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Conserved domains on  [gi|496059679|ref|WP_008784186|]
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MULTISPECIES: excinuclease ABC subunit UvrB [Citrobacter]

Protein Classification

excinuclease ABC subunit UvrB( domain architecture ID 11480575)

excinuclease ABC subunit UvrB is part of the UvrABC repair system that catalyzes the recognition and processing of DNA lesions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
1-673 0e+00

excinuclease ABC subunit UvrB;


:

Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1361.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   1 MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEF 80
Cdd:PRK05298   1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  81 FPDNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLH 160
Cdd:PRK05298  81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 161 LTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISR 240
Cdd:PRK05298 161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 241 FTIYPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGE 320
Cdd:PRK05298 241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 321 PPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYE 400
Cdd:PRK05298 321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 401 LEKSGDDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDI 480
Cdd:PRK05298 401 LEKSGGVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 481 DTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITAS 560
Cdd:PRK05298 481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 561 MAKAIGETERRREKQQLYNEEHGITPQGLNKKVVDILalgqniaktkakgkgksragaKSEVVELDMTPKALQQKIHELE 640
Cdd:PRK05298 561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDIL---------------------DSVYKKDKLSKKELEKLIKELE 619
                        650       660       670
                 ....*....|....*....|....*....|...
gi 496059679 641 GQMMQHAQNLEFEEAATIRDQLHQLRELFIAAS 673
Cdd:PRK05298 620 KQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
 
Name Accession Description Interval E-value
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
1-673 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1361.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   1 MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEF 80
Cdd:PRK05298   1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  81 FPDNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLH 160
Cdd:PRK05298  81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 161 LTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISR 240
Cdd:PRK05298 161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 241 FTIYPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGE 320
Cdd:PRK05298 241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 321 PPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYE 400
Cdd:PRK05298 321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 401 LEKSGDDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDI 480
Cdd:PRK05298 401 LEKSGGVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 481 DTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITAS 560
Cdd:PRK05298 481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 561 MAKAIGETERRREKQQLYNEEHGITPQGLNKKVVDILalgqniaktkakgkgksragaKSEVVELDMTPKALQQKIHELE 640
Cdd:PRK05298 561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDIL---------------------DSVYKKDKLSKKELEKLIKELE 619
                        650       660       670
                 ....*....|....*....|....*....|...
gi 496059679 641 GQMMQHAQNLEFEEAATIRDQLHQLRELFIAAS 673
Cdd:PRK05298 620 KQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
4-668 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1352.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   4 PFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPD 83
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  84 NAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTV 163
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 164 GMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISRFTI 243
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 244 YPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPP 323
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 324 TLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEK 403
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 404 SGDDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTV 483
Cdd:COG0556  401 SGGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 484 ERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITASMAK 563
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 564 AIGETERRREKQQLYNEEHGITPQGLNKKVVDILalgqniaKTKAKGKGKSRAGAKSEVVElDMTPKALQQKIHELEGQM 643
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDIL-------EGTYEADEETEELVAEADAA-KLSKEELEKLIKELEKEM 632
                        650       660
                 ....*....|....*....|....*
gi 496059679 644 MQHAQNLEFEEAATIRDQLHQLREL 668
Cdd:COG0556  633 KEAAKNLEFEEAARLRDEIKELKKE 657
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
4-666 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: 1205.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679    4 PFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPD 83
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   84 NAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTV 163
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  164 GMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISRFTI 243
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  244 YPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPP 323
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  324 TLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEK 403
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  404 SGdDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTV 483
Cdd:TIGR00631 401 SG-NVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  484 ERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITASMAK 563
Cdd:TIGR00631 480 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQK 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  564 AIGETERRREKQQLYNEEHGITPQGLNKKVVDILALGQNIaktkakgKGKSRAGAKSEVVELDMTPKALQQKIHELEGQM 643
Cdd:TIGR00631 560 AIEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKE-------KEDAAKKKKKGEDLSDLSKKELKKLIKQLEKEM 632
                         650       660
                  ....*....|....*....|...
gi 496059679  644 MQHAQNLEFEEAATIRDQLHQLR 666
Cdd:TIGR00631 633 KQAARNLEFEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
5-414 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: 529.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   5 FKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPDN 84
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  85 AVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDvvvvasvsaiyglgdpdlylkmmlhltvg 164
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 165 miidqrailrrlaelqytrndqafqrgtfrvrgeVIdifpaesddialrvelfdeeverlslfdpltgqVESTISrfTIY 244
Cdd:cd17916  132 ----------------------------------VI---------------------------------VVASVS--CIY 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 245 PkthyvtprerivQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPPT 324
Cdd:cd17916  143 E------------RAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 325 LFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEKS 404
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290
                        410
                 ....*....|
gi 496059679 405 GdDVVDQVVR 414
Cdd:cd17916  291 G-QVVEQIIR 299
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
159-249 1.66e-42

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: 148.31  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  159 LHLTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTI 238
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 496059679  239 SRFTIYPKTHY 249
Cdd:pfam17757  81 DEVTIYPASHY 91
HELICc smart00490
helicase superfamily c-terminal domain;
460-544 7.78e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.49  E-value: 7.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   460 EDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADkegflRSERSLIQTI 539
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 496059679   540 GRAAR 544
Cdd:smart00490  76 GRAGR 80
 
Name Accession Description Interval E-value
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
1-673 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1361.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   1 MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEF 80
Cdd:PRK05298   1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  81 FPDNAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLH 160
Cdd:PRK05298  81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 161 LTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISR 240
Cdd:PRK05298 161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 241 FTIYPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGE 320
Cdd:PRK05298 241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 321 PPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYE 400
Cdd:PRK05298 321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 401 LEKSGDDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDI 480
Cdd:PRK05298 401 LEKSGGVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 481 DTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITAS 560
Cdd:PRK05298 481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 561 MAKAIGETERRREKQQLYNEEHGITPQGLNKKVVDILalgqniaktkakgkgksragaKSEVVELDMTPKALQQKIHELE 640
Cdd:PRK05298 561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDIL---------------------DSVYKKDKLSKKELEKLIKELE 619
                        650       660       670
                 ....*....|....*....|....*....|...
gi 496059679 641 GQMMQHAQNLEFEEAATIRDQLHQLRELFIAAS 673
Cdd:PRK05298 620 KQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
4-668 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1352.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   4 PFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPD 83
Cdd:COG0556    1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  84 NAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTV 163
Cdd:COG0556   81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 164 GMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISRFTI 243
Cdd:COG0556  161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 244 YPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPP 323
Cdd:COG0556  241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 324 TLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEK 403
Cdd:COG0556  321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 404 SGDDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTV 483
Cdd:COG0556  401 SGGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 484 ERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITASMAK 563
Cdd:COG0556  481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 564 AIGETERRREKQQLYNEEHGITPQGLNKKVVDILalgqniaKTKAKGKGKSRAGAKSEVVElDMTPKALQQKIHELEGQM 643
Cdd:COG0556  561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDIL-------EGTYEADEETEELVAEADAA-KLSKEELEKLIKELEKEM 632
                        650       660
                 ....*....|....*....|....*
gi 496059679 644 MQHAQNLEFEEAATIRDQLHQLREL 668
Cdd:COG0556  633 KEAAKNLEFEEAARLRDEIKELKKE 657
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
4-666 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: 1205.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679    4 PFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPD 83
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   84 NAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTV 163
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  164 GMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTISRFTI 243
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  244 YPKTHYVTPRERIVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPP 323
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  324 TLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEK 403
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  404 SGdDVVDQVVRPTGLLDPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTV 483
Cdd:TIGR00631 401 SG-NVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTL 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  484 ERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITASMAK 563
Cdd:TIGR00631 480 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQK 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  564 AIGETERRREKQQLYNEEHGITPQGLNKKVVDILALGQNIaktkakgKGKSRAGAKSEVVELDMTPKALQQKIHELEGQM 643
Cdd:TIGR00631 560 AIEETERRRKIQMAYNEEHGITPQTIRKPIRDILDIELKE-------KEDAAKKKKKGEDLSDLSKKELKKLIKQLEKEM 632
                         650       660
                  ....*....|....*....|...
gi 496059679  644 MQHAQNLEFEEAATIRDQLHQLR 666
Cdd:TIGR00631 633 KQAARNLEFEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
5-414 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: 529.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   5 FKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPDN 84
Cdd:cd17916    1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  85 AVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKALLERRDvvvvasvsaiyglgdpdlylkmmlhltvg 164
Cdd:cd17916   81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRD----------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 165 miidqrailrrlaelqytrndqafqrgtfrvrgeVIdifpaesddialrvelfdeeverlslfdpltgqVESTISrfTIY 244
Cdd:cd17916  132 ----------------------------------VI---------------------------------VVASVS--CIY 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 245 PkthyvtprerivQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSGRGPGEPPPT 324
Cdd:cd17916  143 E------------RAIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 325 LFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEKS 404
Cdd:cd17916  211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290
                        410
                 ....*....|
gi 496059679 405 GdDVVDQVVR 414
Cdd:cd17916  291 G-QVVEQIIR 299
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
420-590 6.00e-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: 341.92  E-value: 6.00e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 420 DPVIEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDV 499
Cdd:cd18790    1 DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 500 LVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNINGKAILYGDKITASMAKAIGETERRREKQQLYN 579
Cdd:cd18790   81 LVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITDSMQKAIEETERRREIQMEYN 160
                        170
                 ....*....|.
gi 496059679 580 EEHGITPQGLN 590
Cdd:cd18790  161 EEHGITPKTII 171
Mfd COG1197
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ...
31-524 1.42e-42

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


Pssm-ID: 440810 [Multi-domain]  Cd Length: 1130  Bit Score: 166.01  E-value: 1.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   31 GLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPDNAVEYFvsyydyyqpeayvPSSDTFIE 110
Cdd:COG1197     1 GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLF-------------PAWETLPY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  111 KDASVNEHIEQMRLSATKALLERRDVvvvasvsaIY---------GLGDPDLYLKMMLHLTVGMIIDQRAILRRLAELQY 181
Cdd:COG1197    68 DRFSPSPDIVSERLATLRRLASGKPG--------IVvtpvrallqRLPPPELLAAASLSLKVGDELDLEELRERLVAAGY 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  182 TRNDQAFQRGTFRVRGEVIDIFPAESDDiALRVELFDEEVERLSLFDPLTGQVESTISRFTIYPKTHYVTPRERIVQAME 261
Cdd:COG1197   140 ERVDQVEEPGEFAVRGGILDIFPPGSEH-PVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDEEAIERFRE 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  262 eikvelaerrkvllannKLLEEQRLSQRTQFDLEMMNELGYCSGIENYSRYLSgrgpgEPPPTLFDYLPADGLLVVDESH 341
Cdd:COG1197   219 -----------------RLRELFGLDPKLDELYEALSEGIAFAGIEYYLPLFY-----EELATLFDYLPEDALVVLDEPE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  342 VTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALA--PQTIYVSATPGNYEleksGDDVVDQVVRPtgll 419
Cdd:COG1197   277 RIEEAAEEFWEEIEERYEARRHDRGRPLLPPEELFLDPEELFAALkrRPRVTLSPFAALPE----GAGVVNLGARP---- 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  420 dpvieVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSdidtvermeiIRDLRLGEFDV 499
Cdd:COG1197   349 -----LPSFAGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPARLVES----------LAELSPGGVAI 413
                         490       500
                  ....*....|....*....|....*
gi 496059679  500 LVGInlLREGLDMPEVSLVAILDAD 524
Cdd:COG1197   414 TVGP--LEHGFELPDAKLAVITESE 436
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
159-249 1.66e-42

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: 148.31  E-value: 1.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  159 LHLTVGMIIDQRAILRRLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQVESTI 238
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 496059679  239 SRFTIYPKTHY 249
Cdd:pfam17757  81 DEVTIYPASHY 91
UvrB pfam12344
Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and ...
552-593 2.79e-21

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: 87.06  E-value: 2.79e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 496059679  552 LYGDKITASMAKAIGETERRREKQQLYNEEHGITPQGLNKKV 593
Cdd:pfam12344   1 LYADKITDSMQRAIDETERRREIQEAYNEEHGITPKTIKKKI 42
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
432-544 3.51e-20

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 86.11  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  432 VDDLLSEIRTRaaINERVLVTTLTKRMAeDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLD 511
Cdd:pfam00271   3 LEALLELLKKE--RGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 496059679  512 MPEVSLVAILDADKegflrSERSLIQTIGRAAR 544
Cdd:pfam00271  80 LPDVDLVINYDLPW-----NPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
460-544 7.78e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.49  E-value: 7.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679   460 EDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADkegflRSERSLIQTI 539
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 496059679   540 GRAAR 544
Cdd:smart00490  76 GRAGR 80
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
429-553 5.52e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.69  E-value: 5.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 429 ATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLRE 508
Cdd:COG1061  288 AERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNE 367
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 496059679 509 GLDMPEVSLVAILDAdkegfLRSERSLIQTIGRAARNINGK--AILY 553
Cdd:COG1061  368 GVDVPRLDVAILLRP-----TGSPREFIQRLGRGLRPAPGKedALVY 409
mfd TIGR00580
transcription-repair coupling factor (mfd); All proteins in this family for which functions ...
176-340 2.71e-14

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: 76.63  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  176 LAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDiALRVELFDEEVERLSLFDPLTGQVESTISRFTIYPKthyvtpRER 255
Cdd:TIGR00580   1 LVELGYERVDLVEEEGEFSVRGEILDIFPPGSEL-PVRIEFFGDEIESIREFDVDSQRSLEELLEITILPA------KEF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  256 IVQAMEEIKVELAERRKVLLANNKLLEEQRLSQRTQFDLEMMNELGYcsgienysrylsgrgpgEPPPTLFDYLPADGLL 335
Cdd:TIGR00580  74 ILLEEETIARLKDNAARVEDAKHLETIEALSEGTLPAGEEMFLPLFF-----------------EDLSSLFDYLPDNTPI 136

                  ....*
gi 496059679  336 VVDES 340
Cdd:TIGR00580 137 LLDDP 141
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
433-552 7.35e-13

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 65.99  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 433 DDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDM 512
Cdd:cd18787   14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496059679 513 PEVSLVAILDadkegFLRSERSLIQTIGRAAR-NINGKAIL 552
Cdd:cd18787   94 PGVDHVINYD-----LPRDAEDYVHRIGRTGRaGRKGTAIT 129
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
389-565 1.74e-12

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: 69.90  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 389 TIYVSATPGNYELE--KSGDDVVDQV-VRPTGLLDPVIEVR---PVATQV------DDLLSEIRTRAAINERVLVTTLTK 456
Cdd:COG4098  250 LIYLTATPSKALQRqvKRGKLKVVKLpARYHGHPLPVPKFKwlgNWKKRLrrgklpRKLLKWLKKRLKEGRQLLIFVPTI 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 457 RMAEDLTEYLEEH--GERVRYLHSDiDTvERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSlVAILDADKEGFlrSERS 534
Cdd:COG4098  330 ELLEQLVALLQKLfpEERIAGVHAE-DP-ERKEKVQAFRDGEIPILVTTTILERGVTFPNVD-VAVLGADHPVF--TEAA 404
                        170       180       190
                 ....*....|....*....|....*....|....
gi 496059679 535 LIQTIGRAARNI---NGKAILYGDKITASMAKAI 565
Cdd:COG4098  405 LVQIAGRVGRSAdypTGEVIFFHHGKTRAMKRAI 438
DEXDc smart00487
DEAD-like helicases superfamily;
5-92 2.27e-12

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 66.36  E-value: 2.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679     5 FKLNSAFKPSGDQPEAIRRLEEGLEDGLahqtLLGVTGSGKTFTIANVIADL-----QRPTMVLAPNKTLAAQLYGEMKE 79
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVI----LAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKK 76
                           90
                   ....*....|...
gi 496059679    80 FFPDNAVEYFVSY 92
Cdd:smart00487  77 LGPSLGLKVVGLY 89
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
455-552 1.82e-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: 64.57  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 455 TKRMAEDLTEYLEEhgerVRYLHSDIDTVERM----EIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFL- 529
Cdd:cd18804  103 TERVEEELKTLFPE----ARIARIDRDTTRKKgaleKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSGLNSp 178
                         90       100       110
                 ....*....|....*....|....*....|
gi 496059679 530 --RS-ERS---LIQTIGRAAR-NINGKAIL 552
Cdd:cd18804  179 dfRAsERAfqlLTQVSGRAGRgDKPGKVII 208
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
420-518 7.19e-10

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 61.70  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 420 DPV-IEVRPVATQVD---------------DLLSEIrTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTV 483
Cdd:COG0513  200 NPVrIEVAPENATAEtieqryylvdkrdklELLRRL-LRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQG 278
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496059679 484 ERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLV 518
Cdd:COG0513  279 QRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
34-102 7.88e-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: 57.80  E-value: 7.88e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059679  34 HQTLLGVTGSGKTFTIANVIADL---QRP-TMVLAPNKTLAAQLYGEMKEFF-PDNAVEYFVSYYDYYQPEAYV 102
Cdd:cd00046    3 NVLITAPTGSGKTLAALLAALLLllkKGKkVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSAEEREKNK 76
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
444-549 2.79e-09

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: 55.26  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 444 AINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSD-IDTVERMEIIRDLRLGE--FDVLVGINLLREGLDMPEVSLVAi 520
Cdd:cd18799    4 YVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDySDRERGDEALILLFFGElkPPILVTVDLLTTGVDIPEVDNVV- 82
                         90       100       110
                 ....*....|....*....|....*....|..
gi 496059679 521 ldadkegFLRSERSLI---QTIGRAARNINGK 549
Cdd:cd18799   83 -------FLRPTESRTlflQMLGRGLRLHEGK 107
ResIII pfam04851
Type III restriction enzyme, res subunit;
17-85 2.91e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 56.53  E-value: 2.91e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059679   17 QPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQ-----RPTMVLAPNKTLAAQLYGEMKEFFPDNA 85
Cdd:pfam04851   8 QIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFkkgpiKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
422-552 8.00e-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: 54.67  E-value: 8.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 422 VIEVRPVATQVDDLLSEI--RTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYL----HSDIDTVERM------EII 489
Cdd:cd18801    4 VEKIHPKLEKLEEIVKEHfkKKQEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGKSSKGMsqkeqkEVI 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059679 490 RDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKegflrSERSLIQTIGRAARNINGKAIL 552
Cdd:cd18801   84 EQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASP-----SPIRMIQRMGRTGRKRQGRVVV 141
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
34-96 1.78e-07

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: 49.05  E-value: 1.78e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059679  34 HQTLLGVTGSGKTFTIANVIADL---QRPTMVLAPNKTLAAQLYGEMKEFFPDNAVEYFVSYYDYY 96
Cdd:cd17912    1 NILHLGPTGSGKTLVAIQKIASAmssGKSVLVVTPTKLLAHEILIVIDEIQ*ILDPAAGWAWATRA 66
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
448-553 1.83e-07

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: 48.85  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 448 RVLVTTLTKRMAEDLTEYLEehgervrylhsdidtvermeiirdlrlgefdVLVGINLLREGLDMPEVSLVAILDADkeg 527
Cdd:cd18785    5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP--- 50
                         90       100
                 ....*....|....*....|....*...
gi 496059679 528 flRSERSLIQTIGRAARN--INGKAILY 553
Cdd:cd18785   51 --SSAASYIQRVGRAGRGgkDEGEVILF 76
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
499-554 1.98e-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: 48.31  E-value: 1.98e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496059679 499 VLVGINLLREGLDMPEVSLVAILDADkegflRSERSLIQTIGRAARNIN-GKAILYG 554
Cdd:cd09300    8 VLIAVN*ALTGFDAPELNTIIVDKNL-----RSYRGLNQAFGRANRIYTfGGIVTYR 59
uvrC PRK00558
excinuclease ABC subunit UvrC;
636-669 4.48e-07

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 53.20  E-value: 4.48e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 496059679 636 IHELEGQMMQHAQNLEFEEAATIRDQLHQLRELF 669
Cdd:PRK00558 204 LKELEEKMEEASENLEFERAARYRDQIQALRRVQ 237
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
636-669 4.64e-07

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


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 53.20  E-value: 4.64e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 496059679 636 IHELEGQMMQHAQNLEFEEAATIRDQLHQLRELF 669
Cdd:COG0322  205 IKELEEKMEEAAEELEFERAARLRDQIRALEKVQ 238
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
11-87 4.89e-07

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 50.49  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  11 FKPSGDQPEAIRRLEEGLEDGLAHQTLL-GVTGSGKT--FTIANVIA-DLQRPTMVLAPNKTLAAQLYGEMKEFFPDNAV 86
Cdd:cd17918   14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLsGDVGSGKTlvALGAALLAyKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93

                 .
gi 496059679  87 E 87
Cdd:cd17918   94 E 94
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
435-553 4.93e-07

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 53.20  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 435 LLSEIRTrAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYL--HSDIDTV------ERMEIIRDLRLGEFDVLVGINLL 506
Cdd:COG1111  343 ILKEQLG-TNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgQASKEGDkgltqkEQIEILERFRAGEFNVLVATSVA 421
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 496059679 507 REGLDMPEVSLVAILDAdkegfLRSE-RSlIQTIGRAARNINGKAILY 553
Cdd:COG1111  422 EEGLDIPEVDLVIFYEP-----VPSEiRS-IQRKGRTGRKREGRVVVL 463
PRK05580 PRK05580
primosome assembly protein PriA; Validated
455-552 9.07e-07

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 52.08  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 455 TKRMAEDLTEYLEEHgeRVRYLHSD-IDTVERME-IIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDAD---KEGFL 529
Cdd:PRK05580 439 TERLEEELAELFPEA--RILRIDRDtTRRKGALEqLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDADlglFSPDF 516
                         90       100
                 ....*....|....*....|....*...
gi 496059679 530 R-SERS---LIQTIGRAAR-NINGKAIL 552
Cdd:PRK05580 517 RaSERTfqlLTQVAGRAGRaEKPGEVLI 544
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
170-336 3.63e-06

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 50.51  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  170 RAILR-RLAELQYTRNDQAFQRGTFRVRGEVIDIFPAESDDiALRVELFDEEVERLSLFDPLTGQVESTISRFTIYPKTH 248
Cdd:PRK10689  138 RDALRaQLEQAGYRHVDQVMEHGEYATRGALLDLFPMGSEE-PYRIDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679  249 YVTPRErivqAMEEIKVELAERRKVLLANNKLLeeQRLSQRTqfdlemmnelgYCSGIEnysrYLSGRGPGEPPPTLFDY 328
Cdd:PRK10689  217 FPTDKA----AIELFRSQWRDTFEVKRDAEHIY--QQVSKGT-----------LPAGIE----YWQPLFFSEPLPPLFSY 275

                  ....*...
gi 496059679  329 LPADGLLV 336
Cdd:PRK10689  276 FPANTLLV 283
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
25-89 5.48e-06

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: 46.53  E-value: 5.48e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059679  25 EEGLEDGLAHQ-----TLLGVTGSGKTFTIANVIADL-QRPTMVLAPNKTLAAQLYGEMKEFFPDNAVEYF 89
Cdd:cd17926    6 EEALEAWLAHKnnrrgILVLPTGSGKTLTALALIAYLkELRTLIVVPTDALLDQWKERFEDFLGDSSIGLI 76
PRK13766 PRK13766
Hef nuclease; Provisional
446-551 1.32e-05

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 48.33  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 446 NERVLVTTLTKRMAEDLTEYLEEHG-ERVRYL-HSDIDTVERM------EIIRDLRLGEFDVLVGINLLREGLDMPEVSL 517
Cdd:PRK13766 365 DSRIIVFTQYRDTAEKIVDLLEKEGiKAVRFVgQASKDGDKGMsqkeqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDL 444
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496059679 518 VAILDAdkegfLRSE-RSlIQTIGRAARNINGKAI 551
Cdd:PRK13766 445 VIFYEP-----VPSEiRS-IQRKGRTGRQEEGRVV 473
PTZ00424 PTZ00424
helicase 45; Provisional
455-544 1.52e-05

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 47.90  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 455 TKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKegflrSERS 534
Cdd:PTZ00424 276 TRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA-----SPEN 350
                         90
                 ....*....|
gi 496059679 535 LIQTIGRAAR 544
Cdd:PTZ00424 351 YIHRIGRSGR 360
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
446-553 2.21e-05

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: 44.93  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 446 NERVLVTT----LTKRMAEDLTEYleehgervrYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSlVAIL 521
Cdd:cd18789   49 GDKIIVFTdnveALYRYAKRLLKP---------FITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPEAN-VAIQ 118
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496059679 522 DADKEGflrSERSLIQTIG---RAARNINGKAILY 553
Cdd:cd18789  119 ISGHGG---SRRQEAQRLGrilRPKKGGGKNAFFY 150
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
446-542 2.43e-05

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: 44.50  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 446 NERVLVTTLTKRMAEDL-------TEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLV 518
Cdd:cd18802   33 ERRATAVVLSRLLKEHPstlafirCGFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLV 112
                         90       100
                 ....*....|....*....|....
gi 496059679 519 AILDadkegFLRSERSLIQTIGRA 542
Cdd:cd18802  113 IRFD-----LPKTLRSYIQSRGRA 131
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
487-552 3.73e-05

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


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 47.04  E-value: 3.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059679 487 EIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADkEGF----LR-SERS---LIQTIGRAAR-NINGKAIL 552
Cdd:COG1198  522 KLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDAD-LGLnspdFRaAERTfqlLTQVAGRAGRaEKPGEVLI 595
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
424-544 3.75e-05

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: 43.74  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 424 EVRPV-ATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVG 502
Cdd:cd18794    7 SVRPKdKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496059679 503 INLLREGLDMPEVSLVAILDADK--EGFLrsersliQTIGRAAR 544
Cdd:cd18794   87 TVAFGMGIDKPDVRFVIHYSLPKsmESYY-------QESGRAGR 123
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
17-85 6.43e-05

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: 43.70  E-value: 6.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059679  17 QPEAIRRLEEGLEDGlaHQTLLGV--TGSGKTFTIANVIADLQRPT-----MVLAPNKTLAAQLYGEMKEFFPDNA 85
Cdd:cd18032    5 QQEAIEALEEAREKG--QRRALLVmaTGTGKTYTAAFLIKRLLEANrkkriLFLAHREELLEQAERSFKEVLPDGS 78
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
423-545 2.02e-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: 44.30  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 423 IEVRPVATQVDDLLSEIRTRAAINERVLVTTLTKRMAEDLTEYLEE--HGERVRYLHSDIDTVERMEIIRDLRL----GE 496
Cdd:COG1203  343 VELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQELYEALKEklPDEEVYLLHSRFCPADRSEIEKEIKErlerGK 422
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496059679 497 FDVLVGINLLREGLDmpevslvaiLDADkegFLRSE----RSLIQTIGRAARN 545
Cdd:COG1203  423 PCILVSTQVVEAGVD---------IDFD---VVIRDlaplDSLIQRAGRCNRH 463
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
434-505 2.08e-04

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 44.45  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 434 DLLSEIRTRaaiNERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLG-EFDVL--------VGIN 504
Cdd:COG0553  540 ELLEELLAE---GEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPVFlislkaggEGLN 616

                 .
gi 496059679 505 L 505
Cdd:COG0553  617 L 617
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
387-544 4.47e-04

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


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 43.67  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 387 PQTIYVSATPGNYE--LEK-SGDDV--VDQVVRPTG-----LLDPVI----EVRPVATQVDDLLSE-IRTRAaineRVLV 451
Cdd:COG1205  218 PQFILASATIGNPAehAERlTGRPVtvVDEDGSPRGertfvLWNPPLvddgIRRSALAEAARLLADlVREGL----RTLV 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 452 TTLTKRMAEDLTEYLEEH------GERVR-----YLHSdidtvERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVaI 520
Cdd:COG1205  294 FTRSRRGAELLARYARRAlrepdlADRVAayragYLPE-----ERREIERGLRSGELLGVVSTNALELGIDIGGLDAV-V 367
                        170       180
                 ....*....|....*....|....
gi 496059679 521 LDadkeGFLRSERSLIQTIGRAAR 544
Cdd:COG1205  368 LA----GYPGTRASFWQQAGRAGR 387
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
456-548 5.56e-04

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: 41.14  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 456 KRMAEDLTEYLEEHGERVRYLHSDidtveRMEIIRDLRLGEFDVLVGI----NLLREGLDMPEVSLVAIldadkegFLRS 531
Cdd:cd18798   37 KEYAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLPERIKYAI-------FYGV 104
                         90
                 ....*....|....*...
gi 496059679 532 E-RSLIQTIGRAARNING 548
Cdd:cd18798  105 PvTTYIQASGRTSRLYAG 122
McsA COG3880
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ...
630-667 5.95e-04

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


Pssm-ID: 443088 [Multi-domain]  Cd Length: 173  Bit Score: 41.03  E-value: 5.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 496059679 630 KALQQKIHELEGQMMQHAQNLEFEEAATIRDQLHQLRE 667
Cdd:COG3880  129 LRIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEK 166
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
430-505 6.15e-04

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 40.54  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 430 TQVDDLLSEIRTRaaiNERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLR--LGEFDVL------- 500
Cdd:cd18793   14 EALLELLEELREP---GEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNedPDIRVFLlstkagg 90

                 ....*
gi 496059679 501 VGINL 505
Cdd:cd18793   91 VGLNL 95
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
449-549 6.79e-04

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


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 40.71  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 449 VLVTTLTKRMAEDLTEYL------EEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILD 522
Cdd:cd18796   41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
                         90       100
                 ....*....|....*....|....*..
gi 496059679 523 ADKegflrSERSLIQTIGRAARNINGK 549
Cdd:cd18796  121 SPK-----SVARLLQRLGRSGHRPGAA 142
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
17-84 1.03e-03

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 42.52  E-value: 1.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059679  17 QPEAIRRLEEGLEDGlaHQTLLGV--TGSGKTFTIANVIADLQRPTMV-----LAPNKTLAAQLYGEMKEFFPDN 84
Cdd:COG4096  163 QIEAIRRVEEAIAKG--QRRALLVmaTGTGKTRTAIALIYRLLKAGRAkrilfLADRNALVDQAKNAFKPFLPDL 235
UVR pfam02151
UvrB/uvrC motif;
633-668 1.42e-03

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 36.61  E-value: 1.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 496059679  633 QQKIHELEGQMMQHAQNLEFEEAATIRDQLHQLREL 668
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
459-544 1.92e-03

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: 39.25  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 459 AEDLTEYLEEH--GE-RVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFlrseRSL 535
Cdd:cd18811   47 AVAMYEYLKERfrPElNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGL----SQL 122

                 ....*....
gi 496059679 536 IQTIGRAAR 544
Cdd:cd18811  123 HQLRGRVGR 131
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
470-553 2.02e-03

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 41.31  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 470 GERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDadkegFLRSERSLIQTIGRAARNIN-G 548
Cdd:PLN00206 392 GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFD-----MPNTIKEYIHQIGRASRMGEkG 466

                 ....*
gi 496059679 549 KAILY 553
Cdd:PLN00206 467 TAIVF 471
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
447-544 2.26e-03

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 41.08  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 447 ERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADke 526
Cdd:PRK11192 246 TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMP-- 323
                         90
                 ....*....|....*...
gi 496059679 527 gflRSERSLIQTIGRAAR 544
Cdd:PRK11192 324 ---RSADTYLHRIGRTGR 338
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
16-81 2.39e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.15  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059679   16 DQPEAIRRLEEGlEDGLAHqtllGVTGSGKT----FTIANVIADLQRP--TMVLAPNKTLAAQLYGEMKEFF 81
Cdd:pfam00270   3 IQAEAIPAILEG-RDVLVQ----APTGSGKTlaflLPALEALDKLDNGpqALVLAPTRELAEQIYEELKKLG 69
DEXHc_priA cd17929
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ...
17-88 2.44e-03

DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350687 [Multi-domain]  Cd Length: 178  Bit Score: 39.50  E-value: 2.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059679  17 QPEAIRRLEEGLEDGlaHQTLL-GVTGSGKT----FTIANVIADlQRPTMVLAPNKTLAAQLYGEMKEFFPDNAVEY 88
Cdd:cd17929    1 QRKAYEAIVSSLGGF--KTFLLhGVTGSGKTevyiELIEKVLAK-GKQVLVLVPEISLTPQLIKRFKKRFGDKVAVL 74
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
459-527 3.94e-03

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: 38.40  E-value: 3.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059679 459 AEDLTEYLEEH-GE-RVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEG 527
Cdd:cd18792   47 IEALAEELKELvPEaRVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFG 117
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
443-539 6.26e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 38.46  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059679 443 AAINERVLV----TTLTKRMAEDLTEYLEEHGERVR--YLHSDIDTVERMEIIRDLRLGEFDVLVGINLL----REGLDM 512
Cdd:cd17924   57 ASKGKRSYLifptKSLVKQAYERLSKYAEKAGVEVKilVYHSRLKKKEKEELLEKIEKGDFDILVTTNQFlsknFDLLSN 136
                         90       100
                 ....*....|....*....|....*..
gi 496059679 513 PEVSLVAILDADkeGFLRSERSlIQTI 539
Cdd:cd17924  137 KKFDFVFVDDVD--AVLKSSKN-IDRL 160
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
14-73 9.77e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 37.93  E-value: 9.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059679   14 SGDQPEAIRRLeegLEDGLAHQTLLGVTGSGKTFT---IANVIADLQRPTMVLAPNKTLAAQL 73
Cdd:pfam13604   3 NAEQAAAVRAL---LTSGDRVAVLVGPAGTGKTTAlkaLREAWEAAGYRVIGLAPTGRAAKVL 62
 
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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