|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00166 |
PTZ00166 |
DNA polymerase delta catalytic subunit; Provisional |
65-1072 |
0e+00 |
|
DNA polymerase delta catalytic subunit; Provisional
Pssm-ID: 240301 [Multi-domain] Cd Length: 1054 Bit Score: 1325.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 65 QILEVEtYHEDGSATSYDRTN------------VKLYGVTKSGNSICVIVTDYFPHFYFQAPQGFGVEHIgtaQSAICNM 132
Cdd:PTZ00166 45 FQLDAD-YTEKDDKSQGNPHNtvsgvrhvevpiIRLYGVTKEGHSVLVNVHNFFPYFYIEAPPNFLPEDS---QKLKREL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 133 VAAAKRRGGSGqaqlpgKVVDNLVHVEIVHGENLYYFRGaDTKVPFVKVsgsTEALHK----ARMELKNGVNLMGKG--P 206
Cdd:PTZ00166 121 NAQLSEQSQFK------KYQNTVLDIEIVKKESLMYYKG-NGEKDFLKI---TVQLPKmvprLRSLIESGVVVCGGGwdG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 207 VNVGNLYESNINVIVMFLAKTNIVGCGWIEIPAGKCRILSNSEKSSRCQIEVTVPVKNLIVHESDGEWAGIAPIRTLSLD 286
Cdd:PTZ00166 191 IRLFQTYESNVPFVLRFLIDNNITGGSWLTLPKGKYKIRPPKKKTSTCQIEVDCSYEDLIPLPPEGEYLTIAPLRILSFD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 287 IECIGRRGV-FPEAIKDPIIQIANLVKIEG-EAEPFVRNCFVLGTCAPVVGSNIIQCVNEKVLLEKWAEFVREVDPDIIT 364
Cdd:PTZ00166 271 IECIKLKGLgFPEAENDPVIQISSVVTNQGdEEEPLTKFIFTLKECASIAGANVLSFETEKELLLAWAEFVIAVDPDFLT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 365 GYNILNFDLPYILDRAKVLSLPQVSHLGRQKEKGSVVRDAAISSKQMGSRVNKSIDIHGRIIFDVLQVVLRDYKLRSYTL 444
Cdd:PTZ00166 351 GYNIINFDLPYLLNRAKALKLNDFKYLGRIKSTRSVIKDSKFSSKQMGTRESKEINIEGRIQFDVMDLIRRDYKLKSYSL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 445 NSVSYQFLSEQKEDVEHNIIPDLQRGDEQTRRRLAQYCLKDAYLPLRLLDKLMSIINYIEMARVTGVPMNFLLTKGQQIK 524
Cdd:PTZ00166 431 NYVSFEFLKEQKEDVHYSIISDLQNGSPETRRRIAVYCLKDAILPLRLLDKLLLIYNYVEMARVTGTPIGWLLTRGQQIK 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 525 ILSMMLRRCKQNNFFLPVIE-ANSGDGEGYEGATVIDPIRGFYNEPIATLDFASLYPSIMIAHNLCYTTLLKSPQ--GVE 601
Cdd:PTZ00166 511 VTSQLLRKCKKLNYVIPTVKySGGGSEEKYEGATVLEPKKGFYDEPIATLDFASLYPSIMIAHNLCYSTLVPPNDanNYP 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 602 NEDYIRTPSGQYFATKSKRRGLLPEILEDILAARKRAKNDMKNEKDEFKRMVYNGRQLALKISANSVYGFTGATV-GKLP 680
Cdd:PTZ00166 591 EDTYVTTPTGDKFVKKEVRKGILPLIVEELIAARKKAKKEMKDEKDPLLKKVLNGRQLALKISANSVYGYTGAQVgGQLP 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 681 CLEISQSVTAFGRKMIDMTKLEVERIYKKgalDGKCPADAKVIYGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIFTPP 760
Cdd:PTZ00166 671 CLEVSTSITSFGRQMIDKTKELVEKHYTK---ANGYKHDATVIYGDTDSVMVKFGTDDIQEAMDLGKEAAERISKKFLKP 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 761 IKLEFEKVYSPYLLINKKRYAGLYFTKPDVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISD 840
Cdd:PTZ00166 748 IKLEFEKVYCPYLLMNKKRYAGLLYTNPEKYDKIDCKGIETVRRDNCLLVQQMVETVLNKILIEKDVESAIEFTKGKISD 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 841 LLCNKIDISLLIISKELTKsgDKYQAKQAHVELAARMKKRDAGSAPRLGDRVPYVFVAAAKNVPAYERAEDPTFVLQNNI 920
Cdd:PTZ00166 828 LLQNRIDISLLVITKSLGK--DDYEGRLAHVELAKKLRQRDPGSAPNVGDRVSYVIVKGAKGAPQYERAEDPLYVLENNI 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 921 PLDTKHYLtNQLAKPLARIFEPILGDraEKILVEGEHTRVRTVVQSKVGGLAAFTTKSATCLGCKSVLPraesENAVCKH 1000
Cdd:PTZ00166 906 PIDTQYYL-DQIKNPLLRIFEGVMDN--PDSLFSGEHTRHITISSSSKGGLSKFVKKQLQCLGCKSVIK----EGALCDN 978
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 1001 C-EPKLPTIFASRMNTMHELENHFGRLWTECQNCAKTMQDKVNCSARDCPIYYMREKVRNELSEASAVIERFG 1072
Cdd:PTZ00166 979 CnQNKEPSIYGKKLAKRRHKEAEYSQLWTQCQRCQGSLHQEVICTNRDCPIFYRRKKVQKDLAELQELLSRFG 1051
|
|
| POLBc_delta |
cd05533 |
DNA polymerase type-B delta subfamily catalytic domain. Three DNA-dependent DNA polymerases ... |
551-944 |
0e+00 |
|
DNA polymerase type-B delta subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. Presently, no direct data is available regarding the strand specificity of DNA polymerase during DNA replication in vivo. However, mutation analysis supports the hypothesis that DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand.
Pssm-ID: 99916 Cd Length: 393 Bit Score: 784.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 551 EGYEGATVIDPIRGFYNEPIATLDFASLYPSIMIAHNLCYTTLLKSPQGVEN--EDYIRTPSGQYFATKSKRRGLLPEIL 628
Cdd:cd05533 1 EQYEGATVIEPIKGYYDVPIATLDFASLYPSIMMAHNLCYTTLLNKNTAKKLppEDYIKTPNGDYFVKSSVRKGLLPEIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 629 EDILAARKRAKNDMKNEKDEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIYK 708
Cdd:cd05533 81 EELLAARKRAKKDLKEETDPFKKAVLDGRQLALKISANSVYGFTGATVGKLPCLEISSSVTSFGRQMIEKTKKLVEEKYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 709 KgalDGKCPADAKVIYGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIFTPPIKLEFEKVYSPYLLINKKRYAGLYFTKP 788
Cdd:cd05533 161 K---ANGYSHDAKVIYGDTDSVMVKFGVSDVEEAMKLGKEAAEYVSKKFIKPIKLEFEKVYFPYLLINKKRYAGLLWTNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 789 DVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISDLLCNKIDISLLIISKELTKSGDKYQAKQ 868
Cdd:cd05533 238 DKHDKMDTKGIETVRRDNCLLVQNVVETCLNKILIERDVEGAIEFVKGVISDLLQNKIDISLLVITKALTKTADDYAGKQ 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17559488 869 AHVELAARMKKRDAGSAPRLGDRVPYVFVAAAKNVPAYERAEDPTFVLQNNIPLDTKHYLTNQLAKPLARIFEPIL 944
Cdd:cd05533 318 AHVELAERMRKRDPGSAPNVGDRVPYVIIKGAKGAKAYEKAEDPIYVLENNIPIDTQYYLENQLSKPLLRIFEPIL 393
|
|
| DNA_pol_B |
pfam00136 |
DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one ... |
511-943 |
0e+00 |
|
DNA polymerase family B; This region of DNA polymerase B appears to consist of more than one structural domain, possibly including elongation, DNA-binding and dNTP binding activities.
Pssm-ID: 395085 Cd Length: 439 Bit Score: 610.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 511 VPMNFLLTKGQQIKILSMMLRRCKQNNFFLPVIEANSGDGEGYEGATVIDPIRGFYNEPIATLDFASLYPSIMIAHNLCY 590
Cdd:pfam00136 1 IPQSRVLEGGQQIRVESCLLRLALEEGFILPDRPSAKGDEDGYQGATVIEPKKGFYDKPVLVLDFNSLYPSIIQAHNLCY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 591 TTLLKS-------PQGVENEDYIRTPSGQYFATKSKRRGLLPEILEDILAARKRAKNDMKNEKDEFKRMVYNGRQLALKI 663
Cdd:pfam00136 81 TTLVRSvdeannlPPEDNLITVECTPRGVYFVKDHVREGLLPKLLKDLLAKRKAIKKLLKEETDPFERAILDKQQLALKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 664 SANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVEriykkgaldGKCPADAKVIYGDTDSVMVKFGVETVAQAM 743
Cdd:pfam00136 161 TANSVYGFTGFANGRLPCLPIAASVTAIGREMLENTKDLVE---------GMYTYNFRVIYGDTDSVFIEFGGKDVEEAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 744 EIGLDAAKEVSK-IFTPPIKLEFEKVYSPYLLINKKRYAGLYFTKPDVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLL 822
Cdd:pfam00136 232 KIGDELAEHVNQdLFKSPIKLEFEKVYKPLLLISKKKYAGLKYTAPSNFNKLDMKGVDLVRRDNCPLVKEVIKKVLDLLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 823 IERDQQSALDFAKRTI----SDLLCNKIDISLLIISKELTKSGDKYQAKQ-AHVELAARMKKRDaGSAPRLGDRVPYVFV 897
Cdd:pfam00136 312 SDRGLPVGLEFVISILndarSDLRNNKVPLEKFVISKELSKPPDNYKSKNlPHVEVALRMNKRN-GEAPEVGDRIPYVIV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 17559488 898 AAAK---NVPAYERAEDPTFVLQNNIPLDTKHYLTNQLAKPLARIFEPI 943
Cdd:pfam00136 391 KAAKglkNLLIYERAEDPEYVLENNLPIDYEYYFSNQLIPPVARLLEPI 439
|
|
| PolB |
COG0417 |
DNA polymerase B elongation subunit [Replication, recombination and repair]; |
80-943 |
1.18e-165 |
|
DNA polymerase B elongation subunit [Replication, recombination and repair];
Pssm-ID: 440186 [Multi-domain] Cd Length: 794 Bit Score: 508.21 E-value: 1.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 80 SYDRTN----VKLYGVTKSGNSICVIVTDYFPHFYFQAPQGFGVEHIGTAQSAIcnmvaaakrrggsgqaqlpgkvvdnl 155
Cdd:COG0417 11 SYRDEDgkpvIELWGRTEDGPSVLLDVTGFRPYFYVPLPDEEKLEELLRDIKEI-------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 156 VHVEIVHGENlyyFRGadTKVPFVKVSGST-EALHKARMELKNGVnlmgkgpvnvGNLYESNINVIVMFLAKTNIVGCGW 234
Cdd:COG0417 65 TEVEPVKLKS---FFG--EPVPVLKIYTRDpRDVRELRDRLKEGG----------IDVYEADIRFHDRYLIDRFLTPGVW 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 235 IEIPAGKCRILSNSEKSSRCQIEVTVPvknlivhesdgewagIAPIRTLSLDIECIGRRGVFPEAIKDPIIQIAnlvkIE 314
Cdd:COG0417 130 YEGEVEEDGGKLDYEVKENPRLKPEDY---------------RPKLKVLSFDIEVSTPRGFPDPERDGPIISIG----LA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 315 GEAEpfVRNCFVLGtcAPVVGSNIIQCVNEKVLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVLSLPqvSHLGRq 394
Cdd:COG0417 191 GSDG--EKKVLMLG--REGVDFEVEYFDDEKALLEAFFEIIREYDPDIIIGWNVDNFDLPYLQKRAERLGIP--LDLGR- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 395 keKGSVVRdaaisskQMGSRVNKSIDIHGRIIFDVLQVVLRD-YKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDeq 473
Cdd:COG0417 264 --DGSEPS-------WREHGGQGFASIPGRVVIDLYDALKSAtYKFKSYSLDAVAEELLGEGKLIVDGGEIERLWDDD-- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 474 tRRRLAQYCLKDAYLPLRLLDKLMsIIN-YIEMARVTGVPMNFLLTKGQQIKILSMMLRRCKQNNFFLPvieaNSGD--G 550
Cdd:COG0417 333 -KPALAEYNLRDAELTLRIFEKTL-LLPfLIELSRITGLPLDDVGRAGSSAAFENLLLPEAHRRGYLAP----NKGEikG 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 551 EGYEGATVIDPIRGFYnEPIATLDFASLYPSIMIAHNLCYTTLLKsPQGVENEDYIRTPS-GQYFAtkSKRRGLLPEILE 629
Cdd:COG0417 407 EAYPGGYVLDPKPGLY-ENVLVLDFKSLYPSIIRTFNISPETLVE-GGEEPCGDEDVAPGfGHRFC--REPKGILPSILE 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 630 DILAARKRAKNDMKNEK-DEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIyk 708
Cdd:COG0417 483 ELWDERDEAKKKMKKAKpDSEEYRLYDALQQALKILMNSFYGVLGSEGCRFYDPELAESITARGREIIKQTIEKAEEL-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 709 kgaldgkcpaDAKVIYGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIFTPPIKLEFEKVYSPYLLIN-KKRYAGLYftk 787
Cdd:COG0417 561 ----------GYKVIYGDTDSLFVWLPKASLEEAIEIGKELAEEINAWWPSGLELEFEKHYRRFFFPGsKKRYAGLT--- 627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 788 pdVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISDLLCNKIDISLLIISKELTKSGDKYQAK 867
Cdd:COG0417 628 --EDGKIDIKGLEAVRSDWTELAKEFQQEVYERILKEEDVEKAVEYVRDVIEKLRAGEVDLDDLVIRKRLRKPLSEYEKN 705
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559488 868 -QAHVELAARMKKRdaGSAPRLGDRVPYVFVAAAknvpayERAEDPTFVLQNNIPLDTKHYLTNQLAKPLARIFEPI 943
Cdd:COG0417 706 vPPHVRAARKLDER--GRPYQRGDKISYVITKGG------GRVEPVELAKERESEIDYDYYIEKQLKPTADRILEAF 774
|
|
| DNA_polB_delta_exo |
cd05777 |
DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase delta, a family-B DNA polymerase; ... |
274-503 |
2.74e-145 |
|
DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase delta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase delta. DNA polymerase delta is a family-B DNA polymerase with a catalytic subunit that contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (alpha and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase delta is the enzyme responsible for both elongation and maturation of Okazaki fragments on the lagging strand. It is also implicated in mismatch repair (MMR) and base excision repair (BER). The catalytic subunit displays both polymerase and 3'-5' exonuclease activities. The exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues necessary for metal binding and catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation.
Pssm-ID: 99820 [Multi-domain] Cd Length: 230 Bit Score: 433.93 E-value: 2.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 274 WAGIAPIRTLSLDIECIGRRGVFPEAIKDPIIQIANLVKIEGEAEPFVRNCFVLGTCAPVVGSNIIQCVNEKVLLEKWAE 353
Cdd:cd05777 1 WSKIAPLRILSFDIECAGRKGVFPEPEKDPVIQIANVVTRQGEGEPFIRNIFTLKTCAPIVGAQVFSFETEEELLLAWRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 354 FVREVDPDIITGYNILNFDLPYILDRAKVLSLPQVSHLGRQKEKGSVVRDAAISSKQMGSRVNKSIDIHGRIIFDVLQVV 433
Cdd:cd05777 81 FVQEVDPDIITGYNICNFDLPYLLERAKALKLNTFPFLGRIKNIKSTIKDTTFSSKQMGTRETKEINIEGRIQFDLLQVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 434 LRDYKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDEQTRRRLAQYCLKDAYLPLRLLDKLMSIINYI 503
Cdd:cd05777 161 QRDYKLRSYSLNSVSAHFLGEQKEDVHYSIITDLQNGNPETRRRLAVYCLKDAYLPLRLLDKLMCLVNYI 230
|
|
| POLBc |
smart00486 |
DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), ... |
279-735 |
4.12e-134 |
|
DNA polymerase type-B family; DNA polymerase alpha, delta, epsilon and zeta chain (eukaryota), DNA polymerases in archaea, DNA polymerase II in e. coli, mitochondrial DNA polymerases and and virus DNA polymerases
Pssm-ID: 214691 [Multi-domain] Cd Length: 474 Bit Score: 414.62 E-value: 4.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECIGRRGVFPEAI--KDPIIQIANLVKIEGEAEPFVRNCFVLGTCAPVVGSNIIQCVNEKVLLEKWAEFVR 356
Cdd:smart00486 2 PLKILSFDIETYTDGGNFPDAEifDDEIIQISLVINDGDKKGANRRILFTLGTCKEIDGIEVYEFNNEKELLLAFFEFIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 357 EVDPDIITGYNILNFDLPYILDRAKVLSLPQVSHLGRQKEKGSVVRDAAISSKQMGSRVNKSIDIHGRIIFDVLQVVLRD 436
Cdd:smart00486 82 KYDPDIIYGHNISNFDLPYIISRLEKLKIDPLSKIGRLKIGLRIPNKKPLFGSKSFGLSDIKVYIKGRLVIDLYRLYKNK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 437 YKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDEQTRRRLAQYCLKDAYLPLRLLDKLMSIINYIEMARVTGVPMNFL 516
Cdd:smart00486 162 LKLPSYKLDTVAEYLLGKEKDDLPYKDIPELYNGNYEERDELLRYCIQDAVLTLKLFNKLNVIPLIIELARIAGIPLRRT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 517 LTKGQQIKILSMMLRRCKQNNFFLPVIEANSGDG--------EGYEGATVIDPIRGFYNEPIATLDFASLYPSIMIAHNL 588
Cdd:smart00486 242 LYYGSQIRVESLLLREAKKNNYILPSKELYDFKGsepdlkkkVKYEGGKVLEPKKGFYDNPVLVLDFNSLYPSIIIAHNL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 589 CYTTLL------KSPQGVENEDYIRTPSGQ----YFATKSKRRGLLPEILEDILAARKRAKNDMKNEKDEFK--RMVYNG 656
Cdd:smart00486 322 CYSTLVgvgevvIKGDLIIPEDLLTIKYEKgnkyRFVKKNIRKGILPKLLKKLLDKRKEIKKLMKKEKDESEelKKLLDS 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17559488 657 RQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIykkgaldGKCPADAKVIYGDTDSVMVKFG 735
Cdd:smart00486 402 RQLALKLTANSVYGYLGFTNSRLPCKPLAASVTALGREILEKTKELIEEN-------GYPKPGFKVIYGDTDSIFVTKP 473
|
|
| POLBc |
cd00145 |
DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by ... |
551-941 |
3.51e-114 |
|
DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication, repair, and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A), E. coli polymerase II (class B), E. coli polymerase III (class C), euryarchaeota polymerase II (class D), human polymerase beta (class x), E. coli UmuC/DinB, and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon, and zeta), and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general, the architecture of the Pol domain has been likened to a right hand with fingers, thumb, and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis.
Pssm-ID: 99912 [Multi-domain] Cd Length: 323 Bit Score: 356.29 E-value: 3.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 551 EGYEGATVIDPIRGfYNEPIATLDFASLYPSIMIAHNLCYTTLLKSPQGVENEDYIrtpsGQYFATKSKRRGLLPEILED 630
Cdd:cd00145 1 EPYEGGYVFDPIPG-LYENVIVLDFKSLYPSIIITYNLSPTTLVGNGEIAAPEDYI----GVGFRSPKDRKGLLPRILEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 631 ILAARKRAKNDMKNEK-DEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIykk 709
Cdd:cd00145 76 LLNFRDEAKKRMKAAKlAPEERVLYDNRQQALKVLANSFYGYLGAKFFRFYDPEVAASITSFGREIIQDTIALVEEH--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 710 galdgkcpaDAKVIYGDTDSVMVKFGVetvaqaMEIGLDAAKEVSKIF-----TPPIKLEFEKVYSPYLLINKKRYAGLY 784
Cdd:cd00145 153 ---------GARVIYGDTDSIFVSLPK------MGTKEDAIKEGREILqeladEHLLELEFEKVYLPFFLGKKKRYAGLD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 785 FTKPDVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDqqsALDFAKRTISDLlcnkidislliiskeltksgdky 864
Cdd:cd00145 218 IWKGQDEGKIDIKGLETRRRDSPPLVKKFQKEVLELILEEER---KVEAVKEYIDEL----------------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17559488 865 qakqahvelaarmkkrdagsaprlgDRVPYVFVAAAKNVPAYERAEDPTFVLQNNIPLDTKHYLTNQLAKPLARIFE 941
Cdd:cd00145 272 -------------------------DKVKYVVTRGGKGVPDYERADPPLEDLDKRHRIDYEYYLERLLQPPLERIFE 323
|
|
| PRK05762 |
PRK05762 |
DNA polymerase II; Reviewed |
279-946 |
1.88e-109 |
|
DNA polymerase II; Reviewed
Pssm-ID: 235595 [Multi-domain] Cd Length: 786 Bit Score: 359.17 E-value: 1.88e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECigrrgvfpeAIKDPIIQIAnlvkIEGEAEPFVrncFVLGTCAPVVGSNIIQCVNEKVLLEKWAEFVREV 358
Cdd:PRK05762 154 PLKVVSLDIET---------SNKGELYSIG----LEGCGQRPV---IMLGPPNGEALDFLEYVADEKALLEKFNAWFAEH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 359 DPDIITGYNILNFDLPYILDRAKVLSLPQvsHLGRqkekgsvvRDAAISSKQMGSRVNK-SIDIHGRIIFDVLQVVLR-D 436
Cdd:PRK05762 218 DPDVIIGWNVVQFDLRLLQERAERYGIPL--RLGR--------DGSELEWREHPFRSGYgFASVPGRLVLDGIDALKSaT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 437 YKLRSYTLNSVSYQFLSEQKEdvehnIIPDLQRGDEQTRR------RLAQYCLKDAYLPLRLLDKLMsIINY-IEMARVT 509
Cdd:PRK05762 288 WVFDSFSLEYVSQRLLGEGKA-----IDDPYDRMDEIDRRfaedkpALARYNLKDCELVTRIFEKTK-LLPFlLERATVT 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 510 GVPMNflLTKGQQIKILSMMLRRCKQNNFFLPvieaNSGD--GEGYEGATVIDPIRGFYnEPIATLDFASLYPSIMIAHN 587
Cdd:PRK05762 362 GLPLD--RVGGSVAAFEHLYLPRAHRAGYVAP----NLGErpGEASPGGYVMDSKPGLY-DSVLVLDFKSLYPSIIRTFN 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 588 LCYTTLLKSPQGVENEDyIRTPSGQYFatkSKRRGLLPEILEDILAARKRAKNDMKNEkdefkrmvyngRQLALKISANS 667
Cdd:PRK05762 435 IDPDGLVEGLAQPPEES-VAGFLGARF---SREKHFLPEIVERLWEGRDEAKREMNKP-----------LSQAIKIIMNA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 668 VYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERiykKGaldgkcpadAKVIYGDTDSVMVKFGVE-TVAQAMEIG 746
Cdd:PRK05762 500 FYGVLGSSGCRFFDPRLASSITMRGHEIMKQTRELIEA---QG---------YQVIYGDTDSTFVWLGGAhDEEDAAKIG 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 747 LDAAKEVSKIFTPPIK----------LEFEKVYSPYLLI--------NKKRYAGLYfTKPDVHDKMDCKGLETVRRDNCP 808
Cdd:PRK05762 568 RALVQEINQWWQEHLQqefglesaleLEFEKHYRRFFMPtirgaeegSKKRYAGLI-QEGDGDGRIVFKGLETVRTDWTP 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 809 LVAKVLGVCLEKLLIERDQQsalDFAKRTISDLLCNKIDiSLLIISKELTKSGDKYQAKQA-HVELAARMKKR--DAGSA 885
Cdd:PRK05762 647 LAKEFQQELYERIFRGEPYV---DYVREVIDKLRAGELD-EKLVYRKRLRRPLDEYQRNVPpHVRAARLADEMgyKVGRP 722
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 886 PRL--GDRVPYVfVAAAKNVPAYERaedptfvlqnNIPLDTKHYLTNQLaKPLARIFEPILGD 946
Cdd:PRK05762 723 LQYqnGGKIGYV-ITVNGPEPLEYR----------KSPIDYDYYIEKQL-QPVADRILPFFGD 773
|
|
| POLBc_zeta |
cd05534 |
DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member ... |
520-943 |
3.25e-100 |
|
DNA polymerase type-B zeta subfamily catalytic domain. DNA polymerase (Pol) zeta is a member of the eukaryotic B-family of DNA polymerases and distantly related to DNA Pol delta. Pol zeta plays a major role in translesion replication and the production of either spontaneous or induced mutations. Apart from its role in translesion replication, Pol zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen.
Pssm-ID: 99917 Cd Length: 451 Bit Score: 323.78 E-value: 3.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 520 GQQIKILSMMLRRCKQNNFFLPVIeanSGDGEGYEGAT-----VIDPIRGFYNEPIATLDFASLYPSIMIAHNLCYTTLL 594
Cdd:cd05534 1 GSQFRVESMLLRLAKPENYILPSP---SRQQVAQQRALeclplVMEPESGFYSDPVIVLDFQSLYPSIMIAYNYCYSTCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 595 KSPQGVENE-----------------------DYIR-TPSGQYFATKSKRRGLLPEILEDILAARKRAKNDMKNEKDE-- 648
Cdd:cd05534 78 GRVEELNGGgkfgflgvklylppppldllllkDDVTiSPNGVMFVKKSVRKGILPKMLEEILDTRIMVKKAMKKYKDDkk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 649 FKRMvYNGRQLALKISANSVYGFTGATV-GKLPCLEISQSVTAFGR----KMIDMtkleVERIYKKGAldgkcpadaKVI 723
Cdd:cd05534 158 LQRI-LDARQLALKLLANVTYGYTAASFsGRMPCVEIADSIVQTGRetleRAIEL----IESTPKWGA---------KVV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 724 YGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIFTPPIKLEFEKVYSPYLLINKKRYAGLYFTKPDVHD-KMDCKGLETV 802
Cdd:cd05534 224 YGDTDSLFVLLPGRTKEEAFKIGKEIAEAVTAANPSPIKLKFEKVYHPCVLVTKKRYVGYKYESPDQTEpTFDAKGIETV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 803 RRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISDLLCNKIDISLLIISKELTKSGDKYQAK-QAHVELAARMKKRD 881
Cdd:cd05534 304 RRDGCPAVQKILEKSLRILFETKDLSTVKSYLQRQWSKLLQGRVSIQDFIFAKEVRLGTYKEGATlPAGAIVALRRMEKD 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 882 AGSAPRLGDRVPYVFVAAAKNVPAYERAEDPTFVLQN-NIPLDTKHYLTNQLAKPLARIFEPI 943
Cdd:cd05534 384 PRAEPQYGERVPYVVVRGEPGSRLIDLVVSPEEFLADpSLRLDAEYYITKQIIPALDRLFNLV 446
|
|
| pol2 |
TIGR00592 |
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA ... |
213-941 |
1.25e-87 |
|
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA polymerases.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273159 [Multi-domain] Cd Length: 1172 Bit Score: 307.37 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 213 YESNINVIVMFLAKTNIVGCGWIEIPAGKcriLSNSEKSSRCQIEVTVpVKNLIVHEsdGEWAGIAPIRTLSLDIecigr 292
Cdd:TIGR00592 445 FGSNTGNLERFLLLRKIKGPCWLAVKGPD---ELEYPRRSWCKYEGGY-VKPPNVEK--GLDKTPPPLVVLDFSM----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 293 RGVFPEAIKDPIIQIANLVKIEGEAE-PFVRNCFVLGTCapvVGSNIIQC---------------------VNEKVLLEK 350
Cdd:TIGR00592 514 KSLNPSIIRNEIVSIPDTLHREFALDkPPPEPPYDVHPC---VGTRPKDCsfpldlkgefpgkkpslvedlATERALIKK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 351 WAEFVREVDPDIITGYNILNFDLPYILDRAKVLSLPQVSHLGRQKEkgsvvrdaaisSKQMGSRVNKSIDihGRIIFDVL 430
Cdd:TIGR00592 591 FMAKVKKIDPDEIVGHDYQQRALKVLANRINDLKIPTWSKIGRLRR-----------SPKFGRRFGERTC--GRMICDVE 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 431 QVVLRDYKLRSYTLNSVSYQFL-SEQKEDVEHNIIPDLQRGDEQTRrrLAQYCLKDAYLPLRLLDKLMSIINYIEMARVT 509
Cdd:TIGR00592 658 ISAKELIRCKSYDLSELVQQILkTERKVIPIDNINNMYSESSSLTY--LLEHTWKDAMFILQIMCELNVLPLALQITNIA 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 510 GVPMNFLLTKGQQIKILSMMLRRCKQNNFFLPVIEANS-----------------GDGEGYEGATVIDPIRGFYNEPIAT 572
Cdd:TIGR00592 736 GNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRkqqklgdedeeidgykkGKKAAYAGGLVLEPKVGLYDKYVLL 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 573 LDFASLYPSIMIAHNLCYTTLlkspQGVENEDYIRTpsgqyFATKSKRRGLLPEILEDILAARKRAKNDMKNEKDEFKRM 652
Cdd:TIGR00592 816 MDFNSLYPSIIQEFNICFTTV----QQKVDEDELPE-----LPDSELEMGILPRELRKLVERRKEVKKLMKQDLNPDLRL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 653 VYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIYkkgaldgkcpadAKVIYGDTDSVMV 732
Cdd:TIGR00592 887 QYDIRQKALKLTANSMYGCLGYSKSRFYAKPLAALVTAKGREILEHTRQLVEEMN------------LEVIYGDTDSIMI 954
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 733 KFGVETVAQAMEIGLDAAKEVSKIFtPPIKLEFEKVYSPYLLINKKRYAGLYFTKPD---VHDKMDCKGLETVRRDNCPL 809
Cdd:TIGR00592 955 NTPGTKYEEVFKIGKEFKSEVNKLY-KLLELDIDGVFKRLLLLKKKKYAAIKVEGDSdgnYTTKQEVKGLDIVRRDWSPL 1033
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 810 VAKVLGVCLEKLLIERDQQSALDFAKRTISDL----LCNKIDISLLIISKELTKSGDKY--QAKQAHVELAARMKKRdAG 883
Cdd:TIGR00592 1034 AKETGKKVLDTILSDKDVEEAVEEVQEVLEKIgknvLNGEVPLEKFVINKQLTRDPKDYpdGASLPHVHVALRINAR-GG 1112
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559488 884 SAPRLGDRVPYVFVAAAKNVPAYERA---EDPTFvLQNNIPLDTKHYLTNQLAKPLARIFE 941
Cdd:TIGR00592 1113 RKVKAGDVVSYVICKDGGNLSARQRAyalEELQR-KHNNLIYDTQYYLEHQIHPVVLRILE 1172
|
|
| POLBc_alpha |
cd05532 |
DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases ... |
553-951 |
8.24e-82 |
|
DNA polymerase type-B alpha subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha, delta, and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. In most organisms no specific repair role, other than check point control, has been assigned to this enzyme. Pol alpha contains both polymerase and exonuclease domains, but lacks exonuclease activity suggesting that the exonuclease domain may be for structural purposes only.
Pssm-ID: 99915 Cd Length: 400 Bit Score: 272.14 E-value: 8.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 553 YEGATVIDPIRGFYNEPIATLDFASLYPSIMIAHNLCYTTLLKSPQGVENEDYIRTPSgqyfatKSKRRGLLPEILEDIL 632
Cdd:cd05532 8 YAGGLVLEPKKGLYDKFILLLDFNSLYPSIIQEYNICFTTVDRADPDDEDDEEPPLPP------SDQEKGILPRIIRKLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 633 AARKRAKNDMKNEKDEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERIykkgal 712
Cdd:cd05532 82 ERRRQVKKLMKSEKDPDKKAQLDIRQLALKLTANSMYGCLGFSYSRFYAKPLAALITSKGREILQKTKDLVEKM------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 713 dgkcpaDAKVIYGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIFTpPIKLEFEKVYSPYLLINKKRYAGLYFTK-PDVH 791
Cdd:cd05532 156 ------NLEVIYGDTDSIMINTGTTDYEEAKKLGNKIKKEVNKSYK-KLEIDIDGVFKRLLLLKKKKYAALKVVDdDKGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 792 DKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAK---RTIS-DLLCNKIDISLLIISKELTKSGDKYQAK 867
Cdd:cd05532 229 LKKEVKGLDIVRRDWCPLSKEIGNYVLDQILSDKSREDIVENIHeylRKINeDLRNGKIPLEKFIITKQLTKNPEEYPDK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 868 --QAHVELAARMKKRDAGSapRLGDRVPYVFVAAAKNVPAYERAEDPT-FVLQNNIPLDTKHYLTNQLAKPLARIFEPIL 944
Cdd:cd05532 309 ksLPHVQVALRMNKRGRKV--KAGDTIPYIICKDGSSKSLADRAYHPDeVKKNENLKIDIEYYLSQQILPPISRLCEPIE 386
|
....*..
gi 17559488 945 GDRAEKI 951
Cdd:cd05532 387 GTDAVRL 393
|
|
| POLBc_B3 |
cd05536 |
DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in ... |
551-941 |
1.70e-72 |
|
DNA polymerase type-B B3 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some members of the archaea also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases. Structural comparison of the thermostable DNA polymerase type B to its mesostable homolog suggests several adaptations to high temperature such as shorter loops, disulfide bridges, and increasing electrostatic interaction at subdomain interfaces.
Pssm-ID: 99919 Cd Length: 371 Bit Score: 245.31 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 551 EGYEGATVIDPIRGFYnEPIATLDFASLYPSIMIAHNLcyttllkSPQGVENEDYIRTPSGQYFATKSKRR--GLLPEIL 628
Cdd:cd05536 2 ESYEGGIVLEPEKGLH-ENIVVLDFSSLYPSIMIKYNI-------SPDTLVREGCEDCDVEPQVGHKFRKDppGFIPSVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 629 EDILAARKRAKNDMKNEKDEF-KRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVEriy 707
Cdd:cd05536 74 EDLLEERRRIKEKMKKLDPESeEYKLLDERQRAIKILANSFYGYMGWANARWYCKECAEAVTAWGREYIKTTIKIAE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 708 KKGAldgkcpadaKVIYGDTDSVMVKFGvetvaqameiGLDAAKEVSKIFTP------PIKLEFEKVYSPYLLINKKRYA 781
Cdd:cd05536 151 EKGF---------KVIYGDTDSLFVKID----------GADAVKKKVKKLLKyineelPLELEIEKFYKRGFFVTKKRYA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 782 GLyftkpDVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISDLLCNKIDISLLIISKELTKSG 861
Cdd:cd05536 212 GL-----TEDGKIDVVGLEVVRRDWSEIAKETQARVLEAILKEGDVEEAVKIVKEVIEKLKRGEVPPEKLVIWKQLTKDL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 862 DKYQAKQAHVELAARMKKRdaGSAPRLGDRVPYVFVAAAKNVpaYERAEdPTFVLQNNIPLDTKHYLTNQLAKPLARIFE 941
Cdd:cd05536 287 SEYKATGPHVAAAKKLAKR--GYKVRPGTKIGYVIVKGSGKI--SDRAY-PYDMVDEKHKYDAEYYIDNQVLPAVLRILE 361
|
|
| DNA_pol_B_exo1 |
pfam03104 |
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and ... |
91-447 |
1.91e-71 |
|
DNA polymerase family B, exonuclease domain; This domain has 3' to 5' exonuclease activity and adopts a ribonuclease H type fold.
Pssm-ID: 397292 Cd Length: 333 Bit Score: 241.17 E-value: 1.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 91 VTKSGNSICVIVTDYFPHFYFQAPQGFGVEHIgtaqSAICNMVAAAKRRggsgqaqlpgkvvdnLVHVEIVHGENLYYFR 170
Cdd:pfam03104 1 KTDEGVSVCVNVFGFKPYFYCLAPDGKELEEV----IEEIKELYEGLDK---------------IEKIELKLKKSLYGYE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 171 GadTKVPFVKVSgsteaLHKARMELKNGVNLMgkgPVNVGNLYESNINVIVMFLAKTNIVGCGWIEIPaGKCRILSNseK 250
Cdd:pfam03104 62 E--DPVPYLKVS-----FANPRPLLKIRKYLS---PENISDVYEYDVDYLERFLIDNDIVGFGWYKVK-VYPFRAEG--R 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 251 SSRCQIEVTVPVKNLIVHESDGEWAgiaPIRTLSLDIECIGRRGVFPEA--IKDPIIQIANLVKIEGEAEPFVRNCFVLG 328
Cdd:pfam03104 129 ISNCDVEIDCDSPDLISVPFEKEWP---PLRVLSFDIECTSLPGKFPDAenVKDPIIQISCMLDGQGEPEPEPRFLFTLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 329 TCAP-------------VVGSNIIQCVNEKVLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVLSLPQVSHLGRQK 395
Cdd:pfam03104 206 ECDSediedfeytpkpiYPGVKVFEFPSEKELLRRFFEFIRQYDPDIITGYNGDNFDWPYILNRAKELYIVKLSSIGRLN 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17559488 396 EKG-SVVRDAAIsskqmGSRVNKSIDIHGRIIFDVLQVVLRDYKLRSYTLNSV 447
Cdd:pfam03104 286 RGGrSKVREIGF-----GTRSYEKVKISGRLHLDLYRVIKRDYKLPSYKLNAV 333
|
|
| DEDDy_DNA_polB_exo |
cd05160 |
DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; The 3'-5' exonuclease domain of ... |
283-493 |
8.20e-52 |
|
DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; The 3'-5' exonuclease domain of family-B DNA polymerases. This domain has a fundamental role in reducing polymerase errors and is involved in proofreading activity. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The exonuclease domain of family B polymerase also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members include Escherichia coli DNA polymerase II, some eubacterial phage DNA polymerases, nuclear replicative DNA polymerases (alpha, delta, epsilon and zeta), and eukaryotic viral and plasmid-borne enzymes. Nuclear DNA polymerases alpha and zeta lack the four conserved acidic metal-binding residues. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.
Pssm-ID: 176646 [Multi-domain] Cd Length: 199 Bit Score: 180.63 E-value: 8.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 283 LSLDIECIGRRGvFPEAIKDPIIQIANLVKIEGEAEPFVRNCFVLGTCAPV-VGSNIIQCVNEKVLLEKWAEFVREVDPD 361
Cdd:cd05160 2 LSFDIETTPPVG-GPEPDRDPIICITYADSFDGVKVVFLLKTSTVGDDIEFiDGIEVEYFADEKELLKRFFDIIREYDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 362 IITGYNILNFDLPYILDRAKVLSLPQVSHLGRqkekgsvvrdaaISSKQMGSRVNKSIDIHGRIIFDVLQVVLRDYKLRS 441
Cdd:cd05160 81 ILTGYNIDDFDLPYLLKRAEALGIKLTDGIYR------------RSGGEKSSGSTERIAVKGRVVFDLLAAYKRDFKLKS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559488 442 YTLNSVSYQFLSEQKEDVEHNIIPDLqrGDEQTRRRLAQYCLKDAYLPLRLL 493
Cdd:cd05160 149 YTLDAVAEELLGEGKEKVDGEIIEDA--EWEEDPERLIEYNLKDAELTLQIL 198
|
|
| PRK05761 |
PRK05761 |
DNA-directed DNA polymerase I; |
156-945 |
2.09e-50 |
|
DNA-directed DNA polymerase I;
Pssm-ID: 235594 [Multi-domain] Cd Length: 787 Bit Score: 191.83 E-value: 2.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 156 VHVEIVHGENLYYFRgadtKVPFVKVSGSTEAlhkARMELKNGVNLMGKgpvnvgnLYESNINVIVMFLAKTNIVGCGWI 235
Cdd:PRK05761 80 DHLEIVEKYDGLRDK----KVKVTKIVVKDPL---AVRRLRLSVRDIPR-------AWEADIKYEFRYIYDNGLIPGMPY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 236 EIPAGKCRILSNSEKSSrcQIEVTVPVKNLIVHESDGEWAGIAPIRTLSLDIECIGR-RGVFPEaikdpiiqianlvkie 314
Cdd:PRK05761 146 DVKNGLESVEPEILVEE--IKKAFKDERKLAEDWLPIFEAPIPKIKRIAIDIEVYTPaKGRIPD---------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 315 geaepfvrncfvlgtcapvvgsniiqcVNEKVLLEKWAEFVREVDPDIItgYNILNFDLPYILDRAKVLSLPQvSHLGRQ 394
Cdd:PRK05761 208 ---------------------------DSEKELLAELFDIILEYPPVVT--FNGDNFDLPYLYNRALKLGIPK-EEIPIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 395 KEKGSVVRD-------AAISSKQMGSRvnksidihgriifdvlqvvlrdYKLRSYTLNSVSYQFLSEQKEDVEHNIipdl 467
Cdd:PRK05761 258 PGRAGIHIDlykffqnKAVRSYAFYGK----------------------YRHREARLDAVGRALLGISKVELETNI---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 468 qrgDEQTRRRLAQYCLKDAYLPLRLL----DKLMSIInyIEMARVTGVPMNFL--LTKGQQIKilSMMLRRCKQNNFFLP 541
Cdd:PRK05761 312 ---SELDLEELAEYNFRDAEITLKLTffnnELVLKLI--LLLSRISKLPIEELsrATISTWIS--NLEYWEHRKRGWLIP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 542 V---IEANSGD--------GEGYEGATVIDPIRGFYnEPIATLDFASLYPSIMIAHNLCYTTLlkSPQGVENEDYIRTPS 610
Cdd:PRK05761 385 WkedILRLDHEvykkaiikGKKYRGGLVFQPPPGIF-FNVYVLDFASLYPSIIVKWNLSPETV--RIPECKCHYDDEVPE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 611 GQYfATKSKRRGLLPEILEDILAARKRAKNDMKNEK--DEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSV 688
Cdd:PRK05761 462 LGH-SVCDDRPGLTSVLVGLLRDFRVKIYKKKAKDPnlDEERRAWYDVVQRALKVFLNASYGVFGAENFKLYRIEVAESI 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 689 TAFGRKMIDMTKLEVERIykkgaldgkcpaDAKVIYGDTDSVMVKFGVETVAQAMeigldaAKEVSKIFTppIKLEFEKV 768
Cdd:PRK05761 541 TALGREILLSTKKKAEEL------------GLKVLYGDTDSLFVWGPTKESLEEL------IKEIEERTG--IDLEVDKT 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 769 YSpYLLIN--KKRYAGLYFTkpdvhDKMDCKGLETVRRDNCPLVAKVLGVCLEKL-------LIERDQQSALDFAKRTIS 839
Cdd:PRK05761 601 YD-WVAFSglKKNYFGVLKD-----GKVKIKGIVAKKRNTPEFVKELQREVLEVLksirspeDVEKVKDEIEDVLKRYYE 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 840 DLLCNKIDISLLIISKELTKSGDKY-QAKQAHVelAARMKKRDAGSAPRLGDRVPYVFVAAAKNVPAYERAEDPTFvlqn 918
Cdd:PRK05761 675 KLRAKDYPLDELAIRVRLSKPLDEYtKNTPQHV--KAALQLRDYGVEVSPGDIISYVKVDDKRGVKPVQLAKLSEI---- 748
|
810 820
....*....|....*....|....*..
gi 17559488 919 niplDTKHYLTNqlakpLARIFEPILG 945
Cdd:PRK05761 749 ----DVEKYIEL-----LRSALEQILS 766
|
|
| POLBc_Pol_II |
cd05537 |
DNA polymerase type-II subfamily catalytic domain. Bacteria contain five DNA polymerases (I, ... |
555-944 |
1.87e-45 |
|
DNA polymerase type-II subfamily catalytic domain. Bacteria contain five DNA polymerases (I, II, III, IV and V). DNA polymerase II (Pol II) is a prototype for the B-family of polymerases. The role of Pol II in a variety of cellular activities, such as repair of DNA damaged by UV irradiation or oxidation has been proven by genetic studies. DNA polymerase III is the main enzyme responsible for replication of the bacterial chromosome; however, In vivo studies have also shown that Pol II is able to participate in chromosomal DNA replication with larger role in lagging-strand replication.
Pssm-ID: 99920 Cd Length: 371 Bit Score: 168.21 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 555 GATVIDPIRGFYNEpIATLDFASLYPSIMIAHNLCYTTLLKSPQGVENEDYIRTPSGQYFatkSKRRGLLPEILEDILAA 634
Cdd:cd05537 5 GGYVMDSKPGLYKN-VLVLDFKSLYPSIIRTFLIDPLGLIEGLKAPDPEDLIPGFLGARF---SREKHILPDLIARLWAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 635 RKRAKNDmKNEkdefkRMVYngrqlALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEVERiykkgaldg 714
Cdd:cd05537 81 RDEAKRE-KNA-----PLSQ-----AIKIIMNSFYGVLGSTGCRFFDPRLASSITLRGHEIMKQTRAWIEQ--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 715 kcpADAKVIYGDTDSVMVKFGVE-TVAQAMEIGLDAAKEVSKIFTPPIK----------LEFEKVYSPYLLI-------- 775
Cdd:cd05537 141 ---QGYQVIYGDTDSTFVWLGEElDAAEAQAIGKELASQINQWWAQKLKeefglesfleIEFETHYSRFFMPtirgsdeg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 776 NKKRYAGLYFTkpDVHDKMDCKGLETVRRDNCPLVAKvlgvcLEKLLIER--DQQSALDFAKRTISDLLCNKIDiSLLII 853
Cdd:cd05537 218 SKKRYAGLKST--DGGDELVFKGLETVRSDWTPLARQ-----FQKELYERvfNDEPYEGFIKETVEELLAGELD-ELLVY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 854 SKELTKSGDKYQAKQA-HVElAARMKKRdagSAPRLGDRVPYVFVAAAKNVPAYERAEdptfvlQNNIPLDTKHYLTNQL 932
Cdd:cd05537 290 RKRLRRPLSEYTKNVPpHVQ-AARLADQ---INRELGRPRQYQWIEYVITVNGPEPLE------YRTSPLDYQHYIDKQL 359
|
410
....*....|..
gi 17559488 933 aKPLArifEPIL 944
Cdd:cd05537 360 -KPIA---DSIL 367
|
|
| PHA03036 |
PHA03036 |
DNA polymerase; Provisional |
279-920 |
1.48e-34 |
|
DNA polymerase; Provisional
Pssm-ID: 222962 [Multi-domain] Cd Length: 1004 Bit Score: 143.62 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECiGRRGVFPEAIKDPIIQIA------------------NLVKIEGEAEPFVRNCFVLGTCAPVVGSNIIQ 340
Cdd:PHA03036 159 PRSYLFLDIEC-HFDKKFPSVFINPVSHISccyidlsgkekrftlineDMLSEDEIEEAVKRGYYEIESLLDMDYSKELI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 341 CVNEKVLLeKWAEFVREVDPDIITGYNILNFDLPYILDRAKVLSLPQV---SHLGRQKEKGSVVRDAAISSKQMGSRVNK 417
Cdd:PHA03036 238 LCSEIVLL-RIAKKLLELEFDYVVTFNGHNFDLRYISNRLELLTGEKIifrSPDGKETVHLCIYERNLSSHKGVGGVANT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 418 SIDI---HGRIIFDVLQVVLRDYKLRSYTLNSVSYQ-----FLSEQKEDVEHNIIPDLQRGDEQTRR------RLAQYCL 483
Cdd:PHA03036 317 TYHInnnNGTIFFDLYTFIQKTEKLDSYKLDSISKNafncnAKVLSENNNEVTFIGDNTTDAKGKASifsevlSTGNYVT 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 484 KDAYLPLRLLDKlmSII------------------------------------NY-----IEMARVT------------- 509
Cdd:PHA03036 397 INDDDICKILDK--DIIensftvkvicknnyipgdtytlsfgkddvdlsdmykNYnleiaLEMARYCihdaclckylwey 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 510 -GVP---------------MNF-----LLTKGQQIKIL----SMMLRRCKQNNFFlpvieansgdgegYEGATVIDPIRG 564
Cdd:PHA03036 475 yGIEtkidagastyllpqsMVFeyrasTLIKGPLLKLLleekTILVRSETKNKFP-------------YEGGKVFAPKQK 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 565 FYNEPIATLDFASLYPSIMIAHNLCYTTL---LKSPQGVENE-------------DYI------RTPSGQY-FATKSKRR 621
Cdd:PHA03036 542 MFDNNVLIFDYNSLYPNVCIFGNLSPETLvgvVVNDNRLEAEinkqelrrkypypRYIyvhcepRSPDLVSeIAVFDRRI 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 622 -GLLPEILEDILAARKRAKNDMKNEKDEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMT- 699
Cdd:PHA03036 622 eGIIPKLLKTFLEERARYKKLLKEATSSVEKAIYDSMQYTYKIVANSVYGLMGFRNSALYSYASAKSCTAIGRNMIKYLn 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 700 -----------KLEVER----IYKKGALDGKCPADA----------KVIYGDTDSVMVKFGVETVaqamEIGLDAAKEVS 754
Cdd:PHA03036 702 svlngsklingKLILANcpinPFFKDDRSIDTNYDTnlpveynftfRSVYGDTDSVFLEINTKDV----DKSIKIAKELE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 755 -----KIFTPPIKLEFEKVYSPYLLINKKRYAGL----YFTKPDVhDKMDCKGLETVRRDNCP---LVAKVLGVCLEKLL 822
Cdd:PHA03036 778 riineKVLFDNFKIEFEAVYKNLIMQSKKKYTTLkyiaSSTDGSV-PERVNKGTSETRRDVSKfhkYMIKIYKTRLLDML 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 823 IERD---QQSALDFAKRTISDLLCN----KIDISLLIISKelTKSGDKYQAKQAHVELAARMKKRDAGSApRLGDRVPYV 895
Cdd:PHA03036 857 SEGNmnsNQVCIDILRSLEKDLIIEfdsrSAPLEMFLLSR--THHCNYKSPDNPNMYLVNEYNKNNPEKI-EIGERYYFA 933
|
810 820 830
....*....|....*....|....*....|...
gi 17559488 896 FVAAAK--------NVPAYERAEDPTFVLQNNI 920
Cdd:PHA03036 934 YICPINlpwqkklvNIKTYERIIDRSFKLKSNE 966
|
|
| POLBc_B2 |
cd05531 |
DNA polymerase type-B B2 subfamily catalytic domain. Archaeal proteins that are involved in ... |
555-945 |
9.28e-31 |
|
DNA polymerase type-B B2 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaeal members also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases.
Pssm-ID: 99914 Cd Length: 352 Bit Score: 124.76 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 555 GATVIDPIRGFYnEPIATLDFASLYPSIMIAHNLcyttllkSPQGVENEDYIRTPSGQY-FATKSKRRGLLPEILEDILA 633
Cdd:cd05531 7 GGLVFQPEPGLY-ENVAQIDFSSMYPSIIVKYNI-------SPETINCRCCECRDHVYLgHRICLKRRGFLPEVLEPLLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 634 ARKRAKNDMKNEKdefkrmVYNGRQLALKISANSVYGFTG---ATVGKLPCLEisqSVTAFGRKMIDMTKlevERIYKKG 710
Cdd:cd05531 79 RRLEYKRLKKEED------PYAGRQKALKWILVTSFGYLGyknAKFGRIEVHE---AITAYGRKILLRAK---EIAEEMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 711 aldgkcpadAKVIYGDTDSVMVKfGVETVAQameigldAAKEVSKIFTPPIKLefEKVYSPYLLINKKRYAGL---YFTK 787
Cdd:cd05531 147 ---------FRVLHGIVDSLWIQ-GRGDIEE-------LAREIEERTGIPLKL--EGHYDWIVFLPERDGLGApnrYFGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 788 pDVHDKMDCKGLETVRRDNCPLVAKVLGVCLEKLlieRDQQSALDF--AKRTISDLL------CNKIDISLLIISKELTK 859
Cdd:cd05531 208 -LSDGEMKVRGIELRRRDTPPFVKKFQEEALDIL---ASAKTPEELlkLREEALDLFrrylqrLREGDLEDLIIEKKISK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 860 SGDKYQAKQAHVELAArmkkRDAGSAPRLGDRVPYVFVAAAKNVPayeraedptfVLQNNIPLDTKHYLTNqlakpLARI 939
Cdd:cd05531 284 RSSEYKVLASTALKAL----RAKGVSVVPGMKIEYIVRDGKRPVP----------DLGNDEGYDTKYYREL-----LERA 344
|
....*.
gi 17559488 940 FEPILG 945
Cdd:cd05531 345 AEELLF 350
|
|
| POLBc_B1 |
cd05530 |
DNA polymerase type-B B1 subfamily catalytic domain. Archaeal proteins that are involved in ... |
550-909 |
4.23e-29 |
|
DNA polymerase type-B B1 subfamily catalytic domain. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaeal members also possess multiple family B DNA polymerases (B1, B2 and B3). So far there is no specific function(s) has been assigned for different members of the archaea type B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B DNA polymerases are support independent gene duplications during the evolution of archaeal and eukaryotic family B DNA polymerases.
Pssm-ID: 99913 Cd Length: 372 Bit Score: 120.53 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 550 GEGYEGATVIDPIRG-FYNepIATLDFASLYPSIMIAHNLCYTTLLKSPqgvENEDYIRTPSGQYFATKsKRRGLLPEI- 627
Cdd:cd05530 10 GKKYRGAIVLEPPPGiFFN--VVVLDFASLYPSIIKVWNLSYETVNCPH---CECKTNEVPEVGHWVCK-KRPGITSQIi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 628 --LEDILAAR--KRAKNDMKNEKDefkRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIDMTKLEV 703
Cdd:cd05530 84 glLRDLRVKIykKKAKDKSLDEEM---RQWYDVVQSAMKVFINASYGVFGAENFPLYCPPVAESTTALGRYIITSTIKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 704 ERIykkgaldgkcpaDAKVIYGDTDSVMVKFGVETVAQameiglDAAKEVSKIFTppIKLEFEKVYSPYLLIN-KKRYAG 782
Cdd:cd05530 161 REL------------GLKVLYGDTDSLFLWNPPQEQLE------DLVEWVEKELG--LDLELDKEYRYVVFSGlKKNYLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 783 LYftkpdVHDKMDCKGLeTVRRDNCPLVAKVLGVCLEKLLIERDQQSALDFAKRTISDLLCN--------KIDISLLIIS 854
Cdd:cd05530 221 VT-----KDGSVDIKGL-LGKKRNTPEFVKELFYEVIEILSAVNSPEDFEKAREKIRDIVKGvykrlkkkEYTLDQLAFK 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17559488 855 KELTKSGDKY-QAKQAHVElAARMKKRdAGSAPRLGDRVPYVFVAAAKNVPAYERA 909
Cdd:cd05530 295 VMLSKPPEEYtKNTPQHVK-AARQLEK-YGRNVEAGDIISYVKVKGKEGVKPVQLA 348
|
|
| 43 |
PHA02528 |
DNA polymerase; Provisional |
280-835 |
1.02e-28 |
|
DNA polymerase; Provisional
Pssm-ID: 177369 [Multi-domain] Cd Length: 881 Bit Score: 124.42 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 280 IRTLSLDIECIGRRGvFPEA--IKDPIIQIANLVKIEGEAepFVrncFVLGTCAP------VVGSNIIQ------CVNEK 345
Cdd:PHA02528 106 IRIANLDIEVTAEDG-FPDPeeAKYEIDAITHYDSIDDRF--YV---FDLGSVEEwdakgdEVPQEILDkvvympFDTER 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 346 VLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAK-VLSLPQVSHL---GRQKEKgsvvrdaaISSKQMGSRvNKSIDI 421
Cdd:PHA02528 180 EMLLEYINFWEENTPVIFTGWNVELFDVPYIINRIKnILGEKTAKRLspwGKVKER--------TIENMYGRE-EIAYDI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 422 HGRIIFDVLQVvlrdYK------LRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDEQtrrRLAQYCLKDAYLPLRLLDK 495
Cdd:PHA02528 251 SGISILDYLDL----YKkftftnQPSYRLDYIAEVELGKKKLDYSDGPFKKFRETDHQ---KYIEYNIIDVELVDRLDDK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 496 LMSIINYIEMARVTGVPMNFLLTkgqQIKIL-SMMLRRCKQNNFFLPviEANSGDGEGYEGATVIDPIRGFYNEpIATLD 574
Cdd:PHA02528 324 RKLIELVLSMAYYAKINFEDVFS---PIKTWdAIIFNSLKEEKIVIP--ENKSHKKQKYAGAFVKEPVPGAYRW-VVSFD 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 575 FASLYPSIMIAHNLCYTTLLKSPQGVENEDYIRT----PSGQYFAT------KSKRRGLLPEILEDILAARKRAKNDMKN 644
Cdd:PHA02528 398 LTSLYPSIIRQVNISPETIAGTFHVAPVHEYINKtaprPSDEYSCSpngwmyRKDIRGVIPTEIKKVFDQRKIYKKKMLA 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 645 EK------------------------------DEFKRMV---------------------YNGRQLALKISANSVYGFTG 673
Cdd:PHA02528 478 AErnaeliktiledlndsvdtpidvdyyfdfsDEFKAELktltksslkalleecekeialCNTIQMARKILINSLYGALG 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 674 ATVGKLPCLEISQSVTAFGrkmidmtKLEVERIYKK--GALDGKCPADAK--VIYGDTDSVMVKFG--VETVAQAMEigL 747
Cdd:PHA02528 558 NEHFRYYDLRNAEAITLFG-------QLAIQWIERKmnEYLNKLCKTEDEdyVIYGDTDSIYVNLDplVEKVGEDKF--K 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 748 DAAKEVSKI-------FTPPIKLEF------------------EKVYSPYLLINKKRYA-------GLYFTKPdvhdKMD 795
Cdd:PHA02528 629 DTNHWVDFLdkfckerMEPYIDSSYrelceymnnyehlmfmdrEAIAGPGFWTAKKRYAlnvwdseGTRYAEP----KLK 704
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 17559488 796 CKGLETVRRDNCPLVAKVLGVCLEKLLIErDQQSALDFAK 835
Cdd:PHA02528 705 IMGIETQRSSTPKAVQKALKEAIRRILQE-GEESLQEYIK 743
|
|
| DNA_polB_Kod1_like_exo |
cd05780 |
DEDDy 3'-5' exonuclease domain of Pyrococcus kodakaraensis Kod1 and similar archaeal family-B ... |
281-496 |
1.32e-27 |
|
DEDDy 3'-5' exonuclease domain of Pyrococcus kodakaraensis Kod1 and similar archaeal family-B DNA polymerases; The 3'-5' exonuclease domain of archaeal family-B DNA polymerases with similarity to Pyrococcus kodakaraensis Kod1, including polymerases from Desulfurococcus (D. Tok Pol) and Thermococcus gorgonarius (Tgo Pol). Kod1, D. Tok Pol, and Tgo Pol are thermostable enzymes that exhibit both polymerase and 3'-5' exonuclease activities. They are family-B DNA polymerases. Their amino termini harbor a DEDDy-type DnaQ-like 3'-5' exonuclease domain that contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Members of this subfamily show similarity to eukaryotic DNA polymerases involved in DNA replication. Some archaea possess multiple family-B DNA polymerases. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family-B DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases.
Pssm-ID: 99823 [Multi-domain] Cd Length: 195 Bit Score: 110.91 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 281 RTLSLDIECIGRRGVfPEAIKDPIIQI-------ANLVKIEGEAEPFVRncfvlgtcapVVGsniiqcvNEKVLLEKWAE 353
Cdd:cd05780 4 KILSFDIEVLNHEGE-PNPEKDPIIMIsfadeggNKVITWKKFDLPFVE----------VVK-------TEKEMIKRFIE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 354 FVREVDPDIITGYNILNFDLPYILDRAKVLSLPqvSHLGRQKEKgsvvrdaaISSKQMGSRvNKSiDIHGRIIFDVLQVV 433
Cdd:cd05780 66 IVKEKDPDVIYTYNGDNFDFPYLKKRAEKLGIE--LDLGRDGSE--------IKIQRGGFN-NAS-EIKGRIHVDLYPVA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 434 LRDYKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDEQtRRRLAQYCLKDAYLPLRLLDKL 496
Cdd:cd05780 134 RRTLNLTRYTLERVYEELFGIEKEDVPGEEIAEAWDSGEN-LERLFRYSMEDAKYTYEIGKEF 195
|
|
| POLBc_Pol_II_B |
cd05538 |
DNA polymerase type-II B subfamily catalytic domain. Bacteria contain five DNA polymerases (I, ... |
553-938 |
4.19e-26 |
|
DNA polymerase type-II B subfamily catalytic domain. Bacteria contain five DNA polymerases (I, II, III, IV and V). DNA polymerase II (Pol II) is a prototype for the B-family of polymerases. The role of Pol II in a variety of cellular activities, such as repair of DNA damaged by UV irradiation or oxidation has been proved by genetic studies. DNA polymerase III is the main enzyme responsible for replication of the bacterial chromosome; however, In vivo studies have also shown that Pol II is able to participate in chromosomal DNA replication with larger role in lagging-strand replication.
Pssm-ID: 99921 Cd Length: 347 Bit Score: 111.04 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 553 YEGATVIDPIRGFYNePIATLDFASLYPSIMIAHNLCyttllkspqgvenedyirtpsgqyfaTKSKRRGLLPEILEDIL 632
Cdd:cd05538 3 FEGGYAYVFITGVLG-PIVHADVASLYPSIMLAYRIC--------------------------PARDSLGIFLALLKYLV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 633 AARKRAKNDMKNEKDEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSVTAFGRKMIdmtKLEVERIYKKGal 712
Cdd:cd05538 56 ELRLAAKESARAAARPAERDAFKAKQAAFKVLINSFYGYLGTGLHAFSDPEAAAEVTRLGRELL---KLMIRWLRRRG-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 713 dgkcpadAKVIYGDTDSV--MVKFGVETVAQAMEIgldaAKEVSKIFTPPIKLEFEKVYSPYLLINKKRYAGLyftkpDV 790
Cdd:cd05538 131 -------ATPVEVDTDGIyfIPPNGVDTEDEEEEL----VRELSSTLPKGITVEFDGRYRAMFSYKIKNYALL-----DY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 791 HDKMDCKGLETVRRDNCPLVAKVLGVCLeKLLIERDQQSALDFAKRTISDLLCNKIDISLLIISKELTKSGDKY------ 864
Cdd:cd05538 195 DGKLIVKGSAFRSRGIEPFLREFLREAV-RLLLQGDGAGVHDLYEDYLRRLRSHELPISDLARTETLKESPEEYlqkvra 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 865 --QAKQAHVELAARmkkrdAGSAPRLGDRVPYVFVAAAKNVPAYERAE-----DPTFVLQNnipldTKHYLT--NQLAKP 935
Cdd:cd05538 274 gkRNPAAAYEIALA-----RPREWRAGDRVTYYVSGTGKGVSVYENCRlvadyDPAHPDEN-----TGFYAErlLQLAAR 343
|
...
gi 17559488 936 LAR 938
Cdd:cd05538 344 LLP 346
|
|
| DNA_polB_II_exo |
cd05784 |
DEDDy 3'-5' exonuclease domain of Escherichia coli DNA polymerase II and similar bacterial ... |
279-494 |
2.82e-22 |
|
DEDDy 3'-5' exonuclease domain of Escherichia coli DNA polymerase II and similar bacterial family-B DNA polymerases; The 3'-5' exonuclease domain of Escherichia coli DNA polymerase II (Pol II) and similar bacterial proteins. Pol II is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain has a fundamental role in the proofreading activity of polII. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Pol II is involved in a variety of cellular activities, such as the repair of DNA damaged by UV irradiation or oxidation. It plays a pivotal role in replication-restart, a process that bypasses DNA damage in an error-free manner. Pol II is also involved in lagging strand synthesis.
Pssm-ID: 99827 [Multi-domain] Cd Length: 193 Bit Score: 95.71 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECIGRRGVFpeaikdpiiQIAnlvkIEGEAEpfvRNCFVLGTCAPVVGSNIIQCVNEKVLLEKWAEFVREV 358
Cdd:cd05784 2 KLKVVSLDIETSMDGELY---------SIG----LYGEGQ---ERVLMVGDPEDDAPDNIEWFADEKSLLLALIAWFAQY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 359 DPDIITGYNILNFDLPYILDRAKVLSLPqvSHLGRQkekgsvvrDAAISSKQMGSRVNKSIDIHGRIIFDVLQvVLRD-- 436
Cdd:cd05784 66 DPDIIIGWNVINFDLRLLQRRAEAHGLP--LRLGRG--------GSPLNWRQSGKPGQGFLSLPGRVVLDGID-ALKTat 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559488 437 YKLRSYTLNSVSYQFLSEQKEdvehnIIPDLQRGDEQTRR------RLAQYCLKDAYLPLRLLD 494
Cdd:cd05784 135 YHFESFSLENVAQELLGEGKL-----IHDVDDRGAEIERLfredklALARYNLQDCELVWRIFE 193
|
|
| DNA_polB_zeta_exo |
cd05778 |
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA ... |
282-494 |
1.83e-20 |
|
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase zeta. DNA polymerase zeta is a family-B DNA polymerase which is distantly related to DNA polymerase delta. It plays a major role in translesion replication and the production of either spontaneous or induced mutations. In addition, DNA polymerase zeta also appears to be involved in somatic hypermutability in B lymphocytes, an important element for the production of high affinity antibodies in response to an antigen. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The DnaQ-like 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis.
Pssm-ID: 99821 [Multi-domain] Cd Length: 231 Bit Score: 91.53 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 282 TLSLDIECIGRRGVFPEAIKDPIIQIAnlVKIEGEAEPFVRN---CFVLGTCAPVVGSNIIQCV------------NEKV 346
Cdd:cd05778 6 ILSLEVHVNTRGDLLPDPEFDPISAIF--YCIDDDVSPFILDankVGVIIVDELKSNASNGRIRsglsgipvevveSELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 347 LLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVL----SLPQVSHLGRQKEKGSVVRDAAISSKQMgsrvnKSIDIH 422
Cdd:cd05778 84 LFEELIDLVRRFDPDILSGYEIQRSSWGYLIERAAALgiddLLDEISRVPSDSNGKFGDRDDEWGYTHT-----SGIKIV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 423 GRIIFDVLQVVLRDYKLRSYTLNSVSYQFLSEQKEDVEHNIIPD-LQRGDEQTRRRLAQYCLKDAYLPLRLLD 494
Cdd:cd05778 159 GRHILNVWRLMRSELALTNYTLENVVYHVLHQRIPLYSNKTLTEwYKSGSASERWRVLEYYLKRVRLNLEILD 231
|
|
| pol2 |
TIGR00592 |
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA ... |
256-699 |
4.77e-20 |
|
DNA polymerase (pol2); All proteins in this superfamily for which functions are known are DNA polymerases.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273159 [Multi-domain] Cd Length: 1172 Bit Score: 96.66 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 256 IEVTVPVKNLIVHESDGEWAGIAPIRTLSLDIECI--GRRGVFP--EAIKDPIIQIAN----LVKIEGEAEPFVRNCFVL 327
Cdd:TIGR00592 174 ILIPVPLKRAEFAGGDVQMEGDPELKLASFDIETYfhDGKDFFPgdENPADEEIMISTtpviAKQWDYESEPEARVVTWK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 328 GTCAPVVGSNIIQCVNEKVLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVL-----SLPQVSHLGRQKEKGSVVR 402
Cdd:TIGR00592 254 KPDKPTTGSYVESVSEEISMIKRFWDVIDQEDTDVEITVNGDNFDLVYLADRQVFQfywdaYEDPAEKLGVVLLFGRDVD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 403 DAAISSKQMG-SRVNKSIDIHGRIIFDVLQVVLRDYKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQRGDEQTrrRLAQY 481
Cdd:TIGR00592 334 HVSPCVQVKGiNRDLFFLPREGKIDFDLGKVTRRTINLPDYYLEFVSELALGYKKEKFRAKPIAKKYEFEAPD--IDAPY 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 482 CLKDAYLPLRLLDKLMSIINYIEMARVTGVPMNFLLTKGQQIKILsmMLRRCKQNNFFLP----VIEANSGDGEGYEGAT 557
Cdd:TIGR00592 412 SSEYLEVTYELGKEFAPMEALPSDLKGQTFWHVFGSNTGNLERFL--LLRKIKGPCWLAVkgpdELEYPRRSWCKYEGGY 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 558 V----IDPIRGFYNEPIATLDFA--SLYPSIMIAHNLCYTTL------LKSPQGVENEDyIRTPSGQYFATKSKRRGL-- 623
Cdd:TIGR00592 490 VkppnVEKGLDKTPPPLVVLDFSmkSLNPSIIRNEIVSIPDTlhrefaLDKPPPEPPYD-VHPCVGTRPKDCSFPLDLkg 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 624 -----LPEILEDILAARKRAKNDMKNEK--DEFKRMVYNGRQLALKISANSVYGFTGATVGKLPCLEISQSvtaFGRKMI 696
Cdd:TIGR00592 569 efpgkKPSLVEDLATERALIKKFMAKVKkiDPDEIVGHDYQQRALKVLANRINDLKIPTWSKIGRLRRSPK---FGRRFG 645
|
...
gi 17559488 697 DMT 699
Cdd:TIGR00592 646 ERT 648
|
|
| zf-C4pol |
pfam14260 |
C4-type zinc-finger of DNA polymerase delta; In fission yeast this zinc-finger domain appears ... |
981-1054 |
1.23e-19 |
|
C4-type zinc-finger of DNA polymerase delta; In fission yeast this zinc-finger domain appears is the region of Pol3 that binds directly to the B-subunit, Cdc1. Pol delta is a hetero-tetrameric enzyme comprising four evolutionarily well-conserved proteins: the catalytic subunit Pol3 and three smaller subunits Cdc1, Cdc27 and Cdm1.
Pssm-ID: 464119 Cd Length: 68 Bit Score: 83.58 E-value: 1.23e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17559488 981 CLGCKSVlpraesENAVCKHC-EPKLPTIFASrMNTMHELENHFGRLWTECQNCAKTMQDKVNCSARDCPIYYMR 1054
Cdd:pfam14260 1 CLGCGAP------EEPLCKNCrSDPQASYLEL-LSRLRELERRFNRLWTICQRCQGSLHEEVLCDSRDCPVFYMR 68
|
|
| DNA_polB_B3_exo |
cd05781 |
DEDDy 3'-5' exonuclease domain of Sulfurisphaera ohwakuensis DNA polymerase B3 and similar ... |
279-486 |
2.00e-18 |
|
DEDDy 3'-5' exonuclease domain of Sulfurisphaera ohwakuensis DNA polymerase B3 and similar archaeal family-B DNA polymerases; The 3'-5' exonuclease domain of archaeal proteins with similarity to Sulfurisphaera ohwakuensis DNA polymerase B3. B3 is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. B3 exhibits both polymerase and 3'-5' exonuclease activities. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family B polymerases also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Archaeal proteins that are involved in DNA replication are similar to those from eukaryotes. Some archaea possess multiple family-B DNA polymerases. B3 is mainly found in crenarchaea. Phylogenetic analyses of eubacterial, archaeal, and eukaryotic family B-DNA polymerases support independent gene duplications during the evolution of archaeal and eukaryotic family-B DNA polymerases.
Pssm-ID: 99824 [Multi-domain] Cd Length: 188 Bit Score: 84.30 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECIGRRGvFPEAIKDPIIQIANLVKiEGEAEPFVRNCFvlgtcapvvgsniiqcvNEKVLLEKWAEFVREV 358
Cdd:cd05781 2 DLKTLAFDIEVYSKYG-TPNPRRDPIIVISLATS-NGDVEFILAEGL-----------------DDRKIIREFVKYVKEY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 359 DPDIITGYNILNFDLPYILDRAKVLSLpqvshlgrqkeKGSVVRDaaiSSKQMGSRVNKSIDIHGRIIFDVLQVVLRDYK 438
Cdd:cd05781 63 DPDIIVGYNSNAFDWPYLVERARVLGV-----------KLDVGRR---GGSEPSTGVYGHYSITGRLNVDLYDFAEEIPE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17559488 439 LRSYTLNSVSyQFL----SEQKEDVEHNIIPDLQRgDEQTRRRLAQYCLKDA 486
Cdd:cd05781 129 VKVKTLENVA-EYLgvmkKSERVLIEWYRIYEYWD-DEKKRDILLKYNRDDA 178
|
|
| DNA_polB_alpha_exo |
cd05776 |
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha, a family-B DNA ... |
336-496 |
1.74e-16 |
|
inactive DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase alpha. DNA polymerase alpha is a family-B DNA polymerase with a catalytic subunit that contains a DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (delta and epsilon are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase alpha is almost exclusively required for the initiation of DNA replication and the priming of Okazaki fragments during elongation. It associates with DNA primase and is the only enzyme able to start DNA synthesis de novo. The catalytic subunit contains both polymerase and 3'-5' exonuclease domains, but only exhibits polymerase activity. The 3'-5' exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, without the four conserved acidic residues that are crucial for metal binding and catalysis. This explains why in most organisms, that no specific repair role, other than check point control, has been assigned to this enzyme. The exonuclease domain may have a structural role.
Pssm-ID: 99819 [Multi-domain] Cd Length: 234 Bit Score: 79.96 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 336 SNIIQCVNEKVLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVLSLPQVSHLGRQKekgsvvRDAAISSKQMGSRV 415
Cdd:cd05776 74 TKVRIFENERALLNFFLAKLQKIDPDVLVGHDLEGFDLDVLLSRIQELKVPHWSRIGRLK------RSVWPKKKGGGKFG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 416 NKSIdIHGRIIFDVlQVVLRD-YKLRSYTLNSVSYQFLSEQKEDVEHNIIPDLQrGDEQTRRRLAQYCLKDAYLPLRLLD 494
Cdd:cd05776 148 EREL-TAGRLLCDT-YLSAKElIRCKSYDLTELSQQVLGIERQDIDPEEILNMY-NDSESLLKLLEHTEKDAYLILQLMF 224
|
..
gi 17559488 495 KL 496
Cdd:cd05776 225 KL 226
|
|
| DNA_polB_like2_exo |
cd05785 |
Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA ... |
280-485 |
8.55e-13 |
|
Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases; A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.
Pssm-ID: 99828 [Multi-domain] Cd Length: 207 Bit Score: 68.59 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 280 IRTLSLDIECIGRRGVF---PEAIKDPIIQIAnlVKIEGEAEPFVRncfvlgtcapvvgsniIQCVNEKVLLEKWAEFVR 356
Cdd:cd05785 9 LRRLQLDIETYSLPGFFfsnPDRGDDRIIIVA--LRDNRGWEEVLH----------------AEDAAEKELLEELVAIIR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 357 EVDPDIITGYNILNFDLPYILDRAKVLSLPQVshLGRQkekGSVVRdaaisskQMGSRVN---KSID-----IHGRIIFD 428
Cdd:cd05785 71 ERDPDVIEGHNIFRFDLPYLRRRCRRHGVPLA--IGRD---GSIPR-------QRPSRFRfaeRLIDyprydIPGRHVID 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 429 VLQVVLR----DYKLRSYTLNSVSYQF--LSEQKEDVEHNIIPDLQRGDeqtRRRLAQYCLKD 485
Cdd:cd05785 139 TYFLVQLfdvsSRDLPSYGLKAVAKHFglASPDRTYIDGRQIAEVWRSD---PARLLAYALDD 198
|
|
| DNA_polB_B1_exo |
cd05783 |
DEDDy 3'-5' exonuclease domain of Sulfolobus solfataricus DNA polymerase B1 and similar ... |
277-492 |
1.61e-12 |
|
DEDDy 3'-5' exonuclease domain of Sulfolobus solfataricus DNA polymerase B1 and similar archaeal family-B DNA polymerases; The 3'-5' exonuclease domain of Sulfolobus solfataricus DNA polymerase B1 and similar archaeal proteins. B1 is a family-B DNA polymerase. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. B1displays thermostable polymerase and 3'-5' exonuclease activities. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. The exonuclease domain of family-B polymerases also contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation. Family-B DNA polymerases from thermophilic archaea are unique in that they are able to recognize the presence of uracil in the template strand, leading to the stalling of DNA synthesis. This is an additional safeguard mechanism against increased levels of deaminated bases during genome duplication at high temperatures. S. solfataricus B1 also interacts with DNA polymerase Y and may contribute to genome stability mechanisms.
Pssm-ID: 99826 [Multi-domain] Cd Length: 204 Bit Score: 67.73 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 277 IAPIRTLSLDIEcigrrgVFPEA---IKDP------IIQIAnLVKIEGeaepfVRNCFVLGTCAPVVGSNIIQCVNEKVL 347
Cdd:cd05783 2 IPKLKRIAIDIE------VYTPIkgrIPDPktaeypVISVA-LAGSDG-----LKRVLVLKREGVEGLEGLLPEGAEVEF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 348 LEKWAEFVREVdPDIITGYNIL------NFDLPYILDRAKVLSLPqvshlgRQKEKGSVVRDAAisskqmgsRVNKSIDI 421
Cdd:cd05783 70 FDSEKELIREA-FKIISEYPIVltfngdNFDLPYLYNRALKLGIP------KEEIPIYLKRDYA--------TLKHGIHI 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17559488 422 HGRIIFDV--LQVVLRDYKLRSYTLNSVSYQFLSEQKEDVEHNIipdlqrgDEQTRRRLAQYCLKDAYLPLRL 492
Cdd:cd05783 135 DLYKFFSNraIQVYAFGNKYREYTLDAVAKALLGEGKVELEKNI-------SELNLYELAEYNYRDAELTLEL 200
|
|
| PHA03334 |
PHA03334 |
putative DNA polymerase catalytic subunit; Provisional |
345-731 |
4.21e-12 |
|
putative DNA polymerase catalytic subunit; Provisional
Pssm-ID: 223049 [Multi-domain] Cd Length: 1545 Bit Score: 70.66 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 345 KVLLEKWAEFV----REVDPDIITGYNILN---FDLPYILDRAKVLSLPQVSHLGRQKE--------KGSVVRDAAISSK 409
Cdd:PHA03334 379 KALMEAWEAFLskdpQLVPAQLLFGSDILNsnyLELLDVIESHKAQFKATCRKAAARKEeigsymktRDTVQDFNDNDKK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 410 QMGSRVNKsidiHGRIIFDVLQVVLR---DYKLRSYTLNSVSYQFLSEQK-----------EDVEHNIIPDLQRGDEQTR 475
Cdd:PHA03334 459 YLNSTSHG----FGAHIIDLMRVCNTksiKAKCSSRKLDTVARLIISKSKphknppkigkmDDVKYTEMDGMFTAGGAAL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 476 RRLAQYCLKDAYLPLRLLDKLMSIINYIEMARVT----------GVpMNFL----LTKGQQIKILSMMLR--------RC 533
Cdd:PHA03334 535 ARYLIYNLVDSELLIRIAKNLDPVIEFLNRLRATynidyvahgrGV-MNFCgfvqSTKSVEVPLLKARLRigifvatgRI 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 534 KQNNFFLPVIEANSGDGEGYEGATVIDPIRGF-----YNEPIATLDFASLYPSIMIAHNLCYTTLL-------------- 594
Cdd:PHA03334 614 AESLCMPEKYARDCRQKIKLKGGYVFAPLTGLtfagpYQGTELTLDFASLYPSNMCDANISPEAIVdpdctarvrgwvvf 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 595 ---KSPQGVENEDYIRTPSGQYFATKSKRRglLPEI----LEDILAARKRAKNDMKNEKDEFKRMVYNGRQLALKISANS 667
Cdd:PHA03334 694 dwkKIDRGFGKATLMYTILRTKPEEPSWRR--FTTYttssLNHYLSMRTEYKGAMKQAKDPKLKSYHNQLQNEMKICANS 771
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17559488 668 VYGFTGATVGKLpcleisqsVTAFGRKMIdmtkLEVERIYKKGaldgkcpADAKVIYGDTDSVM 731
Cdd:PHA03334 772 HYGVAPHACQHL--------ITTLGRHKI----KLVEEFIKKE-------PGMTVNYGDTDSVM 816
|
|
| 43A |
PHA02524 |
DNA polymerase subunit A; Provisional |
347-642 |
3.00e-09 |
|
DNA polymerase subunit A; Provisional
Pssm-ID: 164925 [Multi-domain] Cd Length: 498 Bit Score: 60.78 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 347 LLEKWAEFVREVDPDIITGYNILNFDLPYILDRakvlslpqVSHLGRQKEKGSVVRDAAISSKQMGSRVNKSI--DIHGR 424
Cdd:PHA02524 183 LLLNYIQLWKANTPDLVFGWNSEGFDIPYIITR--------ITNILGEKAANQLSPYGKITSKTITNLYGEKIiyKIHGI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 425 IIFDVLQV-------VLRDYKlrsytLNSVSYQFLSEQKEDVEhNIIPDLQRGDEQtrrRLAQYCLKDAYLPLRL----- 492
Cdd:PHA02524 255 ALMDYMDVfkkfsftPMPDYK-----LGNVGYREVKADKLDYE-GPINKFRKADHQ---RYVDYCVRDTDIILLIdgrrc 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 493 -LDKLMSIINY--IEMARVTGVpmnflltkgqqIKIL-SMMLRRCKQNNFFLPVIEANSgdGEGYEGATVIDPIRGFYNE 568
Cdd:PHA02524 326 fIDLILSLSYYakIRFDDVLGT-----------IKVWdSIIFNSLVESNVVIPAMKASP--KQSFPGAYVKEPVPGGYRY 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 569 PIaTLDFASLYPSIMIAHNLCYTTLLKSPQGVENEDYIR----TPSGQY------FATKSKRRGLLPEILEDILAARKRA 638
Cdd:PHA02524 393 GL-SFDLTSLYPSILRLLNISPEMIAGMFSPARLEDYINkvapKPSDQFscapngMMYKKGVVGVLPNETEKVFLQRKSE 471
|
....
gi 17559488 639 KNDM 642
Cdd:PHA02524 472 KKMM 475
|
|
| DNA_polB_epsilon_exo |
cd05779 |
DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase epsilon, a family-B DNA polymerase; ... |
279-385 |
6.10e-08 |
|
DEDDy 3'-5' exonuclease domain of eukaryotic DNA polymerase epsilon, a family-B DNA polymerase; The 3'-5' exonuclease domain of eukaryotic DNA polymerase epsilon. DNA polymerase epsilon is a family-B DNA polymerase with a catalytic subunit that contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain. It is one of the three DNA-dependent type B DNA polymerases (alpha and delta are the other two) that have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase epsilon plays a role in elongating the leading strand during DNA replication. It is also involved in DNA repair. The catalytic subunit contains both polymerase and 3'-5' exonuclease activities. The N-terminal exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and are involved in metal binding and catalysis. DNA polymerase epsilon also carries a unique large C-terminal domain with an unknown function. Phylogenetic analyses indicate that it is orthologous to the archaeal DNA polymerase B3 rather than to the eukaryotic alpha, delta, or zeta polymerases. The exonuclease domain of family-B polymerases contains a beta hairpin structure that plays an important role in active site switching in the event of nucleotide misincorporation
Pssm-ID: 99822 [Multi-domain] Cd Length: 204 Bit Score: 54.19 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 279 PIRTLSLDIECIGRRGVFPEAIKDPIIQIAnlVKIEGEAEpfvrncfvLGTCAPVVGSNI--------------IQCVN- 343
Cdd:cd05779 1 DPRVLAFDIETTKLPLKFPDAETDQIMMIS--YMIDGQGY--------LIVNREIVSEDIedfeytpkpeyegpFKVFNe 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17559488 344 --EKVLLEKWAEFVREVDPDIITGYNILNFDLPYILDRAKVLSL 385
Cdd:cd05779 71 pdEKALLQRFFEHIREVKPHIIVTYNGDFFDWPFVEARAAIHGL 114
|
|
| ABC_sub_bind |
pfam04392 |
ABC transporter substrate binding protein; This family contains many hypothetical proteins and ... |
695-789 |
7.63e-03 |
|
ABC transporter substrate binding protein; This family contains many hypothetical proteins and some ABC transporter substrate binding proteins.
Pssm-ID: 427918 Cd Length: 293 Bit Score: 39.78 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559488 695 MIDMTKLEVERIYKKGALDGKCPadakVIYGDTDSVMVKFGVETVAQAMEIGLDAAKEVSKIF--TPPIKLEFEKVYSPY 772
Cdd:pfam04392 191 LTDNTIVSGFETLVHYANFAKIP----VFASDTESVKRGAIAAVGIDYKEIGVQTGHMAVKILkgIKPGDIPFVVAKSPK 266
|
90
....*....|....*..
gi 17559488 773 LLINKKRYAGLYFTKPD 789
Cdd:pfam04392 267 LFINLKAAQELGITIPE 283
|
|
| |
