|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-668 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1172.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 1 MDRNAAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 81 MLSLENAFTDGDIAEFDARVKRALAlpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIP 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLG---DEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 161 LRLEGENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFG 240
Cdd:COG0272 158 LRLKGDDVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEGLLPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 241 SQGEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:COG0272 238 TQSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 321 RQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSG 400
Cdd:COG0272 318 EEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 401 SERFLPIPAACPECGSEVVKIPDEVAVRCMG-LSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:COG0272 398 DEKPFVMPTHCPVCGSPLVREEGEAALRCTNgLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVA 559
Cdd:COG0272 478 TKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 560 QSITTFFHNEGNRETIRRMVEAGVEPTVEEKK--VGGKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYV 637
Cdd:COG0272 558 ESIVEFFAEPHNRELIERLRAAGVNMEEEEAEaaADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYV 637
|
650 660 670
....*....|....*....|....*....|.
gi 490646737 638 VAGDEAGSKLDKARQLGVTVLAEDEFLQMLE 668
Cdd:COG0272 638 VAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
2-669 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1085.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 2 DRNAAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 82 LSLENAFTDGDIAEFDARVKRALALPageEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPL 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDP---PLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 162 RLEgENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEI-RGADFG 240
Cdd:PRK07956 158 RLH-GNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVeGGELPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 241 SQGEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:PRK07956 237 SQSEALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 321 RQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSG 400
Cdd:PRK07956 317 EEATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 401 SERFLPIPAACPECGSEVVKIPDEVAVRCMG-LSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:PRK07956 397 DEREIVMPTHCPVCGSELVRVEGEAVLRCTNgLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVA 559
Cdd:PRK07956 477 TAEDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 560 QSITTFFHNEGNRETIRRMVEAGVEPTVEEKKVGgkFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVA 639
Cdd:PRK07956 557 QSIVEFFAVEENRELIDELLEAGVNMEYKGEEVD--LAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVA 634
|
650 660 670
....*....|....*....|....*....|
gi 490646737 640 GDEAGSKLDKARQLGVTVLAEDEFLQMLEG 669
Cdd:PRK07956 635 GEAAGSKLAKAQELGIEVLDEEEFLRLLGE 664
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
13-663 |
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: 934.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 13 LRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLENAFTDGD 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 93 IAEFDARVKRALALPAgeeiAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEGENPPELL 172
Cdd:TIGR00575 81 LAAFIKRIRRQLGLKV----EYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 173 EVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFGSQGEFLSALRQR 252
Cdd:TIGR00575 157 EVRGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDATQYEALAWLKKW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 253 GLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPRQAVTVIEDIVP 332
Cdd:TIGR00575 237 GFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 333 SVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSGSERFLPIPAACP 412
Cdd:TIGR00575 317 QVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 413 ECGSEVVKIPDEVAVRCMGLSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTLTRDDFMKFDRMGE 492
Cdd:TIGR00575 397 SCGSPLVKIEEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 493 KLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSITTFFHNEGNR 572
Cdd:TIGR00575 477 KSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 573 ETIRRMVEAGVEPTVEEKKV-----GGKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEAGSKL 647
Cdd:TIGR00575 557 QLIKKLEELGVEMESLPEKVnaelaGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKL 636
|
650
....*....|....*.
gi 490646737 648 DKARQLGVTVLAEDEF 663
Cdd:TIGR00575 637 AKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-450 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 656.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 6 AERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLE 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 86 NAFTDGDIAEFDARVKRALalpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEG 165
Cdd:smart00532 81 NAFDEDELRAFDERIEKAL----GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 166 EnPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGAD-FGSQGE 244
Cdd:smart00532 157 D-VPERLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFlPKTQSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 245 FLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPRQAV 324
Cdd:smart00532 236 ALKWLKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 325 TVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSGSERF 404
Cdd:smart00532 316 TKLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDERE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 490646737 405 LPIPAACPECGSEVVKIPDEVAVRCMGLSCPAQIRESIIHFASRNA 450
Cdd:smart00532 396 IEMPTHCPSCGSELVREEGEVDIRCPNPLCPAQLIERIIHFASRKA 441
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-320 |
1.03e-167 |
|
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: 482.09 E-value: 1.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 8 RRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLENA 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 88 FTDGDIAEFDARVKRALalpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEGen 167
Cdd:cd00114 81 FDEEELRAFDERIKRFL----GEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 168 PPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFGSQGEFLS 247
Cdd:cd00114 155 APETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLGPKTQSEALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490646737 248 ALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:cd00114 235 FLKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
5-321 |
8.70e-158 |
|
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: 457.19 E-value: 8.70e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 5 AAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSL 84
Cdd:pfam01653 2 EAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 85 ENAFTDGDIAEFDARVKRALalPAGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLE 164
Cdd:pfam01653 82 DNAFNLDELQAFIERIRRAL--GNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 165 GENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGAD--FGSQ 242
Cdd:pfam01653 160 GDNPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHElgFDTQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490646737 243 GEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPR 321
Cdd:pfam01653 240 YQALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-668 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1172.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 1 MDRNAAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 81 MLSLENAFTDGDIAEFDARVKRALAlpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIP 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLG---DEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 161 LRLEGENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFG 240
Cdd:COG0272 158 LRLKGDDVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEGLLPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 241 SQGEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:COG0272 238 TQSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 321 RQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSG 400
Cdd:COG0272 318 EEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 401 SERFLPIPAACPECGSEVVKIPDEVAVRCMG-LSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:COG0272 398 DEKPFVMPTHCPVCGSPLVREEGEAALRCTNgLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVA 559
Cdd:COG0272 478 TKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 560 QSITTFFHNEGNRETIRRMVEAGVEPTVEEKK--VGGKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYV 637
Cdd:COG0272 558 ESIVEFFAEPHNRELIERLRAAGVNMEEEEAEaaADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYV 637
|
650 660 670
....*....|....*....|....*....|.
gi 490646737 638 VAGDEAGSKLDKARQLGVTVLAEDEFLQMLE 668
Cdd:COG0272 638 VAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
2-669 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1085.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 2 DRNAAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 82 LSLENAFTDGDIAEFDARVKRALALPageEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPL 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDP---PLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 162 RLEgENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEI-RGADFG 240
Cdd:PRK07956 158 RLH-GNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVeGGELPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 241 SQGEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:PRK07956 237 SQSEALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 321 RQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSG 400
Cdd:PRK07956 317 EEATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 401 SERFLPIPAACPECGSEVVKIPDEVAVRCMG-LSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:PRK07956 397 DEREIVMPTHCPVCGSELVRVEGEAVLRCTNgLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVA 559
Cdd:PRK07956 477 TAEDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 560 QSITTFFHNEGNRETIRRMVEAGVEPTVEEKKVGgkFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVA 639
Cdd:PRK07956 557 QSIVEFFAVEENRELIDELLEAGVNMEYKGEEVD--LAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVA 634
|
650 660 670
....*....|....*....|....*....|
gi 490646737 640 GDEAGSKLDKARQLGVTVLAEDEFLQMLEG 669
Cdd:PRK07956 635 GEAAGSKLAKAQELGIEVLDEEEFLRLLGE 664
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
13-663 |
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: 934.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 13 LRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLENAFTDGD 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 93 IAEFDARVKRALALPAgeeiAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEGENPPELL 172
Cdd:TIGR00575 81 LAAFIKRIRRQLGLKV----EYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNPPERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 173 EVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFGSQGEFLSALRQR 252
Cdd:TIGR00575 157 EVRGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDATQYEALAWLKKW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 253 GLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPRQAVTVIEDIVP 332
Cdd:TIGR00575 237 GFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 333 SVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSGSERFLPIPAACP 412
Cdd:TIGR00575 317 QVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 413 ECGSEVVKIPDEVAVRCMGLSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTLTRDDFMKFDRMGE 492
Cdd:TIGR00575 397 SCGSPLVKIEEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 493 KLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSITTFFHNEGNR 572
Cdd:TIGR00575 477 KSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 573 ETIRRMVEAGVEPTVEEKKV-----GGKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEAGSKL 647
Cdd:TIGR00575 557 QLIKKLEELGVEMESLPEKVnaelaGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKL 636
|
650
....*....|....*.
gi 490646737 648 DKARQLGVTVLAEDEF 663
Cdd:TIGR00575 637 AKAQELGIPIINEEEL 652
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
1-669 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 684.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 1 MDRNAAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHpELVTPDSPSRRVGGAPLEKFKQVTHRIP 80
Cdd:PRK14351 27 LSEDEAEEQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 81 MLSLENAFTDGDIAEFDARVKRALAlpageEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIP 160
Cdd:PRK14351 106 MLSIDQSGEADDVREFDERVRREVG-----AVEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 161 LRLEGEnPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEiRGADFG 240
Cdd:PRK14351 181 QKLRGD-YPDFLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLD-ASELFD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 241 SQGEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:PRK14351 259 SHWEELERFPEWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 321 RQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSG 400
Cdd:PRK14351 339 RAEETTIRDIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEKDSEG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 401 SERFlpiPAACPECGSEVVKipDEVAVRCMG-LSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:PRK14351 419 TFEF---PDTCPVCDSAVER--DGPLAFCTGgLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDL 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVA 559
Cdd:PRK14351 494 TVADLAELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVA 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 560 QSITTFFHNEGNRETIRRMVEAGVEPTVEEKKVGGKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVA 639
Cdd:PRK14351 574 EEIREFFDSERNRAVIDDLLDHGVDPQPAESEGGDALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVV 653
|
650 660 670
....*....|....*....|....*....|.
gi 490646737 640 GDEAG-SKLDKARQLGVTVLAEDEFLQMLEG 669
Cdd:PRK14351 654 GENPGqSKRDDAEANDVPTLDEEEFEELLAE 684
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-450 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 656.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 6 AERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLE 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 86 NAFTDGDIAEFDARVKRALalpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEG 165
Cdd:smart00532 81 NAFDEDELRAFDERIEKAL----GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 166 EnPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGAD-FGSQGE 244
Cdd:smart00532 157 D-VPERLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFlPKTQSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 245 FLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPRQAV 324
Cdd:smart00532 236 ALKWLKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 325 TVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSGSERF 404
Cdd:smart00532 316 TKLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDERE 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 490646737 405 LPIPAACPECGSEVVKIPDEVAVRCMGLSCPAQIRESIIHFASRNA 450
Cdd:smart00532 396 IEMPTHCPSCGSELVREEGEVDIRCPNPLCPAQLIERIIHFASRKA 441
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-320 |
1.03e-167 |
|
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: 482.09 E-value: 1.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 8 RRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLENA 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 88 FTDGDIAEFDARVKRALalpaGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLEGen 167
Cdd:cd00114 81 FDEEELRAFDERIKRFL----GEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 168 PPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGADFGSQGEFLS 247
Cdd:cd00114 155 APETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLGPKTQSEALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490646737 248 ALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPP 320
Cdd:cd00114 235 FLKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
5-321 |
8.70e-158 |
|
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: 457.19 E-value: 8.70e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 5 AAERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSL 84
Cdd:pfam01653 2 EAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 85 ENAFTDGDIAEFDARVKRALalPAGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLE 164
Cdd:pfam01653 82 DNAFNLDELQAFIERIRRAL--GNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 165 GENPPELLEVRGEVFLPLAAFQRLNAQREEEGEPPFANPRNAAAGSLRQLDSRITARRPLTMFCYAPGEIRGAD--FGSQ 242
Cdd:pfam01653 160 GDNPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHElgFDTQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490646737 243 GEFLSALRQRGLPVTSLARQVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFPPR 321
Cdd:pfam01653 240 YQALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
7-659 |
1.11e-122 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 379.56 E-value: 1.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 7 ERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGAPLEKFKQVTHRIPMLSLEN 86
Cdd:PRK14350 6 QDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPILSLDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 87 AFtdgDIAEFDARVKRAL--ALPAGEEIAYVCEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIPLRLe 164
Cdd:PRK14350 86 VY---DLKLLKLWIEKMDleNSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLFI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 165 GENPPelLEVRGEVFLPLAAFQRLNAQREEegepPFANPRNAAAGSLRQLDSRITARRPLTMFCYapgEI--RGADFGSQ 242
Cdd:PRK14350 162 DEKVE--LVLRGEIYITKENFLKINKTLEK----PYTNARNLASGILRRIDSREVANFPLDIFVY---DIlySSLELKTN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 243 GEFLSALRQRGLPVTSLAR---QVTGVAGVLAYYREMTEKRDTLPYEIDGVVVKVDSFPLQRELGEKSRSPRWAVAVKFP 319
Cdd:PRK14350 233 HDAFDKLKKFGFKVNPFCRffdGKNSIEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 320 PRQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRS 399
Cdd:PRK14350 313 SLSGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEKLSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 400 GserFLPIPAACPECGSEVVKipDEVAVRCMGLSCPAQIRESIIHFASRNAMDMEGLGEKYIEQLLRLGLVGNVADLYTL 479
Cdd:PRK14350 393 G---FFKIPDNCPSCKTALIK--EGAHLFCVNNHCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 480 TRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRHVGEHTAKLL----ATAFGSIDNLARATE---AELLSIR 552
Cdd:PRK14350 468 NFDRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLinnnLNSFDKISTLCQDREfalSKLLKIK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 553 EIGPQVAQSITTFFHNEGNRETIR-------RMVEAGVEPTVEEKKVggkfTGKTFVFTGTLIRFSRSEAQKMVESEGGH 625
Cdd:PRK14350 548 GIGEKIALNIIEAFNDKIILDKFNffknlgfKMEEDSINIDVENSFL----FGKKFCITGSFNGYSRSVLIDKLTKKGAI 623
|
650 660 670
....*....|....*....|....*....|....
gi 490646737 626 AAGSVSKKTDYVVAGDEAGSKLDKARQLGVTVLA 659
Cdd:PRK14350 624 FNTCVTKYLDFLLVGEKAGLKLKKANNLGIKIMS 657
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
6-584 |
1.58e-47 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 176.26 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 6 AERRIAELRAEIRRHDHLYYVLDRPELTDAEYDALYRELLKLEEEHPELVTPDSPSRRVGGaplekfkQVTHRIP----- 80
Cdd:PRK08097 30 AQEEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVPLPPLNG-------KVLHPVAhtgvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 81 MLSLENAftdgdiaefdarVKRALAlpaGEEIAYVcEPKLDGLAVELVYEYGTLTVGSTRGDGVVGENVTQNLKTVKSIP 160
Cdd:PRK08097 103 KLADKQA------------LARWMA---GRSDLWV-QPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 161 LRLEGenPPELLEVRGEVFLPLAAFQrlnaQREEEGeppfANPRNAAAGSL-RQLDSRITARrpLTMFCYA----PGeir 235
Cdd:PRK08097 167 QQLPG--ALANLVLQGELFLRREGHI----QQQMGG----INARAKVAGLMmRKDPSPTLNQ--IGVFVWAwpdgPA--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 236 gadfgSQGEFLSALRQRGLPVTSL-ARQVTGVAGV----LAYYREmtekrdTLPYEIDGVVVKVDsfplQRELGEKSR-- 308
Cdd:PRK08097 232 -----SMPERLAQLATAGFPLTQRyTHPVKNAEEVarwrERWYRA------PLPFVTDGVVVRQA----KEPPGRYWQpg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 309 SPRWAVAVKFPPRQAVTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSR---ATLHNWEEMerkDIRIGDTVVIERAGD 385
Cdd:PRK08097 297 QGEWAVAWKYPPVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRvniGSVRRWQQW---DIAPGDQVLVSLAGQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 386 VIPAVVKVLTEkrsGSERFLPIPaacpecgsevvkiPDEV---AVRCMGLS--CPAQIRESIIHFASRNAMDMEGLGEKY 460
Cdd:PRK08097 374 GIPRLDKVVWR---GAERTKPTP-------------PDADrfhSLSCFRASpgCQEQFLARLVWLSGKQGLGLDGIGEGT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 461 IEQLLRLGLVGNVADLYTLTRDDFMKFDRMGEKLAENLLNAIEASKKRELSRFIFALGIRhVGEHTAKLLATAfgSIDNL 540
Cdd:PRK08097 438 WRALHQTGLFEHLFSWLALTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIP-LPQAALNALDDR--SWQQL 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 490646737 541 ARATEAELLSIREIGPQVAQSITTFFHNEGNRETIRRMVEAGVE 584
Cdd:PRK08097 515 LSRSEQQWQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQGIT 558
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
324-402 |
2.40e-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: 2.40e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490646737 324 VTVIEDIVPSVGRTGVITPTANLRPVEVSGVTVSRATLHNWEEMERKDIRIGDTVVIERAGDVIPAVVKVLTEKRSGSE 402
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
512-575 |
6.46e-31 |
|
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: 114.93 E-value: 6.46e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490646737 512 RFIFALGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSITTFFHNEGNRETI 575
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
596-666 |
4.98e-29 |
|
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349379 [Multi-domain] Cd Length: 76 Bit Score: 110.26 E-value: 4.98e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490646737 596 FTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEAGSKLD-----KARQLGVTVLAEDEFLQM 666
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
596-668 |
6.16e-23 |
|
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: 93.05 E-value: 6.16e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490646737 596 FTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEAG-SKLDKARQLGVTVLAEDEFLQMLE 668
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
467-669 |
1.62e-12 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 69.04 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 467 LGLVGNVADLYTLTRDDFMKFDRMgeKLAENLLNAIEASKKRELSRFifaLGI--RHvgeHTAKLLATAFGSIdNLARAT 544
Cdd:PRK06195 92 ISVLRKTLELYNIPMPSFEYICTM--KLAKNFYSNIDNARLNTVNNF---LGYefKH---HDALADAMACSNI-LLNISK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490646737 545 EAELLSIREIGPQVAQSITTFFHN-------EGnrETIRRMVEAGVEPTVEEKKVGGK--FTGKTFVFTGTLIRFSRSEA 615
Cdd:PRK06195 163 ELNSKDINEISKLLGVTLGYVNENgykpssrKG--RILKRSNRQAPRKKKKIIESFGFtaFKEEVVVFTGGLASMTRDEA 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490646737 616 QKMVESEGGHAAGSVSKKTDYVVAGD---------EAGSKLDKARQL-----GVTVLAEDEFLQMLEG 669
Cdd:PRK06195 241 MILVRRLGGTVGSSVTKKTTYLVTNTkdiedlnreEMSNKLKKAIDLkkkgqNIKFLNEEEFLQKCKE 308
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
594-667 |
2.92e-10 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 57.00 E-value: 2.92e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490646737 594 GKFTGKTFVFTGTLIRFSRSEAQKMVESEGGHAAGSVSKK-TDYVVAGDEAGSKLD--KARQLGVTVLAEDEFLQML 667
Cdd:smart00292 2 KLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDCL 78
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
411-435 |
4.49e-10 |
|
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: 54.75 E-value: 4.49e-10
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
591-667 |
5.68e-09 |
|
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: 53.07 E-value: 5.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490646737 591 KVGGKFTGKTFVFTGtLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAgDEAGSKLDKARQLGVTVLAEDEFLQML 667
Cdd:pfam00533 1 PKEKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV-EARTKKYLKAKELGIPIVTEEWLLDCI 75
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
506-569 |
1.00e-06 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 52.05 E-value: 1.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490646737 506 KKRELSRFIFAL-GIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSITTFFHNE 569
Cdd:COG0322 539 KLRSKARLKSVLdEIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
506-569 |
9.82e-06 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 48.58 E-value: 9.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490646737 506 KKRELSRFIFAL-GIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSITTFFHNE 569
Cdd:PRK00558 534 KKRSKARLTSALdDIPGIGPKRRKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
596-665 |
1.10e-05 |
|
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: 43.67 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490646737 596 FTGKTFVFTGTLiRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEA----GSKLDKARQLGVTVLAEDeFLQ 665
Cdd:cd17747 1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEvekmSKKMKEAKEAGVPVVSED-FLE 72
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
518-562 |
1.36e-04 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 43.63 E-value: 1.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490646737 518 GIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSI 562
Cdd:COG1948 159 SLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERI 203
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
513-562 |
1.77e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 39.78 E-value: 1.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490646737 513 FIFALGIRHVGEHTA-KLLATAFGSIDNLARATEAELLSIREIGPQVAQSI 562
Cdd:pfam14520 1 FEELLSISGIGPKTAlALLSAGIGTVEDLAEADVDELAEIPGIGEKTAQRI 51
|
|
| PRK06063 |
PRK06063 |
DEDDh family exonuclease; |
623-667 |
8.89e-04 |
|
DEDDh family exonuclease;
Pssm-ID: 180377 [Multi-domain] Cd Length: 313 Bit Score: 42.00 E-value: 8.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490646737 623 GGHAAGSVSKKTDYVVAGDEAG--SKLDKARQLGVTVLAEDEFLQML 667
Cdd:PRK06063 259 GLAYSDSVDRDTSLVVCNDPAPeqGKGYHARQLGVPVLDEAAFLELL 305
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
451-503 |
1.77e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 37.08 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490646737 451 MDMEGLGEKYIEQLLRlGLVGNVADLYTLTRDDFMKFDRMGEKLAENLLNAIE 503
Cdd:pfam14520 5 LSISGIGPKTALALLS-AGIGTVEDLAEADVDELAEIPGIGEKTAQRIILELR 56
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
508-562 |
2.81e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.01 E-value: 2.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490646737 508 RELSRFIFAlGIRHVGEHTAKLLATAFGSIDNLARATEAELLSIREIGPQVAQSI 562
Cdd:PRK13766 710 KEQQEYIVE-SLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRI 763
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
600-661 |
5.30e-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: 35.80 E-value: 5.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490646737 600 TFVFTGtLIRFSRSEAQKMVESEGGHAAGSVSKKTDYVVAGDEAGSK-LDKARQLGVTVLAED 661
Cdd:cd00027 2 VICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSPE 63
|
|
| |
