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Conserved domains on  [gi|489074241|ref|WP_002984194|]
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excinuclease ABC subunit UvrB [Streptococcus pyogenes]

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];
9-660 0e+00

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


:

Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1368.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   9 PFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRP 168
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 169 GQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVL 248
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 249 FPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPY 328
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 329 TLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQ 408
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 409 TNT-IIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTL 487
Cdd:COG0556  401 SGGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 488 ERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQR 567
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 568 AIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISK--EEMDYESMSRGERKEAINALQKQMQEAAELLD 645
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEElvAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*
gi 489074241 646 FELAAQMRDLILELK 660
Cdd:COG0556  641 FEEAARLRDEIKELK 655
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
9-660 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1368.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   9 PFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRP 168
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 169 GQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVL 248
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 249 FPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPY 328
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 329 TLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQ 408
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 409 TNT-IIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTL 487
Cdd:COG0556  401 SGGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 488 ERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQR 567
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 568 AIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISK--EEMDYESMSRGERKEAINALQKQMQEAAELLD 645
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEElvAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*
gi 489074241 646 FELAAQMRDLILELK 660
Cdd:COG0556  641 FEEAARLRDEIKELK 655
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-660 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1363.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   6 DDKPFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEF 85
Cdd:PRK05298   1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  86 FPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVS 165
Cdd:PRK05298  81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 166 LRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDH 245
Cdd:PRK05298 161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 246 LVLFPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGE 325
Cdd:PRK05298 241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 326 PPYTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYE 405
Cdd:PRK05298 321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 406 MSQTN-TIIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDI 484
Cdd:PRK05298 401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 485 KTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDS 564
Cdd:PRK05298 481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 565 MQRAIDETARRREIQIAYNKAHGIVPQTIKKDIRglisisktshnDISKEEMDYESMSRGERKEAINALQKQMQEAAELL 644
Cdd:PRK05298 561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIR-----------DILDSVYKKDKLSKKELEKLIKELEKQMKEAAKNL 629
                        650
                 ....*....|....*.
gi 489074241 645 DFELAAQMRDLILELK 660
Cdd:PRK05298 630 EFEEAARLRDEIKELK 645
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
9-660 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: 1209.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241    9 PFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRP 168
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  169 GQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVL 248
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  249 FPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPY 328
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  329 TLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQ 408
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  409 TNTIIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLE 488
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  489 RTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQRA 568
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  569 IDETARRREIQIAYNKAHGIVPQTIKKDIRGLISI---SKTSHNDISKEEMDYESMSRGERKEAINALQKQMQEAAELLD 645
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIelkEKEDAAKKKKKGEDLSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 489074241  646 FELAAQMRDLILELK 660
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: 558.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  10 FKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYglgspkeyadsavslrpg 169
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 170 qeisrdtllnqlvdiqferndidfqrgcfrvrgdvvevfpasrdehafrveffgdeidriceiesltgktigevdhlvlf 249
Cdd:cd17916      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 250 pathfvtndehmEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPYT 329
Cdd:cd17916  143 ------------ERAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 330 LLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQT 409
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                 ....*....
gi 489074241 410 NTIIEQIIR 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 2.81e-43

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: 150.24  E-value: 2.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  164 VSLRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEV 243
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 489074241  244 DHLVLFPATHF 254
Cdd:pfam17757  81 DEVTIYPASHY 91
HELICc smart00490
helicase superfamily c-terminal domain;
464-548 3.82e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.18  E-value: 3.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   464 EDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADkegflRNERGLIQTI 543
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 489074241   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];
9-660 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1368.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   9 PFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRP 168
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 169 GQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVL 248
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 249 FPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPY 328
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 329 TLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQ 408
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 409 TNT-IIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTL 487
Cdd:COG0556  401 SGGqVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 488 ERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQR 567
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 568 AIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISK--EEMDYESMSRGERKEAINALQKQMQEAAELLD 645
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEETEElvAEADAAKLSKEELEKLIKELEKEMKEAAKNLE 640
                        650
                 ....*....|....*
gi 489074241 646 FELAAQMRDLILELK 660
Cdd:COG0556  641 FEEAARLRDEIKELK 655
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
6-660 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1363.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   6 DDKPFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEF 85
Cdd:PRK05298   1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  86 FPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVS 165
Cdd:PRK05298  81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 166 LRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDH 245
Cdd:PRK05298 161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 246 LVLFPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGE 325
Cdd:PRK05298 241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 326 PPYTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYE 405
Cdd:PRK05298 321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 406 MSQTN-TIIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDI 484
Cdd:PRK05298 401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 485 KTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDS 564
Cdd:PRK05298 481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 565 MQRAIDETARRREIQIAYNKAHGIVPQTIKKDIRglisisktshnDISKEEMDYESMSRGERKEAINALQKQMQEAAELL 644
Cdd:PRK05298 561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIR-----------DILDSVYKKDKLSKKELEKLIKELEKQMKEAAKNL 629
                        650
                 ....*....|....*.
gi 489074241 645 DFELAAQMRDLILELK 660
Cdd:PRK05298 630 EFEEAARLRDEIKELK 645
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
9-660 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: 1209.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241    9 PFKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPD 88
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   89 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRP 168
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  169 GQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVL 248
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  249 FPATHFVTNDEHMEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPY 328
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  329 TLLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQ 408
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  409 TNTIIEQIIRPTGLLDPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLE 488
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  489 RTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQRA 568
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  569 IDETARRREIQIAYNKAHGIVPQTIKKDIRGLISI---SKTSHNDISKEEMDYESMSRGERKEAINALQKQMQEAAELLD 645
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIelkEKEDAAKKKKKGEDLSDLSKKELKKLIKQLEKEMKQAARNLE 640
                         650
                  ....*....|....*
gi 489074241  646 FELAAQMRDLILELK 660
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: 558.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  10 FKLKSKYKPSGDQPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  90 AVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYglgspkeyadsavslrpg 169
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCIY------------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 170 qeisrdtllnqlvdiqferndidfqrgcfrvrgdvvevfpasrdehafrveffgdeidriceiesltgktigevdhlvlf 249
Cdd:cd17916      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 250 pathfvtndehmEQSIAKIQAELAEQLQLFESEGKLLEAQRLRQRTEYDIEMLREMGYTSGVENYSRHMDGRSPGEPPYT 329
Cdd:cd17916  143 ------------ERAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 330 LLDFFPEDFLIMIDESHMTMGQIKGMYNGDQARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGEYEMSQT 409
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                 ....*....
gi 489074241 410 NTIIEQIIR 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 8.15e-115

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: 341.15  E-value: 8.15e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 424 DPEIDVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDV 503
Cdd:cd18790    1 DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 504 LIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNVDGHVIMYADKMTDSMQRAIDETARRREIQIAYN 583
Cdd:cd18790   81 LVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITDSMQKAIEETERRREIQMEYN 160
                        170
                 ....*....|.
gi 489074241 584 KAHGIVPQTIK 594
Cdd:cd18790  161 EEHGITPKTII 171
Mfd COG1197
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ...
36-528 1.43e-44

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


Pssm-ID: 440810 [Multi-domain]  Cd Length: 1130  Bit Score: 171.79  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   36 GEKAQILLGATGTGKTYTMSQVISKVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSY----YDyyqpeAYVPSSD 111
Cdd:COG1197     1 GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLFPAWetlpYD-----RFSPSPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  112 TyiekdssVNDEIDKLRHsatssLLERNDVIVVASVSCIYGLGSPKEY-ADSAVSLRPGQEISRDTLLNQLVDIQFERND 190
Cdd:COG1197    76 I-------VSERLATLRR-----LASGKPGIVVTPVRALLQRLPPPELlAAASLSLKVGDELDLEELRERLVAAGYERVD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  191 IDFQRGCFRVRGDVVEVFPASrDEHAFRVEFFGDEIDRICEIESLTGKTIGEVDHLVLFPATHFVTNDEHMEQSIAKIQA 270
Cdd:COG1197   144 QVEEPGEFAVRGGILDIFPPG-SEHPVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDEEAIERFRERLRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  271 ELaeqlqlfesegklleaqRLRQRTEYDIEMLREMGYTSGVENYsrhmdgrSP--GEPPYTLLDFFPEDFLIMIDESHMT 348
Cdd:COG1197   223 LF-----------------GLDPKLDELYEALSEGIAFAGIEYY-------LPlfYEELATLFDYLPEDALVVLDEPERI 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  349 MGQIKGMYNGDQAR-KQMLVDYGfRLPSALDNRPLRREEFESHV--HQIVYVSATPgeyEMSQTNTIIEQIIRPtglldp 425
Cdd:COG1197   279 EEAAEEFWEEIEERyEARRHDRG-RPLLPPEELFLDPEELFAALkrRPRVTLSPFA---ALPEGAGVVNLGARP------ 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  426 eidVRSSMGQMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSdiktlerteiIRDLRLGVFDVLI 505
Cdd:COG1197   349 ---LPSFAGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPARLVES----------LAELSPGGVAITV 415
                         490       500
                  ....*....|....*....|...
gi 489074241  506 GInlLREGIDVPEVSLVAILDAD 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 2.81e-43

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: 150.24  E-value: 2.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  164 VSLRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASRDEHAFRVEFFGDEIDRICEIESLTGKTIGEV 243
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 489074241  244 DHLVLFPATHF 254
Cdd:pfam17757  81 DEVTIYPASHY 91
UvrB pfam12344
Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and ...
556-598 2.17e-26

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: 101.70  E-value: 2.17e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 489074241  556 MYADKMTDSMQRAIDETARRREIQIAYNKAHGIVPQTIKKDIR 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 1.54e-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: 81.49  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  434 GQMDDLLGEINQRvaRDERTFITTLTKKMAEdlTDYLKEM-GVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLRE 512
Cdd:pfam00271   1 EKLEALLELLKKE--RGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489074241  513 GIDVPEVSLVAILDADKegflrNERGLIQTIGRAAR 548
Cdd:pfam00271  77 GLDLPDVDLVINYDLPW-----NPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
464-548 3.82e-18

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 79.18  E-value: 3.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241   464 EDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADkegflRNERGLIQTI 543
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 489074241   544 GRAAR 548
Cdd:smart00490  76 GRAGR 80
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
331-661 5.62e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.14  E-value: 5.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 331 LDFFPEDF-LIMIDESH--------MTMGQIKGMY-----------NGDQARKQMLVD--YGFRLPSALDNRPLRReefe 388
Cdd:COG1061  181 LDELGDRFgLVIIDEAHhagapsyrRILEAFPAAYrlgltatpfrsDGREILLFLFDGivYEYSLKEAIEDGYLAP---- 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 389 sHVHQIVYVSATPGEYEMSQTNTIIEQIIRPTGLldpeidvrssmgQMDDLLGEINQRVARDERTFITTLTKKMAEDLTD 468
Cdd:COG1061  257 -PEYYGIRVDLTDERAEYDALSERLREALAADAE------------RKDKILRELLREHPDDRKTLVFCSSVDHAEALAE 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 469 YLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDAdkegfLRNERGLIQTIGRAAR 548
Cdd:COG1061  324 LLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP-----TGSPREFIQRLGRGLR 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 549 NVDG----HVIMYADKMTDSMQRAIDETARRREIQIAYNKAHGIVPQTIKKDIRGLISISKTSHNDISKEEMDYESMSRG 624
Cdd:COG1061  399 PAPGkedaLVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLL 478
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 489074241 625 ERKEAINALQKQMQEAAELLDFELAAQMRDLILELKL 661
Cdd:COG1061  479 VLAELLLLELLALALELLELAKAEGKAEEEEEEKELL 515
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
394-579 1.13e-14

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: 76.84  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 394 IVYVSATPGEYEMSQTNTIIEQIIR------------PTGLLDPEIDVRSSMGQM-DDLLGEINQRVARDERTFITTLTK 460
Cdd:COG4098  250 LIYLTATPSKALQRQVKRGKLKVVKlparyhghplpvPKFKWLGNWKKRLRRGKLpRKLLKWLKKRLKEGRQLLIFVPTI 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 461 KMAEDLTDYLKE--MGVKVKYMHSdiKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSlVAILDADKEGFlrNERG 538
Cdd:COG4098  330 ELLEQLVALLQKlfPEERIAGVHA--EDPERKEKVQAFRDGEIPILVTTTILERGVTFPNVD-VAVLGADHPVF--TEAA 404
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489074241 539 LIQTIGRAARNVD---GHVIMYADKMTDSMQRAIdetarrREIQ 579
Cdd:COG4098  405 LVQIAGRVGRSADyptGEVIFFHHGKTRAMKRAI------REIK 442
ResIII pfam04851
Type III restriction enzyme, res subunit;
22-90 4.90e-12

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 64.62  E-value: 4.90e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489074241   22 QPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVI-----SKVNKPTLVIAHNKTLAGQLYGEFKEFFPDNA 90
Cdd:pfam04851   8 QIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIarlfkKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
DEXDc smart00487
DEAD-like helicases superfamily;
10-97 1.65e-11

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 64.05  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241    10 FKLKSKYKPSGDQPQAIESLVDNIEGGekaqILLGATGTGKTYTMSQVI-----SKVNKPTLVIAHNKTLAGQLYGEFKE 84
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDV----ILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKK 76
                           90
                   ....*....|...
gi 489074241    85 FFPDNAVEYFVSY 97
Cdd:smart00487  77 LGPSLGLKVVGLY 89
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
435-548 2.52e-11

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: 61.37  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 435 QMDDLLGEINQRVARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGI 514
Cdd:cd18787   12 EKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGL 91
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489074241 515 DVPEVSLVAILDA--DKEGFlrnerglIQTIGRAAR 548
Cdd:cd18787   92 DIPGVDHVINYDLprDAEDY-------VHRIGRTGR 120
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
163-262 1.06e-09

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 62.07  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  163 AVSLRPGQEISRDTLLNQLVDIQFERNDIDFQRGCFRVRGDVVEVFPASrDEHAFRVEFFGDEIDRICEIESLTGKTIGE 242
Cdd:PRK10689  127 ALVMKKGQRLSRDALRAQLEQAGYRHVDQVMEHGEYATRGALLDLFPMG-SEEPYRIDFFDDEIDSLRVFDVDSQRTLEE 205
                          90       100
                  ....*....|....*....|
gi 489074241  243 VDHLVLFPATHFVTNDEHME 262
Cdd:PRK10689  206 VEAINLLPAHEFPTDKAAIE 225
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
22-90 1.26e-09

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: 57.57  E-value: 1.26e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489074241  22 QPQAIESLVDNIEGGEKAQILLGATGTGKTYTMSQVI-----SKVNKPTLVIAHNKTLAGQLYGEFKEFFPDNA 90
Cdd:cd18032    5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIkrlleANRKKRILFLAHREELLEQAERSFKEVLPDGS 78
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
37-144 3.65e-09

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: 55.87  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  37 EKAQILLGATGTGKT--YTMS--QVISKVNKPTLVIAHNKTLAGQLYGEFKEFF-PDNAVEYFVSYYDYYQPEAyvpssd 111
Cdd:cd00046    1 GENVLITAPTGSGKTlaALLAalLLLLKKGKKVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSAEEREK------ 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489074241 112 tYIEKDSSV----NDEIDKLRHSATSSLLERNDVIVV 144
Cdd:cd00046   75 -NKLGDADIiiatPDMLLNLLLREDRLFLKDLKLIIV 110
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
40-101 6.07e-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: 6.07e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489074241  40 QILLGATGTGKTYTMSQVISKVN---KPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYY 101
Cdd:cd17912    2 ILHLGPTGSGKTLVAIQKIASAMssgKSVLVVTPTKLLAHEILIVIDEIQ*ILDPAAGWAWATRA 66
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
388-578 8.74e-09

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 58.23  E-value: 8.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 388 ESHVHQIVYVSATPGEyemsQTNTIIEQIIrptglldpeidVRSSMGQMDDLLGEInQRVARDERTFITTLTKKMAEDLT 467
Cdd:COG0513  195 KRYLKNPVRIEVAPEN----ATAETIEQRY-----------YLVDKRDKLELLRRL-LRDEDPERAIVFCNTKRGADRLA 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 468 DYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVaI---LDADKEGFL-RnergliqtI 543
Cdd:COG0513  259 EKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV-InydLPEDPEDYVhR--------I 329
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489074241 544 GRAAR-NVDGHVIMYAD----KMTDSMQRAIDETARRREI 578
Cdd:COG0513  330 GRTGRaGAEGTAISLVTpderRLLRAIEKLIGQKIEEEEL 369
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
503-558 1.82e-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: 51.01  E-value: 1.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489074241 503 VLIGINLLREGIDVPEVSLVAILDADkegflRNERGLIQTIGRAARNVD-GHVIMYA 558
Cdd:cd09300    8 VLIAVN*ALTGFDAPELNTIIVDKNL-----RSYRGLNQAFGRANRIYTfGGIVTYR 59
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
436-577 2.19e-08

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 57.43  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 436 MDDLLGEINQRVA--RDERTFITTLTKKMAEDLTDYLKEMGVKV-----KYMHSDIKTL---ERTEIIRDLRLGVFDVLI 505
Cdd:COG1111  337 LSKLREILKEQLGtnPDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgQASKEGDKGLtqkEQIEILERFRAGEFNVLV 416
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489074241 506 GINLLREGIDVPEVSLVAILDAdkegfLRNERGLIQTIGRAARNVDGHVIMYADKMTdsmqraIDET----ARRRE 577
Cdd:COG1111  417 ATSVAEEGLDIPEVDLVIFYEP-----VPSEIRSIQRKGRTGRKREGRVVVLIAKGT------RDEAyywsSRRKE 481
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
453-555 2.45e-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: 55.33  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 453 TFITTLTKKMAEDLTDYLKEmgVKVKYMHSDI--KTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADK- 529
Cdd:cd18804   97 VFKGIGTERVEEELKTLFPE--ARIARIDRDTtrKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSg 174
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489074241 530 ---EGFLRNERG---LIQTIGRAAR-NVDGHVI 555
Cdd:cd18804  175 lnsPDFRASERAfqlLTQVSGRAGRgDKPGKVI 207
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
447-548 4.00e-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: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 447 VARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERT-EIIRDL--RLGVFDVLIGINLLREGIDVPEVSLVA 523
Cdd:cd18799    3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLffGELKPPILVTVDLLTTGVDIPEVDNVV 82
                         90       100
                 ....*....|....*....|....*...
gi 489074241 524 ildadkegFLRNERGLI---QTIGRAAR 548
Cdd:cd18799   83 --------FLRPTESRTlflQMLGRGLR 102
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
437-557 4.79e-08

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: 52.21  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 437 DDLLGEINQRvARDERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDV 516
Cdd:cd18794   18 LDLLKRIKVE-HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDK 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489074241 517 PEVSLVAILDADK--EGFLrnergliQTIGRAARnvDG---HVIMY 557
Cdd:cd18794   97 PDVRFVIHYSLPKsmESYY-------QESGRAGR--DGlpsECILF 133
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
22-94 4.85e-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: 52.31  E-value: 4.85e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489074241  22 QPQAIESLVDNiEGGEKAQILLgATGTGKTYTMSQVISKV-NKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYF 94
Cdd:cd17926    5 QEEALEAWLAH-KNNRRGILVL-PTGSGKTLTALALIAYLkELRTLIVVPTDALLDQWKERFEDFLGDSSIGLI 76
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
433-556 1.54e-06

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: 48.12  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 433 MGQMDDLLGEINQR--VARDERTFITTLTKKMAEDLTDYLKEMGVKVKYM----HSDIKTL------ERTEIIRDLRLGV 500
Cdd:cd18801   11 LEKLEEIVKEHFKKkqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGKSSkgmsqkEQKEVIEQFRKGG 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489074241 501 FDVLIGINLLREGIDVPEVSLVAILDADKEGfLRNerglIQTIGRAARNVDGHVIM 556
Cdd:cd18801   91 YNVLVATSIGEEGLDIGEVDLIICYDASPSP-IRM----IQRMGRTGRKRQGRVVV 141
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
609-656 2.29e-06

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


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 50.89  E-value: 2.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489074241 609 NDISKEemDYESMSR-------GERKEAINALQKQMQEAAELLDFELAAQMRDLI 656
Cdd:COG0322  179 GLISEE--EYREDVEqarrfleGKTKELIKELEEKMEEAAEELEFERAARLRDQI 231
UVR pfam02151
UvrB/uvrC motif;
627-660 2.89e-06

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 44.31  E-value: 2.89e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 489074241  627 KEAINALQKQMQEAAELLDFELAAQMRDLILELK 660
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALK 34
uvrC PRK00558
excinuclease ABC subunit UvrC;
609-656 4.94e-06

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 49.73  E-value: 4.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489074241 609 NDISKEemDYESMSR-------GERKEAINALQKQMQEAAELLDFELAAQMRDLI 656
Cdd:PRK00558 178 GLISKE--EYAELVDeaklflsGKTDEVLKELEEKMEEASENLEFERAARYRDQI 230
PTZ00424 PTZ00424
helicase 45; Provisional
459-548 5.47e-06

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 49.05  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 459 TKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILD--ADKEGFlrne 536
Cdd:PTZ00424 276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDlpASPENY---- 351
                         90
                 ....*....|..
gi 489074241 537 rglIQTIGRAAR 548
Cdd:PTZ00424 352 ---IHRIGRSGR 360
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
467-556 6.87e-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: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 467 TDYLKEMG--VKVKYMHSDIKtlERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDadkegFLRNERGLIQTIG 544
Cdd:cd18802   57 CGFLIGRGnsSQRKRSLMTQR--KQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFD-----LPKTLRSYIQSRG 129
                         90
                 ....*....|..
gi 489074241 545 RAARNVDGHVIM 556
Cdd:cd18802  130 RARAPNSKYILM 141
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
458-576 9.33e-06

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: 46.11  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 458 LTKKMAEDLTDYLKEM--GVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRn 535
Cdd:cd18792   42 LDLKSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQ- 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489074241 536 ergLIQTIGRAARnvdGHVIMYADKMTDSmQRAIDETARRR 576
Cdd:cd18792  121 ---LHQLRGRVGR---GKHQSYCYLLYPD-PKKLTETAKKR 154
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
461-567 1.40e-05

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: 45.80  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 461 KMAEDLTDYLKEM---GVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRner 537
Cdd:cd18811   45 KAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQ--- 121
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489074241 538 gLIQTIGRAAR-NVDGH-VIMYADKMTD-SMQR 567
Cdd:cd18811  122 -LHQLRGRVGRgDHQSYcLLVYKDPLTEtAKQR 153
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
452-549 2.20e-05

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: 43.08  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 452 RTFITTLTKKMAEDLTDYLKemgvkvkymhsdiktlerteiirdlrlgvfdVLIGINLLREGIDVPEVSLVAILDADkeg 531
Cdd:cd18785    5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP--- 50
                         90
                 ....*....|....*...
gi 489074241 532 flRNERGLIQTIGRAARN 549
Cdd:cd18785   51 --SSAASYIQRVGRAGRG 66
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
22-89 6.87e-05

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 45.99  E-value: 6.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489074241  22 QPQAIESLVDNIEGGEKaQILLG-ATGTGKTYTMSQVI-----SKVNKPTLVIAHNKTLAGQLYGEFKEFFPDN 89
Cdd:COG4096  163 QIEAIRRVEEAIAKGQR-RALLVmATGTGKTRTAIALIyrllkAGRAKRILFLADRNALVDQAKNAFKPFLPDL 235
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
429-576 1.13e-04

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: 42.72  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 429 VRSSMGQMDDLL--GEINQRVARDERTFITTLTKKMAEDLTDYLKEM--GVKVKYMHSDIKTLERTEIIRDLRLGVFDVL 504
Cdd:cd18810    2 VRTYVMPYDDELirEAIERELLRGGQVFYVHNRIESIEKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDIL 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489074241 505 IGINLLREGIDVPEVSLVAILDADKEGFLRnergLIQTIGRAARnvdGHVIMYADKMTDSmQRAIDETARRR 576
Cdd:cd18810   82 VCTTIIESGIDIPNANTIIIERADKFGLAQ----LYQLRGRVGR---SKERAYAYFLYPD-QKKLTEDALKR 145
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
16-92 3.08e-04

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: 42.02  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241  16 YKPSGDQPQAIESLVDNIEGGEKAQILL-GATGTGKTYT-MSQVISKVNKP--TLVIAHNKTLAGQLYGEFKEFFPDNAV 91
Cdd:cd17918   14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLsGDVGSGKTLVaLGAALLAYKNGkqVAILVPTEILAHQHYEEARKFLPFINV 93

                 .
gi 489074241  92 E 92
Cdd:cd17918   94 E 94
PRK13766 PRK13766
Hef nuclease; Provisional
450-577 3.84e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 3.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 450 DERTFITTLTKKMAEDLTDYLKEMGVKV--------KYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSL 521
Cdd:PRK13766 365 DSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqasKDGDKGMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489074241 522 V--------AIldadkegflRNerglIQTIGRAARNVDGHVIMYADKMTDsmqraiDET----ARRRE 577
Cdd:PRK13766 445 VifyepvpsEI---------RS----IQRKGRTGRQEEGRVVVLIAKGTR------DEAyywsSRRKE 493
PRK05580 PRK05580
primosome assembly protein PriA; Validated
459-555 4.87e-04

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 43.22  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 459 TKKMAEDLTDYLKEmgVKVKYMHSD----IKTLErtEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADkeGFLR 534
Cdd:PRK05580 439 TERLEEELAELFPE--ARILRIDRDttrrKGALE--QLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDAD--LGLF 512
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489074241 535 N------ERG---LIQTIGRAAR-NVDGHVI 555
Cdd:PRK05580 513 SpdfrasERTfqlLTQVAGRAGRaEKPGEVL 543
PTZ00110 PTZ00110
helicase; Provisional
427-548 2.81e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 40.91  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 427 IDVRSSMGQMDDLLgeinQRVARD-ERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLI 505
Cdd:PTZ00110 357 VEEHEKRGKLKMLL----QRIMRDgDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMI 432
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489074241 506 GINLLREGIDVPEVSLVAILDadkegFLRNERGLIQTIGRAAR 548
Cdd:PTZ00110 433 ATDVASRGLDVKDVKYVINFD-----FPNQIEDYVHRIGRTGR 470
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
460-562 3.14e-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: 39.21  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489074241 460 KKMAEDLTDYLKEMGVKVK-YMHSDIKTLErteiirDLRLGVFDVLIGI----NLLREGIDVPEVSLVAIldadkegFLR 534
Cdd:cd18798   37 KEYAEELKEFLERHGIKAElALSSTEKNLE------KFEEGEIDVLIGVasyyGVLVRGIDLPERIKYAI-------FYG 103
                         90       100
                 ....*....|....*....|....*....
gi 489074241 535 NE-RGLIQTIGRAARnvdghviMYADKMT 562
Cdd:cd18798  104 VPvTTYIQASGRTSR-------LYAGGLT 125
 
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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