|
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: 1185.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 1 MSKEIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 81 MLSLGNAFNEGDLLDFDRRVRQGIDDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRL 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLGDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 161 NEEV---TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHS 237
Cdd:COG0272 161 KGDDvpeVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEGLLPDTQS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 238 ESLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEV 317
Cdd:COG0272 241 EALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 318 VTRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEE 397
Cdd:COG0272 321 TTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 398 EYRMPTHCPACESELVRLEEEVALRCINP-TCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKE 476
Cdd:COG0272 401 PFVMPTHCPVCGSPLVREEGEAALRCTNGlSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 477 QLLQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSV 556
Cdd:COG0272 481 DLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 557 VTYFDNEDVLELLQQFKEYGVNMTYKGIKSAdlqnVESYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDL 636
Cdd:COG0272 561 VEFFAEPHNRELIERLRAAGVNMEEEEAEAA----ADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDY 636
|
650 660 670
....*....|....*....|....*....|..
gi 1267289226 637 VVAGEAAGSKLAQAEKHNVEVWNEERFLQELN 668
Cdd:COG0272 637 VVAGENAGSKLDKAEELGVPILDEAEFLELLG 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: 1153.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 2 SKEIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 82 LSLGNAFNEGDLLDFDRRVRQGIDDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLN 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 162 EEV--TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEE-KTISSHSE 238
Cdd:PRK07956 161 GNEpeRLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGgELPDSQSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 239 SLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVV 318
Cdd:PRK07956 241 ALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 319 TRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEE 398
Cdd:PRK07956 321 TKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDERE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 399 YRMPTHCPACESELVRLEEEVALRCINP-TCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQ 477
Cdd:PRK07956 401 IVMPTHCPVCGSELVRVEGEAVLRCTNGlSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 478 LLQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVV 557
Cdd:PRK07956 481 LLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 558 TYFDNEDVLELLQQFKEYGVNMTYKGIKSAdlqnvesyFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLV 637
Cdd:PRK07956 561 EFFAVEENRELIDELLEAGVNMEYKGEEVD--------LAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLV 632
|
650 660 670
....*....|....*....|....*....|..
gi 1267289226 638 VAGEAAGSKLAQAEKHNVEVWNEERFLQELNK 669
Cdd:PRK07956 633 VAGEAAGSKLAKAQELGIEVLDEEEFLRLLGE 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: 939.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 13 LRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLGNAFNEGD 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 93 LLDFDRRVRQGIDDAnVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRL---NEEVTLEAR 169
Cdd:TIGR00575 81 LAAFIKRIRRQLGLK-VEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLagdNPPERLEVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 170 GEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHSESLDFLGELGFK 249
Cdd:TIGR00575 160 GEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDATQYEALAWLKKWGFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 250 TNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVVTRLTGIELSVG 329
Cdd:TIGR00575 240 VSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 330 RTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEEYRMPTHCPACE 409
Cdd:TIGR00575 320 RTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPSCG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 410 SELVRLEEEVALRCINPTCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQLLQLERFGEKSA 489
Cdd:TIGR00575 400 SPLVKIEEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGEKSA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 490 TNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVTYFDNEDVLELL 569
Cdd:TIGR00575 480 QNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNRQLI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 570 QQFKEYGVNMTYKGIKSADLQNVeSYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSKLAQ 649
Cdd:TIGR00575 560 KKLEELGVEMESLPEKVNAELAG-SPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKLAK 638
|
650
....*....|....
gi 1267289226 650 AEKHNVEVWNEERF 663
Cdd:TIGR00575 639 AQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-444 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 675.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 6 AKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLG 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 86 NAFNEGDLLDFDRRVRQGIDDaNVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNEEV- 164
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGS-PFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGDVp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 165 -TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEK-TISSHSESLDF 242
Cdd:smart00532 160 eRLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELfLPKTQSEALKW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 243 LGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVVTRLT 322
Cdd:smart00532 240 LKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 323 GIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEEYRMP 402
Cdd:smart00532 320 DIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMP 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1267289226 403 THCPACESELVRLEEEVALRCINPTCPAQIREGLIHFVSRNA 444
Cdd:smart00532 400 THCPSCGSELVREEGEVDIRCPNPLCPAQLIERIIHFASRKA 441
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-314 |
3.85e-170 |
|
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: 488.25 E-value: 3.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 8 KRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLGNA 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 88 FNEGDLLDFDRRVRQGIDDaNVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNEE-VTL 166
Cdd:cd00114 81 FDEEELRAFDERIKRFLGE-EPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAGApETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 167 EARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHSESLDFLGEL 246
Cdd:cd00114 160 EVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLGPKTQSEALAFLKEW 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267289226 247 GFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPA 314
Cdd:cd00114 240 GFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-315 |
4.54e-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: 457.96 E-value: 4.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 4 EIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLS 83
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 84 LGNAFNEGDLLDFDRRVRQGI-DDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNE 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALgNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 163 E---VTLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKT--ISSHS 237
Cdd:pfam01653 161 DnppERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHElgFDTQY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267289226 238 ESLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAE 315
Cdd:pfam01653 241 QALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 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: 1185.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 1 MSKEIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 81 MLSLGNAFNEGDLLDFDRRVRQGIDDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRL 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLGDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 161 NEEV---TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHS 237
Cdd:COG0272 161 KGDDvpeVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVEGLLPDTQS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 238 ESLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEV 317
Cdd:COG0272 241 EALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAEEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 318 VTRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEE 397
Cdd:COG0272 321 TTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGDEK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 398 EYRMPTHCPACESELVRLEEEVALRCINP-TCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKE 476
Cdd:COG0272 401 PFVMPTHCPVCGSPLVREEGEAALRCTNGlSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLTKE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 477 QLLQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSV 556
Cdd:COG0272 481 DLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAESI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 557 VTYFDNEDVLELLQQFKEYGVNMTYKGIKSAdlqnVESYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDL 636
Cdd:COG0272 561 VEFFAEPHNRELIERLRAAGVNMEEEEAEAA----ADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDY 636
|
650 660 670
....*....|....*....|....*....|..
gi 1267289226 637 VVAGEAAGSKLAQAEKHNVEVWNEERFLQELN 668
Cdd:COG0272 637 VVAGENAGSKLDKAEELGVPILDEAEFLELLG 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: 1153.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 2 SKEIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 82 LSLGNAFNEGDLLDFDRRVRQGIDDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLN 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 162 EEV--TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEE-KTISSHSE 238
Cdd:PRK07956 161 GNEpeRLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGgELPDSQSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 239 SLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVV 318
Cdd:PRK07956 241 ALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 319 TRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEE 398
Cdd:PRK07956 321 TKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDERE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 399 YRMPTHCPACESELVRLEEEVALRCINP-TCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQ 477
Cdd:PRK07956 401 IVMPTHCPVCGSELVRVEGEAVLRCTNGlSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 478 LLQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVV 557
Cdd:PRK07956 481 LLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSIV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 558 TYFDNEDVLELLQQFKEYGVNMTYKGIKSAdlqnvesyFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLV 637
Cdd:PRK07956 561 EFFAVEENRELIDELLEAGVNMEYKGEEVD--------LAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLV 632
|
650 660 670
....*....|....*....|....*....|..
gi 1267289226 638 VAGEAAGSKLAQAEKHNVEVWNEERFLQELNK 669
Cdd:PRK07956 633 VAGEAAGSKLAKAQELGIEVLDEEEFLRLLGE 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: 939.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 13 LRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLGNAFNEGD 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 93 LLDFDRRVRQGIDDAnVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRL---NEEVTLEAR 169
Cdd:TIGR00575 81 LAAFIKRIRRQLGLK-VEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLagdNPPERLEVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 170 GEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHSESLDFLGELGFK 249
Cdd:TIGR00575 160 GEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDATQYEALAWLKKWGFP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 250 TNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVVTRLTGIELSVG 329
Cdd:TIGR00575 240 VSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 330 RTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEEYRMPTHCPACE 409
Cdd:TIGR00575 320 RTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPSCG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 410 SELVRLEEEVALRCINPTCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQLLQLERFGEKSA 489
Cdd:TIGR00575 400 SPLVKIEEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGEKSA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 490 TNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVTYFDNEDVLELL 569
Cdd:TIGR00575 480 QNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNRQLI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 570 QQFKEYGVNMTYKGIKSADLQNVeSYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSKLAQ 649
Cdd:TIGR00575 560 KKLEELGVEMESLPEKVNAELAG-SPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKLAK 638
|
650
....*....|....
gi 1267289226 650 AEKHNVEVWNEERF 663
Cdd:TIGR00575 639 AQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-444 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 675.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 6 AKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLG 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 86 NAFNEGDLLDFDRRVRQGIDDaNVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNEEV- 164
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGS-PFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGDVp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 165 -TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEK-TISSHSESLDF 242
Cdd:smart00532 160 eRLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELfLPKTQSEALKW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 243 LGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVVTRLT 322
Cdd:smart00532 240 LKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 323 GIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEEEEYRMP 402
Cdd:smart00532 320 DIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMP 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1267289226 403 THCPACESELVRLEEEVALRCINPTCPAQIREGLIHFVSRNA 444
Cdd:smart00532 400 THCPSCGSELVREEGEVDIRCPNPLCPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
1-663 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 602.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 1 MSKEIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENpEFMSEDSPSVRVGGTVLDIFEKVTHKSP 80
Cdd:PRK14351 27 LSEDEAEEQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 81 MLSLGNAFNEGDLLDFDRRVRQGIDDanVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRL 160
Cdd:PRK14351 106 MLSIDQSGEADDVREFDERVRREVGA--VEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 161 NEEV--TLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKtISSHSE 238
Cdd:PRK14351 184 RGDYpdFLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLDASEL-FDSHWE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 239 SLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAEEVV 318
Cdd:PRK14351 263 ELERFPEWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 319 TRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGeeeE 398
Cdd:PRK14351 343 TTIRDIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEKDSEG---T 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 399 YRMPTHCPACESELVRlEEEVALRCINPTCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQL 478
Cdd:PRK14351 420 FEFPDTCPVCDSAVER-DGPLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDLTVADL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 479 LQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVT 558
Cdd:PRK14351 499 AELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEEIRE 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 559 YFDNEDVLELLQQFKEYGVnmtykgiksaDLQNVESY----FAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKST 634
Cdd:PRK14351 579 FFDSERNRAVIDDLLDHGV----------DPQPAESEggdaLDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNT 648
|
650 660 670
....*....|....*....|....*....|
gi 1267289226 635 DLVVAGEAAG-SKLAQAEKHNVEVWNEERF 663
Cdd:PRK14351 649 DYLVVGENPGqSKRDDAEANDVPTLDEEEF 678
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-314 |
3.85e-170 |
|
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: 488.25 E-value: 3.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 8 KRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLSLGNA 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 88 FNEGDLLDFDRRVRQGIDDaNVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNEE-VTL 166
Cdd:cd00114 81 FDEEELRAFDERIKRFLGE-EPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAGApETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 167 EARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHSESLDFLGEL 246
Cdd:cd00114 160 EVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLGPKTQSEALAFLKEW 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267289226 247 GFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPA 314
Cdd:cd00114 240 GFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-315 |
4.54e-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: 457.96 E-value: 4.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 4 EIAKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSPMLS 83
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 84 LGNAFNEGDLLDFDRRVRQGI-DDANVRYICELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNE 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALgNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 163 E---VTLEARGEAYMPKRSFVKLNEEKEQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKT--ISSHS 237
Cdd:pfam01653 161 DnppERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHElgFDTQY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267289226 238 ESLDFLGELGFKTNPNRRTCETIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAE 315
Cdd:pfam01653 241 QALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
1-657 |
5.86e-131 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 401.13 E-value: 5.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 1 MSKEIaKKRIEELRDLLNTFNYQYHVLDNPSVSDAEYDRNMQELIKLEAENPEFMSEDSPSVRVGGTVLDIFEKVTHKSP 80
Cdd:PRK14350 1 MSKDI-QDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 81 MLSLGNAFNEGDLLDF-DRRVRQGIDDANVRYI-CELKIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPL 158
Cdd:PRK14350 80 ILSLDKVYDLKLLKLWiEKMDLENSNLGFDFGIsVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 159 RLNEEVTLEARGEAYMPKRSFVKLNeekeQNGEDVFANPRNAAAGSIRQLDTKIAAKRNLSMFVYGLANVEEKTISSHsE 238
Cdd:PRK14350 160 FIDEKVELVLRGEIYITKENFLKIN----KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDILYSSLELKTNH-D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 239 SLDFLGELGFKTNPNRRTCE---TIEEVIAYVEEWQEKRPNLDYEIDGIVIKVDDVALQESLGTTAKSPRWAIAYKFPAE 315
Cdd:PRK14350 235 AFDKLKKFGFKVNPFCRFFDgknSIEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFESL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 316 EVVTRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGe 395
Cdd:PRK14350 315 SGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEKLSVG- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 396 eeEYRMPTHCPACESELVRleEEVALRCINPTCPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTK 475
Cdd:PRK14350 394 --FFKIPDNCPSCKTALIK--EGAHLFCVNNHCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTFNF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 476 EQLLQLERFGEKSATNLIQAIENSKENSLERLLFGLGIRHVGAKAART-FAEHFETMDALVKATEEE------LKSINEI 548
Cdd:PRK14350 470 DRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLlINNNLNSFDKISTLCQDRefalskLLKIKGI 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 549 GEKMAQSVVTYFDNEDVLELLQQFKEYGVNMTYKGIKSADlqnVESYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTG 628
Cdd:PRK14350 550 GEKIALNIIEAFNDKIILDKFNFFKNLGFKMEEDSINIDV---ENSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFNT 626
|
650 660
....*....|....*....|....*....
gi 1267289226 629 SVSKSTDLVVAGEAAGSKLAQAEKHNVEV 657
Cdd:PRK14350 627 CVTKYLDFLLVGEKAGLKLKKANNLGIKI 655
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
116-577 |
1.74e-44 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 167.79 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 116 KIDGLAVSLHYEKGRFIQGATRGDGITGEDITQNLKTIKAIPLRLNEE---VTLEarGEAYMpkrsfvKLNEEKEQngED 192
Cdd:PRK08097 125 KVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLPGAlanLVLQ--GELFL------RREGHIQQ--QM 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 193 VFANPRNAAAGSI-RQLDTKIAAKrnLSMFVY----GLANVEEKtisshsesLDFLGELGFK-TNPNRRTCETIEEVIAY 266
Cdd:PRK08097 195 GGINARAKVAGLMmRKDPSPTLNQ--IGVFVWawpdGPASMPER--------LAQLATAGFPlTQRYTHPVKNAEEVARW 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 267 VEEWQekRPNLDYEIDGIVIKVDdvalQESLGT--TAKSPRWAIAYKFPAEEVVTRLTGIELSVGRTGVVTPTAELEPVR 344
Cdd:PRK08097 265 RERWY--RAPLPFVTDGVVVRQA----KEPPGRywQPGQGEWAVAWKYPPVQQVAEVRAVQFAVGRTGKITVVLELEPVM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 345 VAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFdkRTGEEEEYRMPT----HcpaceselvrleeevA 420
Cdd:PRK08097 339 LDDKRVSRVNIGSVRRWQQWDIAPGDQVLVSLAGQGIPRLDKVVW--RGAERTKPTPPDadrfH---------------S 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 421 LRCINPT--CPAQIREGLIHFVSRNAMNIDGLGERVITQLFDADYIRTFADLYALTKEQLLQLERFGEKSATNLIQAIEN 498
Cdd:PRK08097 402 LSCFRASpgCQEQFLARLVWLSGKQGLGLDGIGEGTWRALHQTGLFEHLFSWLALTPEQLANTPGIGKARAEQLWHQFNL 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267289226 499 SKENSLERLLFGLGIRhVGAKAARTFAEHfeTMDALVKATEEELKSINEIGEKMAQSVVTYFDNEDVLELLQQFKEYGV 577
Cdd:PRK08097 482 ARQQPFSRWLKALGIP-LPQAALNALDDR--SWQQLLSRSEQQWQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQGI 557
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
318-396 |
3.12e-43 |
|
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. This family is a small domain found after the adenylation domain pfam01653 in NAD dependent ligases. OB-fold domains generally are involved in nucleic acid binding.
Pssm-ID: 460813 [Multi-domain] Cd Length: 79 Bit Score: 149.82 E-value: 3.12e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267289226 318 VTRLTGIELSVGRTGVVTPTAELEPVRVAGTIVRRASLHNEDLIREKDIRIGDYVVVKKAGDIIPEVVNVIFDKRTGEE 396
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
506-569 |
1.17e-26 |
|
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: 102.99 E-value: 1.17e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267289226 506 RLLFGLGIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVTYFDNEDVLELL 569
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
596-665 |
6.90e-26 |
|
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: 101.02 E-value: 6.90e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267289226 596 FAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSKLA-----QAEKHNVEVWNEERFLQ 665
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLD 75
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
596-665 |
3.10e-19 |
|
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: 82.26 E-value: 3.10e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267289226 596 FAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAG-SKLAQAEKHNVEVWNEERFLQ 665
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFD 76
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
591-665 |
1.67e-12 |
|
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: 63.08 E-value: 1.67e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267289226 591 NVESYFAGKTVVLTGKLEvMGRSEAKKKIEALGGKVTGSVSKSTDLVVAgEAAGSKLAQAEKHNVEVWNEERFLQ 665
Cdd:pfam00533 1 PKEKLFSGKTFVITGLDG-LERDELKELIEKLGGKVTDSLSKKTTHVIV-EARTKKYLKAKELGIPIVTEEWLLD 73
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
593-665 |
3.14e-12 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 62.39 E-value: 3.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267289226 593 ESYFAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVS-KSTDLVVAGEAAGSKL--AQAEKHNVEVWNEERFLQ 665
Cdd:smart00292 1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLelLKAIALGIPIVKEEWLLD 76
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
404-429 |
2.37e-11 |
|
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: 58.60 E-value: 2.37e-11
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
596-666 |
7.39e-09 |
|
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.
Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 52.92 E-value: 7.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267289226 596 FAGKTVVLTGKLEvMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAA----GSKLAQAEKHNVEVWNEErFLQE 666
Cdd:cd17747 1 LTGMKFALIGKLS-KSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEvekmSKKMKEAKEAGVPVVSED-FLED 73
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
596-665 |
8.93e-08 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 54.40 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267289226 596 FAGKTVVLTGKLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAG---------EAAGSKLAQA-----EKHNVEVWNEE 661
Cdd:PRK06195 221 FKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAidlkkKGQNIKFLNEE 300
|
....
gi 1267289226 662 RFLQ 665
Cdd:PRK06195 301 EFLQ 304
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
512-556 |
2.94e-05 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 45.55 E-value: 2.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1267289226 512 GIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSV 556
Cdd:COG1948 159 SLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERI 203
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
512-553 |
5.15e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 46.41 E-value: 5.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1267289226 512 GIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMA 553
Cdd:PRK13766 719 SLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTA 760
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
600-657 |
1.20e-04 |
|
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: 40.42 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267289226 600 TVVLTGkLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSK-LAQAEKHNVEV 657
Cdd:cd00027 2 VICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPI 59
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
445-498 |
3.21e-04 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 39.01 E-value: 3.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1267289226 445 MNIDGLGERVITQLFDAdYIRTFADLYALTKEQLLQLERFGEKSATNLIQAIEN 498
Cdd:pfam14520 5 LSISGIGPKTALALLSA-GIGTVEDLAEADVDELAEIPGIGEKTAQRIILELRD 57
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
511-557 |
1.27e-03 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 37.47 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1267289226 511 LGIRHVGAKAARTFAEH-FETMDALVKATEEELKSINEIGEKMAQSVV 557
Cdd:pfam14520 5 LSISGIGPKTALALLSAgIGTVEDLAEADVDELAEIPGIGEKTAQRII 52
|
|
| UvrC |
COG0322 |
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair]; |
512-563 |
1.67e-03 |
|
Excinuclease UvrABC, nuclease subunit [Replication, recombination and repair];
Pssm-ID: 440091 [Multi-domain] Cd Length: 603 Bit Score: 41.65 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1267289226 512 GIRHVGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVTYFDNE 563
Cdd:COG0322 552 EIPGIGPKRRKALLKHFGSLKAIKEASVEELAAVPGISKKLAEAIYEYLHKE 603
|
|
| uvrC |
PRK00558 |
excinuclease ABC subunit UvrC; |
516-563 |
1.79e-03 |
|
excinuclease ABC subunit UvrC;
Pssm-ID: 234792 [Multi-domain] Cd Length: 598 Bit Score: 41.26 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1267289226 516 VGAKAARTFAEHFETMDALVKATEEELKSINEIGEKMAQSVVTYFDNE 563
Cdd:PRK00558 551 IGPKRRKALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEALHKK 598
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
596-654 |
1.92e-03 |
|
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.
Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 37.52 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267289226 596 FAGKTVVLTGkLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSKLAQAEKHN 654
Cdd:cd17731 3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWN 60
|
|
| BRCT_PAXIP1_rpt5 |
cd17712 |
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
601-665 |
2.51e-03 |
|
fifth 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 fifth BRCT domain.
Pssm-ID: 349344 Cd Length: 75 Bit Score: 37.22 E-value: 2.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267289226 601 VVLTGkLEVMGRSEAKKKIEALGGKVTGSVSKSTDLVVAGEAAGSKLAQA---EKHNVEV-WNEERFLQ 665
Cdd:cd17712 4 VLFTG-FDPVQVRKLTKKVTILGGEVVESPQECTHLVAPKVSRTVKFLTAisvCKHIVTPeWLEESFKQ 71
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
530-559 |
6.22e-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: 34.70 E-value: 6.22e-03
10 20 30
....*....|....*....|....*....|
gi 1267289226 530 TMDALVKATEEELKSINEIGEKMAQSVVTY 559
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| |
