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Conserved domains on  [gi|515497727|ref|WP_016930981|]
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MULTISPECIES: excinuclease ABC subunit UvrB [Staphylococcus]

Protein Classification

excinuclease ABC subunit UvrB( domain architecture ID 11426127)

excinuclease ABC subunit B is part of the UvrABC repair system, which catalyzes the recognition and processing of DNA lesions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
6-660 0e+00

Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];


:

Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1363.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 T-DEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL 484
Cdd:COG0556  401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQY 564
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 565 ALDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDE-TNEKQQTELPKKMTKKERQKTIENIEKEMKKAAKDLD 643
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEeTEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*..
gi 515497727 644 FEKATELRDMLFELKAE 660
Cdd:COG0556  641 FEEAARLRDEIKELKKE 657
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
6-660 0e+00

Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1363.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 T-DEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL 484
Cdd:COG0556  401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQY 564
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 565 ALDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDE-TNEKQQTELPKKMTKKERQKTIENIEKEMKKAAKDLD 643
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEeTEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*..
gi 515497727 644 FEKATELRDMLFELKAE 660
Cdd:COG0556  641 FEEAARLRDEIKELKKE 657
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-660 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1349.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:PRK05298   4 PFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEFFPE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:PRK05298  84 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:PRK05298 164 GQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:PRK05298 244 YPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPY 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:PRK05298 324 TLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYELEK 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 TD-EMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL 484
Cdd:PRK05298 404 SGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQY 564
Cdd:PRK05298 484 ERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQK 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 565 ALDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDetnekqqtelpkKMTKKERQKTIENIEKEMKKAAKDLDF 644
Cdd:PRK05298 564 AIDETERRREIQIAYNEEHGITPKTIKKKIRDILDSVYKKD------------KLSKKELEKLIKELEKQMKEAAKNLEF 631
                        650
                 ....*....|....*.
gi 515497727 645 EKATELRDMLFELKAE 660
Cdd:PRK05298 632 EEAARLRDEIKELKEE 647
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
6-658 0e+00

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. 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: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 1175.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727    6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  406 TDEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLE 485
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  486 RIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQYA 565
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  566 LDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDETNEK--QQTELPKKMTKKERQKTIENIEKEMKKAAKDLD 643
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAKkkKKGEDLSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 515497727  644 FEKATELRDMLFELK 658
Cdd:TIGR00631 641 FEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
7-415 0e+00

DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like 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: 350674 [Multi-domain]  Cd Length: 299  Bit Score: 558.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   7 FKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPEN 86
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  87 RVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYglgnpeeykdlvvsvrvg 166
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 167 memdrsellrklvdvqysrndidfQRGtfrvrgdVVEIfpasREEMCIRVEFFgdeidrirevnyltgevirerehfaif 246
Cdd:cd17916  143 ------------------------ERA-------IKSI----EEELEERLKYF--------------------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 247 pashfvtreekmkvaieriekeleerlkelKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYT 326
Cdd:cd17916  161 ------------------------------RAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 327 LLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEHT 406
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                 ....*....
gi 515497727 407 DEMIEQIIR 415
Cdd:cd17916  291 GQVVEQIIR 299
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
161-251 9.01e-45

UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the UvrA protein.


Pssm-ID: 465486 [Multi-domain]  Cd Length: 91  Bit Score: 154.47  E-value: 9.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  161 VSVRVGMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIRER 240
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 515497727  241 EHFAIFPASHF 251
Cdd:pfam17757  81 DEVTIYPASHY 91
HELICc smart00490
helicase superfamily c-terminal domain;
461-545 2.60e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.95  E-value: 2.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   461 EDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADkegflRSNRSLIQTI 540
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 515497727   541 GRAAR 545
Cdd:smart00490  76 GRAGR 80
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
6-660 0e+00

Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1363.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 T-DEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL 484
Cdd:COG0556  401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQY 564
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 565 ALDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDE-TNEKQQTELPKKMTKKERQKTIENIEKEMKKAAKDLD 643
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEeTEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*..
gi 515497727 644 FEKATELRDMLFELKAE 660
Cdd:COG0556  641 FEEAARLRDEIKELKKE 657
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-660 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1349.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:PRK05298   4 PFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEFFPE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:PRK05298  84 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:PRK05298 164 GQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:PRK05298 244 YPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPY 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:PRK05298 324 TLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYELEK 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 TD-EMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL 484
Cdd:PRK05298 404 SGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQY 564
Cdd:PRK05298 484 ERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQK 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 565 ALDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDetnekqqtelpkKMTKKERQKTIENIEKEMKKAAKDLDF 644
Cdd:PRK05298 564 AIDETERRREIQIAYNEEHGITPKTIKKKIRDILDSVYKKD------------KLSKKELEKLIKELEKQMKEAAKNLEF 631
                        650
                 ....*....|....*.
gi 515497727 645 EKATELRDMLFELKAE 660
Cdd:PRK05298 632 EEAARLRDEIKELKEE 647
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
6-658 0e+00

excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. 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: 273185 [Multi-domain]  Cd Length: 655  Bit Score: 1175.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727    6 PFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPE 85
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   86 NRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRV 165
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  246 FPASHFVTREEKMKVAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPY 325
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  326 TLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEH 405
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  406 TDEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLE 485
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  486 RIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQYA 565
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  566 LDETQRRRDIQMAHNEKYGITPKTINKKIHDVISATVDNDETNEK--QQTELPKKMTKKERQKTIENIEKEMKKAAKDLD 643
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAKkkKKGEDLSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 515497727  644 FEKATELRDMLFELK 658
Cdd:TIGR00631 641 FEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
7-415 0e+00

DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II) and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA, but its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a member of the DEAD-like 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: 350674 [Multi-domain]  Cd Length: 299  Bit Score: 558.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   7 FKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPEN 86
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  87 RVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYglgnpeeykdlvvsvrvg 166
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 167 memdrsellrklvdvqysrndidfQRGtfrvrgdVVEIfpasREEMCIRVEFFgdeidrirevnyltgevirerehfaif 246
Cdd:cd17916  143 ------------------------ERA-------IKSI----EEELEERLKYF--------------------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 247 pashfvtreekmkvaieriekeleerlkelKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYT 326
Cdd:cd17916  161 ------------------------------RAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 327 LLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEHT 406
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                 ....*....
gi 515497727 407 DEMIEQIIR 415
Cdd:cd17916  291 GQVVEQIIR 299
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
421-591 1.38e-109

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 327.67  E-value: 1.38e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 421 DPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDV 500
Cdd:cd18790    1 DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 501 VVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQYALDETQRRRDIQMAHN 580
Cdd:cd18790   81 LVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITDSMQKAIEETERRREIQMEYN 160
                        170
                 ....*....|.
gi 515497727 581 EKYGITPKTIN 591
Cdd:cd18790  161 EEHGITPKTII 171
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
161-251 9.01e-45

UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the UvrA protein.


Pssm-ID: 465486 [Multi-domain]  Cd Length: 91  Bit Score: 154.47  E-value: 9.01e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  161 VSVRVGMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIRER 240
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 515497727  241 EHFAIFPASHF 251
Cdd:pfam17757  81 DEVTIYPASHY 91
Mfd COG1197
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ...
33-525 5.66e-43

Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];


Pssm-ID: 440810 [Multi-domain]  Cd Length: 1130  Bit Score: 166.78  E-value: 5.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   33 GKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFvsyydyyqpeayvPSTDTFIE 112
Cdd:COG1197     1 GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLF-------------PAWETLPY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  113 KDASINDEIDQLRHSATSALFERDDVIIIASV-SCIYGLGNPEEYKDLVVSVRVGMEMDRSELLRKLVDVQYSRNDIDFQ 191
Cdd:COG1197    68 DRFSPSPDIVSERLATLRRLASGKPGIVVTPVrALLQRLPPPELLAAASLSLKVGDELDLEELRERLVAAGYERVDQVEE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  192 RGTFRVRGDVVEIFPASrEEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAIFPASHFVTREEkmkvAIERIekelee 271
Cdd:COG1197   148 PGEFAVRGGILDIFPPG-SEHPVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDEE----AIERF------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  272 rlkelkdENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSvhltlrPL-GSTPYTLLDYFGDDWLVMIDESHVTLPQIR 350
Cdd:COG1197   217 -------RERLRELFGLDPKLDELYEALSEGIAFAGIEYYL------PLfYEELATLFDYLPEDALVVLDEPERIEEAAE 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  351 GMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTN--QLVYVSATPGPYEIEHTdemIEQIIRPtglldpkidVRP 428
Cdd:COG1197   284 EFWEEIEERYEARRHDRGRPLLPPEELFLDPEELFAALKrrPRVTLSPFAALPEGAGV---VNLGARP---------LPS 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  429 TKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVnylhseiktlERIEIIRDLRMGTYDVVVGInlLR 508
Cdd:COG1197   352 FAGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPA----------RLVESLAELSPGGVAITVGP--LE 419
                         490
                  ....*....|....*..
gi 515497727  509 EGIDIPEVSLVVILDAD 525
Cdd:COG1197   420 HGFELPDAKLAVITESE 436
UvrB pfam12344
Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and ...
553-595 1.16e-22

Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam00271, pfam02151, pfam04851. There are two conserved sequence motifs: YAD and RRR. This family is the C terminal region of the UvrB protein which conveys mutational resistance against UV light to various different species.


Pssm-ID: 463540 [Multi-domain]  Cd Length: 43  Bit Score: 90.91  E-value: 1.16e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 515497727  553 MYADKITDSMQYALDETQRRRDIQMAHNEKYGITPKTINKKIH 595
Cdd:pfam12344   1 LYADKITDSMQRAIDETERRREIQEAYNEEHGITPKTIKKKIR 43
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
433-545 3.87e-20

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: 86.11  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  433 IDDLLSEIQERidRDERVLVTTLTKKMSeDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGID 512
Cdd:pfam00271   3 LEALLELLKKE--RGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 515497727  513 IPEVSLVVILDADKegflrSNRSLIQTIGRAAR 545
Cdd:pfam00271  80 LPDVDLVINYDLPW-----NPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
461-545 2.60e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.95  E-value: 2.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   461 EDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADkegflRSNRSLIQTI 540
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 515497727   541 GRAAR 545
Cdd:smart00490  76 GRAGR 80
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
328-549 1.32e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 86.62  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 328 LDYFGDDW-LVMIDESH-VTLPQIRGMFNGDRARkqvlvdhgFRL-----PSAMDNRPLKFEEFEQKTnqlvyvsatpgp 400
Cdd:COG1061  181 LDELGDRFgLVIIDEAHhAGAPSYRRILEAFPAA--------YRLgltatPFRSDGREILLFLFDGIV------------ 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 401 YEIEHTDEMIEQIIRPTGLLDPKIDVRPTKNQIDDL------------------LSEIQERIDRDERVLVTTLTKKMSED 462
Cdd:COG1061  241 YEYSLKEAIEDGYLAPPEYYGIRVDLTDERAEYDALserlrealaadaerkdkiLRELLREHPDDRKTLVFCSSVDHAEA 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 463 LTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDAdkegfLRSNRSLIQTIGR 542
Cdd:COG1061  321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP-----TGSPREFIQRLGR 395

                 ....*..
gi 515497727 543 AARNEKG 549
Cdd:COG1061  396 GLRPAPG 402
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
434-552 1.79e-13

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise 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. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 67.53  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 434 DDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDI 513
Cdd:cd18787   14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 515497727 514 PEVSLVVILDA--DKEGFlrsnrslIQTIGRAAR-NEKGEVI 552
Cdd:cd18787   94 PGVDHVINYDLprDAEDY-------VHRIGRTGRaGRKGTAI 128
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
36-141 7.38e-13

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: 66.27  E-value: 7.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  36 HQTLLGATGTGKTFTMSNVIKEV----GKPTLIIAHNKTLAGQLYSEFKEFFPEN-RVEYFVSYYDYYQPEAYvpstdtf 110
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELFGPGiRVAVLVGGSSAEEREKN------- 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515497727 111 IEKDASI----NDEIDQLRHSATSALFERDDVIII 141
Cdd:cd00046   76 KLGDADIiiatPDMLLNLLLREDRLFLKDLKLIIV 110
ResIII pfam04851
Type III restriction enzyme, res subunit;
19-141 3.03e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 62.30  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727   19 QPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEV-----GKPTLIIAHNKTLAGQLYSEFKEFFPENrveyfVS 93
Cdd:pfam04851   8 QIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLfkkgpIKKVLFLVPRKDLLEQALEEFKKFLPNY-----VE 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515497727   94 YYDYYQPEAYVPSTDT----FIEKDASINDEIDQLRHsatsALFERDDVIII 141
Cdd:pfam04851  83 IGEIISGDKKDESVDDnkivVTTIQSLYKALELASLE----LLPDFFDVIII 130
DEXDc smart00487
DEAD-like helicases superfamily;
7-94 3.65e-11

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 62.89  E-value: 3.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727     7 FKLNSEFDPQGDQPQAIEKIVkgvkEGKRHQTLLGATGTGKTFTMSNVI-----KEVGKPTLIIAHNKTLAGQLYSEFKE 81
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALL----SGLRDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKK 76
                           90
                   ....*....|...
gi 515497727    82 FFPENRVEYFVSY 94
Cdd:smart00487  77 LGPSLGLKVVGLY 89
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
436-649 4.15e-11

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 66.29  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 436 LLSEIQER--IDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYL-----HSEIKTL---ERIEIIRDLRMGTYDVVVGIN 505
Cdd:COG1111  340 LREILKEQlgTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqasKEGDKGLtqkEQIEILERFRAGEFNVLVATS 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 506 LLREGIDIPEVSLVVILDADKEGfLRSnrslIQTIGRAARNEKGEVIMYADKITdsmqyaLDET----QRRRDIQMahne 581
Cdd:COG1111  420 VAEEGLDIPEVDLVIFYEPVPSE-IRS----IQRKGRTGRKREGRVVVLIAKGT------RDEAyywsSRRKEKKM---- 484
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497727 582 kygitpKTINKKIHDVISAtVDNDETNEKQQTELPKKMTKKERQKTIENIEKEMKKAAKDLDFEKATE 649
Cdd:COG1111  485 ------KSILKKLKKLLDK-QEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENGAHVDWR 545
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
435-626 4.56e-11

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 65.17  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 435 DLLSEIQERIDrDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIP 514
Cdd:COG0513  230 ELLRRLLRDED-PERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDID 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 515 EVSLVVILD--ADKEGFL-RsnrsliqtIGRAAR-NEKGEVIMYADKitdsmqyalDETQRRRDIQmahnekygitpKTI 590
Cdd:COG0513  309 DVSHVINYDlpEDPEDYVhR--------IGRTGRaGAEGTAISLVTP---------DERRLLRAIE-----------KLI 360
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515497727 591 NKKIHDVisaTVDNDETNEKQQTELPKKMTKKERQK 626
Cdd:COG0513  361 GQKIEEE---ELPGFEPVEEKRLERLKPKIKEKLKG 393
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
178-259 6.01e-10

transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273152 [Multi-domain]  Cd Length: 926  Bit Score: 62.76  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  178 LVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMcIRVEFFGDEIDRIREVNYLTGEVIREREHFAIFPASHFVTREEK 257
Cdd:TIGR00580   1 LVELGYERVDLVEEEGEFSVRGEILDIFPPGSELP-VRIEFFGDEIESIREFDVDSQRSLEELLEITILPAKEFILLEEE 79

                  ..
gi 515497727  258 MK 259
Cdd:TIGR00580  80 TI 81
PRK13766 PRK13766
Hef nuclease; Provisional
417-649 2.43e-09

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 60.66  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 417 TGLLDPKIDvrptknQIDDLLSEIQErIDRDERVLVTTLTKKMSEDLTTYMKEAGIKV-------NYLHSE-IKTLERIE 488
Cdd:PRK13766 342 LDIEHPKLE------KLREIVKEQLG-KNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqaSKDGDKgMSQKEQIE 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 489 IIRDLRMGTYDVVVGINLLREGIDIPEVSLVVildadkegF-------LRSnrslIQTIGRAARNEKGEVIMYADKITds 561
Cdd:PRK13766 415 ILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI--------FyepvpseIRS----IQRKGRTGRQEEGRVVVLIAKGT-- 480
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 562 mqyaLDET----QRRRDIQMahnekygitpKTINKKIHDVIsatvdnDETNEKQQTELPKKMTKKERQKTIENIEKEMKK 637
Cdd:PRK13766 481 ----RDEAyywsSRRKEKKM----------KEELKNLKGIL------NKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGK 540
                        250
                 ....*....|..
gi 515497727 638 AAKDLDFEKATE 649
Cdd:PRK13766 541 EEEEEEEKEEKD 552
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
36-98 4.51e-09

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


Pssm-ID: 350670 [Multi-domain]  Cd Length: 81  Bit Score: 53.68  E-value: 4.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497727  36 HQTLLGATGTGKTFTMSNVIKEV---GKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYY 98
Cdd:cd17912    1 NILHLGPTGSGKTLVAIQKIASAmssGKSVLVVTPTKLLAHEILIVIDEIQ*ILDPAAGWAWATRA 66
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
19-86 1.01e-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: 54.87  E-value: 1.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497727  19 QPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEV-----GKPTLIIAHNKTLAGQLYSEFKEFFPEN 86
Cdd:cd18032    5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLleanrKKRILFLAHREELLEQAERSFKEVLPDG 77
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
456-552 1.69e-08

C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350191 [Multi-domain]  Cd Length: 238  Bit Score: 55.71  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 456 TKKMSEDLTTYMKEAGI-KVNYLHSEIKTLERiEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNR 534
Cdd:cd18804  103 TERVEEELKTLFPEARIaRIDRDTTRKKGALE-KLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSGLNSPDFR 181
                         90       100
                 ....*....|....*....|....*.
gi 515497727 535 S-------LIQTIGRAAR-NEKGEVI 552
Cdd:cd18804  182 AserafqlLTQVSGRAGRgDKPGKVI 207
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
446-545 4.19e-08

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 51.79  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 446 RDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLER-IEIIRDLRMGTY--DVVVGINLLREGIDIPEVSLVVil 522
Cdd:cd18799    5 VEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELkpPILVTVDLLTTGVDIPEVDNVV-- 82
                         90       100
                 ....*....|....*....|....*.
gi 515497727 523 dadkegFLRSNRSLI---QTIGRAAR 545
Cdd:cd18799   83 ------FLRPTESRTlflQMLGRGLR 102
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
500-555 4.84e-08

C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved 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: 350171 [Multi-domain]  Cd Length: 59  Bit Score: 49.85  E-value: 4.84e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515497727 500 VVVGINLLREGIDIPEVSLVVILDADkegflRSNRSLIQTIGRAARN-EKGEVIMYA 555
Cdd:cd09300    8 VLIAVN*ALTGFDAPELNTIIVDKNL-----RSYRGLNQAFGRANRIyTFGGIVTYR 59
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
500-554 6.05e-08

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: 50.01  E-value: 6.05e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515497727 500 VVVGINLLREGIDIPEVSLVVILDADkegflRSNRSLIQTIGRAARNEK--GEVIMY 554
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPP-----SSAASYIQRVGRAGRGGKdeGEVILF 76
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
19-91 8.52e-08

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: 51.92  E-value: 8.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497727  19 QPQAIEKIVKgvKEGKRHQTLLGATGTGKTFTMSNVIKEVGK-PTLIIAHNKTLAGQLYSEFKEFFPENRVEYF 91
Cdd:cd17926    5 QEEALEAWLA--HKNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGDSSIGLI 76
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
485-553 3.67e-07

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 50.05  E-value: 3.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497727 485 ERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKegflrSNRSLIQTIGRAARNEKGEVIM 553
Cdd:cd18801   78 EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASP-----SPIRMIQRMGRTGRKRQGRVVV 141
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
13-89 3.93e-07

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the 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: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.49  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  13 FDPQGDQPQAIEKIVKGVKEGKRHQTLL-GATGTGKTFTMSNVIK---EVGKPTLIIAHNKTLAGQLYSEFKEFFPENRV 88
Cdd:cd17918   14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLsGDVGSGKTLVALGAALlayKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93

                 .
gi 515497727  89 E 89
Cdd:cd17918   94 E 94
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
444-554 5.25e-07

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 49.56  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 444 IDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTL-------ERIEIIRDLRMGTYDVVVGINLLREGIDIPEV 516
Cdd:cd18797   32 VRAGVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASYragylaeDRREIEAELFNGELLGVVATNALELGIDIGGL 111
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515497727 517 SLVVILdadkeGFLRSNRSLIQTIGRAARNEKGEVIMY 554
Cdd:cd18797  112 DAVVLA-----GYPGSLASLWQQAGRAGRRGKDSLVIL 144
UVR pfam02151
UvrB/uvrC motif;
625-660 6.50e-07

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 45.85  E-value: 6.50e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 515497727  625 QKTIENIEKEMKKAAKDLDFEKATELRDMLFELKAE 660
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
459-561 7.28e-07

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It 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: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 49.26  E-value: 7.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 459 MSEDLTTYMKeAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFlrsnRSLIQ 538
Cdd:cd18811   50 MYEYLKERFR-PELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGL----SQLHQ 124
                         90       100
                 ....*....|....*....|....*
gi 515497727 539 TIGRAARNEKGE--VIMYADKITDS 561
Cdd:cd18811  125 LRGRVGRGDHQSycLLVYKDPLTET 149
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
423-545 1.39e-06

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 47.97  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 423 KIDVRP-TKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVV 501
Cdd:cd18794    5 FYSVRPkDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515497727 502 VGINLLREGIDIPEVSLVVILDADK--EGFLrsnrsliQTIGRAAR 545
Cdd:cd18794   85 VATVAFGMGIDKPDVRFVIHYSLPKsmESYY-------QESGRAGR 123
PRK05580 PRK05580
primosome assembly protein PriA; Validated
488-552 5.85e-06

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 49.38  E-value: 5.85e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497727 488 EIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADkeGFLRSN--RS-------LIQTIGRAARNEK-GEVI 552
Cdd:PRK05580 471 QLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDAD--LGLFSPdfRAsertfqlLTQVAGRAGRAEKpGEVL 543
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
447-548 8.14e-06

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 46.05  E-value: 8.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 447 DERVLVTTLTKKMSE------DLTT-YMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLV 519
Cdd:cd18802   33 ERRATAVVLSRLLKEhpstlaFIRCgFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLV 112
                         90       100       110
                 ....*....|....*....|....*....|.
gi 515497727 520 VILDadkegfLRSN-RSLIQTIGRA-ARNEK 548
Cdd:cd18802  113 IRFD------LPKTlRSYIQSRGRArAPNSK 137
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
444-545 1.30e-05

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 48.29  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 444 IDRDERVLVTTLTKKMSEDLTTYMKEA------GIKV-----NYLHSEiktleRIEIIRDLRMGTYDVVVGINLLREGID 512
Cdd:COG1205  285 VREGLRTLVFTRSRRGAELLARYARRAlrepdlADRVaayraGYLPEE-----RREIERGLRSGELLGVVSTNALELGID 359
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515497727 513 IPEVSLVVILdadkeGFLRSNRSLIQTIGRAAR 545
Cdd:COG1205  360 IGGLDAVVLA-----GYPGTRASFWQQAGRAGR 387
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
433-545 2.06e-05

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 44.95  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 433 IDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEA------GIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINL 506
Cdd:cd18796   24 GADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSS 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515497727 507 LREGIDIPEVSLVVILDADKegflrSNRSLIQTIGRAAR 545
Cdd:cd18796  104 LELGIDIGDVDLVIQIGSPK-----SVARLLQRLGRSGH 137
PTZ00424 PTZ00424
helicase 45; Provisional
456-545 2.40e-05

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 47.13  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 456 TKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKegflrSNRS 535
Cdd:PTZ00424 276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA-----SPEN 350
                         90
                 ....*....|
gi 515497727 536 LIQTIGRAAR 545
Cdd:PTZ00424 351 YIHRIGRSGR 360
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
458-573 6.89e-05

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. 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: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 43.79  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 458 KMSEDLTTYMKEAgiKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFlrsnRSLI 537
Cdd:cd18792   49 ALAEELKELVPEA--RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGL----SQLH 122
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515497727 538 QTIGRAARNEKGE--VIMYADKItdsmqyALDETQRRR 573
Cdd:cd18792  123 QLRGRVGRGKHQSycYLLYPDPK------KLTETAKKR 154
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
471-554 8.34e-05

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 45.55  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 471 GIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDadkegFLRSNRSLIQTIGRAAR-NEKG 549
Cdd:PLN00206 392 GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFD-----MPNTIKEYIHQIGRASRmGEKG 466

                 ....*
gi 515497727 550 EVIMY 554
Cdd:PLN00206 467 TAIVF 471
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
428-549 1.32e-04

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: 42.62  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 428 PTKNQIddlLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIkvnylHSEIKTLERIEIIRDLRMGTYDVVVGINLL 507
Cdd:cd18789   33 PNKLRA---LEELLKRHEQGDKIIVFTDNVEALYRYAKRLLKPFI-----TGETPQSEREEILQNFREGEYNTLVVSKVG 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 515497727 508 REGIDIPEVSLVVILdadkEGFLRSNRSLIQTIGRAARNEKG 549
Cdd:cd18789  105 DEGIDLPEANVAIQI----SGHGGSRRQEAQRLGRILRPKKG 142
uvrC PRK00558
excinuclease ABC subunit UvrC;
625-654 1.75e-04

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 44.72  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 515497727 625 QKTIENIEKEMKKAAKDLDFEKATELRDML 654
Cdd:PRK00558 201 DEVLKELEEKMEEASENLEFERAARYRDQI 230
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
488-552 2.02e-04

Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 44.72  E-value: 2.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497727 488 EIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADkEGF----LRSN-RS---LIQTIGRAARNEK-GEVI 552
Cdd:COG1198  522 KLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDAD-LGLnspdFRAAeRTfqlLTQVAGRAGRAEKpGEVL 594
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
406-552 2.54e-04

CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 43.92  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 406 TDEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAG--IKVNYLHSEIKT 483
Cdd:COG1203  325 PDEPEELPEYFRAFVRKRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLpdEEVYLLHSRFCP 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 484 LERIEIIRDLRM----GTYDVVVG---InllregidipEVSL-----VVI-----LDadkegflrsnrSLIQTIGRAARN 546
Cdd:COG1203  405 ADRSEIEKEIKErlerGKPCILVStqvV----------EAGVdidfdVVIrdlapLD-----------SLIQRAGRCNRH 463
                        170
                 ....*....|
gi 515497727 547 ----EKGEVI 552
Cdd:COG1203  464 grkeEEGNVY 473
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
166-263 2.65e-04

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 44.35  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727  166 GMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMcIRVEFFGDEIDRIREVNYLTGEVIREREHFAI 245
Cdd:PRK10689  133 GQRLSRDALRAQLEQAGYRHVDQVMEHGEYATRGALLDLFPMGSEEP-YRIDFFDDEIDSLRVFDVDSQRTLEEVEAINL 211
                          90
                  ....*....|....*...
gi 515497727  246 FPASHFVTReekmKVAIE 263
Cdd:PRK10689  212 LPAHEFPTD----KAAIE 225
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
628-659 3.47e-04

Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 43.57  E-value: 3.47e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 515497727 628 IENIEKEMKKAAKDLDFEKATELRDMLFELKA 659
Cdd:COG0322  205 IKELEEKMEEAAEELEFERAARLRDQIRALEK 236
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
19-87 6.11e-04

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 42.91  E-value: 6.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497727  19 QPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTM---------SNVIKEVgkptLIIAHNKTLAGQLYSEFKEFFPENR 87
Cdd:COG4096  163 QIEAIRRVEEAIAKGQRRALLVMATGTGKTRTAialiyrllkAGRAKRI----LFLADRNALVDQAKNAFKPFLPDLD 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
433-523 1.48e-03

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 41.75  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 433 IDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINL--LREG 510
Cdd:COG0553  535 LEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLkaGGEG 614
                         90
                 ....*....|...
gi 515497727 511 IDIPEVSLVVILD 523
Cdd:COG0553  615 LNLTAADHVIHYD 627
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
411-556 1.51e-03

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 39.46  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 411 EQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMkeAGIKvnYLHSEIKTLERiEII 490
Cdd:cd18795    7 EYVLGFNGLGIKLRVDVMNKFDSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDL--AGIA--FHHAGLTREDR-ELV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 491 RDL-RMGTYDVVV-------GINLlregidiPeVSLVVILD---ADKEGFLR-SNRSLIQTIGRAAR---NEKGEVIMYA 555
Cdd:cd18795   82 EELfREGLIKVLVatstlaaGVNL-------P-ARTVIIKGtqrYDGKGYRElSPLEYLQMIGRAGRpgfDTRGEAIIMT 153

                 .
gi 515497727 556 D 556
Cdd:cd18795  154 K 154
McsA COG3880
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ...
616-661 2.76e-03

Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443088 [Multi-domain]  Cd Length: 173  Bit Score: 39.11  E-value: 2.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 515497727 616 PKKM-TKKERQKTIENIEKEMKKAAKDLDFEKATELRDMLFELKAEG 661
Cdd:COG3880  122 PKRAgGRLRIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEKEL 168
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
473-573 2.94e-03

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF 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: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 38.86  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497727 473 KVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRsnrsLIQTIGRAARnekGEVI 552
Cdd:cd18810   53 RIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQ----LYQLRGRVGR---SKER 125
                         90       100
                 ....*....|....*....|.
gi 515497727 553 MYADKITDSmQYALDETQRRR 573
Cdd:cd18810  126 AYAYFLYPD-QKKLTEDALKR 145
DEXHc_priA cd17929
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ...
19-90 7.80e-03

DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA 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: 350687 [Multi-domain]  Cd Length: 178  Bit Score: 37.96  E-value: 7.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497727  19 QPQAIEKIVKGVKEGKRHqtLL-GATGTGKTFTMSNVIKEV---GKPTLIIAHNKTLAGQLYSEFKEFFPENRVEY 90
Cdd:cd17929    1 QRKAYEAIVSSLGGFKTF--LLhGVTGSGKTEVYIELIEKVlakGKQVLVLVPEISLTPQLIKRFKKRFGDKVAVL 74
 
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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