|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-671 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1117.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 1 MATTSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 81 MLSLGNVFNQEDLFAFARRVEERLPNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVL 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLGDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 161 HSDHfeIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEpNHSLT 240
Cdd:COG0272 161 KGDD--VPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVE-GLLPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 241 TMHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:COG0272 238 TQSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 321 QAALTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSA 400
Cdd:COG0272 318 EEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 401 DAEIVHLPESCPVCASPVVMPEGEALARCSGGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHL 480
Cdd:COG0272 398 DEKPFVMPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 481 heHRETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDI 560
Cdd:COG0272 478 --TKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 561 TAEWIADFFLAPHNIEVLDRLIAAGIHWDAPTAPTR--QPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTK 638
Cdd:COG0272 556 VAESIVEFFAEPHNRELIERLRAAGVNMEEEEAEAAadSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTD 635
|
650 660 670
....*....|....*....|....*....|...
gi 500622385 639 CVVAGEKAGSKLEKAAKLGIVVMNETDFLSLMA 671
Cdd:COG0272 636 YVVAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
2-672 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1045.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 2 ATTSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 82 LSLGNVFNQEDLFAFARRVEERLPNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLH 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 162 SDHfeiPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHSLTT 241
Cdd:PRK07956 161 GNE---PERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 242 MHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQ 321
Cdd:PRK07956 238 QSEALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 322 AALTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSAD 401
Cdd:PRK07956 318 EATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 402 AEIVHLPESCPVCASPVVMPEGEALARCSGGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLH 481
Cdd:PRK07956 398 EREIVMPTHCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 482 EhrETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDIT 561
Cdd:PRK07956 478 A--EDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 562 AEWIADFFLAPHNIEVLDRLIAAGIHWDAPTAPTrqPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVV 641
Cdd:PRK07956 556 AQSIVEFFAVEENRELIDELLEAGVNMEYKGEEV--DLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVV 633
|
650 660 670
....*....|....*....|....*....|.
gi 500622385 642 AGEKAGSKLEKAAKLGIVVMNETDFLSLMAN 672
Cdd:PRK07956 634 AGEAAGSKLAKAQELGIEVLDEEEFLRLLGE 664
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
13-666 |
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: 863.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 13 LIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNVFNQED 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 93 LFAFARRVEERLpNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHSDHFeiPRLLE 172
Cdd:TIGR00575 81 LAAFIKRIRRQL-GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNP--PERLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 173 VRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAqcePNHSLT--TMHDSLQWLT 250
Cdd:TIGR00575 158 VRGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG---EGLELPdaTQYEALAWLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 251 QLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQAALTTVDQI 330
Cdd:TIGR00575 235 KWGFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 331 DWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADAEIVHLPES 410
Cdd:TIGR00575 315 VVQVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 411 CPVCASPVVMPEGEALARCSgGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLHEhrETLLGI 490
Cdd:TIGR00575 395 CPSCGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKK--EDLLEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 491 EKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEWIADFFL 570
Cdd:TIGR00575 472 EGFGEKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFH 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 571 APHNIEVLDRLIAAGIHWDA-----PTAPTRQPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEK 645
Cdd:TIGR00575 552 DPNNRQLIKKLEELGVEMESlpekvNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEK 631
|
650 660
....*....|....*....|.
gi 500622385 646 AGSKLEKAAKLGIVVMNETDF 666
Cdd:TIGR00575 632 AGSKLAKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-451 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 631.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 6 VIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLG 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 86 NVFNQEDLFAFARRVEERLPNQkVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHsdhF 165
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGSP-FAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLS---G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 166 EIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHSLTTMHDS 245
Cdd:smart00532 157 DVPERLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 246 LQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQAALT 325
Cdd:smart00532 237 LKWLKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 326 TVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADAEIV 405
Cdd:smart00532 317 KLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREI 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 500622385 406 HLPESCPVCASPVVMPEGEALARCSGGLyCAAQRIEAIRHFVSRKA 451
Cdd:smart00532 397 EMPTHCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-320 |
3.17e-160 |
|
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: 463.22 E-value: 3.17e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 8 EQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNV 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 88 FNQEDLFAFARRVEERLPnQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHsdhfEI 167
Cdd:cd00114 81 FDEEELRAFDERIKRFLG-EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLA----GA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 168 PRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHsLTTMHDSLQ 247
Cdd:cd00114 156 PETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500622385 248 WLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:cd00114 235 FLKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-321 |
7.50e-156 |
|
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: 452.57 E-value: 7.50e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 4 TSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLS 83
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 84 LGNVFNQEDLFAFARRVEERLPNQ-KVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHS 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALGNKeKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 163 DhfEIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPnHSL--T 240
Cdd:pfam01653 161 D--NPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEG-HELgfD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 241 TMHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:pfam01653 238 TQYQALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPA 317
|
.
gi 500622385 321 Q 321
Cdd:pfam01653 318 E 318
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
1-671 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 1117.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 1 MATTSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVP 80
Cdd:COG0272 1 MTPEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 81 MLSLGNVFNQEDLFAFARRVEERLPNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVL 160
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFLGDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 161 HSDHfeIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEpNHSLT 240
Cdd:COG0272 161 KGDD--VPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEVE-GLLPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 241 TMHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:COG0272 238 TQSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 321 QAALTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSA 400
Cdd:COG0272 318 EEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 401 DAEIVHLPESCPVCASPVVMPEGEALARCSGGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHL 480
Cdd:COG0272 398 DEKPFVMPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 481 heHRETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDI 560
Cdd:COG0272 478 --TKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 561 TAEWIADFFLAPHNIEVLDRLIAAGIHWDAPTAPTR--QPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTK 638
Cdd:COG0272 556 VAESIVEFFAEPHNRELIERLRAAGVNMEEEEAEAAadSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTD 635
|
650 660 670
....*....|....*....|....*....|...
gi 500622385 639 CVVAGEKAGSKLEKAAKLGIVVMNETDFLSLMA 671
Cdd:COG0272 636 YVVAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
2-672 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1045.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 2 ATTSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPM 81
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 82 LSLGNVFNQEDLFAFARRVEERLPNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLH 161
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLPDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 162 SDHfeiPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHSLTT 241
Cdd:PRK07956 161 GNE---PERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 242 MHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQ 321
Cdd:PRK07956 238 QSEALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 322 AALTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSAD 401
Cdd:PRK07956 318 EATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 402 AEIVHLPESCPVCASPVVMPEGEALARCSGGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLH 481
Cdd:PRK07956 398 EREIVMPTHCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 482 EhrETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDIT 561
Cdd:PRK07956 478 A--EDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 562 AEWIADFFLAPHNIEVLDRLIAAGIHWDAPTAPTrqPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVV 641
Cdd:PRK07956 556 AQSIVEFFAVEENRELIDELLEAGVNMEYKGEEV--DLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVV 633
|
650 660 670
....*....|....*....|....*....|.
gi 500622385 642 AGEKAGSKLEKAAKLGIVVMNETDFLSLMAN 672
Cdd:PRK07956 634 AGEAAGSKLAKAQELGIEVLDEEEFLRLLGE 664
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
13-666 |
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: 863.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 13 LIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNVFNQED 92
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 93 LFAFARRVEERLpNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHSDHFeiPRLLE 172
Cdd:TIGR00575 81 LAAFIKRIRRQL-GLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDNP--PERLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 173 VRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAqcePNHSLT--TMHDSLQWLT 250
Cdd:TIGR00575 158 VRGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLG---EGLELPdaTQYEALAWLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 251 QLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQAALTTVDQI 330
Cdd:TIGR00575 235 KWGFPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 331 DWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADAEIVHLPES 410
Cdd:TIGR00575 315 VVQVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 411 CPVCASPVVMPEGEALARCSgGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLHEhrETLLGI 490
Cdd:TIGR00575 395 CPSCGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKK--EDLLEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 491 EKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEWIADFFL 570
Cdd:TIGR00575 472 EGFGEKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFH 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 571 APHNIEVLDRLIAAGIHWDA-----PTAPTRQPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEK 645
Cdd:TIGR00575 552 DPNNRQLIKKLEELGVEMESlpekvNAELAGSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEK 631
|
650 660
....*....|....*....|.
gi 500622385 646 AGSKLEKAAKLGIVVMNETDF 666
Cdd:TIGR00575 632 AGSKLAKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
6-451 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 631.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 6 VIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLG 85
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 86 NVFNQEDLFAFARRVEERLPNQkVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHsdhF 165
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGSP-FAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLS---G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 166 EIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHSLTTMHDS 245
Cdd:smart00532 157 DVPERLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 246 LQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQAALT 325
Cdd:smart00532 237 LKWLKELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 326 TVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADAEIV 405
Cdd:smart00532 317 KLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREI 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 500622385 406 HLPESCPVCASPVVMPEGEALARCSGGLyCAAQRIEAIRHFVSRKA 451
Cdd:smart00532 397 EMPTHCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
8-677 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 620.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 8 EQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYpDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNV 87
Cdd:PRK14351 34 EQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAPMLSIDQS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 88 FNQEDLFAFARRVEERLpnQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHSDHfei 167
Cdd:PRK14351 113 GEADDVREFDERVRREV--GAVEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRGDY--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 168 PRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGI---AQCEPNHSltTMHD 244
Cdd:PRK14351 188 PDFLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVldaSELFDSHW--EELE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 245 SLQwltQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQAAL 324
Cdd:PRK14351 266 RFP---EWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 325 TTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADAEi 404
Cdd:PRK14351 343 TTIRDIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVVEKDSEGTFE- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 405 vhLPESCPVCASPVvmPEGEALARCSGGLYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLheHR 484
Cdd:PRK14351 422 --FPDTCPVCDSAV--ERDGPLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDL--TV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 485 ETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEW 564
Cdd:PRK14351 496 ADLAELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEE 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 565 IADFFLAPHNIEVLDRLIAAGIHWDAPTAPTRQPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGE 644
Cdd:PRK14351 576 IREFFDSERNRAVIDDLLDHGVDPQPAESEGGDALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGE 655
|
650 660 670
....*....|....*....|....*....|....
gi 500622385 645 KAG-SKLEKAAKLGIVVMNETDFLSLMANYGQTL 677
Cdd:PRK14351 656 NPGqSKRDDAEANDVPTLDEEEFEELLAERGVAL 689
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-320 |
3.17e-160 |
|
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: 463.22 E-value: 3.17e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 8 EQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNV 87
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 88 FNQEDLFAFARRVEERLPnQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHsdhfEI 167
Cdd:cd00114 81 FDEEELRAFDERIKRFLG-EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLA----GA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 168 PRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPNHsLTTMHDSLQ 247
Cdd:cd00114 156 PETLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGEAEGLG-PKTQSEALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500622385 248 WLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:cd00114 235 FLKEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-321 |
7.50e-156 |
|
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: 452.57 E-value: 7.50e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 4 TSVIEQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLS 83
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 84 LGNVFNQEDLFAFARRVEERLPNQ-KVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHS 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALGNKeKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 163 DhfEIPRLLEVRGEVLMPKSGFEKLNADQEAKGDKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEPnHSL--T 240
Cdd:pfam01653 161 D--NPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEG-HELgfD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 241 TMHDSLQWLTQLGFEIAERQYLCNSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPA 320
Cdd:pfam01653 238 TQYQALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPA 317
|
.
gi 500622385 321 Q 321
Cdd:pfam01653 318 E 318
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
8-670 |
1.97e-112 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 353.36 E-value: 1.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 8 EQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQALSKFQSVTHVVPMLSLGNV 87
Cdd:PRK14350 7 DEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPILSLDKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 88 FNQEDLFAFARRV--EERLPNQKVQYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLhSDHF 165
Cdd:PRK14350 87 YDLKLLKLWIEKMdlENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLFI-DEKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 166 EiprlLEVRGEVLMPKSGFEKLNADQEakgdKTFANPRNAAAGSLRQLDPNIAASRPLAFYAYGIAQCEpnHSLTTMHDS 245
Cdd:PRK14350 166 E----LVLRGEIYITKENFLKINKTLE----KPYTNARNLASGILRRIDSREVANFPLDIFVYDILYSS--LELKTNHDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 246 LQWLTQLGFEIAER-QYLC--NSIQEVQQRYEQIQKERPDLQVEIDGMVVKVDDLKQQQQLGFLSREPRWATAYKFPAQA 322
Cdd:PRK14350 236 FDKLKKFGFKVNPFcRFFDgkNSIEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFESLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 323 ALTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADA 402
Cdd:PRK14350 316 GFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVELVIEKLSVGFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 403 EIvhlPESCPVCASpVVMPEGEALArCSGGlYCAAQRIEAIRHFVSRKALDIEGLGDRWVESLLHLDLLKDVADIYHLHE 482
Cdd:PRK14350 396 KI---PDNCPSCKT-ALIKEGAHLF-CVNN-HCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYTFNF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 483 HRetLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARML----ANTFQTLEAL---KAADVEALKKTP 555
Cdd:PRK14350 470 DR--LINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLinnnLNSFDKISTLcqdREFALSKLLKIK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 556 DVGDITAEWIADFF---LAPHNIEVLDRLIAAGIHWDAPTAPTRQPLNGESWVLTGTLEQMTRDQATQMLQALGARVSGS 632
Cdd:PRK14350 548 GIGEKIALNIIEAFndkIILDKFNFFKNLGFKMEEDSINIDVENSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFNTC 627
|
650 660 670
....*....|....*....|....*....|....*...
gi 500622385 633 VSSKTKCVVAGEKAGSKLEKAAKLGIVVMNETDFLSLM 670
Cdd:PRK14350 628 VTKYLDFLLVGEKAGLKLKKANNLGIKIMSLFDIKSYV 665
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
8-587 |
9.11e-39 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 151.22 E-value: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 8 EQMRQLIQLIAKHNHAYYVMDQPTISDSEYDHLFHQLKALEEQYPDQVQPDSPTTKVGGQalskfqsVTHVVPMLSLGNV 87
Cdd:PRK08097 32 EEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVPLPPLNGK-------VLHPVAHTGVKKL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 88 FNQEDLfafARRVEERLPnqkvqYEVELKLDGLAISLWYENGVLTRGVTRGDGETGEDITQNVKTIRNLPKVLHsdhfEI 167
Cdd:PRK08097 105 ADKQAL---ARWMAGRSD-----LWVQPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLP----GA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 168 PRLLEVRGEVlmpksgFEKLNADQEAK--GdktfANPRNAAAGSLRQLDPNIAASRplafyaYGIAQCEPNHSLTTMHDS 245
Cdd:PRK08097 173 LANLVLQGEL------FLRREGHIQQQmgG----INARAKVAGLMMRKDPSPTLNQ------IGVFVWAWPDGPASMPER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 246 LQWLTQLGFEIAERqYL--CNSIQEVQQRYEQIQKERpdLQVEIDGMVVKVDDLKQQQQlgFLSREPRWATAYKFPAQAA 323
Cdd:PRK08097 237 LAQLATAGFPLTQR-YThpVKNAEEVARWRERWYRAP--LPFVTDGVVVRQAKEPPGRY--WQPGQGEWAVAWKYPPVQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 324 LTTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVtlhNIGEIHR---LDVRVGDTVSVYRTGDVIPKVEKV-WpefRS 399
Cdd:PRK08097 312 VAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRV---NIGSVRRwqqWDIAPGDQVLVSLAGQGIPRLDKVvW---RG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 400 ADAEIVHLPE-------SC----PVCaspvvmpEGEALARCS--GGlycaaqrieairhfvsRKALDIEGLGDRWVESLL 466
Cdd:PRK08097 386 AERTKPTPPDadrfhslSCfrasPGC-------QEQFLARLVwlSG----------------KQGLGLDGIGEGTWRALH 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 467 HLDLLKDVADIYHLHEhrETLLGIEKMGEKSVQNLIDAIEASKKTTLARFIYALGIRGVGETTARMLANTFQTLEALKAA 546
Cdd:PRK08097 443 QTGLFEHLFSWLALTP--EQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIPLPQAALNALDDRSWQQLLSRSEQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 500622385 547 DVEALkktPDVGDITAEWIADFFLAPHNIEVLDRLIAAGIH 587
Cdd:PRK08097 521 QWQQL---PGIGEGRARQLIAFLQHPEVKALADWLAAQGIT 558
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
325-402 |
5.04e-38 |
|
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: 135.57 E-value: 5.04e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500622385 325 TTVDQIDWQVGRTGTLTPVARLNPVFVGGVTVSNVTLHNIGEIHRLDVRVGDTVSVYRTGDVIPKVEKVWPEFRSADA 402
Cdd:pfam03120 2 TKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
599-669 |
5.35e-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: 101.40 E-value: 5.35e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500622385 599 LNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEKAGSKLE-----KAAKLGIVVMNETDFLSL 669
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
515-578 |
4.26e-21 |
|
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: 87.19 E-value: 4.26e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500622385 515 RFIYALGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEWIADFFLAPHNIEVL 578
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
599-669 |
2.53e-18 |
|
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.
Pssm-ID: 349383 [Multi-domain] Cd Length: 79 Bit Score: 79.95 E-value: 2.53e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500622385 599 LNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEKAG-SKLEKAAKLGIVVMNETDFLSL 669
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDL 77
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
598-670 |
6.64e-08 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 50.07 E-value: 6.64e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500622385 598 PLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTK-CVVAGEKAGSKLE--KAAKLGIVVMNETDFLSLM 670
Cdd:smart00292 3 LFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTtHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDCL 78
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
594-670 |
7.60e-08 |
|
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: 49.98 E-value: 7.60e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500622385 594 PTRQPLNGESWVLTGtLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEKAgSKLEKAAKLGIVVMNETDFLSLM 670
Cdd:pfam00533 1 PKEKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEART-KKYLKAKELGIPIVTEEWLLDCI 75
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
598-669 |
1.56e-07 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 53.63 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 598 PLNGESWVLTGTLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAG---------EKAGSKLEKAAKL-----GIVVMNE 663
Cdd:PRK06195 220 AFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAIDLkkkgqNIKFLNE 299
|
....*.
gi 500622385 664 TDFLSL 669
Cdd:PRK06195 300 EEFLQK 305
|
|
| HHH_5 |
pfam14520 |
Helix-hairpin-helix domain; |
516-563 |
5.19e-07 |
|
Helix-hairpin-helix domain;
Pssm-ID: 434010 [Multi-domain] Cd Length: 57 Bit Score: 47.10 E-value: 5.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500622385 516 FIYALGIRGVGETTARMLANT-FQTLEALKAADVEALKKTPDVGDITAE 563
Cdd:pfam14520 1 FEELLSISGIGPKTALALLSAgIGTVEDLAEADVDELAEIPGIGEKTAQ 49
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
411-435 |
3.26e-06 |
|
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: 43.96 E-value: 3.26e-06
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
605-667 |
5.88e-06 |
|
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: 44.44 E-value: 5.88e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500622385 605 VLTGTLEqMTRDQATQMLQALGARVSGSVSSKTKCVVA----GEKAGSKLEKAAKLGIVVMNEtDFL 667
Cdd:cd17747 7 ALIGKLS-KSKDELKKLIEKLGGKVASKVTKKVTLCIStkaeVEKMSKKMKEAKEAGVPVVSE-DFL 71
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
515-565 |
3.07e-04 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 42.47 E-value: 3.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 500622385 515 RFIYAlGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEWI 565
Cdd:COG1948 154 LYVVE-SLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERI 203
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
605-663 |
1.60e-03 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 37.34 E-value: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500622385 605 VLTGtLEQMTRDQATQMLQALGARVSGSVSSKTKCVVAGEKAGSK-LEKAAKLGIVVMNE 663
Cdd:cd00027 4 CFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKyYLAALAWGIPIVSP 62
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
509-568 |
1.61e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.78 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500622385 509 KKTTLA---RFIYAlGIRGVGETTARMLANTFQTLEALKAADVEALKKTPDVGDITAEWIADF 568
Cdd:PRK13766 705 KAMTLKeqqEYIVE-SLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRIREV 766
|
|
| |
