|
Name |
Accession |
Description |
Interval |
E-value |
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
1-347 |
1.24e-84 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 265.38 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 1 MDMDFEACRRAFVTRDARFDGRVFAGVKTTGIYCRPICPARTPKAENMTFFPTAAAAQEAGFRPCLRCRPEASPdlgAWR 80
Cdd:COG2169 4 DLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAP---GSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 81 GTSNTVSRALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQeTRLPMAEVALASG 160
Cdd:COG2169 81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 161 FGSVRRFNETFQALFGRPPGQLRRLsgeasaaaaGVTVRLAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGA 240
Cdd:COG2169 160 FGSLSRFYEAFKKLLGMTPSAYRRG---------GAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 241 TGVVVVTPGDGDFLIAEIRFPKLQALPAVI-ARIRRVFDLTADPGLIGAHLSQDPELAPLIAARPGLRAPGAWDGFEMAV 319
Cdd:COG2169 231 FPAAELIGGDAAFEQLVAEVVGFVEGPLLGlDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAA 310
|
330 340
....*....|....*....|....*...
gi 1620919193 320 RAILGQQITVTAARNLAAKLVATYGEPI 347
Cdd:COG2169 311 CAANQLAVAIPCHRVVRADGALSGYRWG 338
|
|
| PRK10308 |
PRK10308 |
3-methyl-adenine DNA glycosylase II; Provisional |
200-489 |
3.56e-63 |
|
3-methyl-adenine DNA glycosylase II; Provisional
Pssm-ID: 236671 [Multi-domain] Cd Length: 283 Bit Score: 207.30 E-value: 3.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 200 LAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTPGDGDFLIAEIRFPKLQAL-PAVIARIRRVFD 278
Cdd:PRK10308 4 LNWQPPYDWSWMLGFLAARAVSGVETVAEGYYARSLAVGEHRGVVTVIPDIARHTLHINLSAGLEPVaAECLAKMSRLFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 279 LTADPGLIGAhlsqdpELAPLIAARPGLRAPGAWDGFEMAVRAILGQQITVTAARNLAAKLVATYGEPIND-PSAVklgl 357
Cdd:PRK10308 84 LQCNPQIVNG------ALGKLGAARPGLRLPGSVDAFEQGVRAILGQLVSVAMAAKLTAKVAQLYGERLDDfPEYV---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 358 thVFPTPERLVGQD---IAALGMPRARGASIEALARTVAADPTIFTPRADLESAIKALSALPGIGAWTAQYIALRELREP 434
Cdd:PRK10308 154 --CFPTPERLAAADpqaLKALGMPLKRAEALIHLANAALEGTLPLTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1620919193 435 DAFPHADIGLLRAMAGAdgvrpTPDQLLARSQAWRPWRAYAAQHLWAADPAAPDL 489
Cdd:PRK10308 232 DVFLPDDYLIKQRFPGM-----TPAQIRRYAERWKPWRSYALLHIWYTEGWQPDE 281
|
|
| AlkA_N |
pfam06029 |
AlkA N-terminal domain; |
197-313 |
2.89e-41 |
|
AlkA N-terminal domain;
Pssm-ID: 428728 [Multi-domain] Cd Length: 118 Bit Score: 143.89 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 197 TVRLAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTPG-DGDFLIAEIRFPKLQALPAVIARIRR 275
Cdd:pfam06029 1 TLRLPYRPPYDWAALLAFLAARAIPGVEWVDDGAYRRTLRLGGGTGWVEVRHDpDRHALRVRLSLSLLRALPPLIARVRR 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1620919193 276 VFDLTADPGLIGAHLSQDPELAPLIAARPGLRAPGAWD 313
Cdd:pfam06029 81 LFDLDADPAAIAAHLAADPLLAPLVAARPGLRVPGAWD 118
|
|
| AlkA_N |
smart01009 |
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA ... |
202-313 |
2.53e-39 |
|
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA (3-methyladenine-DNA glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA flips a 1-azaribose abasic nucleotide out of DNA. This produces a 66 degrees bend in the DNA and a marked widening of the minor groove.
Pssm-ID: 214972 [Multi-domain] Cd Length: 113 Bit Score: 138.48 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 202 YRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTP-GDGDFLIAEIRFPKLQALPAVIARIRRVFDLT 280
Cdd:smart01009 1 YRPPYDWAALLAFLAARAVPGVERVDDGSYRRTLRLGGGAGWVTVRHdPDRHQLRVTLSLSDLRDLPALIARVRRLLDLD 80
|
90 100 110
....*....|....*....|....*....|...
gi 1620919193 281 ADPGLIGAHLSQDPELAPLIAARPGLRAPGAWD 313
Cdd:smart01009 81 ADPEAIDAHLAADPLLGPLVAARPGLRVPGAVD 113
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
315-480 |
1.40e-19 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 85.37 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 315 FEMAVRAILGQQITVTAARNLAAKLVATYGepindpsavklglthvfPTPERLVG---QDIAALGMP---RARGASIEAL 388
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYG-----------------PTPEALAAadeEELRELIRSlgyRRKAKYLKEL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 389 ARTVAADPtiFTPRADLESAIKALSALPGIGAWTAQYIALRELRePDAFPhADIGLLRAMA--GADGVRPTPDQLLARSQ 466
Cdd:cd00056 64 ARAIVEGF--GGLVLDDPDAREELLALPGVGRKTANVVLLFALG-PDAFP-VDTHVRRVLKrlGLIPKKKTPEELEELLE 139
|
170
....*....|....*.
gi 1620919193 467 AWRP--WRAYAAQHLW 480
Cdd:cd00056 140 ELLPkpYWGEANQALM 155
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
323-480 |
3.21e-14 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 69.99 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 323 LGQQITVTAARNLAAKLVATYGEPiNDPSAVklglthvfptPERLVGQDIAALGMPRARGASIEALARTVAADPTiftpr 402
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTP-EDLAAA----------DEEELEELIRGLGFYRRKARYLIELARILVEEYG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 403 ADLESAIKALSALPGIGAWTAQYIALRELREPdaFPHADIGLLRAMA--GADGVRPTPDQLLARSQAWRP---WRAYAAQ 477
Cdd:smart00478 65 GEVPDDREELLKLPGVGRKTANAVLSFALGKP--FIPVDTHVLRIAKrlGLVDKKSTPEEVEKLLEKLLPeedWRELNLL 142
|
...
gi 1620919193 478 HLW 480
Cdd:smart00478 143 LID 145
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
319-472 |
5.22e-12 |
|
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.
Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 63.46 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 319 VRAILGQQITVTAARNLAAKLVATygepindpsavklglthVFPTPERL-------VGQDIAALGMPRARGASIEALART 391
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEK-----------------FFPTPEDLadadeeeLRELIRGLGFYRRKAKYLKELARI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 392 VAADPTIFTPRADLESaikaLSALPGIGAWTAQYIALRELREPDAFPHADIGLLRAMAGADGVRPTPDQLLARSQAWRPW 471
Cdd:pfam00730 64 LVEGYGGEVPLDEEEL----EALLKGVGRWTAEAVLIFALGRPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELW 139
|
.
gi 1620919193 472 R 472
Cdd:pfam00730 140 P 140
|
|
| ogg |
TIGR00588 |
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ... |
271-483 |
4.83e-07 |
|
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 51.45 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 271 ARIRRVFDLTADPGLIGAH-LSQDPELAPLIAARPGLRAPGAwDGFEMAVRAILGQQITVTAARNLAAKLVATYGEPIND 349
Cdd:TIGR00588 76 TKLEKYFQLDVSLAQLYTHwGSVDKHFQYVAQKFQGVRLLRQ-DPFECLISFICSSNNNIARITRMVERLCQAFGPRLIT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 350 PSAVKLgltHVFPTPERLVGQ----DIAALGMP-RARgaSIEALARTVAADPTIFTPR-----ADLESAIKALSALPGIG 419
Cdd:TIGR00588 155 LDGVTY---HGFPSLHALTGPeaeaHLRKLGLGyRAR--YIRETARALLEEQGGRAWLqqirgASYEDAREALCELPGVG 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1620919193 420 AWTAQYIALRELREPDAFPhADIGLLRAMAGADGVRPTPDQLLARS------------QAWRPWRAYAAQHLWAAD 483
Cdd:TIGR00588 230 PKVADCICLMGLDKPQAVP-VDVHVWRIANRDYPWHPKTSRAKGPSpfarkelgnffrSLWGPYAGWAQAVLFSAD 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
1-347 |
1.24e-84 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 265.38 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 1 MDMDFEACRRAFVTRDARFDGRVFAGVKTTGIYCRPICPARTPKAENMTFFPTAAAAQEAGFRPCLRCRPEASPdlgAWR 80
Cdd:COG2169 4 DLLDDDERWQAVLARDARFDGRFFYGVKTTGIYCRPSCPARKPKRENVRFFATAAAAEAAGFRPCKRCRPDLAP---GSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 81 GTSNTVSRALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQeTRLPMAEVALASG 160
Cdd:COG2169 81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 161 FGSVRRFNETFQALFGRPPGQLRRLsgeasaaaaGVTVRLAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGA 240
Cdd:COG2169 160 FGSLSRFYEAFKKLLGMTPSAYRRG---------GAGAAIRFAPTPCSLGLLLVAASARGVCAILLGDDPEALLRDLQDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 241 TGVVVVTPGDGDFLIAEIRFPKLQALPAVI-ARIRRVFDLTADPGLIGAHLSQDPELAPLIAARPGLRAPGAWDGFEMAV 319
Cdd:COG2169 231 FPAAELIGGDAAFEQLVAEVVGFVEGPLLGlDLPLDLRGTAFQQRVWQALRAIPAGETASYAEIAARIGAPKAVRAVAAA 310
|
330 340
....*....|....*....|....*...
gi 1620919193 320 RAILGQQITVTAARNLAAKLVATYGEPI 347
Cdd:COG2169 311 CAANQLAVAIPCHRVVRADGALSGYRWG 338
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
205-482 |
3.12e-70 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 224.38 E-value: 3.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 205 PYDWAAIIGfltaraipgveivsARRYARTlsvDGATGVVVVTPGDGDFLIAeirfpklqaLPAVIARIRRVFDLTADPG 284
Cdd:COG0122 1 PFDLDATLD--------------DGTWRRL---PDGPGVVRMRPGGDALEVE---------LAEAVARLRRLLDLDDDLE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 285 LIGAHLSQDPELAPLIAARPGLRAPGAWDGFEMAVRAILGQQITVTAARNLAAKLVATYGEPINDPSavklGLTHVFPTP 364
Cdd:COG0122 55 AIAALAARDPVLAPLIERYPGLRLPRRPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEPIEGPG----GGLYAFPTP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 365 ERLVG---QDIAALGMPRARGASIEALARTVAADPTIF--TPRADLESAIKALSALPGIGAWTAQYIALRELREPDAFPH 439
Cdd:COG0122 131 EALAAaseEELRACGLSRRKARYLRALARAVADGELDLeaLAGLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAFPA 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1620919193 440 ADIGLLRAMAGA--DGVRPTPDQLLARSQAWRPWRAYAAQHLWAA 482
Cdd:COG0122 211 GDLGLRRALGRLygLGERPTPKELRELAEPWRPYRSYAARYLWRS 255
|
|
| PRK10308 |
PRK10308 |
3-methyl-adenine DNA glycosylase II; Provisional |
200-489 |
3.56e-63 |
|
3-methyl-adenine DNA glycosylase II; Provisional
Pssm-ID: 236671 [Multi-domain] Cd Length: 283 Bit Score: 207.30 E-value: 3.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 200 LAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTPGDGDFLIAEIRFPKLQAL-PAVIARIRRVFD 278
Cdd:PRK10308 4 LNWQPPYDWSWMLGFLAARAVSGVETVAEGYYARSLAVGEHRGVVTVIPDIARHTLHINLSAGLEPVaAECLAKMSRLFD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 279 LTADPGLIGAhlsqdpELAPLIAARPGLRAPGAWDGFEMAVRAILGQQITVTAARNLAAKLVATYGEPIND-PSAVklgl 357
Cdd:PRK10308 84 LQCNPQIVNG------ALGKLGAARPGLRLPGSVDAFEQGVRAILGQLVSVAMAAKLTAKVAQLYGERLDDfPEYV---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 358 thVFPTPERLVGQD---IAALGMPRARGASIEALARTVAADPTIFTPRADLESAIKALSALPGIGAWTAQYIALRELREP 434
Cdd:PRK10308 154 --CFPTPERLAAADpqaLKALGMPLKRAEALIHLANAALEGTLPLTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1620919193 435 DAFPHADIGLLRAMAGAdgvrpTPDQLLARSQAWRPWRAYAAQHLWAADPAAPDL 489
Cdd:PRK10308 232 DVFLPDDYLIKQRFPGM-----TPAQIRRYAERWKPWRSYALLHIWYTEGWQPDE 281
|
|
| AlkA_N |
pfam06029 |
AlkA N-terminal domain; |
197-313 |
2.89e-41 |
|
AlkA N-terminal domain;
Pssm-ID: 428728 [Multi-domain] Cd Length: 118 Bit Score: 143.89 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 197 TVRLAYRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTPG-DGDFLIAEIRFPKLQALPAVIARIRR 275
Cdd:pfam06029 1 TLRLPYRPPYDWAALLAFLAARAIPGVEWVDDGAYRRTLRLGGGTGWVEVRHDpDRHALRVRLSLSLLRALPPLIARVRR 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1620919193 276 VFDLTADPGLIGAHLSQDPELAPLIAARPGLRAPGAWD 313
Cdd:pfam06029 81 LFDLDADPAAIAAHLAADPLLAPLVAARPGLRVPGAWD 118
|
|
| AlkA_N |
smart01009 |
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA ... |
202-313 |
2.53e-39 |
|
AlkA N-terminal domain; This domain is found at the N terminus of bacterial AlkA . AlkA (3-methyladenine-DNA glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA flips a 1-azaribose abasic nucleotide out of DNA. This produces a 66 degrees bend in the DNA and a marked widening of the minor groove.
Pssm-ID: 214972 [Multi-domain] Cd Length: 113 Bit Score: 138.48 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 202 YRAPYDWAAIIGFLTARAIPGVEIVSARRYARTLSVDGATGVVVVTP-GDGDFLIAEIRFPKLQALPAVIARIRRVFDLT 280
Cdd:smart01009 1 YRPPYDWAALLAFLAARAVPGVERVDDGSYRRTLRLGGGAGWVTVRHdPDRHQLRVTLSLSDLRDLPALIARVRRLLDLD 80
|
90 100 110
....*....|....*....|....*....|...
gi 1620919193 281 ADPGLIGAHLSQDPELAPLIAARPGLRAPGAWD 313
Cdd:smart01009 81 ADPEAIDAHLAADPLLGPLVAARPGLRVPGAVD 113
|
|
| Ada_Zn_binding |
pfam02805 |
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine ... |
7-68 |
6.94e-33 |
|
Metal binding domain of Ada; The Escherichia coli Ada protein repairs O6-methylguanine residues and methyl phosphotriesters in DNA by direct transfer of the methyl group to a cysteine residue. This domain contains four conserved cysteines that form a zinc binding site. One of these cysteines is a methyl group acceptor. The methylated domain can then specifically bind to the ada box on a DNA duplex.
Pssm-ID: 460701 [Multi-domain] Cd Length: 62 Bit Score: 119.09 E-value: 6.94e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1620919193 7 ACRRAFVTRDARFDGRVFAGVKTTGIYCRPICPARTPKAENMTFFPTAAAAQEAGFRPCLRC 68
Cdd:pfam02805 1 ARWQAVLARDPRADGSFFYAVKTTGIYCRPSCPARLPKRENVRFFDTAAEAEAAGFRPCKRC 62
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
106-184 |
8.23e-22 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 89.19 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 106 LAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQ-LIQETRLPMAEVALASGFGSVRRFNETFQALFGRPPGQLRR 184
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRlLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
102-183 |
6.51e-21 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 86.84 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 102 DVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPMAEVALASGFGSVRRFNETFQALFGRPPGQ 181
Cdd:smart00342 3 TLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSE 82
|
..
gi 1620919193 182 LR 183
Cdd:smart00342 83 YR 84
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
73-184 |
9.06e-20 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 89.83 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 73 SPDLGAWRGTSNTVSRALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPM 152
Cdd:COG4977 199 SPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSI 278
|
90 100 110
....*....|....*....|....*....|..
gi 1620919193 153 AEVALASGFGSVRRFNETFQALFGRPPGQLRR 184
Cdd:COG4977 279 EEIAAACGFGSASHFRRAFRRRFGVSPSAYRR 310
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
315-480 |
1.40e-19 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 85.37 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 315 FEMAVRAILGQQITVTAARNLAAKLVATYGepindpsavklglthvfPTPERLVG---QDIAALGMP---RARGASIEAL 388
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYG-----------------PTPEALAAadeEELRELIRSlgyRRKAKYLKEL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 389 ARTVAADPtiFTPRADLESAIKALSALPGIGAWTAQYIALRELRePDAFPhADIGLLRAMA--GADGVRPTPDQLLARSQ 466
Cdd:cd00056 64 ARAIVEGF--GGLVLDDPDAREELLALPGVGRKTANVVLLFALG-PDAFP-VDTHVRRVLKrlGLIPKKKTPEELEELLE 139
|
170
....*....|....*.
gi 1620919193 467 AWRP--WRAYAAQHLW 480
Cdd:cd00056 140 ELLPkpYWGEANQALM 155
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
88-184 |
2.49e-17 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 81.75 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 88 RALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPMAEVALASGFGSVRRF 167
Cdd:COG2207 156 LLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHF 235
|
90
....*....|....*..
gi 1620919193 168 NETFQALFGRPPGQLRR 184
Cdd:COG2207 236 SRAFKKRFGVTPSEYRK 252
|
|
| PRK15435 |
PRK15435 |
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada; |
6-277 |
6.12e-17 |
|
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
Pssm-ID: 185333 [Multi-domain] Cd Length: 353 Bit Score: 82.15 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 6 EACRRAFVTRDARFDGRVFAGVKTTGIYCRPICPARTPKAENMTFFPTAAAAQEAGFRPCLRCRPEaspDLGAWRGTSNT 85
Cdd:PRK15435 10 DQRWQSVLARDPNADGEFVFAVRTTGIFCRPSCRARHALRENVRFYANASEALAAGFRPCKRCQPD---KANPQQHRLDK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 86 VSRALALIEAGAldGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRvllAKQLIQETR--LPMAEVALASGFGS 163
Cdd:PRK15435 87 ITHACRLLEQET--PVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWR---ARRLREALAkgESVTTSILNAGFPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 164 VRRFNETFQALFGRPPGQLRRlSGEAsaaaagVTVRLAYRapyDWAaiigfltaraipgveivsarrYARTLSVDGATGV 243
Cdd:PRK15435 162 SSSYYRKADETLGMTAKQFRH-GGEN------LAVRYALA---DCE---------------------LGRCLVAESERGI 210
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1620919193 244 VVVTPGDGD-FLIAEIR--FPKLQALPA---VIARIRRVF 277
Cdd:PRK15435 211 CAILLGDDDaALISELQqmFPAADNAPAdltFQQHVREVI 250
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
323-480 |
3.21e-14 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 69.99 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 323 LGQQITVTAARNLAAKLVATYGEPiNDPSAVklglthvfptPERLVGQDIAALGMPRARGASIEALARTVAADPTiftpr 402
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTP-EDLAAA----------DEEELEELIRGLGFYRRKARYLIELARILVEEYG----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 403 ADLESAIKALSALPGIGAWTAQYIALRELREPdaFPHADIGLLRAMA--GADGVRPTPDQLLARSQAWRP---WRAYAAQ 477
Cdd:smart00478 65 GEVPDDREELLKLPGVGRKTANAVLSFALGKP--FIPVDTHVLRIAKrlGLVDKKSTPEEVEKLLEKLLPeedWRELNLL 142
|
...
gi 1620919193 478 HLW 480
Cdd:smart00478 143 LID 145
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
319-472 |
5.22e-12 |
|
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.
Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 63.46 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 319 VRAILGQQITVTAARNLAAKLVATygepindpsavklglthVFPTPERL-------VGQDIAALGMPRARGASIEALART 391
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEK-----------------FFPTPEDLadadeeeLRELIRGLGFYRRKAKYLKELARI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 392 VAADPTIFTPRADLESaikaLSALPGIGAWTAQYIALRELREPDAFPHADIGLLRAMAGADGVRPTPDQLLARSQAWRPW 471
Cdd:pfam00730 64 LVEGYGGEVPLDEEEL----EALLKGVGRWTAEAVLIFALGRPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELW 139
|
.
gi 1620919193 472 R 472
Cdd:pfam00730 140 P 140
|
|
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
103-187 |
3.08e-10 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 61.52 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 103 VDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPMAEVALASGFGSVRRFNETFQALFGRPPGQL 182
Cdd:PRK09393 237 VASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAY 316
|
....*
gi 1620919193 183 RRLSG 187
Cdd:PRK09393 317 RKRFG 321
|
|
| ogg |
TIGR00588 |
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ... |
271-483 |
4.83e-07 |
|
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 211589 [Multi-domain] Cd Length: 310 Bit Score: 51.45 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 271 ARIRRVFDLTADPGLIGAH-LSQDPELAPLIAARPGLRAPGAwDGFEMAVRAILGQQITVTAARNLAAKLVATYGEPIND 349
Cdd:TIGR00588 76 TKLEKYFQLDVSLAQLYTHwGSVDKHFQYVAQKFQGVRLLRQ-DPFECLISFICSSNNNIARITRMVERLCQAFGPRLIT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 350 PSAVKLgltHVFPTPERLVGQ----DIAALGMP-RARgaSIEALARTVAADPTIFTPR-----ADLESAIKALSALPGIG 419
Cdd:TIGR00588 155 LDGVTY---HGFPSLHALTGPeaeaHLRKLGLGyRAR--YIRETARALLEEQGGRAWLqqirgASYEDAREALCELPGVG 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1620919193 420 AWTAQYIALRELREPDAFPhADIGLLRAMAGADGVRPTPDQLLARS------------QAWRPWRAYAAQHLWAAD 483
Cdd:TIGR00588 230 PKVADCICLMGLDKPQAVP-VDVHVWRIANRDYPWHPKTSRAKGPSpfarkelgnffrSLWGPYAGWAQAVLFSAD 304
|
|
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
114-188 |
3.29e-05 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 45.82 E-value: 3.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1620919193 114 ERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPMAEVALASGFGSVRRFNETFQALFGRPPGQLRRLSGE 188
Cdd:PRK13502 206 ERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQ 280
|
|
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
60-195 |
4.41e-05 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 45.58 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 60 AGFRPCLRCRPEASPDLGAWRGTSNTVSRALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGaapITVAQ---TR 136
Cdd:PRK10371 167 SGWEPILVNKTSRTHKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQ---LTMKQyitAM 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1620919193 137 RVLLAKQLIQETRLPMAEVALASGFGSVRRFNETFQALFGRPPGQLRRLSGEASAAAAG 195
Cdd:PRK10371 244 RINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQRRQTFPG 302
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
102-188 |
6.27e-05 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 44.96 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 102 DVDGLAARLGVGERQLRRLFRQHLGaapITVAQTR---RVLLAKQLIQETRLPMAEVALASGFGSVRRFNETFQALFGRP 178
Cdd:PRK10572 201 DIESVAQHVCLSPSRLAHLFRQQLG---ISVLRWRedqRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGAS 277
|
90
....*....|
gi 1620919193 179 PGQLRRLSGE 188
Cdd:PRK10572 278 PSEFRARCEE 287
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
85-188 |
4.20e-04 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 40.47 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1620919193 85 TVSRALALIEAGALDGGDVDGLAARLGVGERQLRRLFRQHLGAAPITVAQTRRVLLAKQLIQETRLPMAEVALASGFGSV 164
Cdd:PRK11511 10 TIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQ 89
|
90 100
....*....|....*....|....*.
gi 1620919193 165 RRFNETFQALFGRPPGQLR--RLSGE 188
Cdd:PRK11511 90 QTLTRTFKNYFDVPPHKYRmtNMQGE 115
|
|
| |
