATVIIQVSSHYgSRRQEAQRLGRILRPK 651
Cdd:pfam00271  78 LDLPDVDLVINYDLPW-NPASYIQRIGRAGRAG 109
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
319-472 9.45e-10

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 58.73  E-value: 9.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  319 RPYQEKSLSKMFGNGRARSGIIVLPC-GAGKSLSGITAACTVKKS------ILVLCTSAVsVEQWKYQFKLW-------- 383
Cdd:cd17919   2 RPYQLEGLNFLLELYENGPGGILADEmGLGKTLQAIAFLAYLLKEgkergpVLVVCPLSV-LENWEREFEKWtpdlrvvv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  384 ---SNIEERQISKFTSDNKekisnvAGVTITTYTMVafggRRSAESLKIMneitnrEWGLVLLDEVHVV--PAAMFRKVL 458
Cdd:cd17919  81 yhgSQRERAQIRAKEKLDK------FDVVLTTYETL----RRDKASLRKF------RWDLVVVDEAHRLknPKSQLSKAL 144
                       170
                ....*....|....
gi 2058508  459 TVTKAHCKLGLTAT 472
Cdd:cd17919 145 KALRAKRRLLLTGT 158
HELICc smart00490
helicase superfamily c-terminal domain;
577-651 2.61e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 54.53  E-value: 2.61e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2058508     577 KGLGRYFIYGPTSGHERMSILSKFQHDPtVRTIFISKVGDTSIDIPEATVIIQVSSHYgSRRQEAQRLGRILRPK 651
Cdd:smart00490  10 LGIKVARLHGGLSQEEREEILDKFNNGK-IKVLVATDVAERGLDLPGVDLVIIYDLPW-SPASYIQRIGRAGRAG 82
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
319-479 3.60e-08

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 53.72  E-value: 3.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  319 RPYQEKSLSKM---FGNGRaRSGIIVLPCGAGKSlsgITAACTVK--------KSILVLCTSAVSVEQWKYQFKlwsNIE 387
Cdd:cd18032   2 RYYQQEAIEALeeaREKGQ-RRALLVMATGTGKT---YTAAFLIKrlleanrkKRILFLAHREELLEQAERSFK---EVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  388 ERQISKFTSDNKEKISNvAGVTITTY-TMVAfggrrsaeslKIMNEITNRE-WGLVLLDEVHVVPAAMFRKVLtvtkAHC 465
Cdd:cd18032  75 PDGSFGNLKGGKKKPDD-ARVVFATVqTLNK----------RKRLEKFPPDyFDLIIIDEAHHAIASSYRKIL----EYF 139
                       170
                ....*....|....*...
gi 2058508  466 K----LGLTATLLREDEK 479
Cdd:cd18032 140 EpaflLGLTATPERTDGL 157
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
544-649 4.32e-08

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 52.48  E-value: 4.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  544 KFRACEYLIRFHEQRGDKIIVFS------DnvyALQKYAKGLGRYF--IYGPTSGHERMSILSKFQHDPTVRTIFIS-KV 614
Cdd:cd18793  12 KLEALLELLEELREPGEKVLIFSqftdtlD---ILEEALRERGIKYlrLDGSTSSKERQKLVDRFNEDPDIRVFLLStKA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2058508  615 GDTSIDIPEATVIIqvssHYG-----SRrqEAQRLGRILR 649
Cdd:cd18793  89 GGVGLNLTAANRVI----LYDpwwnpAV--EEQAIDRAHR 122
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
321-472 9.78e-06

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 48.06  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    321 YQEKSLSKMFG--NGRARSGIIVLPCGAGKSLSGITAACTVKKS-------ILVLCTSAVsVEQWKYQFKLWSNIEERQI 391
Cdd:pfam00176   1 YQIEGVNWMLSleNNLGRGGILADEMGLGKTLQTISLLLYLKHVdknwggpTLIVVPLSL-LHNWMNEFERWVSPPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508    392 SKFTSDNKEKISNV--------AGVTITTYTMVafggrrsaesLKIMNEITNREWGLVLLDEVHVV--PAAMFRKVLTVT 461
Cdd:pfam00176  80 VVLHGNKRPQERWKndpnfladFDVVITTYETL----------RKHKELLKKVHWHRIVLDEGHRLknSKSKLSKALKSL 149
                         170
                  ....*....|.
gi 2058508    462 KAHCKLGLTAT 472
Cdd:pfam00176 150 KTRNRWILTGT 160
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
326-447 3.62e-05

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 45.83  E-value: 3.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  326 LSKMFGNGRArsGIIVLPCGAGKS------LSGITAACTVKKSILVLCTSAVSVeqWKYQFKLW-----------SNIEE 388
Cdd:cd18001  12 LWSLHDGGKG--GILADDMGLGKTvqicafLSGMFDSGLIKSVLVVMPTSLIPH--WVKEFAKWtpglrvkvfhgTSKKE 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 2058508  389 RQiskftsDNKEKISNVAGVTITTYTMVafggRRSAESLKIMNEITNReWGLVLLDEVH 447
Cdd:cd18001  88 RE------RNLERIQRGGGVLLTTYGMV----LSNTEQLSADDHDEFK-WDYVILDEGH 135
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
338-472 1.11e-04

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: 43.16  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  338 GIIVLPCGAGKSL-SGITAAC---TVKKSILVLCTSAVSVEQWKYQFKLWSNIEERqISKFTSDN--KEKISNVAG---V 408
Cdd:cd00046   4 VLITAPTGSGKTLaALLAALLlllKKGKKVLVLVPTKALALQTAERLRELFGPGIR-VAVLVGGSsaEEREKNKLGdadI 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2058508  409 TITTYTMVAFGGRRSAESLKimneitnREWGLVLLDEVHVVPAAMFRKV---LTVTKAHCK----LGLTAT 472
Cdd:cd00046  83 IIATPDMLLNLLLREDRLFL-------KDLKLIIVDEAHALLIDSRGALildLAVRKAGLKnaqvILLSAT 146
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
345-509 5.99e-04

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 41.89  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  345 GAGKSLSGITAAC-----TVKKSILVLCTSAVsVEQWkyQFKLWS--NIEERQISKFTSDNKEKISNV----AGVTITTY 413
Cdd:cd18011  27 GLGKTIEAGLIIKelllrGDAKRVLILCPASL-VEQW--QDELQDkfGLPFLILDRETAAQLRRLIGNpfeeFPIVIVSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  414 TMVafggRRSAESLKIMNEitnREWGLVLLDEVHVVPAAMFRK--------VLTVTKAHCKLGLTAT-LLREDEKIQDLN 484
Cdd:cd18011 104 DLL----KRSEERRGLLLS---EEWDLVVVDEAHKLRNSGGGKetkryklgRLLAKRARHVLLLTATpHNGKEEDFRALL 176
                       170       180
                ....*....|....*....|....*
gi 2058508  485 FLIGPKLYEANWLDLQKAGFLANVS 509
Cdd:cd18011 177 SLLDPGRFAVLGRFLRLDGLREVLA 201
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
609-653 4.02e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.91  E-value: 4.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 2058508  609 IFISKVGDTSIDIPEATVIIQVSSHyGSRRQEAQRLGRILRPKPK 653
Cdd:cd18785  26 LVATNVLGEGIDVPSLDTVIFFDPP-SSAASYIQRVGRAGRGGKD 69
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
320-484 4.63e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 38.85  E-value: 4.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  320 PYQEKSLSKMFGNGRarSGIIVLPCGAGKSLSGITAACTV----KKSILVLCTSAVSVEqwKYQ-FKLWSNIEER-QISk 393
Cdd:cd18028   4 PPQAEAVRAGLLKGE--NLLISIPTASGKTLIAEMAMVNTllegGKALYLVPLRALASE--KYEeFKKLEEIGLKvGIS- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  394 fTSDNKEKISNVAG--VTITTYTMVAFGGRRSAESLkimneitnREWGLVLLDEVHVVPAAMFRKVLTVTKAHCK----- 466
Cdd:cd18028  79 -TGDYDEDDEWLGDydIIVATYEKFDSLLRHSPSWL--------RDVGVVVVDEIHLISDEERGPTLESIVARLRrlnpn 149
                       170       180
                ....*....|....*....|.
gi 2058508  467 ---LGLTATLLREDEKIQDLN 484
Cdd:cd18028 150 tqiIGLSATIGNPDELAEWLN 170
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
339-483 8.57e-03

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 38.26  E-value: 8.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  339 IIVLPCGAGKSLSGITAAC---TVKKS-ILVLCTSAVSVEQWKYQFKLWSNIEERQIS---KFTSDNKEKISNVAGVTIT 411
Cdd:cd18035  20 LIVLPTGLGKTIIAILVAAdrlTKKGGkVLILAPSRPLVEQHAENLKRVLNIPDKITSltgEVKPEERAERWDASKIIVA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058508  412 TYTMVafggrrsaESLKIMNEITNREWGLVLLDEVH--------VVPAAMFRKvltVTKAHCKLGLTATLLREDEKIQDL 483
Cdd:cd18035 100 TPQVI--------ENDLLAGRITLDDVSLLIFDEAHhavgnyayVYIAHRYKR---EANNPLILGLTASPGSDKEKIMEI 168
 
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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