|
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: 1178.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 1 MSSS-ISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVP 79
Cdd:COG0272 1 MTPEeAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 80 MLSLDNAFSEEEFTAFNRRIKERLmSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLK 159
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFL-GDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 160 LRGD-YPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVaDGSIPED 238
Cdd:COG0272 160 LKGDdVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEV-EGLLPDT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 239 HYQQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQ 318
Cdd:COG0272 239 QSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 319 EEITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDD 398
Cdd:COG0272 319 EATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 399 ASDIEFPVTCPICDSHVEKVEGEAVARCTGGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILK 478
Cdd:COG0272 399 EKPFVMPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 479 QGHFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVAT 558
Cdd:COG0272 479 KEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 559 HVRGFFDEEHNLAVVNALIEQGVNWPALSAPSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALV 638
Cdd:COG0272 559 SIVEFFAEPHNRELIERLRAAGVNMEEEEAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVV 638
|
650 660 670
....*....|....*....|....*....|
gi 1889521512 639 AGEKAGSKLTKAQDLGIDILTEDELIELLK 668
Cdd:COG0272 639 AGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-670 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1149.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 1 MSSSISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPM 80
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 81 LSLDNAFSEEEFTAFNRRIKERLMsTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKL 160
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLP-DPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 161 RGDYPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPEDHY 240
Cdd:PRK07956 160 HGNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 241 QQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEE 320
Cdd:PRK07956 240 EALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 321 ITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDAS 400
Cdd:PRK07956 320 TTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 401 DIEFPVTCPICDSHVEKVEGEAVARCTGGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILKQG 480
Cdd:PRK07956 400 EIVMPTHCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 481 HFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHV 560
Cdd:PRK07956 480 DLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 561 RGFFDEEHNLAVVNALIEQGVNWpalsAPSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAG 640
Cdd:PRK07956 560 VEFFAVEENRELIDELLEAGVNM----EYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAG 635
|
650 660 670
....*....|....*....|....*....|
gi 1889521512 641 EKAGSKLTKAQDLGIDILTEDELIELLKKH 670
Cdd:PRK07956 636 EAAGSKLAKAQELGIEVLDEEEFLRLLGEG 665
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
12-663 |
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: 908.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 12 LRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNAFSEEE 91
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 92 FTAFNRRIkeRLMSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGD-YPKELEV 170
Cdd:TIGR00575 81 LAAFIKRI--RRQLGLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDnPPERLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 171 RGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPeDHYQQLEKLTDWG 250
Cdd:TIGR00575 159 RGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDA-TQYEALAWLKKWG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 251 LPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEEITQLLDVDFQ 330
Cdd:TIGR00575 238 FPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 331 VGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDASDIEFPVTCPI 410
Cdd:TIGR00575 318 VGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 411 CDSHVEKVEGEAVARCTgGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILKQGHFESLERMGP 490
Cdd:TIGR00575 398 CGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 491 KSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFDEEHNL 570
Cdd:TIGR00575 477 KSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 571 AVVNALIEQGVNWPALSAPSEEE---QPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAGSKL 647
Cdd:TIGR00575 557 QLIKKLEELGVEMESLPEKVNAElagSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKL 636
|
650
....*....|....*.
gi 1889521512 648 TKAQDLGIDILTEDEL 663
Cdd:TIGR00575 637 AKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
7-448 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 708.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 7 EQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNA 86
Cdd:smart00532 3 KEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLDNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 87 FSEEEFTAFNRRIKERLmsTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGDYPK 166
Cdd:smart00532 83 FDEDELRAFDERIEKAL--GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGDVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 167 ELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPEDHYQQLEKL 246
Cdd:smart00532 161 RLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEALKWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 247 TDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEEITQLLD 326
Cdd:smart00532 241 KELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 327 VDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDASDIEFPV 406
Cdd:smart00532 321 IIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMPT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1889521512 407 TCPICDSHVEKVEGEAVARCTGGLvCPAQRKQAIKHFASRKA 448
Cdd:smart00532 401 HCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
7-317 |
1.95e-178 |
|
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: 509.44 E-value: 1.95e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 7 EQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNA 86
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 87 FSEEEFTAFNRRIKERLMstDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGdYPK 166
Cdd:cd00114 81 FDEEELRAFDERIKRFLG--EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG-APE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 167 ELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLvADGSIPEDHYQQLEKL 246
Cdd:cd00114 158 TLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGE-AEGLGPKTQSEALAFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889521512 247 TDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPA 317
Cdd:cd00114 237 KEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
3-318 |
3.32e-163 |
|
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: 471.06 E-value: 3.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 3 SSISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLS 82
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 83 LDNAFSEEEFTAFNRRIKERLMSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRG 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALGNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 163 D-YPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPED-HY 240
Cdd:pfam01653 161 DnPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGFDtQY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889521512 241 QQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQ 318
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: 1178.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 1 MSSS-ISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVP 79
Cdd:COG0272 1 MTPEeAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 80 MLSLDNAFSEEEFTAFNRRIKERLmSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLK 159
Cdd:COG0272 81 MLSLDNAFSEEELRDFDRRVRKFL-GDEPVEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 160 LRGD-YPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVaDGSIPED 238
Cdd:COG0272 160 LKGDdVPEVLEVRGEVYMPKADFEALNEEREEAGEKPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGLGEV-EGLLPDT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 239 HYQQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQ 318
Cdd:COG0272 239 QSEALELLKEWGFPVNPERRVCKSIEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLGFTSRAPRWAIAYKFPAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 319 EEITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDD 398
Cdd:COG0272 319 EATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAGDVIPEVVGVVLEKRPGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 399 ASDIEFPVTCPICDSHVEKVEGEAVARCTGGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILK 478
Cdd:COG0272 399 EKPFVMPTHCPVCGSPLVREEGEAALRCTNGLSCPAQLKERLKHFASRKAMDIEGLGEKLIEQLVDAGLVKDPADLYRLT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 479 QGHFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVAT 558
Cdd:COG0272 479 KEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDALMAASEEELAAVDGIGPVVAE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 559 HVRGFFDEEHNLAVVNALIEQGVNWPALSAPSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALV 638
Cdd:COG0272 559 SIVEFFAEPHNRELIERLRAAGVNMEEEEAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVV 638
|
650 660 670
....*....|....*....|....*....|
gi 1889521512 639 AGEKAGSKLTKAQDLGIDILTEDELIELLK 668
Cdd:COG0272 639 AGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-670 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 1149.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 1 MSSSISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPM 80
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 81 LSLDNAFSEEEFTAFNRRIKERLMsTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKL 160
Cdd:PRK07956 81 LSLDNAFSEEELRAFDKRVRKRLP-DPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 161 RGDYPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPEDHY 240
Cdd:PRK07956 160 HGNEPERLEVRGEVFMPKADFEALNEERREEGEKPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGVGEVEGGELPDSQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 241 QQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEE 320
Cdd:PRK07956 240 EALEFLKAWGFPVNPYRKLCTSIEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFTAKAPRWAIAYKFPAEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 321 ITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDAS 400
Cdd:PRK07956 320 TTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDVIPEVVGVVLEKRPGDER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 401 DIEFPVTCPICDSHVEKVEGEAVARCTGGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILKQG 480
Cdd:PRK07956 400 EIVMPTHCPVCGSELVRVEGEAVLRCTNGLSCPAQLKERLIHFVSRNAMDIDGLGEKIIEQLFEKGLIHDPADLFKLTAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 481 HFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHV 560
Cdd:PRK07956 480 DLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALRAASEEELAAVEGVGEVVAQSI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 561 RGFFDEEHNLAVVNALIEQGVNWpalsAPSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAG 640
Cdd:PRK07956 560 VEFFAVEENRELIDELLEAGVNM----EYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAG 635
|
650 660 670
....*....|....*....|....*....|
gi 1889521512 641 EKAGSKLTKAQDLGIDILTEDELIELLKKH 670
Cdd:PRK07956 636 EAAGSKLAKAQELGIEVLDEEEFLRLLGEG 665
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
12-663 |
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: 908.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 12 LRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNAFSEEE 91
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 92 FTAFNRRIkeRLMSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGD-YPKELEV 170
Cdd:TIGR00575 81 LAAFIKRI--RRQLGLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAGDnPPERLEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 171 RGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPeDHYQQLEKLTDWG 250
Cdd:TIGR00575 159 RGEVFMPKEDFEALNEERREQGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGEGLELPDA-TQYEALAWLKKWG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 251 LPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEEITQLLDVDFQ 330
Cdd:TIGR00575 238 FPVSPHIRLCDSIEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFPAEEAQTKLLDVVVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 331 VGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDASDIEFPVTCPI 410
Cdd:TIGR00575 318 VGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEKRTGSERPIRFPTHCPS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 411 CDSHVEKVEGEAVARCTgGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILKQGHFESLERMGP 490
Cdd:TIGR00575 398 CGSPLVKIEEEAVIRCP-NLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYALKKEDLLELEGFGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 491 KSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFDEEHNL 570
Cdd:TIGR00575 477 KSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLDKLKAASLEELLSVEGVGPKVAESIVNFFHDPNNR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 571 AVVNALIEQGVNWPALSAPSEEE---QPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAGSKL 647
Cdd:TIGR00575 557 QLIKKLEELGVEMESLPEKVNAElagSPLAGKTFVLTGTLSQMSRDEAKELLENLGGKVASSVSKKTDYVIAGEKAGSKL 636
|
650
....*....|....*.
gi 1889521512 648 TKAQDLGIDILTEDEL 663
Cdd:TIGR00575 637 AKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
7-448 |
0e+00 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 708.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 7 EQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNA 86
Cdd:smart00532 3 KEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLDNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 87 FSEEEFTAFNRRIKERLmsTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGDYPK 166
Cdd:smart00532 83 FDEDELRAFDERIEKAL--GSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLSGDVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 167 ELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPEDHYQQLEKL 246
Cdd:smart00532 161 RLEVRGEVFMPKEDFLALNEELEEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRAFFYGLGTGEELFLPKTQSEALKWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 247 TDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEEITQLLD 326
Cdd:smart00532 241 KELGFPVSPHTRLCKNADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPAEEAETKLLD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 327 VDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDASDIEFPV 406
Cdd:smart00532 321 IIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVGVVKEKRPGDEREIEMPT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1889521512 407 TCPICDSHVEKVEGEAVARCTGGLvCPAQRKQAIKHFASRKA 448
Cdd:smart00532 401 HCPSCGSELVREEGEVDIRCPNPL-CPAQLIERIIHFASRKA 441
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
7-670 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 695.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 7 EQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHpEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNA 86
Cdd:PRK14351 34 EQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAPMLSIDQS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 87 FSEEEFTAFNRRIKERLmstDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGDYPK 166
Cdd:PRK14351 113 GEADDVREFDERVRREV---GAVEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLRGDYPD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 167 ELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYStglVADGSI-PEDHYQQLEK 245
Cdd:PRK14351 190 FLAVRGEVYMPKDAFQAYNRERIERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFD---VLDASElFDSHWEELER 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 246 LTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQEEITQLL 325
Cdd:PRK14351 267 FPEWGLRVTDRTERVDDIDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRWAFAYKFPARAEETTIR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 326 DVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVlERRPDdaSDIEFP 405
Cdd:PRK14351 347 DIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEEVV-EKDSE--GTFEFP 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 406 VTCPICDSHVEKvEGeAVARCTGGLVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFILKQGHFESL 485
Cdd:PRK14351 424 DTCPVCDSAVER-DG-PLAFCTGGLACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLADLYDLTVADLAEL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 486 ERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFD 565
Cdd:PRK14351 502 EGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMDADEEALRAVDDVGPTVAEEIREFFD 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 566 EEHNLAVVNALIEQGVNwPAlSAPSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAG- 644
Cdd:PRK14351 582 SERNRAVIDDLLDHGVD-PQ-PAESEGGDALDGLTFVFTGSLSGYTRSEAQELVEAHGGNATGSVSGNTDYLVVGENPGq 659
|
650 660
....*....|....*....|....*.
gi 1889521512 645 SKLTKAQDLGIDILTEDELIELLKKH 670
Cdd:PRK14351 660 SKRDDAEANDVPTLDEEEFEELLAER 685
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
7-317 |
1.95e-178 |
|
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: 509.44 E-value: 1.95e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 7 EQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLSLDNA 86
Cdd:cd00114 1 ERIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 87 FSEEEFTAFNRRIKERLMstDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGdYPK 166
Cdd:cd00114 81 FDEEELRAFDERIKRFLG--EEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAG-APE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 167 ELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLvADGSIPEDHYQQLEKL 246
Cdd:cd00114 158 TLEVRGEVFMPKADFEALNKEREERGEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGLGE-AEGLGPKTQSEALAFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889521512 247 TDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPA 317
Cdd:cd00114 237 KEWGFPVSPETRLCKNIEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYKFPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
3-318 |
3.32e-163 |
|
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: 471.06 E-value: 3.32e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 3 SSISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPMLS 82
Cdd:pfam01653 1 EEAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 83 LDNAFSEEEFTAFNRRIKERLMSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRG 162
Cdd:pfam01653 81 LDNAFNLDELQAFIERIRRALGNKEKVEYVVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 163 D-YPKELEVRGEVFMDSAGFDKLNTEAQKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTGLVADGSIPED-HY 240
Cdd:pfam01653 161 DnPPERLEVRGEVFMPKEDFEALNEERLEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGLGLLEGHELGFDtQY 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889521512 241 QQLEKLTDWGLPLCPETKLVEGPKAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFPAQ 318
Cdd:pfam01653 241 QALAFLKSLGFPVSPLLALCDGIEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTAKAPRWAIAYKFPAE 318
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
1-659 |
7.02e-121 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 374.93 E-value: 7.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 1 MSSSISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGAALSKFEQVAHQVPM 80
Cdd:PRK14350 1 MSKDIQDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 81 LSLDNAFSEEEFTAFNRRIK-ERLMSTDELTFCCEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLK 159
Cdd:PRK14350 81 LSLDKVYDLKLLKLWIEKMDlENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 160 LrgDYPKELEVRGEVFMDSAGFDKLNteaqKRGEKVFVNPRNAAAGSLRQLDSKITAKRPLMFYAYSTgLVADGSIPEDH 239
Cdd:PRK14350 161 I--DEKVELVLRGEIYITKENFLKIN----KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDI-LYSSLELKTNH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 240 yQQLEKLTDWGLPLCPETKLVEGP---KAALDYYSDILTRRGELKYEIDGVVIKINQKALQERLGFVARAPRWAIAYKFP 316
Cdd:PRK14350 234 -DAFDKLKKFGFKVNPFCRFFDGKnsiEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKWSMAYKFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 317 AQEEITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQItQVVLERRp 396
Cdd:PRK14350 313 SLSGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAV-ELVIEKL- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 397 dDASDIEFPVTCPICDSHVEKvEGeAVARCTGGlVCPAQRKQAIKHFASRKALDIDGLGDKIVDQLVDRELIKTPADLFI 476
Cdd:PRK14350 391 -SVGFFKIPDNCPSCKTALIK-EG-AHLFCVNN-HCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDLYT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 477 LKQGHFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLENII-------NASIDSLTQV 549
Cdd:PRK14350 467 FNFDRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLINNNLNSFDKIstlcqdrEFALSKLLKI 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 550 SDVGEIVATHVRGFFDEEHNLAVVNALIEQGVNWPALS-APSEEEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSG 628
Cdd:PRK14350 547 KGIGEKIALNIIEAFNDKIILDKFNFFKNLGFKMEEDSiNIDVENSFLFGKKFCITGSFNGYSRSVLIDKLTKKGAIFNT 626
|
650 660 670
....*....|....*....|....*....|.
gi 1889521512 629 SVSAKTDALVAGEKAGSKLTKAQDLGIDILT 659
Cdd:PRK14350 627 CVTKYLDFLLVGEKAGLKLKKANNLGIKIMS 657
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
321-399 |
3.13e-44 |
|
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: 152.52 E-value: 3.13e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889521512 321 ITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNATLHNSDEVARLGVKVGDTVIIRRAGDVIPQITQVVLERRPDDA 399
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVLEKRPGDE 79
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
5-581 |
4.68e-39 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 151.99 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 5 ISEQVNHLRTTLEQHNYNYYVLDTPSIPDSEYDRLLRELSALEMQHPEFLTADSPTQKVGGaalskfeQVAHQVPMLSLD 84
Cdd:PRK08097 30 AQEEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVPLPPLNG-------KVLHPVAHTGVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 85 NAFSEeefTAFNRRIKERlmstDELTFccEPKLDGLAVSIIYRDGVLVQAATRGDGFTGENITQNVKTIRNVPLKLRGDy 164
Cdd:PRK08097 103 KLADK---QALARWMAGR----SDLWV--QPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLPGA- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 165 PKELEVRGEVFMdsagfdKLNTEAQKR--GekvfVNPRNAAAGSL-RQLDSKITAKRPLMFYAYSTGlvadgsiPEDHYQ 241
Cdd:PRK08097 173 LANLVLQGELFL------RREGHIQQQmgG----INARAKVAGLMmRKDPSPTLNQIGVFVWAWPDG-------PASMPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 242 QLEKLTDWGLPLCPE-TKLVEGPKAA----LDYYsdiltrRGELKYEIDGVVIKINQKALQERlgFVARAPRWAIAYKFP 316
Cdd:PRK08097 236 RLAQLATAGFPLTQRyTHPVKNAEEVarwrERWY------RAPLPFVTDGVVVRQAKEPPGRY--WQPGQGEWAVAWKYP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 317 AQEEITQLLDVDFQVGRTGAITPVARLKPVFVGGVTVSNAtlhNSDEVAR---LGVKVGDTVIIRRAGDVIPQITQVVLe 393
Cdd:PRK08097 308 PVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRV---NIGSVRRwqqWDIAPGDQVLVSLAGQGIPRLDKVVW- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 394 rRPDDASDIEFP-------VTC----PICDSHVekvegeaVARctggLVCpaqrkqaikhFASRKALDIDGLGDKIVDQL 462
Cdd:PRK08097 384 -RGAERTKPTPPdadrfhsLSCfrasPGCQEQF-------LAR----LVW----------LSGKQGLGLDGIGEGTWRAL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 463 VDRELIKTPADLFILKQGHFESLERMGPKSAKNLVTALEEAKGTTLAKFLYSLGIREAGEATAQNLANHFLTLeniINAS 542
Cdd:PRK08097 442 HQTGLFEHLFSWLALTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIPLPQAALNALDDRSWQQL---LSRS 518
|
570 580 590
....*....|....*....|....*....|....*....
gi 1889521512 543 IDSLTQVSDVGEIVATHVRGFFDEEHNLAVVNALIEQGV 581
Cdd:PRK08097 519 EQQWQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQGI 557
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
596-666 |
7.33e-25 |
|
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: 98.32 E-value: 7.33e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889521512 596 LAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAGSKLT-----KAQDLGIDILTEDELIEL 666
Cdd:cd17748 1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFLDL 76
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
596-668 |
1.29e-21 |
|
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: 89.19 E-value: 1.29e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889521512 596 LAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAG-SKLTKAQDLGIDILTEDELIELLK 668
Cdd:cd17752 6 LEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
510-573 |
4.63e-20 |
|
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: 84.11 E-value: 4.63e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889521512 510 KFLYSLGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFDEEHNLAVV 573
Cdd:pfam12826 1 RLLFALGIRHVGETTAKLLARRFGSLDALAEASLEELLEVDDIGPEIAQSIVEFFADPANRELI 64
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
595-667 |
6.12e-12 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 61.62 E-value: 6.12e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889521512 595 PLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAK-TDALVAGEKAGSKLT--KAQDLGIDILTEDELIELL 667
Cdd:smart00292 3 LFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLEllKAIALGIPIVKEEWLLDCL 78
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
591-667 |
1.00e-11 |
|
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: 60.77 E-value: 1.00e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889521512 591 EEEQPLAGLTYVLTGtLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAGEKAgSKLTKAQDLGIDILTEDELIELL 667
Cdd:pfam00533 1 PKEKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEART-KKYLKAKELGIPIVTEEWLLDCI 75
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
596-668 |
9.29e-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: 52.53 E-value: 9.29e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889521512 596 LAGLTYVLTGTLnTLNRNDAKARLQQLGAKVSGSVSAKTDALVA----GEKAGSKLTKAQDLGIDILTEDELIELLK 668
Cdd:cd17747 1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCIStkaeVEKMSKKMKEAKEAGVPVVSEDFLEDCIK 76
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
407-433 |
7.32e-08 |
|
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor. This family is a small zinc binding motif that is presumably DNA binding. IT is found only in NAD dependent DNA ligases.
Pssm-ID: 460812 [Multi-domain] Cd Length: 26 Bit Score: 48.58 E-value: 7.32e-08
10 20
....*....|....*....|....*..
gi 1889521512 407 TCPICDSHVEKVEGEAVARCTgGLVCP 433
Cdd:pfam03119 1 HCPVCGSPLVREEGEAALRCT-NLSCP 26
|
|
| PRK06195 |
PRK06195 |
DNA polymerase III subunit epsilon; Validated |
592-669 |
8.89e-07 |
|
DNA polymerase III subunit epsilon; Validated
Pssm-ID: 235735 [Multi-domain] Cd Length: 309 Bit Score: 51.32 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889521512 592 EEQPLAGLTYVLTGTLNTLNRNDAKARLQQLGAKVSGSVSAKTDALVAG---------EKAGSKLTKAQDL-----GIDI 657
Cdd:PRK06195 217 GFTAFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnrEEMSNKLKKAIDLkkkgqNIKF 296
|
90
....*....|..
gi 1889521512 658 LTEDELIELLKK 669
Cdd:PRK06195 297 LNEEEFLQKCKE 308
|
|
| MUS81 |
COG1948 |
ERCC4-type crossover junction endonuclease [Replication, recombination and repair]; |
512-567 |
2.41e-05 |
|
ERCC4-type crossover junction endonuclease [Replication, recombination and repair];
Pssm-ID: 441551 [Multi-domain] Cd Length: 214 Bit Score: 45.94 E-value: 2.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1889521512 512 LYSL-GIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFDEE 567
Cdd:COG1948 154 LYVVeSLPGIGPKLARRLLEHFGSVEAVFNASEEELMKVEGIGEKTAERIREVLDSE 210
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
502-567 |
4.45e-05 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 46.79 E-value: 4.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889521512 502 EAKGTTLA---KFLYSlGIREAGEATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVRGFFDEE 567
Cdd:PRK13766 703 EKKAMTLKeqqEYIVE-SLPDVGPVLARNLLEHFGSVEAVMTASEEELMEVEGIGEKTAKRIREVVTSE 770
|
|
| DisA |
COG1623 |
c-di-AMP synthetase DisA, contains DisA_N, linker and DNA-binding domains [Signal transduction ... |
523-561 |
1.79e-03 |
|
c-di-AMP synthetase DisA, contains DisA_N, linker and DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441230 [Multi-domain] Cd Length: 353 Bit Score: 40.89 E-value: 1.79e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1889521512 523 ATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVR 561
Cdd:COG1623 299 AVIENLVEHFGSLQKLLAASIEELDDVEGIGEVRARAIR 337
|
|
| PRK13482 |
PRK13482 |
DNA integrity scanning protein DisA; Provisional |
523-561 |
7.07e-03 |
|
DNA integrity scanning protein DisA; Provisional
Pssm-ID: 237395 [Multi-domain] Cd Length: 352 Bit Score: 38.99 E-value: 7.07e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1889521512 523 ATAQNLANHFLTLENIINASIDSLTQVSDVGEIVATHVR 561
Cdd:PRK13482 298 AVIENLVEHFGSLQGLLAASIEDLDEVEGIGEVRARAIR 336
|
|
| |
