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Conserved domains on  [gi|2754591276|gb|XCL94773|]
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excinuclease ABC subunit UvrB [Enterococcus faecalis]

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];
10-663 0e+00

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


:

Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1396.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  10 FHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:COG0556     2 FKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRVG 169
Cdd:COG0556    82 AVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRVG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 170 MEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIF 249
Cdd:COG0556   162 EEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTIY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 250 PATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYT 329
Cdd:COG0556   242 PASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPPT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 330 LLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQT 409
Cdd:COG0556   322 LLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEKS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 410 ET-VVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLE 488
Cdd:COG0556   402 GGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 489 RTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRA 568
Cdd:COG0556   482 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQRA 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 569 MDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYEDLSRQEKADLLMKLEREMKDAAKALDF 648
Cdd:COG0556   562 IDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLEF 641
                         650
                  ....*....|....*
gi 2754591276 649 ETAATLRDTILELKA 663
Cdd:COG0556   642 EEAARLRDEIKELKK 656
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
10-663 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1396.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  10 FHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:COG0556     2 FKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRVG 169
Cdd:COG0556    82 AVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRVG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 170 MEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIF 249
Cdd:COG0556   162 EEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTIY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 250 PATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYT 329
Cdd:COG0556   242 PASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPPT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 330 LLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQT 409
Cdd:COG0556   322 LLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEKS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 410 ET-VVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLE 488
Cdd:COG0556   402 GGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 489 RTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRA 568
Cdd:COG0556   482 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQRA 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 569 MDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYEDLSRQEKADLLMKLEREMKDAAKALDF 648
Cdd:COG0556   562 IDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLEF 641
                         650
                  ....*....|....*
gi 2754591276 649 ETAATLRDTILELKA 663
Cdd:COG0556   642 EEAARLRDEIKELKK 656
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-663 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1377.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   6 TSNTFHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEF 85
Cdd:PRK05298    1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  86 FPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVS 165
Cdd:PRK05298   81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 166 LRVGMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEH 245
Cdd:PRK05298  161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 246 VAIFPATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGE 325
Cdd:PRK05298  241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 326 PPYTLLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYE 405
Cdd:PRK05298  321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 406 MEQTE-TVVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDI 484
Cdd:PRK05298  401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 485 KTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDS 564
Cdd:PRK05298  481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 565 MQRAMDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKdetvvqldksyedLSRQEKADLLMKLEREMKDAAK 644
Cdd:PRK05298  561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDILDSVYKKDK-------------LSKKELEKLIKELEKQMKEAAK 627
                         650
                  ....*....|....*....
gi 2754591276 645 ALDFETAATLRDTILELKA 663
Cdd:PRK05298  628 NLEFEEAARLRDEIKELKE 646
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
9-662 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: 1211.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   9 TFHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRV 168
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 169 GMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAI 248
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 249 FPATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPY 328
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 329 TLLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQ 408
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 409 TETVVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLE 488
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 489 RTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRA 568
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 569 MDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSY-EDLSRQEKADLLMKLEREMKDAAKALD 647
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAKKKKKGEDlSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 2754591276 648 FETAATLRDTILELK 662
Cdd:TIGR00631 641 FEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
10-418 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: 569.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  10 FHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:cd17916     1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFglgdpreysqqvvslrvg 169
Cdd:cd17916    81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 170 memdrnellkslvdiqferndidfqrgrfrvrgdvveifpasrdehalrveffgdeidrirevdaltgeivgetehvaif 249
Cdd:cd17916       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 250 pathfvtneehmEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYT 329
Cdd:cd17916   143 ------------ERAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 330 LLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQT 409
Cdd:cd17916   211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                  ....*....
gi 2754591276 410 ETVVQQIIR 418
Cdd:cd17916   291 GQVVEQIIR 299
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
164-254 2.42e-44

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: 153.32  E-value: 2.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 164 VSLRVGMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGET 243
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 2754591276 244 EHVAIFPATHF 254
Cdd:pfam17757  81 DEVTIYPASHY 91
HELICc smart00490
helicase superfamily c-terminal domain;
464-548 4.89e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.18  E-value: 4.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  464 EDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADkegflRSERSLVQTM 543
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 2754591276  544 GRAAR 548
Cdd:smart00490  76 GRAGR 80
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
10-663 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1396.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  10 FHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:COG0556     2 FKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRVG 169
Cdd:COG0556    82 AVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRVG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 170 MEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIF 249
Cdd:COG0556   162 EEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTIY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 250 PATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYT 329
Cdd:COG0556   242 PASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPPT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 330 LLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQT 409
Cdd:COG0556   322 LLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEKS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 410 ET-VVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLE 488
Cdd:COG0556   402 GGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTLE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 489 RTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRA 568
Cdd:COG0556   482 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQRA 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 569 MDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYEDLSRQEKADLLMKLEREMKDAAKALDF 648
Cdd:COG0556   562 IDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEELVAEADAAKLSKEELEKLIKELEKEMKEAAKNLEF 641
                         650
                  ....*....|....*
gi 2754591276 649 ETAATLRDTILELKA 663
Cdd:COG0556   642 EEAARLRDEIKELKK 656
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-663 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1377.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   6 TSNTFHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEF 85
Cdd:PRK05298    1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  86 FPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVS 165
Cdd:PRK05298   81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 166 LRVGMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEH 245
Cdd:PRK05298  161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 246 VAIFPATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGE 325
Cdd:PRK05298  241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 326 PPYTLLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYE 405
Cdd:PRK05298  321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 406 MEQTE-TVVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDI 484
Cdd:PRK05298  401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 485 KTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDS 564
Cdd:PRK05298  481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 565 MQRAMDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKdetvvqldksyedLSRQEKADLLMKLEREMKDAAK 644
Cdd:PRK05298  561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDILDSVYKKDK-------------LSKKELEKLIKELEKQMKEAAK 627
                         650
                  ....*....|....*....
gi 2754591276 645 ALDFETAATLRDTILELKA 663
Cdd:PRK05298  628 NLEFEEAARLRDEIKELKE 646
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
9-662 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: 1211.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   9 TFHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREYSQQVVSLRV 168
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 169 GMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAI 248
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 249 FPATHFVTNEEHMEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPY 328
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 329 TLLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQ 408
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 409 TETVVQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLE 488
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 489 RTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRA 568
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 569 MDETARRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSY-EDLSRQEKADLLMKLEREMKDAAKALD 647
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKEKEDAAKKKKKGEDlSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 2754591276 648 FETAATLRDTILELK 662
Cdd:TIGR00631 641 FEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
10-418 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: 569.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  10 FHLASKYEPAGDQPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:cd17916     1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFglgdpreysqqvvslrvg 169
Cdd:cd17916    81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 170 memdrnellkslvdiqferndidfqrgrfrvrgdvveifpasrdehalrveffgdeidrirevdaltgeivgetehvaif 249
Cdd:cd17916       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 250 pathfvtneehmEHAISQIQEELEARLKVLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSRHMDGRQEGEPPYT 329
Cdd:cd17916   143 ------------ERAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 330 LLDFFPDDFLLVIDESHVTMPQIRGMYNGDRARKQMLVDYGFRLPSALDNRPLRLEEFEQHVNQIVYVSATPGPYEMEQT 409
Cdd:cd17916   211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                  ....*....
gi 2754591276 410 ETVVQQIIR 418
Cdd:cd17916   291 GQVVEQIIR 299
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
424-594 4.62e-113

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: 336.52  E-value: 4.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 424 DPEVEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDI 503
Cdd:cd18790     1 DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 504 LIGINLLREGIDVPEVSLIAILDADKEGFLRSERSLVQTMGRAARNAEGKVIMYADKITDSMQRAMDETARRRAIQEAYN 583
Cdd:cd18790    81 LVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITDSMQKAIEETERRREIQMEYN 160
                         170
                  ....*....|.
gi 2754591276 584 EEHGIEPKTII 594
Cdd:cd18790   161 EEHGITPKTII 171
Mfd COG1197
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ...
36-528 7.40e-45

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


Pssm-ID: 440810 [Multi-domain]  Cd Length: 1130  Bit Score: 172.56  E-value: 7.40e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   36 GEKAQILLGATGTGKTFTISNVIQEVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFvsyydyyqpeayvPSSDTYIE 115
Cdd:COG1197      1 GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLF-------------PAWETLPY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  116 KDSSINDEIDKLRHSATSSLLERNDVIVVASVSCIFGLGDPREY-SQQVVSLRVGMEMDRNELLKSLVDIQFERNDIDFQ 194
Cdd:COG1197     68 DRFSPSPDIVSERLATLRRLASGKPGIVVTPVRALLQRLPPPELlAAASLSLKVGDELDLEELRERLVAAGYERVDQVEE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  195 RGRFRVRGDVVEIFPASrDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIFPATHFVTNEEHMEHAISQIQEELEA 274
Cdd:COG1197    148 PGEFAVRGGILDIFPPG-SEHPVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDEEAIERFRERLRELFGL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  275 RlkvlrsenklleaqrleQRTNYDIEMMREMGYTSGIENYSrhmdgrqegepPY------TLLDFFPDDFLLVIDESHVT 348
Cdd:COG1197    227 D-----------------PKLDELYEALSEGIAFAGIEYYL-----------PLfyeelaTLFDYLPEDALVVLDEPERI 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  349 MPQIRGMYNGDRAR-KQMLVDYGfRLPSALDNRPLRLEEFEQHVN--QIVYVSATPgpyEMEQTETVVQQIIRPtglldp 425
Cdd:COG1197    279 EEAAEEFWEEIEERyEARRHDRG-RPLLPPEELFLDPEELFAALKrrPRVTLSPFA---ALPEGAGVVNLGARP------ 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  426 eveIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSdiktlerteiIRDLRLGEFDILI 505
Cdd:COG1197    349 ---LPSFAGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPARLVES----------LAELSPGGVAITV 415
                          490       500
                   ....*....|....*....|...
gi 2754591276  506 GInlLREGIDVPEVSLIAILDAD 528
Cdd:COG1197    416 GP--LEHGFELPDAKLAVITESE 436
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
164-254 2.42e-44

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: 153.32  E-value: 2.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 164 VSLRVGMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASRDEHALRVEFFGDEIDRIREVDALTGEIVGET 243
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 2754591276 244 EHVAIFPATHF 254
Cdd:pfam17757  81 DEVTIYPASHY 91
UvrB pfam12344
Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and ...
556-598 1.04e-25

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: 99.77  E-value: 1.04e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2754591276 556 MYADKITDSMQRAMDETARRRAIQEAYNEEHGIEPKTIIKEIR 598
Cdd:pfam12344   1 LYADKITDSMQRAIDETERRREIQEAYNEEHGITPKTIKKKIR 43
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
434-548 3.37e-18

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: 80.33  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 434 GQIDDLVGEINEriEKDQRVFVTTLTKKMAEdlTDYFKEL-GLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLRE 512
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2754591276 513 GIDVPEVSLIAILDADKegflrSERSLVQTMGRAAR 548
Cdd:pfam00271  77 GLDLPDVDLVINYDLPW-----NPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
464-548 4.89e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.18  E-value: 4.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  464 EDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADkegflRSERSLVQTM 543
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 2754591276  544 GRAAR 548
Cdd:smart00490  76 GRAGR 80
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
394-585 7.32e-18

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 86.85  E-value: 7.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 394 IVYVSATPGPYEMEQtetvVQQIIRPTGLLD------PEVEIRPIM----------GQI-DDLVGEINERIEKDQRVFVT 456
Cdd:COG4098   250 LIYLTATPSKALQRQ----VKRGKLKVVKLParyhghPLPVPKFKWlgnwkkrlrrGKLpRKLLKWLKKRLKEGRQLLIF 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 457 TLTKKMAEDLTDYFKEL--GLKVKYLHSdiKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSlIAILDADKEGFlr 534
Cdd:COG4098   326 VPTIELLEQLVALLQKLfpEERIAGVHA--EDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD-VAVLGADHPVF-- 400
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2754591276 535 SERSLVQTMGRAARNAE---GKVIMYADKITDSMQRAmdetarRRAIQEaYNEE 585
Cdd:COG4098   401 TEAALVQIAGRVGRSADyptGEVIFFHHGKTRAMKRA------IREIKR-MNRE 447
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
331-663 7.85e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.31  E-value: 7.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 331 LDFFPDDF-LLVIDESH-VTMPQIRGMYNGDRARkqmlvdygFRL-----PSALDNRPLRLEEFEqhvnQIVYvsaTPGP 403
Cdd:COG1061   181 LDELGDRFgLVIIDEAHhAGAPSYRRILEAFPAA--------YRLgltatPFRSDGREILLFLFD----GIVY---EYSL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 404 YEMEQtetvvQQIIRPTGLLDPEVEIRPIMGQIDDLVGEINERIEKDQ------------------RVFVTTLTKKMAED 465
Cdd:COG1061   246 KEAIE-----DGYLAPPEYYGIRVDLTDERAEYDALSERLREALAADAerkdkilrellrehpddrKTLVFCSSVDHAEA 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 466 LTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDAdkegfLRSERSLVQTMGR 545
Cdd:COG1061   321 LAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP-----TGSPREFIQRLGR 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 546 AARNAEGK----VIMYADKITDSMQRAMDEtaRRRAIQEAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYE 621
Cdd:COG1061   396 GLRPAPGKedalVYDFVGNDVPVLEELAKD--LRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLE 473
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2754591276 622 DLSRQEKADLLMKLEREMKDAAKALDFETAATLRDTILELKA 663
Cdd:COG1061   474 DALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELL 515
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
453-555 4.66e-12

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: 63.68  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 453 VFVTTltKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDadkegF 532
Cdd:cd18787    32 IFVNT--KKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYD-----L 104
                          90       100
                  ....*....|....*....|....
gi 2754591276 533 LRSERSLVQTMGRAAR-NAEGKVI 555
Cdd:cd18787   105 PRDAEDYVHRIGRTGRaGRKGTAI 128
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
453-555 7.49e-11

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: 62.65  E-value: 7.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 453 VFVTTLTKKMAEDLTDYFKELglKVKYLHSDI--KTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKE 530
Cdd:cd18804    97 VFKGIGTERVEEELKTLFPEA--RIARIDRDTtrKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSG 174
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2754591276 531 GFL---RS-ERS---LVQTMGRAAR-NAEGKVI 555
Cdd:cd18804   175 LNSpdfRAsERAfqlLTQVSGRAGRgDKPGKVI 207
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
37-144 1.40e-10

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: 59.72  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  37 EKAQILLGATGTGKTFTISNVIQEVN----KPTLVIAHNKTLAGQLYGEFKEFF-PDNAVEYFVSYYDYYQPEAyvpssd 111
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLlkkgKKVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSAEEREK------ 74
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2754591276 112 tYIEKDSSI----NDEIDKLRHSATSSLLERNDVIVV 144
Cdd:cd00046    75 -NKLGDADIiiatPDMLLNLLLREDRLFLKDLKLIIV 110
DEXDc smart00487
DEAD-like helicases superfamily;
10-97 2.79e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 60.20  E-value: 2.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276   10 FHLASKYEPAGDQPAAIAELVDGVKGGekaqILLGATGTGKTFTISNVI-----QEVNKPTLVIAHNKTLAGQLYGEFKE 84
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV----ILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKK 76
                           90
                   ....*....|...
gi 2754591276   85 FFPDNAVEYFVSY 97
Cdd:smart00487  77 LGPSLGLKVVGLY 89
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
459-553 5.29e-10

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: 57.18  E-value: 5.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 459 TKKMAEDLTDYFKELGLKVKYLHSDIKTLERT-EIIRDLRLGE--FDILIGINLLREGIDVPEVSLIAildadkegFLRS 535
Cdd:cd18799    15 SIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGElkPPILVTVDLLTTGVDIPEVDNVV--------FLRP 86
                          90       100
                  ....*....|....*....|.
gi 2754591276 536 ERS---LVQTMGRAARNAEGK 553
Cdd:cd18799    87 TESrtlFLQMLGRGLRLHEGK 107
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
181-353 5.52e-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: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 181 LVDIQFERNDIDFQRGRFRVRGDVVEIFPASrDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAIFPATHFVTNEeh 260
Cdd:TIGR00580   1 LVELGYERVDLVEEEGEFSVRGEILDIFPPG-SELPVRIEFFGDEIESIREFDVDSQRSLEELLEITILPAKEFILLE-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 261 mehaisqiqEELEARLK-VLRSENKLLEAQRLEQRTNYDIEMMREMGYTSGIENYSrhmdgrqegeppyTLLDFFPDDFL 339
Cdd:TIGR00580  78 ---------EETIARLKdNAARVEDAKHLETIEALSEGTLPAGEEMFLPLFFEDLS-------------SLFDYLPDNTP 135
                         170
                  ....*....|....
gi 2754591276 340 LVIDESHVTMPQIR 353
Cdd:TIGR00580 136 ILLDDPERFHSAAR 149
ResIII pfam04851
Type III restriction enzyme, res subunit;
22-144 1.05e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 57.68  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  22 QPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEVNK-----PTLVIAHNKTLAGQLYGEFKEFFPDNaveyfVS 96
Cdd:pfam04851   8 QIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKkgpikKVLFLVPRKDLLEQALEEFKKFLPNY-----VE 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2754591276  97 YYDYYQPEAYVPSSDTYIEKDSSInDEIDKLRHSATSSLL-ERNDVIVV 144
Cdd:pfam04851  83 IGEIISGDKKDESVDDNKIVVTTI-QSLYKALELASLELLpDFFDVIII 130
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
429-556 3.13e-09

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: 55.82  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 429 IRPIMGQIDDLVGEINER--IEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYL----HSDIKTL------ERTEIIRDL 496
Cdd:cd18801     7 IHPKLEKLEEIVKEHFKKkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGKSSkgmsqkEQKEVIEQF 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 497 RLGEFDILIGINLLREGIDVPEVSLIAILDADKegflrSERSLVQTMGRAARNAEGKVIM 556
Cdd:cd18801    87 RKGGYNVLVATSIGEEGLDIGEVDLIICYDASP-----SPIRMIQRMGRTGRKRQGRVVV 141
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
446-593 3.75e-09

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 59.39  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 446 RIEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIaI- 524
Cdd:COG0513   237 RDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV-In 315
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2754591276 525 --LDADKEGFL-RSerslvqtmGRAAR-NAEGKVIMYADKitdsmqramDETARRRAIQEAYNEEhgIEPKTI 593
Cdd:COG0513   316 ydLPEDPEDYVhRI--------GRTGRaGAEGTAISLVTP---------DERRLLRAIEKLIGQK--IEEEEL 369
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
40-101 5.16e-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: 53.29  E-value: 5.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2754591276  40 QILLGATGTGKTFTISNVIQEVN---KPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYY 101
Cdd:cd17912     2 ILHLGPTGSGKTLVAIQKIASAMssgKSVLVVTPTKLLAHEILIVIDEIQ*ILDPAAGWAWATRA 66
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
461-580 2.05e-08

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: 53.81  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 461 KMAEDLTDYFKELglKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFlrseRSLV 540
Cdd:cd18792    49 ALAEELKELVPEA--RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGL----SQLH 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2754591276 541 QTMGRAARnaeGKVIMYADKITDSmQRAMDETARRR--AIQE 580
Cdd:cd18792   123 QLRGRVGR---GKHQSYCYLLYPD-PKKLTETAKKRlrAIAE 160
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
169-275 6.64e-08

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 55.91  E-value: 6.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  169 GMEMDRNELLKSLVDIQFERNDIDFQRGRFRVRGDVVEIFPASrDEHALRVEFFGDEIDRIREVDALTGEIVGETEHVAI 248
Cdd:PRK10689   133 GQRLSRDALRAQLEQAGYRHVDQVMEHGEYATRGALLDLFPMG-SEEPYRIDFFDDEIDSLRVFDVDSQRTLEEVEAINL 211
                           90       100
                   ....*....|....*....|....*..
gi 2754591276  249 FPATHFVTNEEHMEHAISQIQEELEAR 275
Cdd:PRK10689   212 LPAHEFPTDKAAIELFRSQWRDTFEVK 238
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
462-569 1.24e-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: 51.58  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 462 MAEDLTDYFKElGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADKEGFlrseRSLVQ 541
Cdd:cd18811    50 MYEYLKERFRP-ELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGL----SQLHQ 124
                          90       100       110
                  ....*....|....*....|....*....|
gi 2754591276 542 TMGRAARNAEGK--VIMYADKITDSMQRAM 569
Cdd:cd18811   125 LRGRVGRGDHQSycLLVYKDPLTETAKQRL 154
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
22-90 1.39e-07

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: 51.41  E-value: 1.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2754591276  22 QPAAIAELVDGVKGGEKAQILLGATGTGKTFTISNVIQEV-----NKPTLVIAHNKTLAGQLYGEFKEFFPDNA 90
Cdd:cd18032     5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKRLleanrKKRILFLAHREELLEQAERSFKEVLPDGS 78
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
503-558 1.46e-07

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: 48.70  E-value: 1.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2754591276 503 ILIGINLLREGIDVPEVSLIAILDADkegflRSERSLVQTMGRAARNAE-GKVIMYA 558
Cdd:cd09300     8 VLIAVN*ALTGFDAPELNTIIVDKNL-----RSYRGLNQAFGRANRIYTfGGIVTYR 59
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
437-580 2.86e-07

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: 50.42  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 437 DDLVGEINER-IEKDQRVFVTTLTKKMAEDLTDYFKEL--GLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREG 513
Cdd:cd18810    11 DELIREAIEReLLRGGQVFYVHNRIESIEKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESG 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2754591276 514 IDVPEVSLIAILDADKEGFLRsersLVQTMGRAARnaeGKVIMYADKITDSmQRAMDETARRR--AIQE 580
Cdd:cd18810    91 IDIPNANTIIIERADKFGLAQ----LYQLRGRVGR---SKERAYAYFLYPD-QKKLTEDALKRleAIQE 151
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
500-557 1.78e-06

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: 46.16  E-value: 1.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 500 EFDILIGINLLREGIDVPEVSLIAILDADkegflRSERSLVQTMGRAARNA--EGKVIMY 557
Cdd:cd18785    22 SLEILVATNVLGEGIDVPSLDTVIFFDPP-----SSAASYIQRVGRAGRGGkdEGEVILF 76
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
490-556 2.45e-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: 47.59  E-value: 2.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2754591276 490 TEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDadkegFLRSERSLVQTMGRaARNAEGKVIM 556
Cdd:cd18802    80 KETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFD-----LPKTLRSYIQSRGR-ARAPNSKYIL 140
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
439-662 2.45e-06

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 50.88  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 439 LVGEINERIEK--DQRVFVTTLTKKMAEDLTDYFKELGLKVKYL-----HSDIKTL---ERTEIIRDLRLGEFDILIGIN 508
Cdd:COG1111   340 LREILKEQLGTnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqasKEGDKGLtqkEQIEILERFRAGEFNVLVATS 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 509 LLREGIDVPEVSLIAILDAdkegfLRSE-RSlVQTMGRAARNAEGKVIMYADKITdsmqraMDETARRRAIQ-------- 579
Cdd:COG1111   420 VAEEGLDIPEVDLVIFYEP-----VPSEiRS-IQRKGRTGRKREGRVVVLIAKGT------RDEAYYWSSRRkekkmksi 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 580 ------EAYNEEHGIEPKTIIKEIRDLISISKTADKDETVVQLDKSYEDLS--RQEKADLLMKLEREMKDAAKALDFETA 651
Cdd:COG1111   488 lkklkkLLDKQEKEKLKESAQATLDEFESIKELAEDEINEKDLDEIESSENgaHVDWREPVLLQVIVSTLAESLELRELG 567
                         250
                  ....*....|.
gi 2754591276 652 ATLRDTILELK 662
Cdd:COG1111   568 EKVDDEVNLIL 578
PRK05580 PRK05580
primosome assembly protein PriA; Validated
459-555 3.15e-06

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 50.54  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 459 TKKMAEDLTDYFKELglKVKYLHSD----IKTLErtEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDAD---KEG 531
Cdd:PRK05580  439 TERLEEELAELFPEA--RILRIDRDttrrKGALE--QLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDADlglFSP 514
                          90       100
                  ....*....|....*....|....*....
gi 2754591276 532 FLR-SERS---LVQTMGRAAR-NAEGKVI 555
Cdd:PRK05580  515 DFRaSERTfqlLTQVAGRAGRaEKPGEVL 543
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
426-548 6.13e-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: 46.05  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 426 EVEIRPIMGQIDDLVGEINERiEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILI 505
Cdd:cd18794     7 SVRPKDKKDEKLDLLKRIKVE-HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIV 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2754591276 506 GINLLREGIDVPEVSLIAILDADK--EGFlrserslVQTMGRAAR 548
Cdd:cd18794    86 ATVAFGMGIDKPDVRFVIHYSLPKsmESY-------YQESGRAGR 123
PRK13766 PRK13766
Hef nuclease; Provisional
431-653 2.69e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 47.56  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 431 PIMGQIDDLVGEINErIEKDQRVFVTTLTKKMAEDLTDYFKELGLKV--------KYLHSDIKTLERTEIIRDLRLGEFD 502
Cdd:PRK13766  347 PKLEKLREIVKEQLG-KNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqasKDGDKGMSQKEQIEILDKFRAGEFN 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 503 ILIGINLLREGIDVPEVSLIAILDAdkegfLRSE-RSlVQTMGRAARNAEGKVIMYADKITdsmqraMDETARRRAIqea 581
Cdd:PRK13766  426 VLVSTSVAEEGLDIPSVDLVIFYEP-----VPSEiRS-IQRKGRTGRQEEGRVVVLIAKGT------RDEAYYWSSR--- 490
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2754591276 582 yNEEhgiepKTIIKEIRDLisiSKTADKDETVVQLDKSYEDLSRQEKADLLMKLEREMKDAAKALDFETAAT 653
Cdd:PRK13766  491 -RKE-----KKMKEELKNL---KGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDK 553
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
22-94 3.49e-05

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: 44.22  E-value: 3.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2754591276  22 QPAAIaELVDGVKGGEKAQILLgATGTGKTFTISNVIQEV-NKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYF 94
Cdd:cd17926     5 QEEAL-EAWLAHKNNRRGILVL-PTGSGKTLTALALIAYLkELRTLIVVPTDALLDQWKERFEDFLGDSSIGLI 76
UVR pfam02151
UvrB/uvrC motif;
634-663 3.87e-05

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 40.84  E-value: 3.87e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2754591276 634 KLEREMKDAAKALDFETAATLRDTILELKA 663
Cdd:pfam02151   6 ELEEEMEEAAENEDFEKAAKLRDQINALKK 35
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
491-555 5.87e-05

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


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 46.26  E-value: 5.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2754591276 491 EIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILDADkEGF----LR-SERS---LVQTMGRAAR-NAEGKVI 555
Cdd:COG1198   522 KLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDAD-LGLnspdFRaAERTfqlLTQVAGRAGRaEKPGEVL 594
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
630-658 1.18e-04

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


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 45.11  E-value: 1.18e-04
                          10        20
                  ....*....|....*....|....*....
gi 2754591276 630 DLLMKLEREMKDAAKALDFETAATLRDTI 658
Cdd:COG0322   203 ELIKELEEKMEEAAEELEFERAARLRDQI 231
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
435-528 1.48e-04

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 45.04  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 435 QIDDLVGEINERIEKDQRVFV-------------TTLTKkMAEDLTDYFKELglKVKYLHSDIKTLERTEIIRDLRLGEF 501
Cdd:COG1200   454 RRDEVYERIREEIAKGRQAYVvcplieesekldlQAAEE-TYEELREAFPGL--RVGLLHGRMKPAEKDAVMAAFKAGEI 530
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2754591276 502 DILIG---InllrE-GIDVPEVSLIAILDAD 528
Cdd:COG1200   531 DVLVAttvI----EvGVDVPNATVMVIENAE 557
uvrC PRK00558
excinuclease ABC subunit UvrC;
630-658 2.82e-04

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 43.95  E-value: 2.82e-04
                          10        20
                  ....*....|....*....|....*....
gi 2754591276 630 DLLMKLEREMKDAAKALDFETAATLRDTI 658
Cdd:PRK00558  202 EVLKELEEKMEEASENLEFERAARYRDQI 230
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
427-553 4.25e-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: 43.53  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 427 VEIRPIMGQIDDLVGEINERIEKDQRVFVTTLTKKMAEDLTDYFKELGL--KVKYLHSDIKTLERTEIIRDLRL----GE 500
Cdd:COG1203   343 VELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEKLPdeEVYLLHSRFCPADRSEIEKEIKErlerGK 422
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2754591276 501 FDILI-------GINllregIDVPEV-SLIAILDadkegflrserSLVQTMGRAARNAEGK 553
Cdd:COG1203   423 PCILVstqvveaGVD-----IDFDVViRDLAPLD-----------SLIQRAGRCNRHGRKE 467
PTZ00424 PTZ00424
helicase 45; Provisional
459-522 5.65e-04

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 42.89  E-value: 5.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2754591276 459 TKKMAEDLTDYFKELGLKVKYLHSDIKTLERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLI 522
Cdd:PTZ00424  276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLV 339
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
488-548 1.26e-03

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: 39.93  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2754591276 488 ERTEIIRDLRLGEFDILIGINLLREGIDVPEVSLIAILdadkEGFLRSERSLVQTMGRAAR 548
Cdd:cd18789    82 EREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQI----SGHGGSRRQEAQRLGRILR 138
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
462-528 2.26e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 41.29  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2754591276 462 MAEDLTDYFKELglKVKYLHSDIKTLERTEIIRDLRLGEFDILIG---InllrE-GIDVPEVSLIAILDAD 528
Cdd:PRK10917  495 TYEELQEAFPEL--RVGLLHGRMKPAEKDAVMAAFKAGEIDILVAttvI----EvGVDVPNATVMVIENAE 559
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
16-92 3.73e-03

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: 38.94  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276  16 YEPAGDQPAAIAELVDGVKGGEKAQILL-GATGTGKT--FTISNVIQ-EVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAV 91
Cdd:cd17918    14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLsGDVGSGKTlvALGAALLAyKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93

                  .
gi 2754591276  92 E 92
Cdd:cd17918    94 E 94
uvrC PRK14666
excinuclease ABC subunit C; Provisional
611-658 5.12e-03

excinuclease ABC subunit C; Provisional


Pssm-ID: 237782 [Multi-domain]  Cd Length: 694  Bit Score: 39.87  E-value: 5.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2754591276 611 ETVVQLDKSYEDLSRQEKADLLMKLEREMKDAAKALDFETAATLRDTI 658
Cdd:PRK14666  182 ETYAALVRKVEMLLSGRSGELVDALRTEMEAASEALEFERAAVLRDQI 229
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
453-524 5.89e-03

C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase 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: 350185 [Multi-domain]  Cd Length: 174  Bit Score: 38.05  E-value: 5.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2754591276 453 VFVTT-LTKKMAEDLTDYFKELGLKVK-YLHSDIKTLErteiirDLRLGEFDILIGI----NLLREGIDVPEVSLIAI 524
Cdd:cd18798    29 IFVSIdYGKEYAEELKEFLERHGIKAElALSSTEKNLE------KFEEGEIDVLIGVasyyGVLVRGIDLPERIKYAI 100
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
447-557 6.19e-03

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: 37.62  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2754591276 447 IEKDQRVFVTTLTKKMAEDLTDYFKELGLKVKYLHSDIKTL-------ERTEIIRDLRLGEFDILIGINLLREGIDVPev 519
Cdd:cd18797    32 VRAGVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASYragylaeDRREIEAELFNGELLGVVATNALELGIDIG-- 109
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2754591276 520 SLIAILDAdkeGFLRSERSLVQTMGRAARNAEGKVIMY 557
Cdd:cd18797   110 GLDAVVLA---GYPGSLASLWQQAGRAGRRGKDSLVIL 144
 
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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