NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1337947954|ref|WP_103423597|]
View 

excinuclease ABC subunit UvrB [Fructilactobacillus sanfranciscensis]

Protein Classification

excinuclease ABC subunit UvrB( domain architecture ID 11426127)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
8-665 0e+00

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


:

Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1323.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   8 KFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPN 87
Cdd:COG0556     1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  88 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVTLHV 167
Cdd:COG0556    81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 168 GEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTL 247
Cdd:COG0556   161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 248 FPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPY 327
Cdd:COG0556   241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 328 TLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELEN 407
Cdd:COG0556   321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 408 S-SQVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTL 486
Cdd:COG0556   401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 487 ERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQA 566
Cdd:COG0556   481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 567 AMDETTRRRKIQIAYNKEHHITPKTIIKPISKAISAYKQDEDDkynKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAK 646
Cdd:COG0556   561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEE---TEELVAEADAAKLSKEELEKLIKELEKEMKEAAK 637
                         650
                  ....*....|....*....
gi 1337947954 647 QLDFEQAASLRDTIKKLKK 665
Cdd:COG0556   638 NLEFEEAARLRDEIKELKK 656
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
8-665 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1323.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   8 KFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPN 87
Cdd:COG0556     1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  88 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVTLHV 167
Cdd:COG0556    81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 168 GEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTL 247
Cdd:COG0556   161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 248 FPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPY 327
Cdd:COG0556   241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 328 TLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELEN 407
Cdd:COG0556   321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 408 S-SQVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTL 486
Cdd:COG0556   401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 487 ERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQA 566
Cdd:COG0556   481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 567 AMDETTRRRKIQIAYNKEHHITPKTIIKPISKAISAYKQDEDDkynKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAK 646
Cdd:COG0556   561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEE---TEELVAEADAAKLSKEELEKLIKELEKEMKEAAK 637
                         650
                  ....*....|....*....
gi 1337947954 647 QLDFEQAASLRDTIKKLKK 665
Cdd:COG0556   638 NLEFEEAARLRDEIKELKK 656
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
5-665 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1307.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   5 SHKKFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKF 84
Cdd:PRK05298    1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  85 FPNNAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVT 164
Cdd:PRK05298   81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 165 LHVGEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQ 244
Cdd:PRK05298  161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 245 VTLFPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGE 324
Cdd:PRK05298  241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 325 PPYTLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYE 404
Cdd:PRK05298  321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 405 LENSS-QVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDI 483
Cdd:PRK05298  401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 484 KTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDS 563
Cdd:PRK05298  481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 564 MQAAMDETTRRRKIQIAYNKEHHITPKTIIKPISKAIsaykqdeDDKYNKKKpfaetdfeqMSYKEQEQMIKNLSDEMRE 643
Cdd:PRK05298  561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDIL-------DSVYKKDK---------LSKKELEKLIKELEKQMKE 624
                         650       660
                  ....*....|....*....|..
gi 1337947954 644 AAKQLDFEQAASLRDTIKKLKK 665
Cdd:PRK05298  625 AAKNLEFEEAARLRDEIKELKE 646
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
8-664 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: 1147.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   8 KFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPN 87
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  88 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVTLHV 167
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 168 GEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTL 247
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 248 FPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPY 327
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 328 TLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELEN 407
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 408 SSQVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLE 487
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 488 RTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQAA 567
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 568 MDETTRRRKIQIAYNKEHHITPKTIIKPIsKAISAYKQDEDDKyNKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAKQ 647
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPI-RDILDIELKEKED-AAKKKKKGEDLSDLSKKELKKLIKQLEKEMKQAARN 638
                         650
                  ....*....|....*..
gi 1337947954 648 LDFEQAASLRDTIKKLK 664
Cdd:TIGR00631 639 LEFEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
9-417 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: 538.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   9 FDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPNN 88
Cdd:cd17916     1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  89 AVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIfglgspkeYQDhtvtlhvg 168
Cdd:cd17916    81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCI--------YER-------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 169 eemerdvllrklvniqfqrndidfdrgrfrvhgdtvevfpasgtqnayrieffgdeidkitqvntltgevlgnpeqvtlf 248
Cdd:cd17916       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 249 pathfltndevmnvALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPYT 328
Cdd:cd17916   145 --------------AIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 329 LLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELENS 408
Cdd:cd17916   211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                  ....*....
gi 1337947954 409 SQVVEQIIR 417
Cdd:cd17916   291 GQVVEQIIR 299
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
163-253 8.06e-41

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: 143.69  E-value: 8.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 163 VTLHVGEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNP 242
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 1337947954 243 EQVTLFPATHF 253
Cdd:pfam17757  81 DEVTIYPASHY 91
HELICc smart00490
helicase superfamily c-terminal domain;
463-547 1.67e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.81  E-value: 1.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  463 EDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADkegflRNPRSLIQTI 542
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 1337947954  543 GRAAR 547
Cdd:smart00490  76 GRAGR 80
 
Name Accession Description Interval E-value
UvrB COG0556
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
8-665 0e+00

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


Pssm-ID: 440322 [Multi-domain]  Cd Length: 657  Bit Score: 1323.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   8 KFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPN 87
Cdd:COG0556     1 PFKLVSPYKPAGDQPQAIEKLVEGIEAGEKHQTLLGVTGSGKTFTMANVIERVQRPTLVLAHNKTLAAQLYGEFKEFFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  88 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVTLHV 167
Cdd:COG0556    81 NAVEYFVSYYDYYQPEAYVPSTDTYIEKDSSINEEIDRLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLSLRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 168 GEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTL 247
Cdd:COG0556   161 GEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFPAYSEERAIRIEFFGDEIERISEFDPLTGEVLGELDRVTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 248 FPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPY 327
Cdd:COG0556   241 YPASHYVTPRERLERAIESIKEELEERLAEFESEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGEPPP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 328 TLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELEN 407
Cdd:COG0556   321 TLLDYFPDDFLLFIDESHVTVPQIRGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEARVPQTIYVSATPGDYELEK 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 408 S-SQVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTL 486
Cdd:COG0556   401 SgGQVVEQIIRPTGLLDPEIEVRPTKGQVDDLLGEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDIDTL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 487 ERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQA 566
Cdd:COG0556   481 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDSMQR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 567 AMDETTRRRKIQIAYNKEHHITPKTIIKPISKAISAYKQDEDDkynKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAK 646
Cdd:COG0556   561 AIDETNRRREIQEAYNEEHGITPQTIKKSIRDILEGTYEADEE---TEELVAEADAAKLSKEELEKLIKELEKEMKEAAK 637
                         650
                  ....*....|....*....
gi 1337947954 647 QLDFEQAASLRDTIKKLKK 665
Cdd:COG0556   638 NLEFEEAARLRDEIKELKK 656
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
5-665 0e+00

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 1307.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   5 SHKKFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKF 84
Cdd:PRK05298    1 MMKPFKLVSPYKPAGDQPQAIEELVEGIEAGEKHQTLLGVTGSGKTFTMANVIARLQRPTLVLAHNKTLAAQLYSEFKEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  85 FPNNAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVT 164
Cdd:PRK05298   81 FPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINEEIERLRHSATKSLLERRDVIVVASVSCIYGLGSPEEYLKMVLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 165 LHVGEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQ 244
Cdd:PRK05298  161 LRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYEERAIRIEFFGDEIERISEFDPLTGEVLGELDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 245 VTLFPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGE 324
Cdd:PRK05298  241 VTIYPASHYVTPRERLERAIESIKEELEERLKELEKEGKLLEAQRLEQRTRYDLEMLRELGYCSGIENYSRHLDGRKPGE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 325 PPYTLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYE 404
Cdd:PRK05298  321 PPYTLLDYFPDDFLLFIDESHVTVPQIGGMYNGDRSRKETLVEYGFRLPSALDNRPLKFEEFEAKVPQTIYVSATPGDYE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 405 LENSS-QVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDI 483
Cdd:PRK05298  401 LEKSGgVVVEQIIRPTGLLDPEIEVRPTKGQVDDLLSEIRKRVAKGERVLVTTLTKRMAEDLTDYLKELGIKVRYLHSDI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 484 KTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDS 563
Cdd:PRK05298  481 DTLERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVILYADKITDS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 564 MQAAMDETTRRRKIQIAYNKEHHITPKTIIKPISKAIsaykqdeDDKYNKKKpfaetdfeqMSYKEQEQMIKNLSDEMRE 643
Cdd:PRK05298  561 MQKAIDETERRREIQIAYNEEHGITPKTIKKKIRDIL-------DSVYKKDK---------LSKKELEKLIKELEKQMKE 624
                         650       660
                  ....*....|....*....|..
gi 1337947954 644 AAKQLDFEQAASLRDTIKKLKK 665
Cdd:PRK05298  625 AAKNLEFEEAARLRDEIKELKE 646
uvrb TIGR00631
excinuclease ABC, B subunit; All proteins in this family for wich functions are known are DNA ...
8-664 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: 1147.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   8 KFDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPN 87
Cdd:TIGR00631   1 LFKLHSPFQPAGDQPKAIAKLVEGLTDGEKHQTLLGVTGSGKTFTMANVIAQVNRPTLVIAHNKTLAAQLYNEFKEFFPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  88 NAVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEYQDHTVTLHV 167
Cdd:TIGR00631  81 NAVEYFVSYYDYYQPEAYVPSKDTYIEKDASINDEIERLRHSATRSLLERRDVIVVASVSCIYGLGSPEEYLKMVLHLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 168 GEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTL 247
Cdd:TIGR00631 161 GKEIDRRELLRRLVELQYERNDVDFQRGTFRVRGDVVEIFPAYEDEFAVRIEFFGDEIERISRVDPLTGEVLRELDSFTI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 248 FPATHFLTNDEVMNVALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPY 327
Cdd:TIGR00631 241 FPASHYVTPEERLERAIKNIEKELEERLKYFEEQGKLLEAQRLKQRTEYDLEMLREMGYCSGIENYSRHLSGRAPGEPPY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 328 TLLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELEN 407
Cdd:TIGR00631 321 TLLDYFPDDFLLVIDESHVTLPQIGGMYNGDRSRKQTLVEYGFRLPSALDNRPLKFEEFEERINQVVYVSATPGPYELEQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 408 SSQVVEQIIRPTGLLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLE 487
Cdd:TIGR00631 401 SGNVVEQIIRPTGLLDPEIEVRPTDGQVDDLLSEIRQRVARNERVLVTTLTKKMAEDLTDYLKELGIKVRYLHSEIDTLE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 488 RTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQAA 567
Cdd:TIGR00631 481 RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKVIMYADKITDSMQKA 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 568 MDETTRRRKIQIAYNKEHHITPKTIIKPIsKAISAYKQDEDDKyNKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAKQ 647
Cdd:TIGR00631 561 IEETERRRKIQMAYNEEHGITPQTIRKPI-RDILDIELKEKED-AAKKKKKGEDLSDLSKKELKKLIKQLEKEMKQAARN 638
                         650
                  ....*....|....*..
gi 1337947954 648 LDFEQAASLRDTIKKLK 664
Cdd:TIGR00631 639 LEFEEAARLRDEILELK 655
DEXHc_UvrB cd17916
DEXH-box helicase domain of excinuclease ABC subunit B; Excinuclease ABC subunit B (or UvrB) ...
9-417 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: 538.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   9 FDLVSKYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPNN 88
Cdd:cd17916     1 FKLVSPFKPAGDQPQAIAKLVEGLKRGVKFQTLLGVTGSGKTFTIANVIAQVNKPTLVIAHNKTLAAQLYSEFKEFFPEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  89 AVEYFVSYYDYYQPEAYVPSSDTYIEKDASINDEIDQLRHAATSALLSRNDVIVVASVSSIfglgspkeYQDhtvtlhvg 168
Cdd:cd17916    81 AVEYFVSYYDYYQPEAYVPQTDTYIEKDASINDEIDRLRHSATRSLLERRDVIVVASVSCI--------YER-------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 169 eemerdvllrklvniqfqrndidfdrgrfrvhgdtvevfpasgtqnayrieffgdeidkitqvntltgevlgnpeqvtlf 248
Cdd:cd17916       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 249 pathfltndevmnvALPEIKTDMEKQVAAMEKSGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDRRKPGEPPYT 328
Cdd:cd17916   145 --------------AIKSIEEELEERLKYFRAQGKLLEAQRLEQRTRYDLEMLREMGFCSGIENYSRHLSGRKPGEPPYT 210
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 329 LLDFFPKDFLMFVDESHQTLPQVHGMIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHIHQVIYMSATPGTYELENS 408
Cdd:cd17916   211 LLDYFPDDFLLVIDESHVTVPQLRGMYNGDRSRKQSLVDYGFRLPSALDNRPLKFEEFEEKVNQVIYVSATPGDYELEHS 290

                  ....*....
gi 1337947954 409 SQVVEQIIR 417
Cdd:cd17916   291 GQVVEQIIR 299
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
423-593 6.28e-114

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: 338.84  E-value: 6.28e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 423 DPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDV 502
Cdd:cd18790     1 DPEIEVRPTEGQVDDLLGEIRKRVARGERVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 503 LVGINLLREGIDVPEVSLVAILDADKEGFLRNPRSLIQTIGRAARNENGHVIMYADRVTDSMQAAMDETTRRRKIQIAYN 582
Cdd:cd18790    81 LVGINLLREGLDLPEVSLVAILDADKEGFLRSETSLIQTIGRAARNVNGKVILYADKITDSMQKAIEETERRREIQMEYN 160
                         170
                  ....*....|.
gi 1337947954 583 KEHHITPKTII 593
Cdd:cd18790   161 EEHGITPKTII 171
Mfd COG1197
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ...
35-527 3.61e-46

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


Pssm-ID: 440810 [Multi-domain]  Cd Length: 1130  Bit Score: 176.80  E-value: 3.61e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   35 GDKEQTLLGATGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPNNAVEYFvsyydyyqpeayvPSSDTYIE 114
Cdd:COG1197      1 GGGRLTLSGLPGSARALLLAALARALGRPLLVVTADEREAERLAEDLRFFLPDLPVLLF-------------PAWETLPY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  115 KDASINDEIDQLRHAATSALLSRNDVIVVASVSSIFGLGSPKEY-QDHTVTLHVGEEMERDVLLRKLVNIQFQRNDIDFD 193
Cdd:COG1197     68 DRFSPSPDIVSERLATLRRLASGKPGIVVTPVRALLQRLPPPELlAAASLSLKVGDELDLEELRERLVAAGYERVDQVEE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  194 RGRFRVHGDTVEVFPAsGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTLFPATHFLTNDEVMNVALpeiktdmek 273
Cdd:COG1197    148 PGEFAVRGGILDIFPP-GSEHPVRIEFFGDEIESIRTFDPETQRSLEKVDEVELLPAREFPLDEEAIERFR--------- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  274 qvaameksGKLLEAQRLKQRTTYDIEMMREMGYTTGIENYSRYMDrrkpgEPPYTLLDFFPKDFLMFVDESHQTLPQVHG 353
Cdd:COG1197    218 --------ERLRELFGLDPKLDELYEALSEGIAFAGIEYYLPLFY-----EELATLFDYLPEDALVVLDEPERIEEAAEE 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  354 MIKGDKARKKQLIDYGFRLPSSYDNRPLDFTEFEKHI--HQVIYMSATPGTYELENSSQVveqiirptglldPTVEVRPT 431
Cdd:COG1197    285 FWEEIEERYEARRHDRGRPLLPPEELFLDPEELFAALkrRPRVTLSPFAALPEGAGVVNL------------GARPLPSF 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  432 KDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSdiktlertriIRDLRLGKFDVLVGInlLRE 511
Cdd:COG1197    353 AGQLEALLEELKRLLKDGGRVLLAAESEGRRERLLELLRDHGIPARLVES----------LAELSPGGVAITVGP--LEH 420
                          490
                   ....*....|....*.
gi 1337947954  512 GIDVPEVSLVAILDAD 527
Cdd:COG1197    421 GFELPDAKLAVITESE 436
UvrB_inter pfam17757
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ...
163-253 8.06e-41

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: 143.69  E-value: 8.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 163 VTLHVGEEMERDVLLRKLVNIQFQRNDIDFDRGRFRVHGDTVEVFPASGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNP 242
Cdd:pfam17757   1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEDEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
                          90
                  ....*....|.
gi 1337947954 243 EQVTLFPATHF 253
Cdd:pfam17757  81 DEVTIYPASHY 91
UvrB pfam12344
Ultra-violet resistance protein B; This domain family is found in bacteria, archaea and ...
555-597 9.79e-25

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


Pssm-ID: 463540 [Multi-domain]  Cd Length: 43  Bit Score: 96.69  E-value: 9.79e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1337947954 555 MYADRVTDSMQAAMDETTRRRKIQIAYNKEHHITPKTIIKPIS 597
Cdd:pfam12344   1 LYADKITDSMQRAIDETERRREIQEAYNEEHGITPKTIKKKIR 43
HELICc smart00490
helicase superfamily c-terminal domain;
463-547 1.67e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.81  E-value: 1.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  463 EDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADkegflRNPRSLIQTI 542
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-----WSPASYIQRI 75

                   ....*
gi 1337947954  543 GRAAR 547
Cdd:smart00490  76 GRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
433-547 3.31e-21

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: 89.19  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 433 DQMDDLVGEINEriKKKQRTFVTTLTKKMSEdlTDYLKDL-GIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLRE 511
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1337947954 512 GIDVPEVSLVAILDADKegflrNPRSLIQTIGRAAR 547
Cdd:pfam00271  77 GLDLPDVDLVINYDLPW-----NPASYIQRIGRAGR 107
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
427-666 1.18e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 86.62  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 427 EVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGI 506
Cdd:COG1061   283 ALAADAERKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTV 362
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 507 NLLREGIDVPEVSLVAILDAdkegfLRNPRSLIQTIGRAAR----NENGHVIMYADRVTDSMQAAMDEttRRRKIQIAYN 582
Cdd:COG1061   363 DVLNEGVDVPRLDVAILLRP-----TGSPREFIQRLGRGLRpapgKEDALVYDFVGNDVPVLEELAKD--LRDLAGYRVE 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 583 KEHHITPKTIIKPISKAISAYKQDEDDKYNKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAKQLDFEQAASLRDTIKK 662
Cdd:COG1061   436 FLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELL 515

                  ....
gi 1337947954 663 LKKD 666
Cdd:COG1061   516 LLLA 519
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
426-554 1.37e-15

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: 73.70  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 426 VEVRPTKDQMDDLVGEINERIKKKQrTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVG 505
Cdd:cd18787     5 YVVVEEEEKKLLLLLLLLEKLKPGK-AIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVLVA 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1337947954 506 INLLREGIDVPEVSLVAILDadkegFLRNPRSLIQTIGRAAR-NENGHVI 554
Cdd:cd18787    84 TDVAARGLDIPGVDHVINYD-----LPRDAEDYVHRIGRTGRaGRKGTAI 128
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
37-143 2.97e-11

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: 61.65  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  37 KEQTLLGATGTGKTFTMANVIRDQNRP----TLVLAHNKTLAGQLYTELKKFF-PNNAVEYFVSYYDYYQPEAyvpssdt 111
Cdd:cd00046     2 ENVLITAPTGSGKTLAALLAALLLLLKkgkkVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSAEEREK------- 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1337947954 112 YIEKDASI----NDEIDQLRHAATSALLSRNDVIVV 143
Cdd:cd00046    75 NKLGDADIiiatPDMLLNLLLREDRLFLKDLKLIIV 110
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
458-521 4.30e-10

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 62.09  E-value: 4.30e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337947954 458 TKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLV 521
Cdd:COG0513   250 TKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHV 313
DEXDc smart00487
DEAD-like helicases superfamily;
15-96 5.70e-10

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 59.43  E-value: 5.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   15 YKPTGDQPSAIKKLdqglAAGDKEQTLLGATGTGKTFTMANVI-----RDQNRPTLVLAHNKTLAGQLYTELKKFFPNNA 89
Cdd:smart00487   7 EPLRPYQKEAIEAL----LSGLRDVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLGPSLG 82

                   ....*..
gi 1337947954   90 VEYFVSY 96
Cdd:smart00487  83 LKVVGLY 89
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
450-547 1.15e-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: 56.41  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 450 QRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTR-IIRDL--RLGKFDVLVGINLLREGIDVPEVSLVAilda 526
Cdd:cd18799     7 IKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLffGELKPPILVTVDLLTTGVDIPEVDNVV---- 82
                          90       100
                  ....*....|....*....|....
gi 1337947954 527 dkegFLRNPRSLI---QTIGRAAR 547
Cdd:cd18799    83 ----FLRPTESRTlflQMLGRGLR 102
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
435-667 3.11e-09

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 60.13  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 435 MDDLVGEINERIKKKQ--RTFVTTLTKKMSEDLTDYLKDLGIKVRYL------HSDiKTL---ERTRIIRDLRLGKFDVL 503
Cdd:COG1111   337 LSKLREILKEQLGTNPdsRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGD-KGLtqkEQIEILERFRAGEFNVL 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 504 VGINLLREGIDVPEVSLV--------AIldadkegflrnpRSlIQTIGRAARNENGHVIMYADRVTdsmqaaMDETTRRr 575
Cdd:COG1111   416 VATSVAEEGLDIPEVDLVifyepvpsEI------------RS-IQRKGRTGRKREGRVVVLIAKGT------RDEAYYW- 475
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 576 kiqIAYNKEHHItpKTIIKPISKAIsayKQDEDDKYNKKKPFAETDFEqmSYKEQEQMIKNLSDEMREAAKQLDFEQAAS 655
Cdd:COG1111   476 ---SSRRKEKKM--KSILKKLKKLL---DKQEKEKLKESAQATLDEFE--SIKELAEDEINEKDLDEIESSENGAHVDWR 545
                         250
                  ....*....|..
gi 1337947954 656 LRDTIKKLKKDM 667
Cdd:COG1111   546 EPVLLQVIVSTL 557
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
426-547 6.35e-09

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: 54.52  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 426 VEVRPTKDQMDDLVGEINERiKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVG 505
Cdd:cd18794     8 VRPKDKKDEKLDLLKRIKVE-HLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1337947954 506 INLLREGIDVPEVSLVAILDADK--EGFLrnprsliQTIGRAAR 547
Cdd:cd18794    87 TVAFGMGIDKPDVRFVIHYSLPKsmESYY-------QESGRAGR 123
ResIII pfam04851
Type III restriction enzyme, res subunit;
14-89 6.56e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 55.37  E-value: 6.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  14 KYKPTGDQPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIR-----DQNRPTLVLAHNKTLAGQLYTELKKFFPNN 88
Cdd:pfam04851   1 KLELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIArlfkkGPIKKVLFLVPRKDLLEQALEEFKKFLPNY 80

                  .
gi 1337947954  89 A 89
Cdd:pfam04851  81 V 81
SF2_C_priA cd18804
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ...
452-554 7.07e-09

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: 56.87  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 452 TFVTTLTKKMSEDLTDYLKDlgIKVRYLHSDI--KTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKE 529
Cdd:cd18804    97 VFKGIGTERVEEELKTLFPE--ARIARIDRDTtrKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSG 174
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1337947954 530 GFLRNPRS-------LIQTIGRAAR-NENGHVI 554
Cdd:cd18804   175 LNSPDFRAserafqlLTQVSGRAGRgDKPGKVI 207
UVR pfam02151
UvrB/uvrC motif;
631-665 1.64e-08

UvrB/uvrC motif;


Pssm-ID: 308001 [Multi-domain]  Cd Length: 36  Bit Score: 50.47  E-value: 1.64e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1337947954 631 EQMIKNLSDEMREAAKQLDFEQAASLRDTIKKLKK 665
Cdd:pfam02151   1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKK 35
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
502-557 1.89e-08

C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350171 [Multi-domain]  Cd Length: 59  Bit Score: 51.01  E-value: 1.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1337947954 502 VLVGINLLREGIDVPEVSLVAILDADkegflRNPRSLIQTIGRAARNEN-GHVIMYA 557
Cdd:cd09300     8 VLIAVN*ALTGFDAPELNTIIVDKNL-----RSYRGLNQAFGRANRIYTfGGIVTYR 59
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
451-556 1.77e-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: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 451 RTFVTTLTKKMSEDLTDYLKdlgikvrylhsdiktlertriirdlrlgkfdVLVGINLLREGIDVPEVSLVAILDADkeg 530
Cdd:cd18785     5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPP--- 50
                          90       100
                  ....*....|....*....|....*...
gi 1337947954 531 flRNPRSLIQTIGRAARN--ENGHVIMY 556
Cdd:cd18785    51 --SSAASYIQRVGRAGRGgkDEGEVILF 76
PRK10689 PRK10689
transcription-repair coupling factor; Provisional
34-258 5.31e-07

transcription-repair coupling factor; Provisional


Pssm-ID: 182649 [Multi-domain]  Cd Length: 1147  Bit Score: 53.21  E-value: 5.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954   34 AGDKEQtlLGA-TGTGKTFTMANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFP---NNAVEYFVSYYDYYQPEAYVpss 109
Cdd:PRK10689    13 AGDQRQ--LGElTGAACATEVAEIAERHAGPVVLIAPDMQNALRLHDEIQQFTDqmvMNLADWETLPYDSFSPHQDI--- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  110 dtyiekdasINDEIDQLRHAATsalLSRNDVIVvaSVSSIFGLGSPKEY-QDHTVTLHVGEEMERDVLLRKLVNIQFQRN 188
Cdd:PRK10689    88 ---------ISSRLSTLYQLPT---MQRGVLIL--PVNTLMQRVCPHSFlHGHALVMKKGQRLSRDALRAQLEQAGYRHV 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  189 DIDFDRGRFRVHGDTVEVFPAsGTQNAYRIEFFGDEIDKITQVNTLTGEVLGNPEQVTLFPATHFLTNDE 258
Cdd:PRK10689   154 DQVMEHGEYATRGALLDLFPM-GSEEPYRIDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAHEFPTDKA 222
uvrC PRK00558
excinuclease ABC subunit UvrC;
630-665 8.02e-07

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 52.04  E-value: 8.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1337947954 630 QEQMIKNLSDEMREAAKQLDFEQAASLRDTIKKLKK 665
Cdd:PRK00558  200 TDEVLKELEEKMEEASENLEFERAARYRDQIQALRR 235
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
21-89 9.94e-07

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


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 49.10  E-value: 9.94e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337947954  21 QPSAIKKLDQGLAAGDKEQTLLGATGTGKTFTMANVIR---DQNRP--TLVLAHNKTLAGQLYTELKKFFPNNA 89
Cdd:cd18032     5 QQEAIEALEEAREKGQRRALLVMATGTGKTYTAAFLIKrllEANRKkrILFLAHREELLEQAERSFKEVLPDGS 78
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
489-555 1.49e-06

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 47.97  E-value: 1.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1337947954 489 TRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDadkegFLRNPRSLIQTIGRAARNENGHVIM 555
Cdd:cd18802    80 KETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFD-----LPKTLRSYIQSRGRARAPNSKYILM 141
UvrC COG0322
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
629-665 3.47e-06

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


Pssm-ID: 440091 [Multi-domain]  Cd Length: 603  Bit Score: 50.12  E-value: 3.47e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1337947954 629 EQEQMIKNLSDEMREAAKQLDFEQAASLRDTIKKLKK 665
Cdd:COG0322   200 KTKELIKELEEKMEEAAEELEFERAARLRDQIRALEK 236
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
15-91 4.76e-06

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: 47.41  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  15 YKPTGDQPSAIKKLDQGLAAGDKEQTLL-GATGTGKTFTM---ANVIRDQNRPTLVLAHNKTLAGQLYTELKKFFPNNAV 90
Cdd:cd17918    14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLsGDVGSGKTLVAlgaALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93

                  .
gi 1337947954  91 E 91
Cdd:cd17918    94 E 94
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
44-93 5.64e-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: 5.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1337947954  44 ATGTGKTFTMANVIRD-QNRPTLVLAHNKTLAGQLYTELKKFFPNNAVEYF 93
Cdd:cd17926    26 PTGSGKTLTALALIAYlKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLI 76
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
460-575 6.24e-06

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 46.88  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 460 KMSEDLTDYLKDLgiKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFlrnpRSLI 539
Cdd:cd18792    49 ALAEELKELVPEA--RVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGL----SQLH 122
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1337947954 540 QTIGRAARnenGHVIMYADRVTDSmQAAMDETTRRR 575
Cdd:cd18792   123 QLRGRVGR---GKHQSYCYLLYPD-PKKLTETAKKR 154
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
487-555 7.92e-06

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 46.19  E-value: 7.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337947954 487 ERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKegflrNPRSLIQTIGRAARNENGHVIM 555
Cdd:cd18801    78 EQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASP-----SPIRMIQRMGRTGRKRQGRVVV 141
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
432-549 8.93e-06

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: 46.18  E-value: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 432 KDQMDDLVGEinERIKKKQRTFVTTLTK-------KMSEDLTDYLKDL---GIKVRYLHSDIKTLERTRIIRDLRLGKFD 501
Cdd:cd18811    12 LDKVYEFVRE--EIAKGRQAYVIYPLIEesekldlKAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVD 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1337947954 502 VLVGINLLREGIDVPEVSLVAILDADKEGFlrnpRSLIQTIGRAARNE 549
Cdd:cd18811    90 ILVSTTVIEVGVDVPNATVMVIEDAERFGL----SQLHQLRGRVGRGD 133
PTZ00424 PTZ00424
helicase 45; Provisional
451-547 9.15e-06

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 48.67  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 451 RTFVTTLTKKMSE-DLTdylkdlgikVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKe 529
Cdd:PTZ00424  277 RRKVDYLTKKMHErDFT---------VSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA- 346
                          90
                  ....*....|....*...
gi 1337947954 530 gflrNPRSLIQTIGRAAR 547
Cdd:PTZ00424  347 ----SPENYIHRIGRSGR 360
PRK05580 PRK05580
primosome assembly protein PriA; Validated
490-554 1.32e-05

primosome assembly protein PriA; Validated


Pssm-ID: 235514 [Multi-domain]  Cd Length: 679  Bit Score: 48.23  E-value: 1.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337947954 490 RIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADkeGFLRNP--RS-------LIQTIGRAAR-NENGHVI 554
Cdd:PRK05580  471 QLLAQFARGEADILIGTQMLAKGHDFPNVTLVGVLDAD--LGLFSPdfRAsertfqlLTQVAGRAGRaEKPGEVL 543
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
39-78 1.48e-05

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: 43.66  E-value: 1.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1337947954  39 QTLLGATGTGKTFTMANVIRDQN---RPTLVLAHNKTLAGQLY 78
Cdd:cd17912     2 ILHLGPTGSGKTLVAIQKIASAMssgKSVLVVTPTKLLAHEIL 44
PRK11192 PRK11192
ATP-dependent RNA helicase SrmB; Provisional
450-547 6.84e-05

ATP-dependent RNA helicase SrmB; Provisional


Pssm-ID: 236877 [Multi-domain]  Cd Length: 434  Bit Score: 45.70  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 450 QRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDAdke 529
Cdd:PRK11192  246 TRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDM--- 322
                          90       100
                  ....*....|....*....|.
gi 1337947954 530 gflrnPRS---LIQTIGRAAR 547
Cdd:PRK11192  323 -----PRSadtYLHRIGRTGR 338
SF2_C_TRCF cd18810
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ...
463-575 1.40e-04

C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350197 [Multi-domain]  Cd Length: 151  Bit Score: 42.72  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 463 EDLTDYLKDL--GIKVRYLHSDIKTLERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRnprsLIQ 540
Cdd:cd18810    39 EKLATQLRQLvpEARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQ----LYQ 114
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1337947954 541 TIGRAARnenGHVIMYADRVTDSmQAAMDETTRRR 575
Cdd:cd18810   115 LRGRVGR---SKERAYAYFLYPD-QKKLTEDALKR 145
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
490-554 1.54e-04

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


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 45.11  E-value: 1.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337947954 490 RIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNPRS-------LIQTIGRAARNEN-GHVI 554
Cdd:COG1198   522 KLLEAFARGEADILVGTQMLAKGHDFPNVTLVGVLDADLGLNSPDFRAaertfqlLTQVAGRAGRAEKpGEVL 594
PRK13766 PRK13766
Hef nuclease; Provisional
437-648 2.44e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 44.48  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 437 DLVGEINErIKKKQRTFVTTLTKKMSEDLTDYLKDLGIK-VRYL-------------HSDIKTLERtriirdLRLGKFDV 502
Cdd:PRK13766  354 EIVKEQLG-KNPDSRIIVFTQYRDTAEKIVDLLEKEGIKaVRFVgqaskdgdkgmsqKEQIEILDK------FRAGEFNV 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 503 LVGINLLREGIDVPEVSLV--------AIldadkegflrnpRSlIQTIGRAARNENGHVIMYADRVTdsmqaaMDETTRR 574
Cdd:PRK13766  427 LVSTSVAEEGLDIPSVDLVifyepvpsEI------------RS-IQRKGRTGRQEEGRVVVLIAKGT------RDEAYYW 487
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337947954 575 rkiqIAYNKEHHItpKTIIKPISKAISAYKQDEDDKYNKKKPFAETDFEQMSYKEQEQMIKNLSDEMREAAKQL 648
Cdd:PRK13766  488 ----SSRRKEKKM--KEELKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKET 555
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
446-547 2.47e-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: 44.44  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 446 IKKKQRTFVTTLTKKMSEDLTDYLKD------LGIKVR-----YLHSdiktlERTRIIRDLRLGKFDVLVGINLLREGID 514
Cdd:COG1205   285 VREGLRTLVFTRSRRGAELLARYARRalrepdLADRVAayragYLPE-----ERREIERGLRSGELLGVVSTNALELGID 359
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1337947954 515 VPEVSLVaILDadkeGFLRNPRSLIQTIGRAAR 547
Cdd:COG1205   360 IGGLDAV-VLA----GYPGTRASFWQQAGRAGR 387
SF2_C_reverse_gyrase cd18798
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ...
463-561 2.60e-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: 42.29  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 463 EDLTDYLKDLGIKVR-YLHSDIKTLErtriirDLRLGKFDVLVGI----NLLREGIDVPEVSLVAIldadkegFLRNP-R 536
Cdd:cd18798    41 EELKEFLERHGIKAElALSSTEKNLE------KFEEGEIDVLIGVasyyGVLVRGIDLPERIKYAI-------FYGVPvT 107
                          90       100
                  ....*....|....*....|....*
gi 1337947954 537 SLIQTIGRAARnenghviMYADRVT 561
Cdd:cd18798   108 TYIQASGRTSR-------LYAGGLT 125
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
446-556 3.29e-04

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


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 41.47  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 446 IKKKQRTFVTTLTKKMSEDLTDYLKDLGIKVRYLHSDIKTL-------ERTRIIRDLRLGKFDVLVGINLLREGIDVPev 518
Cdd:cd18797    32 VRAGVKTIVFCRSRKLAELLLRYLKARLVEEGPLASKVASYragylaeDRREIEAELFNGELLGVVATNALELGIDIG-- 109
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1337947954 519 SLVAILDAdkeGFLRNPRSLIQTIGRAARNENGHVIMY 556
Cdd:cd18797   110 GLDAVVLA---GYPGSLASLWQQAGRAGRRGKDSLVIL 144
Cas3 COG1203
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ...
393-548 5.03e-04

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


Pssm-ID: 440816 [Multi-domain]  Cd Length: 535  Bit Score: 43.15  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 393 VIYMSATPGTYELENSSQVVEQIIRPTG--------LLDPTVEVRPTKDQMDDLVGEINERIKKKQRTFVTTLTKKMSED 464
Cdd:COG1203   302 VILMTATLPPLLREELLEAYELIPDEPEelpeyfraFVRKRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQE 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 465 LTDYLKDLG--IKVRYLHSDIKTLERTRIIRDLRL----GKFDVLV-------GINllregIDVPEV-SLVAILDadkeg 530
Cdd:COG1203   382 LYEALKEKLpdEEVYLLHSRFCPADRSEIEKEIKErlerGKPCILVstqvveaGVD-----IDFDVViRDLAPLD----- 451
                         170
                  ....*....|....*...
gi 1337947954 531 flrnprSLIQTIGRAARN 548
Cdd:COG1203   452 ------SLIQRAGRCNRH 463
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
420-551 2.35e-03

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: 39.17  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 420 GLLDPTVEVrPTKDQMDDLVGE-----INERIKKKQR---TFVTTLTKKMSEDLTDYLKDL------GIKVRYLHSDIKT 485
Cdd:cd18796     2 KKLDIKVIL-PVAPEIFPWAGEsgadaYAEVIFLLERhksTLVFTNTRSQAERLAQRLRELcpdrvpPDFIALHHGSLSR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337947954 486 LERTRIIRDLRLGKFDVLVGINLLREGIDVPEVSLVAILDAdkegflrnPRS---LIQTIGRAARNENG 551
Cdd:cd18796    81 ELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGS--------PKSvarLLQRLGRSGHRPGA 141
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
18-77 3.70e-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: 39.08  E-value: 3.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1337947954  18 TGDQPSAIKKLdqgLAAGDKEQTLLGATGTGKTFTM---ANVIRDQNRPTLVLAHNKTLAGQL 77
Cdd:pfam13604   3 NAEQAAAVRAL---LTSGDRVAVLVGPAGTGKTTALkalREAWEAAGYRVIGLAPTGRAAKVL 62
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
43-177 4.32e-03

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It belongs to 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 39.10  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954  43 GATGTGKTFTMA----NVIRDQNRPTLVLAHNKTlAGQLYTElkkffpnnavEYFVSYYDYYQPEAyVPSSDTYIEKDAS 118
Cdd:cd18076    30 GPFGTGKTFTLAmaalEVIREPGTKVLICTHTNS-AADIYIR----------EYFHPYVDKGHPEA-RPLRIKATDRPNA 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 119 INDEIDQ-----------LRHaATSALLSRNDVIVVASVSSiFGLGSPKEYQDHTVTLHVGEEMERDVLL 177
Cdd:cd18076    98 ITDPDTItyccltkdrqcFRL-PTRDELDFHNIVITTTAMA-FNLHVLSGFFTHIFIDEAAQMLECEALI 165
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
433-527 4.63e-03

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


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 40.03  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337947954 433 DQMDDLVGEINERIKKKQRTFV-------------TTLTKkMSEDLTDYLKDLgiKVRYLHSDIKTLERTRIIRDLRLGK 499
Cdd:COG1200   453 ERRDEVYERIREEIAKGRQAYVvcplieesekldlQAAEE-TYEELREAFPGL--RVGLLHGRMKPAEKDAVMAAFKAGE 529
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1337947954 500 FDVLVG---InllrE-GIDVPEVSLVAILDAD 527
Cdd:COG1200   530 IDVLVAttvI----EvGVDVPNATVMVIENAE 557
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH