|
Name |
Accession |
Description |
Interval |
E-value |
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-670 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1256.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 1 MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPML 80
Cdd:PRK07956 2 MEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 81 SLDNVFDEESFLAFNKRVQDRLKSNEkVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLH 160
Cdd:PRK07956 82 SLDNAFSEEELRAFDKRVRKRLPDPP-LTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 161 gENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHL 240
Cdd:PRK07956 161 -GNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 241 GRLMQFKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQ 320
Cdd:PRK07956 240 EALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 321 MTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTR 400
Cdd:PRK07956 320 TTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 401 EVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAG 480
Cdd:PRK07956 400 EIVMPTHCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 481 KLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHV 560
Cdd:PRK07956 480 DLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 561 HNFFAEESNRNVISELLAEGVHWPEpivinaEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVI 640
Cdd:PRK07956 560 VEFFAVEENRELIDELLEAGVNMEY------KGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVV 633
|
650 660 670
....*....|....*....|....*....|
gi 446365854 641 AGEAAGSKLAKAQELGIEVIDETEMLRLLG 670
Cdd:PRK07956 634 AGEAAGSKLAKAQELGIEVLDEEEFLRLLG 663
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-670 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1241.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 1 MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPML 80
Cdd:COG0272 3 PEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 81 SLDNVFDEESFLAFNKRVQDRLKsNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLH 160
Cdd:COG0272 83 SLDNAFSEEELRDFDRRVRKFLG-DEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 161 GENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGgELPDTHL 240
Cdd:COG0272 162 GDDVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEG-LLPDTQS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 241 GRLMQFKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQ 320
Cdd:COG0272 241 EALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 321 MTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTR 400
Cdd:COG0272 321 TTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 401 EVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAG 480
Cdd:COG0272 401 PFVMPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 481 KLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHV 560
Cdd:COG0272 481 DLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 561 HNFFAEESNRNVISELLAEGVHWPEPIVinAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVI 640
Cdd:COG0272 561 VEFFAEPHNRELIERLRAAGVNMEEEEA--EAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVV 638
|
650 660 670
....*....|....*....|....*....|
gi 446365854 641 AGEAAGSKLAKAQELGIEVIDETEMLRLLG 670
Cdd:COG0272 639 AGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
11-665 |
0e+00 |
|
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent DNA ligases. Functions of these proteins include DNA repair, DNA replication, and DNA recombination. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The member of this family from Treponema pallidum differs in having three rather than just one copy of the BRCT (BRCA1 C Terminus) domain (pfam00533) at the C-terminus. It is included in the seed. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273148 [Multi-domain] Cd Length: 652 Bit Score: 1049.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 11 LRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEES 90
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 91 FLAFNKRVQDRLksNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEV 170
Cdd:TIGR00575 81 LAAFIKRIRRQL--GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 171 RGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGvlEGGELPD-THLGRLMQFKAW 249
Cdd:TIGR00575 159 RGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG--EGLELPDaTQYEALAWLKKW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 250 GLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEF 329
Cdd:TIGR00575 237 GFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 330 QVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCP 409
Cdd:TIGR00575 317 QVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 410 VCGSDVERVEGEAVARCTgGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMG 489
Cdd:TIGR00575 397 SCGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 490 PKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESN 569
Cdd:TIGR00575 476 EKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 570 RNVISELLAEGVHWP-EPIVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSK 648
Cdd:TIGR00575 556 RQLIKKLEELGVEMEsLPEKVNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSK 635
|
650
....*....|....*..
gi 446365854 649 LAKAQELGIEVIDETEM 665
Cdd:TIGR00575 636 LAKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
4-448 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 716.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 4 IEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLD 83
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 84 NVFDEESFLAFNKRVQDRLksNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGEn 163
Cdd:smart00532 81 NAFDEDELRAFDERIEKAL--GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 164 IPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRL 243
Cdd:smart00532 158 VPERLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 244 MQFKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTF 323
Cdd:smart00532 238 KWLKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 324 VRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVV 403
Cdd:smart00532 318 LLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446365854 404 FPTHCPVCGSDVERVEGEAVARCTGGLiCGAQRKESLKHFVSRRA 448
Cdd:smart00532 398 MPTHCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
2-669 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 667.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 2 ESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHpELITPDSPTQRVGAAPLAAFSQIRHEVPMLS 81
Cdd:PRK14351 30 DEAEEQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAPMLS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 82 LDNVFDEESFLAFNKRVQDRLKSnekVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHG 161
Cdd:PRK14351 109 IDQSGEADDVREFDERVRREVGA---VEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 162 EnIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVgvLEGGELPDTHLG 241
Cdd:PRK14351 186 D-YPDFLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDV--LDASELFDSHWE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 242 RLMQFKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQM 321
Cdd:PRK14351 263 ELERFPEWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 322 TFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVlSERPEDTRE 401
Cdd:PRK14351 343 TTIRDIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVV-EKDSEGTFE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 402 vvFPTHCPVCGSDVERvEGeAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGK 481
Cdd:PRK14351 422 --FPDTCPVCDSAVER-DG-PLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDLTVAD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 482 LTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVH 561
Cdd:PRK14351 498 LAELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEEIR 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 562 NFFAEESNRNVISELLAEGVHwPEPI-VINAEEIDspfaGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVI 640
Cdd:PRK14351 578 EFFDSERNRAVIDDLLDHGVD-PQPAeSEGGDALD----GLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLV 652
|
650 660 670
....*....|....*....|....*....|
gi 446365854 641 AGEAAG-SKLAKAQELGIEVIDETEMLRLL 669
Cdd:PRK14351 653 VGENPGqSKRDDAEANDVPTLDEEEFEELL 682
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
2-318 |
0e+00 |
|
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. This domain is the catalytic adenylation domain. The NAD+ group is covalently attached to this domain at the lysine in the KXDG motif of this domain. This enzyme- adenylate intermediate is an important feature of the proposed catalytic mechanism.
Pssm-ID: 396292 [Multi-domain] Cd Length: 318 Bit Score: 566.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 2 ESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLS 81
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 82 LDNVFDEESFLAFNKRVQDRLKSNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHG 161
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALGNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 162 ENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELP-DTHL 240
Cdd:pfam01653 161 DNPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGfDTQY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446365854 241 GRLMQFKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQ 318
Cdd:pfam01653 241 QALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
6-317 |
0e+00 |
|
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor, but using the same basic reaction mechanism. The enzyme reacts with the cofactor to form a phosphoamide-linked AMP with the amino group of a conserved Lysine in the KXDG motif, and subsequently transfers it to the DNA substrate to yield adenylated DNA. This alignment contains members of the NAD+ dependent subfamily only.
Pssm-ID: 238062 [Multi-domain] Cd Length: 307 Bit Score: 524.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 6 QQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNV 85
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 86 FDEESFLAFNKRVQDRLksNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGenIP 165
Cdd:cd00114 81 FDEEELRAFDERIKRFL--GEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG--AP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 166 ARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGElPDTHLGRLMQ 245
Cdd:cd00114 157 ETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALAF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446365854 246 FKAWGLPVSDRVTLCESAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPA 317
Cdd:cd00114 236 LKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
2-660 |
9.59e-116 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 361.45 E-value: 9.59e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 2 ESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLS 81
Cdd:PRK14350 3 KDIQDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPILS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 82 LDNVFD-EESFLAFNKRVQDRLKSNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLh 160
Cdd:PRK14350 83 LDKVYDlKLLKLWIEKMDLENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLFI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 161 GENIpaRLEVRGEVFLPQAGFEKINedarRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVgVLEGGELPDTHL 240
Cdd:PRK14350 162 DEKV--ELVLRGEIYITKENFLKIN----KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDI-LYSSLELKTNHD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 241 GrLMQFKAWGLPVSdrvTLCE------SAEEVLAFYHKVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFK 314
Cdd:PRK14350 235 A-FDKLKKFGFKVN---PFCRffdgknSIEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 315 FPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVlse 394
Cdd:PRK14350 311 FESLSGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVI--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 395 rpEDTREVVF--PTHCPVCGSDVERvEGeAVARCTGGLiCGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPA 472
Cdd:PRK14350 388 --EKLSVGFFkiPDNCPSCKTALIK-EG-AHLFCVNNH-CPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEI 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 473 DLFKLTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGL----AAYFGTLEAL---EAASIEE 545
Cdd:PRK14350 463 DLYTFNFDRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLinnnLNSFDKISTLcqdREFALSK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 546 LQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPEPiVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELG 625
Cdd:PRK14350 543 LLKIKGIGEKIALNIIEAFNDKIILDKFNFFKNLGFKMEED-SINIDVENSFLFGKKFCITGSFNGYSRSVLIDKLTKKG 621
|
650 660 670
....*....|....*....|....*....|....*
gi 446365854 626 AKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI 660
Cdd:PRK14350 622 AIFNTCVTKYLDFLLVGEKAGLKLKKANNLGIKIM 656
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
4-582 |
4.30e-51 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 186.28 E-value: 4.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 4 IEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPtqrvgaaPLAAFSQIRHEVPMLSLD 83
Cdd:PRK08097 30 AQEEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVP-------LPPLNGKVLHPVAHTGVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 84 NVFDEESflafnkrVQDRLKSNEKVtWCcELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLhgEN 163
Cdd:PRK08097 103 KLADKQA-------LARWMAGRSDL-WV-QPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQL--PG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 164 IPARLEVRGEVFLPQagfekinEDAR--RTGGkvfANPRNAAAGSLRQLDPRITAKRpltffcYGVGVLEGGELPDTHLG 241
Cdd:PRK08097 172 ALANLVLQGELFLRR-------EGHIqqQMGG---INARAKVAGLMMRKDPSPTLNQ------IGVFVWAWPDGPASMPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 242 RLMQFKAWGLPVSDRVTL-CESAEEV----LAFYHKvekdrpTLGFDIDGVVIKVNSLAQQEQlgFVARAPRWAVAFKFP 316
Cdd:PRK08097 236 RLAQLATAGFPLTQRYTHpVKNAEEVarwrERWYRA------PLPFVTDGVVVRQAKEPPGRY--WQPGQGEWAVAWKYP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 317 AQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVL--SE 394
Cdd:PRK08097 308 PVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRVNIGSVRRWQQWDIAPGDQVLVSLAGQGIPRLDKVVWrgAE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 395 RPedtrEVVFPT----H---C----PVCgsdvervEGEAVARctgglicgaqrkesLKHFVSRRAMDVDGMGDKIIDQLV 463
Cdd:PRK08097 388 RT----KPTPPDadrfHslsCfrasPGC-------QEQFLAR--------------LVWLSGKQGLGLDGIGEGTWRALH 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 464 EKEYVhtpADLFK---LTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAyfgTLEALEA 540
Cdd:PRK08097 443 QTGLF---EHLFSwlaLTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIPLPQAALNALDDR---SWQQLLS 516
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 446365854 541 ASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVH 582
Cdd:PRK08097 517 RSEQQWQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQGIT 558
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
321-399 |
8.34e-43 |
|
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. This family is a small domain found after the adenylation domain pfam01653 in NAD dependent ligases. OB-fold domains generally are involved in nucleic acid binding.
Pssm-ID: 460813 [Multi-domain] Cd Length: 79 Bit Score: 148.67 E-value: 8.34e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446365854 321 MTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDT 399
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
598-668 |
4.17e-29 |
|
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349379 [Multi-domain] Cd Length: 76 Bit Score: 110.26 E-value: 4.17e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446365854 598 FAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLA-----KAQELGIEVIDETEMLRL 668
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
510-573 |
1.62e-23 |
|
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 432812 [Multi-domain] Cd Length: 64 Bit Score: 94.13 E-value: 1.62e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446365854 510 RFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVI 573
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
598-668 |
1.22e-18 |
|
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349383 [Multi-domain] Cd Length: 79 Bit Score: 80.72 E-value: 1.22e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446365854 598 FAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAG-SKLAKAQELGIEVIDETEMLRL 668
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDL 77
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
597-669 |
2.91e-14 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 68.17 E-value: 2.91e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446365854 597 PFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKK-TDLVIAGEAAGSKL--AKAQELGIEVIDETEMLRLL 669
Cdd:smart00292 3 LFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLelLKAIALGIPIVKEEWLLDCL 78
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
597-669 |
3.59e-14 |
|
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.
Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 67.70 E-value: 3.59e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446365854 597 PFAGKTVVLTGsLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAgEAAGSKLAKAQELGIEVIDETEMLRLL 669
Cdd:pfam00533 5 LFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV-EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
536-668 |
1.64e-10 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 62.88 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446365854 536 EALEAASIEELQKVpdVGIVVASHVHNFFA---------EESNRNVISEllaegvhwPEPIVINAEEIdsPFAGKTVVLT 606
Cdd:PRK06195 162 KELNSKDINEISKL--LGVTLGYVNENGYKpssrkgrilKRSNRQAPRK--------KKKIIESFGFT--AFKEEVVVFT 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446365854 607 GSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAG---------EAAGSKLAKAQEL-----GIEVIDETEMLRL 668
Cdd:PRK06195 230 GGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAIDLkkkgqNIKFLNEEEFLQK 305
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
598-662 |
3.22e-10 |
|
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.
Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 56.77 E-value: 3.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446365854 598 FAGKTVVLTGSLSqMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAA----GSKLAKAQELGIEVIDE 662
Cdd:cd17747 1 LTGMKFALIGKLS-KSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEvekmSKKMKEAKEAGVPVVSE 68
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
407-432 |
2.71e-09 |
|
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. This family is a small zinc binding motif that is presumably DNA binding. IT is found only in NAD dependent DNA ligases.
Pssm-ID: 460812 [Multi-domain] Cd Length: 26 Bit Score: 52.44 E-value: 2.71e-09
10 20
....*....|....*....|....*.
gi 446365854 407 HCPVCGSDVERVEGEAVARCTgGLIC 432
Cdd:pfam03119 1 HCPVCGSPLVREEGEAALRCT-NLSC 25
|
|
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
520-567 |
1.56e-06 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 51.27 E-value: 1.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446365854 520 VGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEE 567
Cdd:PRK00558 551 IGPKRRKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
520-567 |
9.74e-06 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 48.58 E-value: 9.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446365854 520 VGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEE 567
Cdd:COG0322 556 IGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
600-670 |
1.61e-05 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 47.39 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446365854 600 GKTVVLTGSLSQmSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAG--SKLAKAQELGIEVIDETEMLRLLG 670
Cdd:PRK06063 235 GMRVALSAEVSR-THEELVERILHAGLAYSDSVDRDTSLVVCNDPAPeqGKGYHARQLGVPVLDEAAFLELLR 306
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
501-557 |
6.96e-05 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 44.40 E-value: 6.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446365854 501 EKAKETTFARFLYAL-GIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVA 557
Cdd:COG1948 143 KKKPKTLREQQLYVVeSLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTA 200
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
511-557 |
1.29e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 40.16 E-value: 1.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446365854 511 FLYALGIREVGEATAAGLA-AYFGTLEALEAASIEELQKVPDVGIVVA 557
Cdd:pfam14520 1 FEELLSISGIGPKTALALLsAGIGTVEDLAEADVDELAEIPGIGEKTA 48
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
445-502 |
1.53e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 1.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446365854 445 SRRAMDVDGMGDKIIDQLVEKEYvHTPADLFKLTAGKLTGLERMGPKSAQNVVNALEK 502
Cdd:pfam14520 1 FEELLSISGIGPKTALALLSAGI-GTVEDLAEADVDELAEIPGIGEKTAQRIILELRD 57
|
|
| BRCT_PAXIP1_rpt4 |
cd17730 |
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
614-660 |
2.11e-04 |
|
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fourth BRCT domain.
Pssm-ID: 349362 [Multi-domain] Cd Length: 73 Bit Score: 39.92 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446365854 614 RDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI 660
Cdd:cd17730 13 REDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVV 59
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
602-660 |
3.89e-04 |
|
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.
Pssm-ID: 463687 [Multi-domain] Cd Length: 63 Bit Score: 39.11 E-value: 3.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446365854 602 TVVLTGsLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI 660
Cdd:pfam12738 2 VICVTG-FDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVV 59
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
534-563 |
6.63e-04 |
|
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 37.40 E-value: 6.63e-04
10 20 30
....*....|....*....|....*....|
gi 446365854 534 TLEALEAASIEELQKVPDVGIVVASHVHNF 563
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
602-662 |
1.87e-03 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 37.34 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446365854 602 TVVLTGsLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSK-LAKAQELGIEVIDE 662
Cdd:cd00027 2 VICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSP 62
|
|
| uvrC |
PRK14666 |
excinuclease ABC subunit C; Provisional |
520-561 |
2.06e-03 |
|
excinuclease ABC subunit C; Provisional
Pssm-ID: 237782 [Multi-domain] Cd Length: 694 Bit Score: 41.41 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446365854 520 VGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVH 561
Cdd:PRK14666 645 IGPATARLLWERFGSLQAMAAAGEEGLAAVPGIGPARAAALH 686
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
597-662 |
2.21e-03 |
|
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.
Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 37.13 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446365854 597 PFAGKTVVLTGsLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELG-IEVIDE 662
Cdd:cd17731 2 PFKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNsIHIVTP 67
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
501-557 |
4.38e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 40.24 E-value: 4.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446365854 501 EKAKETTFARFLYAL-GIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVA 557
Cdd:PRK13766 703 EKKAMTLKEQQEYIVeSLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTA 760
|
|
| PLN03122 |
PLN03122 |
Poly [ADP-ribose] polymerase; Provisional |
595-662 |
7.33e-03 |
|
Poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 39.78 E-value: 7.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446365854 595 DSPFAGKTVVLTGSLSQmSRDDAKARLVELGAKVAGSVSKKTDLVIAG---EAAGS-KLAKAQELGIEVIDE 662
Cdd:PLN03122 187 GKPFSGMMISLSGRLSR-THQYWKKDIEKHGGKVANSVEGVTCLVVSPaerERGGSsKIAEAMERGIPVVRE 257
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