|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
2-687 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 734.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 2 SDEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVL 81
Cdd:COG0272 3 PEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 82 SLDKCYSIDSLENWI-----FKNGQKttniFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPL 156
Cdd:COG0272 83 SLDNAFSEEELRDFDrrvrkFLGDEP----VEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 157 KI---DFKEKIAIRGEIFIKKGDFTIYNSK-YADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIES 229
Cdd:COG0272 159 RLkgdDVPEVLEVRGEVYMPKADFEALNEErEEAGekPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGlGEVEGLLPDT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 230 HLENLLLLKKLGFPLNDEIgffsdSRVDTttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELG 309
Cdd:COG0272 239 QSEALELLKEWGFPVNPER-----RVCKS------------IEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 310 YTQHHPRWAIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRG 389
Cdd:COG0272 302 FTSRAPRWAIAYKFPAEEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 390 DVIPAVEKVIEK---GSSPsPYKIADACPSCKSKLVKE--GAHLFCLNE-ECPARLLGTLQFFVGRDQMDIETLGDKTLE 463
Cdd:COG0272 382 DVIPEVVGVVLEkrpGDEK-PFVMPTHCPVCGSPLVREegEAALRCTNGlSCPAQLKERLKHFASRKAMDIEGLGEKLIE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 464 FLFNKGFVRYIYDLYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDEIvn 543
Cdd:COG0272 461 QLVDAGLVKDPADLYRLTKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDAL-- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 544 icsSNAgsdlfapSPEDfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFETKinEQDQNINRFLSGTKWVITG 623
Cdd:COG0272 539 ---MAA-------SEEE-LAAVDGIGPVVAESIVEFFAEPHNRELIERLRAAGVNMEEE--EAEAAADSPLAGKTFVLTG 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167348137 624 SFENFNpREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEFLLIIE 687
Cdd:COG0272 606 TLETMT-RDEAKELIEALGGKVSGSVSKKTDYVVAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-687 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 678.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 1 MSDEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPV 80
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 81 LSLDKCYSIDSLENWIfKNGQKT--TNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI 158
Cdd:PRK07956 81 LSLDNAFSEEELRAFD-KRVRKRlpDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 159 --DFKEKIAIRGEIFIKKGDFTIYNSKY-ADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE--AFLEQLKIESHL 231
Cdd:PRK07956 160 hgNEPERLEVRGEVFMPKADFEALNEERrEEGekPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGvgEVEGGELPDSQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 232 ENLLLLKKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYT 311
Cdd:PRK07956 240 EALEFLKAWGFPVNPYRKLCTS-----------------IEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 312 QHHPRWAIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDV 391
Cdd:PRK07956 303 AKAPRWAIAYKFPAEEATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 392 IPAVEKVIE---KGSSpSPYKIADACPSCKSKLVK--EGAHLFCLNEE-CPARLLGTLQFFVGRDQMDIETLGDKTLEFL 465
Cdd:PRK07956 383 IPEVVGVVLekrPGDE-REIVMPTHCPVCGSELVRveGEAVLRCTNGLsCPAQLKERLIHFVSRNAMDIDGLGEKIIEQL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 466 FNKGFVRYIYDLYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDEIVnic 545
Cdd:PRK07956 462 FEKGLIHDPADLFKLTAEDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALR--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 546 ssnagsdlfAPSPEDfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFETKINEQDqninrfLSGTKWVITGSF 625
Cdd:PRK07956 539 ---------AASEEE-LAAVEGVGEVVAQSIVEFFAVEENRELIDELLEAGVNMEYKGEEVD------LAGKTVVLTGTL 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167348137 626 ENFnPREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEFLLIIE 687
Cdd:PRK07956 603 EQL-SRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAGSKLAKAQELGIEVLDEEEFLRLLG 663
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
12-682 |
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: 666.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 12 LREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLDKCYSIDS 91
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 92 LENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKID---FKEKIAIRG 168
Cdd:TIGR00575 81 LAAFIKRIRRQLGLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAgdnPPERLEVRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 169 EIFIKKGDF-TIYNSKYADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIESHLENLLLLKKLGFPL 244
Cdd:TIGR00575 161 EVFMPKEDFeALNEERREQGekPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGlGEGLELPDATQYEALAWLKKWGFPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 245 NDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRWAIAYKFD 324
Cdd:TIGR00575 241 SPHIRLCDS-----------------IEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 325 APLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEKVIEK--- 401
Cdd:TIGR00575 304 AEEAQTKLLDVVVQVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEkrt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 402 GSSPsPYKIADACPSCKSKLVK--EGAHLFCLNEECPARLLGTLQFFVGRDQMDIETLGDKTLEFLFNKGFVRYIYDLYS 479
Cdd:TIGR00575 384 GSER-PIRFPTHCPSCGSPLVKieEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 480 FDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDeivnicssnagsDLFAPSPE 559
Cdd:TIGR00575 463 LKKEDLLELEGFGEKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLD------------KLKAASLE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 560 DFFAnIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFE-TKINEQDQNINRFLSGTKWVITGSFENFNpREKAAELI 638
Cdd:TIGR00575 531 ELLS-VEGVGPKVAESIVNFFHDPNNRQLIKKLEELGVEMEsLPEKVNAELAGSPLAGKTFVLTGTLSQMS-RDEAKELL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1167348137 639 KKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEF 682
Cdd:TIGR00575 609 ENLGGKVASSVSKKTDYVIAGEKAGSKLAKAQELGIPIINEEEL 652
|
|
| LIGANc |
smart00532 |
Ligase N family; |
5-450 |
1.83e-165 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 482.51 E-value: 1.83e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 5 VRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLD 84
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 85 KCYSIDSLENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI--DFKE 162
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLsgDVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 163 KIAIRGEIFIKKGDFTIYN-SKYADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCY--EAFLEQLKIESHLENLLLL 237
Cdd:smart00532 161 RLEVRGEVFMPKEDFLALNeELEEEGekPFANPRNAAAGSLRQLDPRITAKRKLRAFFYglGTGEELFLPKTQSEALKWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 238 KKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRW 317
Cdd:smart00532 241 KELGFPVSPHTRLCKN-----------------ADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 318 AIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEK 397
Cdd:smart00532 304 AIAYKFPAEEAETKLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167348137 398 VIEKGSSPS--PYKIADACPSCKSKLVKEG--AHLFCLNEECPARLLGTLQFFVGRD 450
Cdd:smart00532 384 VVKEKRPGDerEIEMPTHCPSCGSELVREEgeVDIRCPNPLCPAQLIERIIHFASRK 440
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-325 |
5.52e-119 |
|
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: 358.44 E-value: 5.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 8 KIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLDKCY 87
Cdd:cd00114 2 RIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 88 SIDSLENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKIDF-KEKIAI 166
Cdd:cd00114 82 DEEELRAFDERIKRFLGEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAGaPETLEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 167 RGEIFIKKGDFTIYNSKYA---DGIYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIESHLENLLLLKKLGF 242
Cdd:cd00114 162 RGEVFMPKADFEALNKEREergEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGlGEAEGLGPKTQSEALAFLKEWGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 243 PLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRWAIAYK 322
Cdd:cd00114 242 PVSPETRLCKN-----------------IEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYK 304
|
...
gi 1167348137 323 FDA 325
Cdd:cd00114 305 FPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-325 |
2.33e-115 |
|
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: 349.34 E-value: 2.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 4 EVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSL 83
Cdd:pfam01653 2 EAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 84 DKCYSIDSLENWIFKNGQKTTNIFELI--VEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKIDFK 161
Cdd:pfam01653 82 DNAFNLDELQAFIERIRRALGNKEKVEyvVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 162 ---EKIAIRGEIFIKKGDFTIYNS---KYADGIYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQ--LKIESHLE 232
Cdd:pfam01653 162 nppERLEVRGEVFMPKEDFEALNEerlEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGlGLLEGheLGFDTQYQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 233 NLLLLKKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQ 312
Cdd:pfam01653 242 ALAFLKSLGFPVSPLLALCDG-----------------IEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTA 304
|
330
....*....|...
gi 1167348137 313 HHPRWAIAYKFDA 325
Cdd:pfam01653 305 KAPRWAIAYKFPA 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lig |
COG0272 |
NAD-dependent DNA ligase [Replication, recombination and repair]; |
2-687 |
0e+00 |
|
NAD-dependent DNA ligase [Replication, recombination and repair];
Pssm-ID: 440042 [Multi-domain] Cd Length: 668 Bit Score: 734.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 2 SDEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVL 81
Cdd:COG0272 3 PEEAKERIEELREELRRHNYRYYVLDAPEISDAEYDALLRELQALEAEHPELITPDSPTQRVGGAPLEGFAKVRHAVPML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 82 SLDKCYSIDSLENWI-----FKNGQKttniFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPL 156
Cdd:COG0272 83 SLDNAFSEEELRDFDrrvrkFLGDEP----VEYVCELKIDGLAISLRYENGRLVRAATRGDGTVGEDVTANVRTIRSIPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 157 KI---DFKEKIAIRGEIFIKKGDFTIYNSK-YADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIES 229
Cdd:COG0272 159 RLkgdDVPEVLEVRGEVYMPKADFEALNEErEEAGekPFANPRNAAAGSLRQLDPKITAKRPLDFFAYGlGEVEGLLPDT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 230 HLENLLLLKKLGFPLNDEIgffsdSRVDTttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELG 309
Cdd:COG0272 239 QSEALELLKEWGFPVNPER-----RVCKS------------IEEVLAYIEEWEEKRHSLPYEIDGVVIKVNDLALQERLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 310 YTQHHPRWAIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRG 389
Cdd:COG0272 302 FTSRAPRWAIAYKFPAEEATTKLLDIEVQVGRTGALTPVARLEPVFVAGVTVSRATLHNEDEIERKDVRIGDTVVVRKAG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 390 DVIPAVEKVIEK---GSSPsPYKIADACPSCKSKLVKE--GAHLFCLNE-ECPARLLGTLQFFVGRDQMDIETLGDKTLE 463
Cdd:COG0272 382 DVIPEVVGVVLEkrpGDEK-PFVMPTHCPVCGSPLVREegEAALRCTNGlSCPAQLKERLKHFASRKAMDIEGLGEKLIE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 464 FLFNKGFVRYIYDLYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDEIvn 543
Cdd:COG0272 461 QLVDAGLVKDPADLYRLTKEDLLGLERMGEKSAQNLLAAIEKSKKTPLARFLFALGIRHVGETTAKLLARHFGSLDAL-- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 544 icsSNAgsdlfapSPEDfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFETKinEQDQNINRFLSGTKWVITG 623
Cdd:COG0272 539 ---MAA-------SEEE-LAAVDGIGPVVAESIVEFFAEPHNRELIERLRAAGVNMEEE--EAEAAADSPLAGKTFVLTG 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167348137 624 SFENFNpREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEFLLIIE 687
Cdd:COG0272 606 TLETMT-RDEAKELIEALGGKVSGSVSKKTDYVVAGENAGSKLDKAEELGVPILDEAEFLELLG 668
|
|
| ligA |
PRK07956 |
NAD-dependent DNA ligase LigA; Validated |
1-687 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Validated
Pssm-ID: 236137 [Multi-domain] Cd Length: 665 Bit Score: 678.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 1 MSDEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPV 80
Cdd:PRK07956 1 TMEEAKKRIEELREELNHHAYAYYVLDAPSISDAEYDRLYRELVALEAEHPELITPDSPTQRVGGAPLDGFEKVRHLVPM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 81 LSLDKCYSIDSLENWIfKNGQKT--TNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI 158
Cdd:PRK07956 81 LSLDNAFSEEELRAFD-KRVRKRlpDPPLTYLCELKIDGLAVSLLYENGVLVRAATRGDGTTGEDITANVRTIRSIPLRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 159 --DFKEKIAIRGEIFIKKGDFTIYNSKY-ADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE--AFLEQLKIESHL 231
Cdd:PRK07956 160 hgNEPERLEVRGEVFMPKADFEALNEERrEEGekPFANPRNAAAGSLRQLDPKITAKRPLSFFAYGvgEVEGGELPDSQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 232 ENLLLLKKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYT 311
Cdd:PRK07956 240 EALEFLKAWGFPVNPYRKLCTS-----------------IEEVLAFYEEIEEERHDLPYDIDGVVIKVDDLALQEELGFT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 312 QHHPRWAIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDV 391
Cdd:PRK07956 303 AKAPRWAIAYKFPAEEATTKLLDIEVQVGRTGAVTPVARLEPVEVAGVTVSRATLHNADEIERKDIRIGDTVVVRRAGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 392 IPAVEKVIE---KGSSpSPYKIADACPSCKSKLVK--EGAHLFCLNEE-CPARLLGTLQFFVGRDQMDIETLGDKTLEFL 465
Cdd:PRK07956 383 IPEVVGVVLekrPGDE-REIVMPTHCPVCGSELVRveGEAVLRCTNGLsCPAQLKERLIHFVSRNAMDIDGLGEKIIEQL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 466 FNKGFVRYIYDLYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDEIVnic 545
Cdd:PRK07956 462 FEKGLIHDPADLFKLTAEDLLGLEGFGEKSAQNLLDAIEKSKETSLARFLYALGIRHVGEKAAKALARHFGSLEALR--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 546 ssnagsdlfAPSPEDfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFETKINEQDqninrfLSGTKWVITGSF 625
Cdd:PRK07956 539 ---------AASEEE-LAAVEGVGEVVAQSIVEFFAVEENRELIDELLEAGVNMEYKGEEVD------LAGKTVVLTGTL 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167348137 626 ENFnPREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEFLLIIE 687
Cdd:PRK07956 603 EQL-SRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAGSKLAKAQELGIEVLDEEEFLRLLG 663
|
|
| dnlj |
TIGR00575 |
DNA ligase, NAD-dependent; All proteins in this family with known functions are NAD-dependent ... |
12-682 |
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: 666.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 12 LREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLDKCYSIDS 91
Cdd:TIGR00575 1 LRKLIRHHDYRYYVLDEPSISDAEYDRLYRELQELEEKHPELITPDSPTQRVGAAPLSRFPKVRHSTPMLSLDNAFDEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 92 LENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKID---FKEKIAIRG 168
Cdd:TIGR00575 81 LAAFIKRIRRQLGLKVEYVVEPKIDGLSVSLTYENGVLVRALTRGDGTVGEDVTANVRTIRSIPLRLAgdnPPERLEVRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 169 EIFIKKGDF-TIYNSKYADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIESHLENLLLLKKLGFPL 244
Cdd:TIGR00575 161 EVFMPKEDFeALNEERREQGekPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGlGEGLELPDATQYEALAWLKKWGFPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 245 NDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRWAIAYKFD 324
Cdd:TIGR00575 241 SPHIRLCDS-----------------IEEVLEYYREIEEKRDSLPYEIDGVVVKVDDLALQDELGFTSKAPRWAIAYKFP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 325 APLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEKVIEK--- 401
Cdd:TIGR00575 304 AEEAQTKLLDVVVQVGRTGAITPVAKLEPVFVAGTTVSRATLHNEDEIEELDIRIGDTVVVRKAGDVIPKVVRVLLEkrt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 402 GSSPsPYKIADACPSCKSKLVK--EGAHLFCLNEECPARLLGTLQFFVGRDQMDIETLGDKTLEFLFNKGFVRYIYDLYS 479
Cdd:TIGR00575 384 GSER-PIRFPTHCPSCGSPLVKieEEAVIRCPNLNCPAQRVERIKHFASRNAMDIEGLGDKVIEQLFEKKLVRSVADLYA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 480 FDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDeivnicssnagsDLFAPSPE 559
Cdd:TIGR00575 463 LKKEDLLELEGFGEKSAQNLLNAIEKSKEKPLARLLFALGIRHVGEVTAKNLAKHFGTLD------------KLKAASLE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 560 DFFAnIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFE-TKINEQDQNINRFLSGTKWVITGSFENFNpREKAAELI 638
Cdd:TIGR00575 531 ELLS-VEGVGPKVAESIVNFFHDPNNRQLIKKLEELGVEMEsLPEKVNAELAGSPLAGKTFVLTGTLSQMS-RDEAKELL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1167348137 639 KKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEF 682
Cdd:TIGR00575 609 ENLGGKVASSVSKKTDYVIAGEKAGSKLAKAQELGIPIINEEEL 652
|
|
| ligA |
PRK14350 |
NAD-dependent DNA ligase LigA; Provisional |
1-676 |
0e+00 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 172826 [Multi-domain] Cd Length: 669 Bit Score: 547.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 1 MSDEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPV 80
Cdd:PRK14350 1 MSKDIQDEILDLKKLIRKWDKEYYVDSSPSVEDFTYDKALLRLQELESKYPEYKTLDSPTLKFGSDLLNDFKEVEHSFPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 81 LSLDKCYSIDSLENWIFK---NGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLK 157
Cdd:PRK14350 81 LSLDKVYDLKLLKLWIEKmdlENSNLGFDFGISVEPKIDGCSIVLYYKDGILEKALTRGDGRFGNDVTENVRTIRNVPLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 158 IDFKEKIAIRGEIFIKKGDFTIYNsKYADGIYSNPRNLASGCVRRLRSSETALFPLNIFCYEAFLEQLKIESHLENLLLL 237
Cdd:PRK14350 161 IDEKVELVLRGEIYITKENFLKIN-KTLEKPYTNARNLASGILRRIDSREVANFPLDIFVYDILYSSLELKTNHDAFDKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 238 KKLGFPLNDEIGFFSDsrvdtttlpfKNhfigKISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRW 317
Cdd:PRK14350 240 KKFGFKVNPFCRFFDG----------KN----SIEEILNYVKDIEKKRNSFEYEIDGVVLKVSDFALREILGYTSHHPKW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 318 AIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEK 397
Cdd:PRK14350 306 SMAYKFESLSGFSKVNDIVVQVGRSGKITPVANIEKVFVAGAFITNASLHNQDYIDSIGLNVGDVVKISRRGDVIPAVEL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 398 VIEKGSSPSpYKIADACPSCKSKLVKEGAHLFCLNEECPARLLGTLQFFVGRDQMDIETLGDKTLEFLFNKGFVRYIYDL 477
Cdd:PRK14350 386 VIEKLSVGF-FKIPDNCPSCKTALIKEGAHLFCVNNHCPSVIVERIKYFCSKKCMNIVGLSDKTIEFLFEKKFISSEIDL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 478 YSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEIL-TKKFKNIDEIVNICSSNAgsdlFAP 556
Cdd:PRK14350 465 YTFNFDRLINLKGFKDKRINNLKRSIEASKKRPFSKLLLSMGIKDLGENTILLLiNNNLNSFDKISTLCQDRE----FAL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 557 SPedfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFEtKINEQDQNINRFLSGTKWVITGSFENFNpREKAAE 636
Cdd:PRK14350 541 SK---LLKIKGIGEKIALNIIEAFNDKIILDKFNFFKNLGFKME-EDSINIDVENSFLFGKKFCITGSFNGYS-RSVLID 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1167348137 637 LIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINI 676
Cdd:PRK14350 616 KLTKKGAIFNTCVTKYLDFLLVGEKAGLKLKKANNLGIKI 655
|
|
| LIGANc |
smart00532 |
Ligase N family; |
5-450 |
1.83e-165 |
|
Ligase N family;
Pssm-ID: 214709 [Multi-domain] Cd Length: 441 Bit Score: 482.51 E-value: 1.83e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 5 VRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLD 84
Cdd:smart00532 1 AQKEISELRKLLNQHDYRYYVLDAPIISDAEYDRLMRELKELEEKHPELKTPDSPTQRVGGKPLEGFNKVRHPVPMLSLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 85 KCYSIDSLENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI--DFKE 162
Cdd:smart00532 81 NAFDEDELRAFDERIEKALGSPFAYVVEPKIDGLSVSLLYENGKLVQAATRGDGTVGEDVTQNVKTIRSIPLRLsgDVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 163 KIAIRGEIFIKKGDFTIYN-SKYADG--IYSNPRNLASGCVRRLRSSETALFPLNIFCY--EAFLEQLKIESHLENLLLL 237
Cdd:smart00532 161 RLEVRGEVFMPKEDFLALNeELEEEGekPFANPRNAAAGSLRQLDPRITAKRKLRAFFYglGTGEELFLPKTQSEALKWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 238 KKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRW 317
Cdd:smart00532 241 KELGFPVSPHTRLCKN-----------------ADEVIEYYEEWEEKRAELPYEIDGVVVKVDDLALQRELGFTSKAPRW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 318 AIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEK 397
Cdd:smart00532 304 AIAYKFPAEEAETKLLDIIVQVGRTGKITPVAELEPVFLAGSTVSRATLHNEDEIEEKDIRIGDTVVVRKAGDVIPKVVG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167348137 398 VIEKGSSPS--PYKIADACPSCKSKLVKEG--AHLFCLNEECPARLLGTLQFFVGRD 450
Cdd:smart00532 384 VVKEKRPGDerEIEMPTHCPSCGSELVREEgeVDIRCPNPLCPAQLIERIIHFASRK 440
|
|
| ligA |
PRK14351 |
NAD-dependent DNA ligase LigA; Provisional |
3-682 |
3.25e-152 |
|
NAD-dependent DNA ligase LigA; Provisional
Pssm-ID: 184640 [Multi-domain] Cd Length: 689 Bit Score: 457.68 E-value: 3.25e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 3 DEVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHpQYKTPDSPTARVGSDIVNELPEKEHSIPVLS 82
Cdd:PRK14351 30 DEAEEQAEQLREAIREHDHRYYVEADPVIADRAYDALFARLQALEDAF-DLDTENSPTRRVGGEPLDELETVEHVAPMLS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 83 LDKCYSIDSLENWIfKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI--DF 160
Cdd:PRK14351 109 IDQSGEADDVREFD-ERVRREVGAVEYVCEPKFDGLSVEVVYEDGEYQRAATRGDGREGDDVTANVRTIRSVPQKLrgDY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 161 KEKIAIRGEIFIKKGDFTIYNSKY---ADGIYSNPRNLASGCVRRLRSSETALFPLNIFCYEAFLEQLKIESHLENLLLL 237
Cdd:PRK14351 188 PDFLAVRGEVYMPKDAFQAYNRERierGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLDASELFDSHWEELERF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 238 KKLGFPLNDEIgffsdSRVDTttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRW 317
Cdd:PRK14351 268 PEWGLRVTDRT-----ERVDD------------IDDAIAYRDRLLAARDDLNYEIDGVVIKVDDRDAREELGATARAPRW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 318 AIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEK 397
Cdd:PRK14351 331 AFAYKFPARAEETTIRDIVVQVGRTGRLTPVALLDPVDVGGVTVSRASLHNPAEIEELGVNVGDRVRVKRAGDVIPYVEE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 398 VIEKGSSpSPYKIADACPSCKSKLVKEGAHLFCLNE-ECPARLLGTLQFFVGRDQMDIETLGDKTLEFLFNKGFVRYIYD 476
Cdd:PRK14351 411 VVEKDSE-GTFEFPDTCPVCDSAVERDGPLAFCTGGlACPAQLERSIEHYASRDALDIEGLGEERVQQLVDAGLVESLAD 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 477 LYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKDIGSKVAEILTKKFKNIDEIVNicssnagsdlfap 556
Cdd:PRK14351 490 LYDLTVADLAELEGWGETSAENLLAELEASREPPLADFLVALGIPEVGPTTARNLAREFGTFEAIMD------------- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 557 SPEDFFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAGLNFEtkinEQDQNINRFLSGTKWVITGSFENFnPREKAAE 636
Cdd:PRK14351 557 ADEEALRAVDDVGPTVAEEIREFFDSERNRAVIDDLLDHGVDPQ----PAESEGGDALDGLTFVFTGSLSGY-TRSEAQE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1167348137 637 LIKKYGGETVDAVSSKTTHLLKGKSPG-SKLEKAIKLKINIVEEAEF 682
Cdd:PRK14351 632 LVEAHGGNATGSVSGNTDYLVVGENPGqSKRDDAEANDVPTLDEEEF 678
|
|
| LIGANc |
cd00114 |
NAD+ dependent DNA ligase adenylation domain. DNA ligases catalyze the crucial step of joining ... |
8-325 |
5.52e-119 |
|
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: 358.44 E-value: 5.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 8 KIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSLDKCY 87
Cdd:cd00114 2 RIAELRELLNKHDYRYYVLDEPSVSDAEYDRLYRELRALEEEHPELKTPDSPTQRVGGTPLSGFKKVRHPVPMLSLDNAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 88 SIDSLENWIFKNGQKTTNIFELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKIDF-KEKIAI 166
Cdd:cd00114 82 DEEELRAFDERIKRFLGEEPAYVVEPKIDGLSISLRYENGVLVQAATRGDGTTGEDVTENVRTIRSIPLTLAGaPETLEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 167 RGEIFIKKGDFTIYNSKYA---DGIYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQLKIESHLENLLLLKKLGF 242
Cdd:cd00114 162 RGEVFMPKADFEALNKEREergEKPFANPRNAAAGSLRQLDPKITAKRPLRFFIYGlGEAEGLGPKTQSEALAFLKEWGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 243 PLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQHHPRWAIAYK 322
Cdd:cd00114 242 PVSPETRLCKN-----------------IEEVLAFYDEIEAKRDSLPYEIDGVVVKVDDLALQRELGFTSKAPRWAIAYK 304
|
...
gi 1167348137 323 FDA 325
Cdd:cd00114 305 FPA 307
|
|
| DNA_ligase_aden |
pfam01653 |
NAD-dependent DNA ligase adenylation domain; DNA ligases catalyze the crucial step of joining ... |
4-325 |
2.33e-115 |
|
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: 349.34 E-value: 2.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 4 EVRNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVNELPEKEHSIPVLSL 83
Cdd:pfam01653 2 EAQQQLEELRELIRKYDYEYYVLDNPSVPDAEYDRLYRELKALEEKHPELITPDSPTQRVGAVPLADFNKVRHLTPMLSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 84 DKCYSIDSLENWIFKNGQKTTNIFELI--VEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKIDFK 161
Cdd:pfam01653 82 DNAFNLDELQAFIERIRRALGNKEKVEyvVEPKIDGLSISLLYENGLLVRAATRGDGTTGEDVTANVKTIRNIPLKLKGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 162 ---EKIAIRGEIFIKKGDFTIYNS---KYADGIYSNPRNLASGCVRRLRSSETALFPLNIFCYE-AFLEQ--LKIESHLE 232
Cdd:pfam01653 162 nppERLEVRGEVFMPKEDFEALNEerlEEGEKPFANPRNAAAGSLRQLDPRITAKRKLRFFAYGlGLLEGheLGFDTQYQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 233 NLLLLKKLGFPLNDEIGFFSDsrvdtttlpfknhfigkISEMSGYIKDFEKKRESLPYEIDGIVIKINDLATRAELGYTQ 312
Cdd:pfam01653 242 ALAFLKSLGFPVSPLLALCDG-----------------IEEVLAYYADWEKKRDSLPYEIDGVVVKVDELALQRELGFTA 304
|
330
....*....|...
gi 1167348137 313 HHPRWAIAYKFDA 325
Cdd:pfam01653 305 KAPRWAIAYKFPA 317
|
|
| DNA_ligase_OB |
pfam03120 |
NAD-dependent DNA ligase OB-fold domain; DNA ligases catalyze the crucial step of joining the ... |
329-400 |
1.74e-32 |
|
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: 120.16 E-value: 1.74e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167348137 329 ETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNISKRGDVIPAVEKVIE 400
Cdd:pfam03120 1 ETKLLDIEFQVGRTGAITPVAVLEPVELAGTTVSRATLHNEDEIKRKDIRIGDTVIVRKAGDVIPEVVGVVL 72
|
|
| ligB |
PRK08097 |
NAD-dependent DNA ligase LigB; |
6-596 |
1.42e-23 |
|
NAD-dependent DNA ligase LigB;
Pssm-ID: 236150 [Multi-domain] Cd Length: 562 Bit Score: 105.39 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 6 RNKIEELREKINLANKAYYMESKPIISDIEYDRLFDTLLQLETEHPQYKTPDSPTARVGSDIVnelpekeHSIPVLSLDK 85
Cdd:PRK08097 31 QEEIAALQQQLAQWDDAYWRQGKSEVDDEVYDQLRARLTQWQRCFGGPEPRDVPLPPLNGKVL-------HPVAHTGVKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 86 CYSIDSLENWIfknGQKTtnifELIVEPKIDGAGIVLYYENGILTGALTRGNGYFGNDITNNVKTIKTVPLKI-DFKEKI 164
Cdd:PRK08097 104 LADKQALARWM---AGRS----DLWVQPKVDGVAVTLVYRDGKLVQAISRGNGLKGEDWTAKARLIPAIPQQLpGALANL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 165 AIRGEIFIKKGDftiyNSKYADGiYSNPRNLASGCVRRlRSSETALFPLNIFCYE---------AFLEQLKieshlenll 235
Cdd:PRK08097 177 VLQGELFLRREG----HIQQQMG-GINARAKVAGLMMR-KDPSPTLNQIGVFVWAwpdgpasmpERLAQLA--------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 236 llkKLGFPLNDEIgffsdsrvdttTLPFKNhfigkisemsgyIKDFEKKRES-----LPYEIDGIVIKINDLAT----RA 306
Cdd:PRK08097 242 ---TAGFPLTQRY-----------THPVKN------------AEEVARWRERwyrapLPFVTDGVVVRQAKEPPgrywQP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 307 ELGYtqhhprWAIAYKFDAPLAETKLESIDVQVGRGGRITPVANLTPVELSGSVISRATLHNQDYIDSLTVNVGDLVNIS 386
Cdd:PRK08097 296 GQGE------WAVAWKYPPVQQVAEVRAVQFAVGRTGKITVVLELEPVMLDDKRVSRVNIGSVRRWQQWDIAPGDQVLVS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 387 KRGDVIPAVEKVIEKGS---SPSPYKIADACP-SCksklvkegahlFCLNEECPARLLGTLQFFVGRDQMDIETLGDKTL 462
Cdd:PRK08097 370 LAGQGIPRLDKVVWRGAertKPTPPDADRFHSlSC-----------FRASPGCQEQFLARLVWLSGKQGLGLDGIGEGTW 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 463 EFLFNKGFVRYIYDLYSFDYRKLLDFEGFKDKKIDNIIFSIEKSKQKDFKTVISSLGLKdigskvaeiLTKKFKNIDEIV 542
Cdd:PRK08097 439 RALHQTGLFEHLFSWLALTPEQLANTPGIGKARAEQLWHQFNLARQQPFSRWLKALGIP---------LPQAALNALDDR 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1167348137 543 NIcssnagSDLFAPSPEDfFANIDGIGPITASLIVKHFTNAKTLKLIQKLKEAG 596
Cdd:PRK08097 510 SW------QQLLSRSEQQ-WQQLPGIGEGRARQLIAFLQHPEVKALADWLAAQG 556
|
|
| BRCT_DNA_ligase_like |
cd17748 |
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ... |
614-683 |
2.94e-15 |
|
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: 70.97 E-value: 2.94e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167348137 614 LSGTKWVITGSFENFnPREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLE-----KAIKLKINIVEEAEFL 683
Cdd:cd17748 1 LAGKTFVFTGTLSSM-SRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKkgeelKAKGLGIKIISEEEFL 74
|
|
| BRCT_RFC1 |
cd17752 |
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ... |
614-687 |
1.23e-14 |
|
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: 69.16 E-value: 1.23e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1167348137 614 LSGTKWVITGSFENFNpREKAAELIKKYGGETVDAVSSKTTHLLKGKSPG-SKLEKAIKLKINIVEEAEFLLIIE 687
Cdd:cd17752 6 LEGLTFVITGVLESLE-REEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGpSKLEKAKELGTKIIDEDGLFDLIR 79
|
|
| HHH_2 |
pfam12826 |
Helix-hairpin-helix motif; The HhH domain of DisA, a bacterial checkpoint control protein, is ... |
514-589 |
1.77e-07 |
|
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: 48.67 E-value: 1.77e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167348137 514 VISSLGLKDIGSKVAEILTKKFKNIDEIvnicsSNAgsdlfapSPEDFFAnIDGIGPITASLIVKHFTNAKTLKLI 589
Cdd:pfam12826 2 LLFALGIRHVGETTAKLLARRFGSLDAL-----AEA-------SLEELLE-VDDIGPEIAQSIVEFFADPANRELI 64
|
|
| PTCB-BRCT |
pfam12738 |
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
629-677 |
1.15e-05 |
|
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.
Pssm-ID: 463687 [Multi-domain] Cd Length: 63 Bit Score: 43.35 E-value: 1.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1167348137 629 NPREKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIV 677
Cdd:pfam12738 11 DDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVV 59
|
|
| BRCT_PARP1 |
cd17747 |
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ... |
614-683 |
1.21e-05 |
|
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.
Pssm-ID: 349378 [Multi-domain] Cd Length: 76 Bit Score: 43.67 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167348137 614 LSGTKWVITGSFENfnPREKAAELIKKYGGETVDAVSSKTTHLL----KGKSPGSKLEKAIKLKINIVEEaEFL 683
Cdd:cd17747 1 LTGMKFALIGKLSK--SKDELKKLIEKLGGKVASKVTKKVTLCIstkaEVEKMSKKMKEAKEAGVPVVSE-DFL 71
|
|
| BRCT |
pfam00533 |
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
612-683 |
1.29e-05 |
|
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: 43.44 E-value: 1.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167348137 612 RFLSGTKWVITGsFENFNpREKAAELIKKYGGETVDAVSSKTTHLLkGKSPGSKLEKAIKLKINIVEEAEFL 683
Cdd:pfam00533 4 KLFSGKTFVITG-LDGLE-RDELKELIEKLGGKVTDSLSKKTTHVI-VEARTKKYLKAKELGIPIVTEEWLL 72
|
|
| BRCT |
cd00027 |
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
619-677 |
1.68e-05 |
|
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.
Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 43.12 E-value: 1.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 619 WVITGSFENFNPREKAAELIKKYGGETVDAVSSKTTHLL-KGKSPGSKLEKAIKLKINIV 677
Cdd:cd00027 1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIaKSPSGEKYYLAALAWGIPIV 60
|
|
| BRCT |
smart00292 |
breast cancer carboxy-terminal domain; |
613-677 |
3.24e-05 |
|
breast cancer carboxy-terminal domain;
Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 42.75 E-value: 3.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167348137 613 FLSGTKWVITGSFENfNPREKAAELIKKYGGETVDAVSSK-TTHLLKGKSPGSKLE--KAIKLKINIV 677
Cdd:smart00292 3 LFKGKTFYITGSFDK-EERDELKELIEALGGKVTSSLSSKtTTHVIVGSPEGGKLEllKAIALGIPIV 69
|
|
| BRCT_Rad4_rpt2 |
cd17746 |
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
631-688 |
7.59e-05 |
|
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one.
Pssm-ID: 349377 [Multi-domain] Cd Length: 91 Bit Score: 41.84 E-value: 7.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167348137 631 REKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVEEAEFLLIIER 688
Cdd:cd17746 22 RSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQR 79
|
|
| DNA_ligase_ZBD |
pfam03119 |
NAD-dependent DNA ligase C4 zinc finger domain; DNA ligases catalyze the crucial step of ... |
414-436 |
1.73e-04 |
|
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: 38.95 E-value: 1.73e-04
|
| BRCT_CHS5_like |
cd17742 |
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ... |
621-690 |
6.53e-04 |
|
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth.
Pssm-ID: 349373 [Multi-domain] Cd Length: 77 Bit Score: 38.85 E-value: 6.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167348137 621 ITGSFENFNP---REKAAELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLKINIVeEAEFLLIIEREK 690
Cdd:cd17742 3 ITVCLGPLDPpesVDELEQCLERIGAKPTDRVAIDTTHFVCTVPSGPEYEKAKEMNIPIV-RPEWLRACEVEK 74
|
|
| BRCT_TopBP1_rpt2_like |
cd17731 |
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
621-677 |
4.50e-03 |
|
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.
Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 36.36 E-value: 4.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167348137 621 ITGsfenFNPREKAA--ELIKKYGGETVDAVSSKTTHLLKGKSPGSKLEKAIKLK-INIV 677
Cdd:cd17731 10 VTG----FDSEERKEiqQLVEQNGGSYSPDLSKNCTHLIAGSPSGQKYEFARKWNsIHIV 65
|
|
| |
