|
Name |
Accession |
Description |
Interval |
E-value |
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
17-684 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1212.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 17 RVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVF 96
Cdd:PRK07956 8 RIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPMLSLDNAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 97 DEESYLAFSKRIGDRLKNgDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEgENIPR 176
Cdd:PRK07956 88 SEEELRAFDKRVRKRLPD-PPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH-GNEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLEGGELPASHWERLMQF 256
Cdd:PRK07956 166 RLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQSEALEFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 257 KAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQEQLTWVRD 336
Cdd:PRK07956 246 KAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEATTKLLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 337 VEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPETVQPIVFPS 416
Cdd:PRK07956 326 IEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDEREIVMPT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 417 ACPVCGSDVERVEGEAVTRCTGGLICGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPADLFRLSAGIMTGLD 496
Cdd:PRK07956 406 HCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAEDLLGLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 497 RMGPKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEE 576
Cdd:PRK07956 486 GFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIVEFFAV 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 577 EHNQTVIRELTDpAGINihwpevvvVKAEEIDSPFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGE 656
Cdd:PRK07956 566 EENRELIDELLE-AGVN--------MEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGE 636
|
650 660
....*....|....*....|....*...
gi 762768056 657 AAGSKLAKAQELGIPVIDEAEMIRLLGE 684
Cdd:PRK07956 637 AAGSKLAKAQELGIEVLDEEEFLRLLGE 664
|
|
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
14-683 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1200.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 14 VALRVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLD 93
Cdd:COG0272 6 AKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPMLSLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 94 NVFDEESYLAFSKRIGDRLkNGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGEN 173
Cdd:COG0272 86 NAFSEEELRDFDRRVRKFL-GDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRLKGDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 174 IPRRVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLEGgELPASHWERL 253
Cdd:COG0272 165 VPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEG-LLPDTQSEAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 254 MQFKAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQEQLTW 333
Cdd:COG0272 244 ELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEATTK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 334 VRDVEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPETVQPIV 413
Cdd:COG0272 324 LLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEKPFV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 414 FPSACPVCGSDVERVEGEAVTRCTGGLICGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPADLFRLSAGIMT 493
Cdd:COG0272 404 MPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKEDLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 494 GLDRMGPKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHF 573
Cdd:COG0272 484 GLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESIVEF 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 574 LEEEHNQTVIRELTDpAGINIHWPEvvvvKAEEIDSPFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVI 653
Cdd:COG0272 564 FAEPHNRELIERLRA-AGVNMEEEE----AEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVV 638
|
650 660 670
....*....|....*....|....*....|
gi 762768056 654 AGEAAGSKLAKAQELGIPVIDEAEMIRLLG 683
Cdd:COG0272 639 AGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
21-678 |
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: 974.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 21 LRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVFDEES 100
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 101 YLAFSKRIGDRLknGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGENIPRRVEV 180
Cdd:TIGR00575 81 LAAFIKRIRRQL--GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 181 RGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGllEGGELP-ASHWERLMQFKAW 259
Cdd:TIGR00575 159 RGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG--EGLELPdATQYEALAWLKKW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 260 GLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQEQLTWVRDVEF 339
Cdd:TIGR00575 237 GFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 340 QVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPETVQPIVFPSACP 419
Cdd:TIGR00575 317 QVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 420 VCGSDVERVEGEAVTRCTgGLICGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPADLFRLSAGIMTGLDRMG 499
Cdd:TIGR00575 397 SCGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 500 PKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEEEHN 579
Cdd:TIGR00575 476 EKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 580 QTVIRELtDPAGINIHwPEVVVVKAEEIDSPFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAG 659
Cdd:TIGR00575 556 RQLIKKL-EELGVEME-SLPEKVNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAG 633
|
650
....*....|....*....
gi 762768056 660 SKLAKAQELGIPVIDEAEM 678
Cdd:TIGR00575 634 SKLAKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
17-458 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 683.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 17 RVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVF 96
Cdd:smart00532 4 EISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLDNAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 97 DEESYLAFSKRIGDRLknGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGEnIPR 176
Cdd:smart00532 84 DEDELRAFDERIEKAL--GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGD-VPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLEGGELPASHWERLMQF 256
Cdd:smart00532 161 RLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEALKWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 257 KAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQEQLTWVRD 336
Cdd:smart00532 241 KELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 337 VEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPETVQPIVFPS 416
Cdd:smart00532 321 IIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMPT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 762768056 417 ACPVCGSDVERVEGEAVTRCTGGLiCGAQRKEALKHFVSRRA 458
Cdd:smart00532 401 HCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
17-684 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 651.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 17 RVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEaDHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVF 96
Cdd:PRK14351 35 QAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALE-DAFDLDTENSPTRRVGGEPLDELETVEHVAPMLSIDQSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 97 DEESYLAFSKRIGDRLkngDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGEnIPR 176
Cdd:PRK14351 114 EADDVREFDERVRREV---GAVEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRGD-YPD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVglLEGGELPASHWERLMQF 256
Cdd:PRK14351 190 FLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDV--LDASELFDSHWEELERF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 257 KAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQEQLTWVRD 336
Cdd:PRK14351 268 PEWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEETTIRD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 337 VEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPETvqpIVFPS 416
Cdd:PRK14351 348 IVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEKDSEGT---FEFPD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 417 ACPVCGSDVERvEGeAVTRCTGGLICGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPADLFRLSAGIMTGLD 496
Cdd:PRK14351 425 TCPVCDSAVER-DG-PLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDLTVADLAELE 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 497 RMGPKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEE 576
Cdd:PRK14351 503 GWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEEIREFFDS 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 577 EHNQTVIRELTDpAGINihwPEVVVVKA-EEIDspfaGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAG 655
Cdd:PRK14351 583 ERNRAVIDDLLD-HGVD---PQPAESEGgDALD----GLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVG 654
|
650 660 670
....*....|....*....|....*....|
gi 762768056 656 EAAG-SKLAKAQELGIPVIDEAEMIRLLGE 684
Cdd:PRK14351 655 ENPGqSKRDDAEANDVPTLDEEEFEELLAE 684
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
17-328 |
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: 519.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 17 RVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVF 96
Cdd:pfam01653 6 QLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSLDNAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 97 DEESYLAFSKRIGDRLKNGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGENIPR 176
Cdd:pfam01653 86 NLDELQAFIERIRRALGNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKGDNPPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLEGGELPA-SHWERLMQ 255
Cdd:pfam01653 166 RLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGFdTQYQALAF 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 762768056 256 FKAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQ 328
Cdd:pfam01653 246 LKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
17-327 |
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: 516.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 17 RVAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVF 96
Cdd:cd00114 2 RIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 97 DEESYLAFSKRIGDRLknGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGenIPR 176
Cdd:cd00114 82 DEEELRAFDERIKRFL--GEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG--APE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEVRGEVFMKHSGFEKLNEEARRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGLLEGGElPASHWERLMQF 256
Cdd:cd00114 158 TLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALAFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 762768056 257 KAWGLPVSDKIKLCTGPAEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPA 327
Cdd:cd00114 237 KEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
18-673 |
1.18e-117 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 366.85 E-value: 1.18e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 18 VAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPTQRVGAAPLAAFEQVRHEVPMLSLDNVFD 97
Cdd:PRK14350 9 ILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPILSLDKVYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 98 EESYLAFSKRIG-DRLKNGDDLTFCCELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEgenipR 176
Cdd:PRK14350 89 LKLLKLWIEKMDlENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLFID-----E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 177 RVEV--RGEVFMKHSGFEKLNeearRTGSKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVgLLEGGELPASH--WER 252
Cdd:PRK14350 164 KVELvlRGEIYITKENFLKIN----KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDI-LYSSLELKTNHdaFDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 253 LMQFkawGLPVSDKIKLCTGP---AEVLDFYRHVEQTRSSLGFDIDGVVVKVDSLELQERLGFVARAPRWAVAFKFPAQE 329
Cdd:PRK14350 239 LKKF---GFKVNPFCRFFDGKnsiEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFESLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 330 QLTWVRDVEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESerpETV 409
Cdd:PRK14350 316 GFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEK---LSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 410 QPIVFPSACPVCGSDVERvEGeAVTRCTGGLiCGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPADLFRLSA 489
Cdd:PRK14350 393 GFFKIPDNCPSCKTALIK-EG-AHLFCVNNH-CPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTFNF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 490 GIMTGLDRMGPKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANL-AAHFGSLEALF--AADEE----TLLAVPDV 562
Cdd:PRK14350 470 DRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLiNNNLNSFDKIStlCQDREfalsKLLKIKGI 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 563 GKVVAAHVrhfLEEEHNQTVIRELTDPAGINIHWPEVVVVKAEEiDSPFAGKTVVLTGSLTILSRDEAKDRLTALGAKVS 642
Cdd:PRK14350 550 GEKIALNI---IEAFNDKIILDKFNFFKNLGFKMEEDSINIDVE-NSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFN 625
|
650 660 670
....*....|....*....|....*....|.
gi 762768056 643 GSVSKKTDMVIAGEAAGSKLAKAQELGIPVI 673
Cdd:PRK14350 626 TCVTKYLDFLLVGEKAGLKLKKANNLGIKIM 656
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
18-592 |
2.96e-48 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 178.57 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 18 VAELRRVLRHHEYKYHVEDAPEIPDVEYDKLMQELKALEADHPELVTSDSPtqrvgaaPLAAFEQVRHEVPMLSLDNVFD 97
Cdd:PRK08097 34 IAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVP-------LPPLNGKVLHPVAHTGVKKLAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 98 EESylafskrIGDRLKNGDDLTFccELKLDGLAVSLLYEDGVLVQAATRGDGTTGENITSNIRTVAAIPLRLEGEniPRR 177
Cdd:PRK08097 107 KQA-------LARWMAGRSDLWV--QPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLPGA--LAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 178 VEVRGEVFMKHSGFEKlneeaRRTGSkvfANPRNAAAGSLRQLDPRITAKRpltffcygVGLL-----EGgelPASHWER 252
Cdd:PRK08097 176 LVLQGELFLRREGHIQ-----QQMGG---INARAKVAGLMMRKDPSPTLNQ--------IGVFvwawpDG---PASMPER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 253 LMQFKAWGLPVSDKIklcTGPAEVLDfyrHVEQTR-----SSLGFDIDGVVVKvdslELQERLG--FVARAPRWAVAFKF 325
Cdd:PRK08097 237 LAQLATAGFPLTQRY---THPVKNAE---EVARWRerwyrAPLPFVTDGVVVR----QAKEPPGryWQPGQGEWAVAWKY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 326 PAQEQLTWVRDVEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIV--ES 403
Cdd:PRK08097 307 PPVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRVNIGSVRRWQQWDIAPGDQVLVSLAGQGIPRLDKVVwrGA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 404 ERPETVQPivfpsacpvcgsDVERVEGEAVTRCTGGliCGAQRKEALKHFVSRRALDVEGMGDKIIDQLVEKEYVKTPAD 483
Cdd:PRK08097 387 ERTKPTPP------------DADRFHSLSCFRASPG--CQEQFLARLVWLSGKQGLGLDGIGEGTWRALHQTGLFEHLFS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 484 LFRLSAGIMTGLDRMGPKSATNLVNALEKAKSTTLARFLYALGIRDVGESTAANLAAhfgSLEALFAADEETLLAVPDVG 563
Cdd:PRK08097 453 WLALTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIPLPQAALNALDDR---SWQQLLSRSEQQWQQLPGIG 529
|
570 580
....*....|....*....|....*....
gi 762768056 564 KVVAAHVRHFLEEEHNQTVIRELtDPAGI 592
Cdd:PRK08097 530 EGRARQLIAFLQHPEVKALADWL-AAQGI 557
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
332-408 |
8.61e-41 |
|
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: 143.28 E-value: 8.61e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 762768056 332 TWVRDVEFQVGRTGAITPVARLEPVAVAGVIVSNATLHNADEIERLGLQIGDRVIVRRAGDVIPQIVGIVESERPET 408
Cdd:pfam03120 2 TKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGD 78
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
611-681 |
1.75e-27 |
|
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: 105.64 E-value: 1.75e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 762768056 611 FAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAGSKLA-----KAQELGIPVIDEAEMIRL 681
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
520-583 |
1.46e-22 |
|
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: 91.43 E-value: 1.46e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 762768056 520 RFLYALGIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEEEHNQTVI 583
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
611-680 |
7.30e-20 |
|
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: 84.19 E-value: 7.30e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 762768056 611 FAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAG-SKLAKAQELGIPVIDEA---EMIR 680
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDglfDLIR 79
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
610-682 |
5.00e-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: 64.62 E-value: 5.00e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 762768056 610 PFAGKTVVLTGsLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAgEAAGSKLAKAQELGIPVIDEAEMIRLL 682
Cdd:pfam00533 5 LFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV-EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
610-682 |
7.14e-13 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 64.32 E-value: 7.14e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 762768056 610 PFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKK-TDMVIAGEAAGSKL--AKAQELGIPVIDEAEMIRLL 682
Cdd:smart00292 3 LFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLelLKAIALGIPIVKEEWLLDCL 78
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
611-675 |
1.14e-08 |
|
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: 52.15 E-value: 1.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 762768056 611 FAGKTVVLTGSLTiLSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAA----GSKLAKAQELGIPVIDE 675
Cdd:cd17747 1 LTGMKFALIGKLS-KSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEvekmSKKMKEAKEAGVPVVSE 68
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
610-684 |
2.29e-08 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 56.33 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 762768056 610 PFAGKTVVLTGSLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAG---------EAAGSKLAKAQELgipvIDEAEMIR 680
Cdd:PRK06195 220 AFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAIDL----KKKGQNIK 295
|
....
gi 762768056 681 LLGE 684
Cdd:PRK06195 296 FLNE 299
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
418-442 |
2.42e-08 |
|
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: 49.74 E-value: 2.42e-08
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
511-577 |
3.85e-08 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 54.41 E-value: 3.85e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762768056 511 EKAKSTTLARFLYAL-GIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEEE 577
Cdd:COG1948 143 KKKPKTLREQQLYVVeSLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERIREVLDSE 210
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
511-577 |
8.05e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 55.65 E-value: 8.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762768056 511 EKAKSTTLARFLYAL-GIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEEE 577
Cdd:PRK13766 703 EKKAMTLKEQQEYIVeSLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRIREVVTSE 770
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
613-683 |
1.43e-06 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 50.85 E-value: 1.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 762768056 613 GKTVVLTGSlTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAG--SKLAKAQELGIPVIDEAEMIRLLG 683
Cdd:PRK06063 235 GMRVALSAE-VSRTHEELVERILHAGLAYSDSVDRDTSLVVCNDPAPeqGKGYHARQLGVPVLDEAAFLELLR 306
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
626-673 |
1.63e-05 |
|
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: 42.96 E-value: 1.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 762768056 626 SRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAGSKLAKAQELGIPVI 673
Cdd:pfam12738 12 DREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVV 59
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
615-675 |
3.78e-05 |
|
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: 41.96 E-value: 3.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 762768056 615 TVVLTGsLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAGSK-LAKAQELGIPVIDE 675
Cdd:cd00027 2 VICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSP 62
|
|
| BRCT_PAXIP1_rpt4 |
cd17730 |
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
627-673 |
6.31e-05 |
|
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: 41.46 E-value: 6.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 762768056 627 RDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAGSKLAKAQELGIPVI 673
Cdd:cd17730 13 REDIKRMIELMGAKYTGYLTRSNTHLICKRPEGEKYEKAKEWRIPVV 59
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
521-567 |
1.22e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 40.16 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 762768056 521 FLYALGIRDVGESTAANLAAH-FGSLEALFAADEETLLAVPDVGKVVA 567
Cdd:pfam14520 1 FEELLSISGIGPKTALALLSAgIGTVEDLAEADVDELAEIPGIGEKTA 48
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
610-676 |
2.22e-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: 40.22 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 762768056 610 PFAGKTVVLTGsLTILSRDEAKDRLTALGAKVSGSVSKKTDMVIAGEAAGSKLAKAQELG-IPVIDEA 676
Cdd:cd17731 2 PFKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNsIHIVTPE 68
|
|
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
526-577 |
1.26e-03 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 42.03 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 762768056 526 GIRDVGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEEE 577
Cdd:PRK00558 547 DIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
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| uvrC |
PRK14666 |
excinuclease ABC subunit C; Provisional |
530-576 |
2.16e-03 |
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excinuclease ABC subunit C; Provisional
Pssm-ID: 237782 [Multi-domain] Cd Length: 694 Bit Score: 41.41 E-value: 2.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 762768056 530 VGESTAANLAAHFGSLEALFAADEETLLAVPDVGKVVAAHVRHFLEE 576
Cdd:PRK14666 645 IGPATARLLWERFGSLQAMAAAGEEGLAAVPGIGPARAAALHEHLKT 691
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| BRCT_p53bp1_rpt2 |
cd17724 |
Second (C-terminal) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ... |
610-674 |
4.12e-03 |
|
Second (C-terminal) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family corresponds to the second BRCT domain.
Pssm-ID: 349356 Cd Length: 87 Bit Score: 36.97 E-value: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 762768056 610 PFAGKTVVLTGSLTILSRDEAKDRLTALGAKV----------SGSVSKKTD-MVIAGEAAGSKLAKAQELGIPVID 674
Cdd:cd17724 1 LFKGLKILVVSKKKKPFRETWSFILKAAGATSvkklpstsaaSSSDIGKIDvVVTDGSCPSTVLKKARQLGIPVVS 76
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| H3TH_53EXO |
cd09898 |
H3TH domain of the 5'-3' exonuclease of Taq DNA polymerase I and homologs; H3TH ... |
526-554 |
6.98e-03 |
|
H3TH domain of the 5'-3' exonuclease of Taq DNA polymerase I and homologs; H3TH (helix-3-turn-helix) domains of the 5'-3' exonuclease (53EXO) of mutli-domain DNA polymerase I and single domain protein homologs are included in this family. Taq DNA polymerase I contains a polymerase domain for synthesizing a new DNA strand and a 53EXO domain for cleaving RNA primers or damaged DNA strands. Taq's 53EXO recognizes and endonucleolytically cleaves a structure-specific DNA substrate that has a bifurcated downstream duplex and an upstream template-primer duplex that overlaps the downstream duplex by 1 bp. The 53EXO cleaves the unpaired 5'-arm of the overlap flap DNA substrate. 5'-3' exonucleases are members of the structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. These nucleases contain a PIN (PilT N terminus) domain with a helical arch/clamp region/I domain (not included here) and inserted within the PIN domain is an atypical helix-hairpin-helix-2 (HhH2)-like region. This atypical HhH2 region, the H3TH domain, has an extended loop with at least three turns between the first two helices, and only three of the four helices appear to be conserved. Both the H3TH domain and the helical arch/clamp region are involved in DNA binding. Studies suggest that a glycine-rich loop in the H3TH domain contacts the phosphate backbone of the template strand in the downstream DNA duplex. The nucleases within this family have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (i. e., Mg2+ or Mn2+ or Zn2+) required for nuclease activity. The first metal binding site is composed entirely of Asp/Glu residues from the PIN domain, whereas, the second metal binding site is composed generally of two Asp residues from the PIN domain and two Asp residues from the H3TH domain. Together with the helical arch and network of amino acids interacting with metal binding ions, the H3TH region defines a positively charged active-site DNA-binding groove in structure-specific 5' nucleases.
Pssm-ID: 188618 [Multi-domain] Cd Length: 73 Bit Score: 35.84 E-value: 6.98e-03
10 20
....*....|....*....|....*....
gi 762768056 526 GIRDVGESTAANLAAHFGSLEALFAADEE 554
Cdd:cd09898 20 GVPGIGPKTAAKLLQEYGSLENILANLDE 48
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| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
544-573 |
7.15e-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: 34.31 E-value: 7.15e-03
10 20 30
....*....|....*....|....*....|
gi 762768056 544 SLEALFAADEETLLAVPDVGKVVAAHVRHF 573
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
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