|
Name |
Accession |
Description |
Interval |
E-value |
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-647 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1214.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:PRK07956 26 LDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPMLSLDNAFSEEELRAFDKRVRKRLPD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDaLTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQgDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:PRK07956 106 PP-LTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH-GNEPERLEVRGEVFMPKADFEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:PRK07956 184 NEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQSEALEFLKAWGFPVNPYRKLCTSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:PRK07956 264 EVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEATTKLLDIEVQVGRTGAVTPVARLE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:PRK07956 344 PVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDEREIVMPTHCPVCGSELVRVEGEAVL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 401 RCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAAK 480
Cdd:PRK07956 424 RCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAEDLLGLEGFGEKSAQNLLDAIEKSK 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 481 ETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKWP 560
Cdd:PRK07956 504 ETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIVEFFAVEENRELIDELLEAGVNME 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 561 apvvvnAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAE 640
Cdd:PRK07956 584 ------YKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAGSKLAKAQELGIEVLDEEE 657
|
....*..
gi 555207888 641 MMRLLGE 647
Cdd:PRK07956 658 FLRLLGE 664
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-646 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1199.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:COG0272 27 LDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPMLSLDNAFSEEELRDFDRRVRKFLGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 sDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:COG0272 107 -EPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRLKGDDVPEVLEVRGEVYMPKADFEAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGgELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:COG0272 186 NEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEG-LLPDTQSEALELLKEWGFPVNPERRVCKSIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:COG0272 265 EVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEATTKLLDIEVQVGRTGALTPVARLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:COG0272 345 PVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEKPFVMPTHCPVCGSPLVREEGEAAL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 401 RCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAAK 480
Cdd:COG0272 425 RCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKEDLLGLERMGEKSAQNLLAAIEKSK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 481 ETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKWP 560
Cdd:COG0272 505 KTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESIVEFFAEPHNRELIERLRAAGVNME 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 561 APVVvnAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAE 640
Cdd:COG0272 585 EEEA--EAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAGSKLDKAEELGVPILDEAE 662
|
....*.
gi 555207888 641 MMRLLG 646
Cdd:COG0272 663 FLELLG 668
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
1-641 |
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: 1012.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLks 80
Cdd:TIGR00575 15 LDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDELAAFIKRIRRQL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:TIGR00575 93 GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERLEVRGEVFMPKEDFEAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGilEGGELPD-THLGRLLQFKAWGLPVSNRVQLCDSP 239
Cdd:TIGR00575 173 NEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG--EGLELPDaTQYEALAWLKKWGFPVSPHIRLCDSI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 240 EAVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARL 319
Cdd:TIGR00575 251 EEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQVGRTGAITPVAKL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 320 EPVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAV 399
Cdd:TIGR00575 331 EPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPSCGSPLVKIEEEAV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 400 ARCTgGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAA 479
Cdd:TIGR00575 411 IRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGEKSAQNLLNAIEKS 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 480 KETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKW 559
Cdd:TIGR00575 490 KEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNRQLIKKLEELGVEM 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 560 P-APVVVNAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDE 638
Cdd:TIGR00575 570 EsLPEKVNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKLAKAQELGIPIINE 649
|
...
gi 555207888 639 AEM 641
Cdd:TIGR00575 650 EEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
1-424 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 682.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:smart00532 22 LDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLDNAFDEDELRAFDERIEKALGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SdaLTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDnIPARLEVRGEVFLPQAGFEKI 160
Cdd:smart00532 102 P--FAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGD-VPERLEVRGEVFMPKEDFLAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:smart00532 179 NEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEALKWLKELGFPVSPHTRLCKNAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:smart00532 259 EVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLLDIIVQVGRTGKITPVAELE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:smart00532 339 PVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMPTHCPSCGSELVREEGEVDI 418
|
410 420
....*....|....*....|....
gi 555207888 401 RCTGGLiCGAQRKESLKHFVSRRA 424
Cdd:smart00532 419 RCPNPL-CPAQLIERIIHFASRKA 441
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
1-294 |
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: 521.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:pfam01653 24 LDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSLDNAFNLDELQAFIERIRRALGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:pfam01653 104 KEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKGDNPPERLEVRGEVFMPKEDFEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELP-DTHLGRLLQFKAWGLPVSNRVQLCDSP 239
Cdd:pfam01653 184 NEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGfDTQYQALAFLKSLGFPVSPLLALCDGI 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 555207888 240 EAVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQ 294
Cdd:pfam01653 264 EEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
2-293 |
1.23e-172 |
|
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: 493.65 E-value: 1.23e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 2 DAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKss 81
Cdd:cd00114 21 DEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNAFDEEELRAFDERIKRFLG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 82 DALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGdnIPARLEVRGEVFLPQAGFEKIN 161
Cdd:cd00114 99 EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG--APETLEVRGEVFMPKADFEALN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 162 EEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGElPDTHLGRLLQFKAWGLPVSNRVQLCDSPEA 241
Cdd:cd00114 177 KEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALAFLKEWGFPVSPETRLCKNIEE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 555207888 242 VLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPA 293
Cdd:cd00114 256 VLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-647 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1214.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:PRK07956 26 LDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPMLSLDNAFSEEELRAFDKRVRKRLPD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDaLTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQgDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:PRK07956 106 PP-LTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH-GNEPERLEVRGEVFMPKADFEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:PRK07956 184 NEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQSEALEFLKAWGFPVNPYRKLCTSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:PRK07956 264 EVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEATTKLLDIEVQVGRTGAVTPVARLE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:PRK07956 344 PVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDEREIVMPTHCPVCGSELVRVEGEAVL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 401 RCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAAK 480
Cdd:PRK07956 424 RCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAEDLLGLEGFGEKSAQNLLDAIEKSK 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 481 ETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKWP 560
Cdd:PRK07956 504 ETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIVEFFAVEENRELIDELLEAGVNME 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 561 apvvvnAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAE 640
Cdd:PRK07956 584 ------YKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAGSKLAKAQELGIEVLDEEE 657
|
....*..
gi 555207888 641 MMRLLGE 647
Cdd:PRK07956 658 FLRLLGE 664
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-646 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1199.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:COG0272 27 LDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPMLSLDNAFSEEELRDFDRRVRKFLGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 sDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:COG0272 107 -EPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRLKGDDVPEVLEVRGEVYMPKADFEAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGgELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:COG0272 186 NEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEG-LLPDTQSEALELLKEWGFPVNPERRVCKSIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:COG0272 265 EVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEATTKLLDIEVQVGRTGALTPVARLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:COG0272 345 PVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEKPFVMPTHCPVCGSPLVREEGEAAL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 401 RCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAAK 480
Cdd:COG0272 425 RCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKEDLLGLERMGEKSAQNLLAAIEKSK 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 481 ETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKWP 560
Cdd:COG0272 505 KTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESIVEFFAEPHNRELIERLRAAGVNME 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 561 APVVvnAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAE 640
Cdd:COG0272 585 EEEA--EAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAGSKLDKAEELGVPILDEAE 662
|
....*.
gi 555207888 641 MMRLLG 646
Cdd:COG0272 663 FLELLG 668
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
1-641 |
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: 1012.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLks 80
Cdd:TIGR00575 15 LDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDELAAFIKRIRRQL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:TIGR00575 93 GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERLEVRGEVFMPKEDFEAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGilEGGELPD-THLGRLLQFKAWGLPVSNRVQLCDSP 239
Cdd:TIGR00575 173 NEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG--EGLELPDaTQYEALAWLKKWGFPVSPHIRLCDSI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 240 EAVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARL 319
Cdd:TIGR00575 251 EEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQVGRTGAITPVAKL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 320 EPVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAV 399
Cdd:TIGR00575 331 EPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPSCGSPLVKIEEEAV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 400 ARCTgGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAA 479
Cdd:TIGR00575 411 IRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGEKSAQNLLNAIEKS 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 480 KETTFARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKW 559
Cdd:TIGR00575 490 KEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNRQLIKKLEELGVEM 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 560 P-APVVVNAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDE 638
Cdd:TIGR00575 570 EsLPEKVNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKLAKAQELGIPIINE 649
|
...
gi 555207888 639 AEM 641
Cdd:TIGR00575 650 EEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
1-424 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 682.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:smart00532 22 LDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLDNAFDEDELRAFDERIEKALGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SdaLTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDnIPARLEVRGEVFLPQAGFEKI 160
Cdd:smart00532 102 P--FAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGD-VPERLEVRGEVFMPKEDFLAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELPDTHLGRLLQFKAWGLPVSNRVQLCDSPE 240
Cdd:smart00532 179 NEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEALKWLKELGFPVSPHTRLCKNAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 241 AVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLE 320
Cdd:smart00532 259 EVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLLDIIVQVGRTGKITPVAELE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 321 PVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDTREVVFPTHCPVCGSDVERVEGEAVA 400
Cdd:smart00532 339 PVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMPTHCPSCGSELVREEGEVDI 418
|
410 420
....*....|....*....|....
gi 555207888 401 RCTGGLiCGAQRKESLKHFVSRRA 424
Cdd:smart00532 419 RCPNPL-CPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
4-647 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 641.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 4 PEVPDAEYDRLMRELRELEAQHpELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLkssDA 83
Cdd:PRK14351 56 PVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAPMLSIDQSGEADDVREFDERVRREV---GA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 84 LTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDnIPARLEVRGEVFLPQAGFEKINEE 163
Cdd:PRK14351 132 VEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRGD-YPDFLAVRGEVYMPKDAFQAYNRE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 164 ARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVgiLEGGELPDTHLGRLLQFKAWGLPVSNRVQLCDSPEAVL 243
Cdd:PRK14351 211 RIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDV--LDASELFDSHWEELERFPEWGLRVTDRTERVDDIDDAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 244 AFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVQ 323
Cdd:PRK14351 289 AYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEETTIRDIVVQVGRTGRLTPVALLDPVD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 324 VAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESeRPDDTREvvFPTHCPVCGSDVERvEGeAVARCT 403
Cdd:PRK14351 369 VGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEK-DSEGTFE--FPDTCPVCDSAVER-DG-PLAFCT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 404 GGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAAKETT 483
Cdd:PRK14351 444 GGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDLTVADLAELEGWGETSAENLLAELEASREPP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 484 FARFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVIGQLLAEGIKwPAPV 563
Cdd:PRK14351 524 LADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEEIREFFDSERNRAVIDDLLDHGVD-PQPA 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 564 -VVNAEEIDspfaGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAG-SKLAKAQELGIEVIDEAEM 641
Cdd:PRK14351 603 eSEGGDALD----GLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGENPGqSKRDDAEANDVPTLDEEEF 678
|
....*.
gi 555207888 642 MRLLGE 647
Cdd:PRK14351 679 EELLAE 684
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
1-294 |
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: 521.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 1 MDAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKS 80
Cdd:pfam01653 24 LDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSLDNAFNLDELQAFIERIRRALGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 81 SDALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGDNIPARLEVRGEVFLPQAGFEKI 160
Cdd:pfam01653 104 KEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKGDNPPERLEVRGEVFMPKEDFEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 161 NEEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGELP-DTHLGRLLQFKAWGLPVSNRVQLCDSP 239
Cdd:pfam01653 184 NEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGfDTQYQALAFLKSLGFPVSPLLALCDGI 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 555207888 240 EAVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQ 294
Cdd:pfam01653 264 EEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
2-293 |
1.23e-172 |
|
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: 493.65 E-value: 1.23e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 2 DAPEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKss 81
Cdd:cd00114 21 DEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNAFDEEELRAFDERIKRFLG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 82 DALTWCSELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGdnIPARLEVRGEVFLPQAGFEKIN 161
Cdd:cd00114 99 EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG--APETLEVRGEVFMPKADFEALN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 162 EEARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGILEGGElPDTHLGRLLQFKAWGLPVSNRVQLCDSPEA 241
Cdd:cd00114 177 KEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALAFLKEWGFPVSPETRLCKNIEE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 555207888 242 VLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPA 293
Cdd:cd00114 256 VLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
4-636 |
2.91e-115 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 359.53 E-value: 2.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 4 PEVPDAEYDRLMRELRELEAQHPELITPDSPTQRVGAEPLGAFSQVRHEVPMLSLDNVFDEESFLAFNKRVQDRLKSSDA 83
Cdd:PRK14350 29 PSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPILSLDKVYDLKLLKLWIEKMDLENSNLGF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 84 LTWCS-ELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLqGDNIpaRLEVRGEVFLPQAGFEKINe 162
Cdd:PRK14350 109 DFGISvEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLFI-DEKV--ELVLRGEIYITKENFLKIN- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 163 earRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVgILEGGELPDTHLGrLLQFKAWGLPVSNRVQLCD---SP 239
Cdd:PRK14350 185 ---KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDI-LYSSLELKTNHDA-FDKLKKFGFKVNPFCRFFDgknSI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 240 EAVLAFYHKVEADRPTLGFDIDGVVIKVNSLALQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARL 319
Cdd:PRK14350 260 EEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFESLSGFSKVNDIVVQVGRSGKITPVANI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 320 EPVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESErpdDTREVVFPTHCPVCGSDVERvEGeAV 399
Cdd:PRK14350 340 EKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEKL---SVGFFKIPDNCPSCKTALIK-EG-AH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 400 ARCTGGLiCGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALEAA 479
Cdd:PRK14350 415 LFCVNNH-CPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTFNFDRLINLKGFKDKRINNLKRSIEAS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 480 KETTFARFLYALGIREVGEATAAGL----AAYFGTLEAL---EKASIEELQKVPDVGIVVATHV------------FNFF 540
Cdd:PRK14350 494 KKRPFSKLLLSMGIKDLGENTILLLinnnLNSFDKISTLcqdREFALSKLLKIKGIGEKIALNIieafndkiildkFNFF 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 541 AEesnrevIGQLLAEGikwpapvVVNAEEIDSPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEA 620
Cdd:PRK14350 574 KN------LGFKMEED-------SINIDVENSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFNTCVTKYLDFLLVGEK 640
|
650
....*....|....*.
gi 555207888 621 AGSKLAKAQELGIEVI 636
Cdd:PRK14350 641 AGLKLKKANNLGIKIM 656
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
5-558 |
1.25e-48 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 178.96 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 5 EVPDAEYDRLMRELRELEAQHPELITPDSPtqrvgaePLGAFSQVRHEVPMLSLDNVFDEESflafnkrVQDRLKSSDAL 84
Cdd:PRK08097 55 EVDDEVYDQLRARLTQWQRCFGGPEPRDVP-------LPPLNGKVLHPVAHTGVKKLADKQA-------LARWMAGRSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 85 tWCsELKLDGLAVSLLYENGVLVRAATRGDGTTGEDITTNVRTIRAIPLKLQGdnIPARLEVRGEVFLPQAGFEKineea 164
Cdd:PRK08097 121 -WV-QPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLPG--ALANLVLQGELFLRREGHIQ----- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 165 RRTGGkvfANPRNAAAGSLRQLDPRITAKRpltffcYGVGILEGGELPDTHLGRLLQFKAWGLPVSNR-VQLCDSPEAV- 242
Cdd:PRK08097 192 QQMGG---INARAKVAGLMMRKDPSPTLNQ------IGVFVWAWPDGPASMPERLAQLATAGFPLTQRyTHPVKNAEEVa 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 243 ---LAFYHKveadrpTLGFDIDGVVIKvnslALQEQLG--FVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVA 317
Cdd:PRK08097 263 rwrERWYRA------PLPFVTDGVVVR----QAKEPPGryWQPGQGEWAVAWKYPPVQQVAEVRAVQFAVGRTGKITVVL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 318 RLEPVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVV--ESER-----PDDTRevvFPTH-C----P 385
Cdd:PRK08097 333 ELEPVMLDDKRVSRVNIGSVRRWQQWDIAPGDQVLVSLAGQGIPRLDKVVwrGAERtkptpPDADR---FHSLsCfrasP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 386 VCgsdvervEGEAVARctgglicgaqrkesLKHFVSRRAMDVDGMGDKIIDQLVEKEYVhtpADLF---RLTAGKLTGLD 462
Cdd:PRK08097 410 GC-------QEQFLAR--------------LVWLSGKQGLGLDGIGEGTWRALHQTGLF---EHLFswlALTPEQLANTP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 463 RMGPKSAQNVVNALEAAKETTFARFLYALGIREVGEATAAGLAAyfgTLEALEKASIEELQKVPDVGIVVATHVFNFFAE 542
Cdd:PRK08097 466 GIGKARAEQLWHQFNLARQQPFSRWLKALGIPLPQAALNALDDR---SWQQLLSRSEQQWQQLPGIGEGRARQLIAFLQH 542
|
570
....*....|....*.
gi 555207888 543 ESNREVIGQLLAEGIK 558
Cdd:PRK08097 543 PEVKALADWLAAQGIT 558
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
297-375 |
2.06e-42 |
|
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: 147.51 E-value: 2.06e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555207888 297 MTFVRDVEFQVGRTGAITPVARLEPVQVAGVLVSNATLHNADEIDRLGLRIGDKVVIRRAGDVIPQVVNVVESERPDDT 375
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
574-644 |
3.29e-28 |
|
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: 107.57 E-value: 3.29e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555207888 574 FAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLA-----KAQELGIEVIDEAEMMRL 644
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
486-549 |
5.11e-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: 92.59 E-value: 5.11e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555207888 486 RFLYALGIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEESNREVI 549
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
574-644 |
4.72e-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: 78.79 E-value: 4.72e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555207888 574 FAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAG-SKLAKAQELGIEVIDEAEMMRL 644
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDL 77
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
573-645 |
3.35e-13 |
|
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: 65.01 E-value: 3.35e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555207888 573 PFAGKTVVLTGsLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAgEAAGSKLAKAQELGIEVIDEAEMMRLL 645
Cdd:pfam00533 5 LFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV-EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
573-641 |
1.56e-12 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 63.16 E-value: 1.56e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555207888 573 PFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKK-TDLVIAGEAAGSKL--AKAQELGIEVIDEAEM 641
Cdd:smart00292 3 LFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLelLKAIALGIPIVKEEWL 74
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
574-638 |
1.20e-09 |
|
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: 54.84 E-value: 1.20e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555207888 574 FAGKTVVLTGSLSQlSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAA----GSKLAKAQELGIEVIDE 638
Cdd:cd17747 1 LTGMKFALIGKLSK-SKDELKKLIEKLGGKVASKVTKKVTLCISTKAEvekmSKKMKEAKEAGVPVVSE 68
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
383-408 |
2.62e-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: 2.62e-09
10 20
....*....|....*....|....*.
gi 555207888 383 HCPVCGSDVERVEGEAVARCTgGLIC 408
Cdd:pfam03119 1 HCPVCGSPLVREEGEAALRCT-NLSC 25
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
561-647 |
8.45e-09 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 57.48 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555207888 561 APVVVNAEEIdsPFAGKTVVLTGSLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAG---------EAAGSKLAKAQEL 631
Cdd:PRK06195 210 KKIIESFGFT--AFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAIDL 287
|
90 100
....*....|....*....|.
gi 555207888 632 -----GIEVIDEAEMMRLLGE 647
Cdd:PRK06195 288 kkkgqNIKFLNEEEFLQKCKE 308
|
|
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
496-543 |
9.28e-07 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 52.04 E-value: 9.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 555207888 496 VGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEE 543
Cdd:PRK00558 551 IGPKRRKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
576-646 |
1.33e-05 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 47.39 E-value: 1.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555207888 576 GKTVVLTGSLSQlSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAG--SKLAKAQELGIEVIDEAEMMRLLG 646
Cdd:PRK06063 235 GMRVALSAEVSR-THEELVERILHAGLAYSDSVDRDTSLVVCNDPAPeqGKGYHARQLGVPVLDEAAFLELLR 306
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
496-543 |
1.86e-05 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 47.81 E-value: 1.86e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 555207888 496 VGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVFNFFAEE 543
Cdd:COG0322 556 IGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
488-533 |
1.32e-04 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 43.63 E-value: 1.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 555207888 488 LYAL-GIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVA 533
Cdd:COG1948 154 LYVVeSLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTA 200
|
|
| BRCT_PAXIP1_rpt4 |
cd17730 |
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
590-636 |
2.09e-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: 2.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 555207888 590 RDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI 636
Cdd:cd17730 13 REDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVV 59
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
487-533 |
2.93e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 2.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 555207888 487 FLYALGIREVGEATAAGLA-AYFGTLEALEKASIEELQKVPDVGIVVA 533
Cdd:pfam14520 1 FEELLSISGIGPKTALALLsAGIGTVEDLAEADVDELAEIPGIGEKTA 48
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
421-477 |
7.16e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 37.85 E-value: 7.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 555207888 421 SRRAMDVDGMGDKIIDQLVEKEYvHTPADLFRLTAGKLTGLDRMGPKSAQNVVNALE 477
Cdd:pfam14520 1 FEELLSISGIGPKTALALLSAGI-GTVEDLAEADVDELAEIPGIGEKTAQRIILELR 56
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
589-636 |
8.07e-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: 37.95 E-value: 8.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 555207888 589 SRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI 636
Cdd:pfam12738 12 DREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVV 59
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
573-639 |
9.14e-04 |
|
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: 38.29 E-value: 9.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555207888 573 PFAGKTVVLTGsLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELG-IEVIDEA 639
Cdd:cd17731 2 PFKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNsIHIVTPE 68
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
578-638 |
1.84e-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: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555207888 578 TVVLTGsLSQLSRDDAKARLVALGAKVAGSVSKKTDLVIAGEAAGSK-LAKAQELGIEVIDE 638
Cdd:cd00027 2 VICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSP 62
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
492-550 |
2.42e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.01 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 555207888 492 GIREVGEATAAGLAAYFGTLEALEKASIEELQKVPDVGIVVATHVfnffaeesnREVIG 550
Cdd:PRK13766 719 SLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRI---------REVVT 768
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
510-539 |
3.61e-03 |
|
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: 35.09 E-value: 3.61e-03
10 20 30
....*....|....*....|....*....|
gi 555207888 510 TLEALEKASIEELQKVPDVGIVVATHVFNF 539
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| |
