|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09532 |
PRK09532 |
DNA polymerase III subunit alpha; Reviewed |
1-874 |
0e+00 |
|
DNA polymerase III subunit alpha; Reviewed
Pssm-ID: 181933 [Multi-domain] Cd Length: 874 Bit Score: 1830.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQERR 80
Cdd:PRK09532 1 MSFVGLHIHSDYSLLDGASQLPALVDRAIELGMPAIALTDHGVMYGAIELLKVCRNKGIKPIIGNEMYVINGDIEKQKRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 81 PKYHQVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVA 160
Cdd:PRK09532 81 RKYHQVVLAKNTQGYKNLVKLTTISHLQGVQGKGIFARPCINKELLEQYHEGLIVTSACLGGEIPQAILSGRPDAARKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 161 QWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMRYSG 240
Cdd:PRK09532 161 KWYKKLFGDDFYLEIQDHGSQEDRIVNVEIVKIARELGIKIIATNDSHFISCYDVEAHDALLCIQTGKLITEDKRLRYSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TEYLKSGEEMRQLFRDHLPDDVIAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRKSR 320
Cdd:PRK09532 241 TEYLKSAEEMRLLFRDHLPDDVIAEAIANTLEVADKIEPYNILGEPRIPNYPVPSGHTPDTYVEEVAWQGLLERLNCKSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 321 QEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLNP 400
Cdd:PRK09532 321 SEVEPVYKERLEYELKMLQQMGFSTYFLVVWDYIKYARDNNIPVGPGRGSAAGSLVAYCLKITNIDPVHHGLLFERFLNP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 401 ERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRGKPTKLK 480
Cdd:PRK09532 401 ERKSMPDIDTDFCIERRDEMIKYVTEKYGEDRVAQIITFNRMTSKAVLKDVARVLDIPYGEADKMAKLIPVSRGKPTKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 481 VMVSDKTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGSVITQYFMEDLESMG 560
Cdd:PRK09532 481 VMISDETPEPEFKEKYDNDPRVRRWLDMAIRIEGTNKTFGVHAAGVVISSEPLDEIVPLQKNNDGAVITQYFMEDLESLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 561 LLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRQERKAQKILAKGEHSSLPKDVQKTYELLEAGELEGIFQLESSG 640
Cdd:PRK09532 561 LLKMDFLGLRNLTTIQKTADLIKENRGVEIDLDQLPLDERKALKILAKGEAKKLPKDVQKTHKLLERGDLEGIFQLESSG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 641 MRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMAGY 720
Cdd:PRK09532 641 MKQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGREPIDYEHQLLEPILNETYGVLVYQEQIMKMAQDLAGY 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 721 SLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEYCLSYETEILTVEYGLLPIGKIVEKRI 800
Cdd:PRK09532 721 SLGEADLLRRAMGKKKISEMQKHREKFIDGAAKNGVSKKVAENLFDQMVKFAEYCLSYDTEVLTVEYGLLPIGKIVEENI 800
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 801 ECTVYSVDNNGNIYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTVDGQMLQIDEIFERKLDLMRVEGL 874
Cdd:PRK09532 801 ECTVYSVDPNGFVYTQPIAQWHHRGEQEVFEYCLEDGSIIRATKDHKFMTTDGEMLPIDEIFERGLELKQIKLP 874
|
|
| DnaE |
COG0587 |
DNA polymerase III, alpha subunit [Replication, recombination and repair]; |
2-774 |
0e+00 |
|
DNA polymerase III, alpha subunit [Replication, recombination and repair];
Pssm-ID: 440352 [Multi-domain] Cd Length: 1050 Bit Score: 1127.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQErrp 81
Cdd:COG0587 4 SFVHLHVHSEYSLLDGASRPEELVARAAELGMPALAITDHGNLFGAVRFYKAAKKAGIKPIIGCELYVAPGSRDDAG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 kYHQVVLAKNTKGYKNLVKLTTISHLQGvQGKGifsRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVAQ 161
Cdd:COG0587 81 -YHLVLLAKNREGYRNLCRLLSRAYLEG-FYKG---KPRIDLEDLAEHSEGLIALSGCLAGEVGQALLAGQYDEAEAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 162 WYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMR-YSG 240
Cdd:COG0587 156 RLKDIFGDRFYLELQRHGLPEDRRVNAALLELARELGLPLVATNDVHYLNPEDAEAHDVLLCIRTGKTLDDPGRRRfANA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TEYLKSGEEMRQLFRDHlpddviAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRKSR 320
Cdd:COG0587 236 ERYLKSPEEMAELFADL------PEALANTLEIAERCNFSLDLGKYQLPKFPVPEGETEEEYLRKLAEEGLERRYPEGIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 321 QEvdsvYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLNP 400
Cdd:COG0587 310 EE----YRERLEYELDVIEKMGFPGYFLIVWDFIRWARSNGIPVGPGRGSAAGSLVAYALGITDVDPIRYDLLFERFLNP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 401 ERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPvvRGKPTKLK 480
Cdd:COG0587 386 ERVSMPDIDIDFCHERREEVIQYVYEKYGRDRVAQIATFGTMRARAAIRDVGRVLGLPYGEVDRLAKLIP--NDPGITLE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 481 VMVSDktpEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNND-GSVITQYFMEDLESM 559
Cdd:COG0587 464 KALEE---EPELRELYDSDPEVRRLLDLARKLEGLPRHLSTHAGGVVISDDPLTDLVPLERAAMgGRPVTQFDKDDVEAL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 560 GLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIprqerkaqkilakgehsslPKDVQKTYELLEAGELEGIFQLESS 639
Cdd:COG0587 541 GLLKFDFLGLRTLTVIRDALDLIKENRGIDIDLADI-------------------PLDDPKTYELLQRGDTIGVFQLESR 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 640 GMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMAG 719
Cdd:COG0587 602 GMRSLLKRLKPDCFEDLVALVALYRPGPMQGGMVPPYIRRKHGREPVEYPHPELEPILKETYGVIVYQEQVMQIAQVLAG 681
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1928662004 720 YSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:COG0587 682 FSLGEADLLRRAMGKKKKEEMAKQREKFVEGAVANGYDEEFAEEIFDQIEKFAGY 736
|
|
| polc |
TIGR00594 |
DNA-directed DNA polymerase III (polc); All proteins in this family for which functions are ... |
3-777 |
0e+00 |
|
DNA-directed DNA polymerase III (polc); All proteins in this family 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: 273161 [Multi-domain] Cd Length: 1022 Bit Score: 1112.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDI----EKQE 78
Cdd:TIGR00594 1 FVHLHVHSDYSLLDGAAKIKPLVKKAKELGMPALALTDHGNMFGAVEFYKACKKAGIKPIIGCEAYVAPGSRfdkkRISK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 79 RRPKYHQVVLAKNTKGYKNLVKLTTISHLqgvqgKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARK 158
Cdd:TIGR00594 81 GKEAYHLILLAKNNTGYRNLMKLSSLAYL-----EGFYYKPRIDKELLEEHSEGLIALSACLSGEVPYLLLLGEERLAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 159 VAQWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMR- 237
Cdd:TIGR00594 156 AALKYQEIFGDDYYLELQDHGIPEQRVVNEALLEISEELGIPLVATNDVHYINPEDAHAHEILLCIQTGKTLSDPKRLKf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 238 YSGTEYLKSGEEMRQLFRDHlpddviAEAVATTEEVADKVEPYHI-MGEPQIPTPPIP-SGHTADTYAEDVAWNGLLERL 315
Cdd:TIGR00594 236 YSDEFYLKSPEEMAELFADI------PEALANTVEIAERCNLVDVkLGPPRLPSYQIPpDFTSQEDYLRHLADEGLRERL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 316 NRKSRQEVD-SVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLF 394
Cdd:TIGR00594 310 AAGPPGYKRrAQYKERLEYELDVINSMGFPGYFLIVWDFIKWAKDHGIPVGPGRGSAAGSLVAYALKITDIDPIKHGLLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 395 ERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRG 474
Cdd:TIGR00594 390 ERFLNPERISMPDIDIDFCDERRDEVIEYVADKYGHDNVAQIITFGTMKAKAALRDVARVLDIPYAEADRIAKLIPPRPG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 475 KPTKLKVMvsdktPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNND-GSVITQYFM 553
Cdd:TIGR00594 470 KTLKEALE-----ASPQLRQLYEEDPEVKQLIDMARKLEGLNRNAGVHAAGVVISSEPLTDYVPLYKDKEgGAISTQYDM 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 554 EDLESMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDpdeiprqerkaqkilakgeHSSLPKDVQKTYELLEAGELEGI 633
Cdd:TIGR00594 545 DDLEAVGLLKMDFLGLKTLTLIQDATELIRKRRGIDLD-------------------IASIPLDDKKTFSLLQEGDTTGV 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 634 FQLESSGMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKI 713
Cdd:TIGR00594 606 FQLESRGMQDLLKRLKPDGFEDIIAVNALYRPGPMESGMIPDFIDRKHGREPIEYPHPLLEPILKETYGVIVYQEQVMQI 685
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 714 AQDMAGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEYCLS 777
Cdd:TIGR00594 686 AQRLAGFSLGEADLLRRAMGKKKAEEMAKEREKFVEGAEKNGYDPEIAENLFDLIEKFAGYGFN 749
|
|
| PHP_PolIIIA_DnaE3 |
cd12113 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III ... |
2-289 |
4.23e-132 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE3; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, the PolIIIA PHP exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such an activity has not been found. It has been shown that the PHP of PolIIIA has a trinuclear metal complex and is capable of proofreading activity. Bacterial genome replication and DNA repair mechanisms is related to the GC content of its genomes. There is a correlation between GC content variations and the dimeric combinations of PolIIIA subunits. Eubacteria can be grouped into different GC variable groups: the full-spectrum or dnaE1 group, the high-GC or dnaE2-dnaE1 group, and the low GC or polC-dnaE3 group.
Pssm-ID: 213997 [Multi-domain] Cd Length: 283 Bit Score: 396.43 E-value: 4.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQERRP 81
Cdd:cd12113 1 DFVHLHVHTEYSLLDGAIRIKDLVKRAKELGMPALAITDHGNMFGAIEFYKAAKKAGIKPIIGCEVYVAPGSRFDKKDKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 K----YHQVVLAKNTKGYKNLVKLTTISHLQgvqgkGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAAR 157
Cdd:cd12113 81 GdkryYHLVLLAKNEEGYRNLMKLVSLAYLE-----GFYYKPRIDKELLAKYSEGLIALSACLAGEIPQLLLNGDEEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 158 KVAQWYKDVFG-DDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRM 236
Cdd:cd12113 156 EAALEYRDIFGkDNFYLELQDHGLPEQKKVNEGLIELAKELGIPLVATNDVHYLNKEDAEAHDVLLCIQTGKTLDDPNRM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 237 RYSGTE-YLKSGEEMRQLFRDhlpddvIAEAVATTEEVADKVEPYHIMGEPQIP 289
Cdd:cd12113 236 RFDTDEfYLKSPEEMRELFPD------VPEALENTLEIAERCNVELDFGKLHLP 283
|
|
| DNA_pol3_alpha |
pfam07733 |
Bacterial DNA polymerase III alpha NTPase domain; |
302-568 |
6.61e-125 |
|
Bacterial DNA polymerase III alpha NTPase domain;
Pssm-ID: 400196 [Multi-domain] Cd Length: 259 Bit Score: 376.84 E-value: 6.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 302 YAEDVAWNGLLERLNRKSRQEvdsvYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMR 381
Cdd:pfam07733 2 YLRKLVEEGLKERYGEGLPEE----YQERLEYELNVIIKMGFAGYFLIVWDLVKWAKDNGILVGPGRGSAAGSLVAYLLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 382 ITNIDPVHHGLLFERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGE 461
Cdd:pfam07733 78 ITEVDPLKHDLLFERFLNPERVSMPDIDIDFEDERREEVIDYVKEKYGRDRVAQIATFGTYAAKSAIRDVGRALGLPYDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 462 ADKMAKLIPVVRGKPTKLkvmvsdKTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQK 541
Cdd:pfam07733 158 IDRLAKLIPFELGILEKA------LEEEPELKELIESDPEVKRLIELAKKLEGLPRHTGQHAGGVVISPDPLTDFVPLYK 231
|
250 260
....*....|....*....|....*...
gi 1928662004 542 -NNDGSVITQYFMEDLESMGLLKMDFLG 568
Cdd:pfam07733 232 aDDDDRPVTQFDKDDLEDLGLLKMDFLG 259
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
6-71 |
1.45e-23 |
|
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family of hypothetical proteins
Pssm-ID: 197753 [Multi-domain] Cd Length: 67 Bit Score: 94.64 E-value: 1.45e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928662004 6 LHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVIN 71
Cdd:smart00481 2 LHVHSDYSLLDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEANIVD 67
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
6-53 |
5.85e-04 |
|
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.
Pssm-ID: 468321 [Multi-domain] Cd Length: 315 Bit Score: 43.08 E-value: 5.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKI 53
Cdd:NF038032 7 LHIHTNHS--DGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAEL 52
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09532 |
PRK09532 |
DNA polymerase III subunit alpha; Reviewed |
1-874 |
0e+00 |
|
DNA polymerase III subunit alpha; Reviewed
Pssm-ID: 181933 [Multi-domain] Cd Length: 874 Bit Score: 1830.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQERR 80
Cdd:PRK09532 1 MSFVGLHIHSDYSLLDGASQLPALVDRAIELGMPAIALTDHGVMYGAIELLKVCRNKGIKPIIGNEMYVINGDIEKQKRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 81 PKYHQVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVA 160
Cdd:PRK09532 81 RKYHQVVLAKNTQGYKNLVKLTTISHLQGVQGKGIFARPCINKELLEQYHEGLIVTSACLGGEIPQAILSGRPDAARKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 161 QWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMRYSG 240
Cdd:PRK09532 161 KWYKKLFGDDFYLEIQDHGSQEDRIVNVEIVKIARELGIKIIATNDSHFISCYDVEAHDALLCIQTGKLITEDKRLRYSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TEYLKSGEEMRQLFRDHLPDDVIAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRKSR 320
Cdd:PRK09532 241 TEYLKSAEEMRLLFRDHLPDDVIAEAIANTLEVADKIEPYNILGEPRIPNYPVPSGHTPDTYVEEVAWQGLLERLNCKSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 321 QEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLNP 400
Cdd:PRK09532 321 SEVEPVYKERLEYELKMLQQMGFSTYFLVVWDYIKYARDNNIPVGPGRGSAAGSLVAYCLKITNIDPVHHGLLFERFLNP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 401 ERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRGKPTKLK 480
Cdd:PRK09532 401 ERKSMPDIDTDFCIERRDEMIKYVTEKYGEDRVAQIITFNRMTSKAVLKDVARVLDIPYGEADKMAKLIPVSRGKPTKLK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 481 VMVSDKTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGSVITQYFMEDLESMG 560
Cdd:PRK09532 481 VMISDETPEPEFKEKYDNDPRVRRWLDMAIRIEGTNKTFGVHAAGVVISSEPLDEIVPLQKNNDGAVITQYFMEDLESLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 561 LLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRQERKAQKILAKGEHSSLPKDVQKTYELLEAGELEGIFQLESSG 640
Cdd:PRK09532 561 LLKMDFLGLRNLTTIQKTADLIKENRGVEIDLDQLPLDERKALKILAKGEAKKLPKDVQKTHKLLERGDLEGIFQLESSG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 641 MRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMAGY 720
Cdd:PRK09532 641 MKQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGREPIDYEHQLLEPILNETYGVLVYQEQIMKMAQDLAGY 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 721 SLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEYCLSYETEILTVEYGLLPIGKIVEKRI 800
Cdd:PRK09532 721 SLGEADLLRRAMGKKKISEMQKHREKFIDGAAKNGVSKKVAENLFDQMVKFAEYCLSYDTEVLTVEYGLLPIGKIVEENI 800
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 801 ECTVYSVDNNGNIYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTVDGQMLQIDEIFERKLDLMRVEGL 874
Cdd:PRK09532 801 ECTVYSVDPNGFVYTQPIAQWHHRGEQEVFEYCLEDGSIIRATKDHKFMTTDGEMLPIDEIFERGLELKQIKLP 874
|
|
| dnaE |
PRK07374 |
DNA polymerase III subunit alpha; Validated |
1-775 |
0e+00 |
|
DNA polymerase III subunit alpha; Validated
Pssm-ID: 168927 [Multi-domain] Cd Length: 1170 Bit Score: 1541.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIE--KQE 78
Cdd:PRK07374 1 MAFVPLHNHSDYSLLDGASQLPKMVERAKELGMPAIALTDHGVMYGAIELLKLCKGKGIKPIIGNEMYVINGSIDdpQPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 79 RRPKYHQVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARK 158
Cdd:PRK07374 81 KEKRYHLVVLAKNATGYKNLVKLTTISHLNGMRGRGIFSRPCIDKELLKQYSEGLIVSTACLGGEIPQAILRGRPDVARD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 159 VAQWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMRY 238
Cdd:PRK07374 161 VAAWYKEVFGDDFYLEIQDHGSIEDRIVNVELVRIAKELGIKLIATNDAHYLSKNDVEAHDALLCVLTGKLISDEKRLRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 239 SGTEYLKSGEEMRQLFRDHLPDDVIAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRK 318
Cdd:PRK07374 241 TGTEYIKSEEEMLRLFRDHLDPEVIQEAIANTVEVAEKVEEYDILGTYRMPRFPIPEGHTAVSYLTEVTEQGLLKRLKLN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 319 SRQEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFL 398
Cdd:PRK07374 321 SLDEIDENYKERLSYELKIIEQMGFPTYFLVVWDYIRFAREQGIPVGPGRGSAAGSLVAYALGITNIDPVKNGLLFERFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 399 NPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRGKPTK 478
Cdd:PRK07374 401 NPERKSMPDIDTDFCIERRGEVIDYVTRRYGEDKVAQIITFNRMTSKAVLKDVARVLDIPYGEADRLAKLIPVVRGKPAK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 479 LKVMVSDKTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGSVITQYFMEDLES 558
Cdd:PRK07374 481 LKAMIGKESPSPEFREKYEKDPRVKKWVDMAMRIEGTNKTFGVHAAGVVIASDPLDELVPLQRNNDGQVITQYFMEDIES 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 559 MGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEiprqerkaqkilakgehssLPKDVQKTYELLEAGELEGIFQLES 638
Cdd:PRK07374 561 LGLLKMDFLGLKNLTMIEKTLELVEQSTGERIDPDN-------------------LPLDDEKTFELLARGDLEGIFQLES 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 639 SGMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMA 718
Cdd:PRK07374 622 SGMRQVVRDLKPSSLEDISSILALYRPGPLDAGLIPKFINRKHGREAIDFAHPLLEPILTETYGIMVYQEQIMKIAQDLA 701
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1928662004 719 GYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEYC 775
Cdd:PRK07374 702 GYSLGQADLLRRAMGKKKVSEMQKHRGIFVEGASKRGVDEKVADELFDQMVLFAEYC 758
|
|
| DnaE |
COG0587 |
DNA polymerase III, alpha subunit [Replication, recombination and repair]; |
2-774 |
0e+00 |
|
DNA polymerase III, alpha subunit [Replication, recombination and repair];
Pssm-ID: 440352 [Multi-domain] Cd Length: 1050 Bit Score: 1127.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQErrp 81
Cdd:COG0587 4 SFVHLHVHSEYSLLDGASRPEELVARAAELGMPALAITDHGNLFGAVRFYKAAKKAGIKPIIGCELYVAPGSRDDAG--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 kYHQVVLAKNTKGYKNLVKLTTISHLQGvQGKGifsRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVAQ 161
Cdd:COG0587 81 -YHLVLLAKNREGYRNLCRLLSRAYLEG-FYKG---KPRIDLEDLAEHSEGLIALSGCLAGEVGQALLAGQYDEAEAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 162 WYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMR-YSG 240
Cdd:COG0587 156 RLKDIFGDRFYLELQRHGLPEDRRVNAALLELARELGLPLVATNDVHYLNPEDAEAHDVLLCIRTGKTLDDPGRRRfANA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TEYLKSGEEMRQLFRDHlpddviAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRKSR 320
Cdd:COG0587 236 ERYLKSPEEMAELFADL------PEALANTLEIAERCNFSLDLGKYQLPKFPVPEGETEEEYLRKLAEEGLERRYPEGIP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 321 QEvdsvYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLNP 400
Cdd:COG0587 310 EE----YRERLEYELDVIEKMGFPGYFLIVWDFIRWARSNGIPVGPGRGSAAGSLVAYALGITDVDPIRYDLLFERFLNP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 401 ERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPvvRGKPTKLK 480
Cdd:COG0587 386 ERVSMPDIDIDFCHERREEVIQYVYEKYGRDRVAQIATFGTMRARAAIRDVGRVLGLPYGEVDRLAKLIP--NDPGITLE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 481 VMVSDktpEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNND-GSVITQYFMEDLESM 559
Cdd:COG0587 464 KALEE---EPELRELYDSDPEVRRLLDLARKLEGLPRHLSTHAGGVVISDDPLTDLVPLERAAMgGRPVTQFDKDDVEAL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 560 GLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIprqerkaqkilakgehsslPKDVQKTYELLEAGELEGIFQLESS 639
Cdd:COG0587 541 GLLKFDFLGLRTLTVIRDALDLIKENRGIDIDLADI-------------------PLDDPKTYELLQRGDTIGVFQLESR 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 640 GMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMAG 719
Cdd:COG0587 602 GMRSLLKRLKPDCFEDLVALVALYRPGPMQGGMVPPYIRRKHGREPVEYPHPELEPILKETYGVIVYQEQVMQIAQVLAG 681
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1928662004 720 YSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:COG0587 682 FSLGEADLLRRAMGKKKKEEMAKQREKFVEGAVANGYDEEFAEEIFDQIEKFAGY 736
|
|
| polc |
TIGR00594 |
DNA-directed DNA polymerase III (polc); All proteins in this family for which functions are ... |
3-777 |
0e+00 |
|
DNA-directed DNA polymerase III (polc); All proteins in this family 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: 273161 [Multi-domain] Cd Length: 1022 Bit Score: 1112.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDI----EKQE 78
Cdd:TIGR00594 1 FVHLHVHSDYSLLDGAAKIKPLVKKAKELGMPALALTDHGNMFGAVEFYKACKKAGIKPIIGCEAYVAPGSRfdkkRISK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 79 RRPKYHQVVLAKNTKGYKNLVKLTTISHLqgvqgKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARK 158
Cdd:TIGR00594 81 GKEAYHLILLAKNNTGYRNLMKLSSLAYL-----EGFYYKPRIDKELLEEHSEGLIALSACLSGEVPYLLLLGEERLAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 159 VAQWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMR- 237
Cdd:TIGR00594 156 AALKYQEIFGDDYYLELQDHGIPEQRVVNEALLEISEELGIPLVATNDVHYINPEDAHAHEILLCIQTGKTLSDPKRLKf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 238 YSGTEYLKSGEEMRQLFRDHlpddviAEAVATTEEVADKVEPYHI-MGEPQIPTPPIP-SGHTADTYAEDVAWNGLLERL 315
Cdd:TIGR00594 236 YSDEFYLKSPEEMAELFADI------PEALANTVEIAERCNLVDVkLGPPRLPSYQIPpDFTSQEDYLRHLADEGLRERL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 316 NRKSRQEVD-SVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLF 394
Cdd:TIGR00594 310 AAGPPGYKRrAQYKERLEYELDVINSMGFPGYFLIVWDFIKWAKDHGIPVGPGRGSAAGSLVAYALKITDIDPIKHGLLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 395 ERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRG 474
Cdd:TIGR00594 390 ERFLNPERISMPDIDIDFCDERRDEVIEYVADKYGHDNVAQIITFGTMKAKAALRDVARVLDIPYAEADRIAKLIPPRPG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 475 KPTKLKVMvsdktPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNND-GSVITQYFM 553
Cdd:TIGR00594 470 KTLKEALE-----ASPQLRQLYEEDPEVKQLIDMARKLEGLNRNAGVHAAGVVISSEPLTDYVPLYKDKEgGAISTQYDM 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 554 EDLESMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDpdeiprqerkaqkilakgeHSSLPKDVQKTYELLEAGELEGI 633
Cdd:TIGR00594 545 DDLEAVGLLKMDFLGLKTLTLIQDATELIRKRRGIDLD-------------------IASIPLDDKKTFSLLQEGDTTGV 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 634 FQLESSGMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKI 713
Cdd:TIGR00594 606 FQLESRGMQDLLKRLKPDGFEDIIAVNALYRPGPMESGMIPDFIDRKHGREPIEYPHPLLEPILKETYGVIVYQEQVMQI 685
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 714 AQDMAGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEYCLS 777
Cdd:TIGR00594 686 AQRLAGFSLGEADLLRRAMGKKKAEEMAKEREKFVEGAEKNGYDPEIAENLFDLIEKFAGYGFN 749
|
|
| dnaE |
PRK05673 |
DNA polymerase III subunit alpha; Validated |
2-774 |
0e+00 |
|
DNA polymerase III subunit alpha; Validated
Pssm-ID: 235554 [Multi-domain] Cd Length: 1135 Bit Score: 1085.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQERRP 81
Cdd:PRK05673 1 RFVHLHVHSEYSLLDGAAKIKPLVKKAAELGMPAVALTDHGNLFGAVEFYKAAKGAGIKPIIGCEAYVAPEKKDDVSGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 KY-HQVVLAKNTKGYKNLVKLTTISHLQGVQGKgifsRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVA 160
Cdd:PRK05673 81 AYtHLTLLAKNETGYRNLFKLSSRAYLEGQYGY----KPRIDREWLAEHSEGLIALSGCPSGEVGTALLAGQYDEAEEAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 161 QWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMRYSG 240
Cdd:PRK05673 157 AEYQEIFGDRFYLELMRHGLPIERRVEHALLELAKELGLPLVATNDVHYLTPEDAEAHEALLCIAEGKTLDDPDRFRFYS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TE-YLKSGEEMRQLFRDhLPddviaEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLERLNRKS 319
Cdd:PRK05673 237 PEqYLKSAEEMRELFAD-LP-----EALDNTVEIAERCNVEVRLGKPFLPRFPTPDGETEEDYLRKEAKEGLEERLAFLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 320 RQEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLN 399
Cdd:PRK05673 311 PDEERPEYVERLEYELDVIIQMGFPGYFLIVADFIQWAKDNGIPVGPGRGSGAGSLVAYALGITDLDPLRFGLLFERFLN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 400 PERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVvrgkptKL 479
Cdd:PRK05673 391 PERVSMPDFDIDFCQDRRDEVIRYVAEKYGRDAVAQIITFGTMKAKAVIRDVGRVLGMPYGFVDRITKLIPP------DP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 480 KVMVSD-KTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKN-NDGSVITQYFMEDLE 557
Cdd:PRK05673 465 GITLAKaYEEEPELRELYESDPEVKRLIDMARKLEGLTRNAGVHAAGVVISPTPLTDFVPLYRDpDSGMPVTQFDMKDVE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 558 SMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDpdeiprqerkaqkilakgeHSSLPKDVQKTYELLEAGELEGIFQLE 637
Cdd:PRK05673 545 AAGLVKFDFLGLRTLTIIDDALKLIKKRRGIDVD-------------------LEAIPLDDPKTYELLQRGETLGVFQLE 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 638 SSGMRQIVRDLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDM 717
Cdd:PRK05673 606 SRGMRDLLKRLKPDCFEDIIALVALYRPGPMESGMIPNFIDRKHGREEIEYPHPELEPILKETYGIIVYQEQVMQIAQVL 685
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1928662004 718 AGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK05673 686 AGYSLGGADLLRRAMGKKKPEEMAKQREIFVEGAKKNGIDEEAADAIFDLLEKFAGY 742
|
|
| dnaE |
PRK06826 |
DNA polymerase III DnaE; Reviewed |
1-774 |
0e+00 |
|
DNA polymerase III DnaE; Reviewed
Pssm-ID: 235868 [Multi-domain] Cd Length: 1151 Bit Score: 992.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDieKQERR 80
Cdd:PRK06826 3 MSFVHLHVHTEYSLLDGSARIKDLIKRAKELGMDSIAITDHGVMYGVVDFYKAAKKQGIKPIIGCEVYVAPRS--RFDKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 81 PK-----YHQVVLAKNTKGYKNLVKLTTISHLQGvqgkgIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDA 155
Cdd:PRK06826 81 PDidnetYHLVLLAKNETGYKNLMKIVSKAFTEG-----FYYKPRVDHELLKEHSEGLIALSACLAGEVPRYILKGNYEK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 156 ARKVAQWYKDVFG-DDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDK 234
Cdd:PRK06826 156 AKEAALFYKDIFGkENFYLELQDHGIPEQRKVNEELIKLSKELGIPLVATNDVHYIRKEDAKAHDVLLCIQTGKTVDDEN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 235 RMRYSGTE-YLKSGEEMRQLFrDHLPddviaEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLLE 313
Cdd:PRK06826 236 RMRFPSDEfYLKSPEEMYELF-SYVP-----EALENTVKIAERCNVEFEFGKSKLPKFPLPEGYDPYEYLRELCYEGLKK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 314 RLNrksrqEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLL 393
Cdd:PRK06826 310 RYP-----NPSEELIERLEYELSVIKQMGYVDYFLIVWDFIRFARENGIMVGPGRGSAAGSLVAYTLGITKIDPIKYNLL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 394 FERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVR 473
Cdd:PRK06826 385 FERFLNPERVSMPDIDIDFCYERRQEVIDYVVEKYGKDRVAQIITFGTMAARAAIRDVGRALNYPYAEVDRIAKMIPTEL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 474 GkptklkvMVSDKTPE--PEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKnNDGSVITQY 551
Cdd:PRK06826 465 G-------ITIDKALElnPELKEAYENDERVRELIDTARALEGLPRHASTHAAGVVISSEPLVEYVPLQK-NDGSIVTQF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 552 FMEDLESMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRqerkaqkilakgehsslpkDVQKTYELLEAGELE 631
Cdd:PRK06826 537 TMTTLEELGLLKMDFLGLRTLTVIRDAVDLIKKNRGIEIDLDKIDY-------------------DDKKVYKMIGEGKTV 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 632 GIFQLESSGMRQIVRDLKPSNIEDISSILALYRPGPLDAglIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIM 711
Cdd:PRK06826 598 GVFQLESAGMRSFMKELKPDSLEDIIAGISLYRPGPMDS--IPRYIKNKNNPEKIEYLHPKLEPILKVTYGCIVYQEQVM 675
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1928662004 712 KIAQDMAGYSLGQADLLRRAMGKKKVSEMQKQREKFV--------DGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK06826 676 QIVRDLAGYSMGRSDLVRRAMSKKKHDVMEEERKNFIygivdeggPGCIRNGIDEETANKIFDSMMDFASY 746
|
|
| dnaE |
PRK06920 |
DNA polymerase III subunit alpha; |
1-774 |
0e+00 |
|
DNA polymerase III subunit alpha;
Pssm-ID: 180749 [Multi-domain] Cd Length: 1107 Bit Score: 698.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQerr 80
Cdd:PRK06920 1 MKFVHLQCQTVFSLLKSACKIDELVVRAKELGYSSLAITDENVMYGVIPFYKACKKHGIHPIIGLTASIFSEEEEKS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 81 pkYHQVVLAKNTKGYKNLVKLTTIshlqgVQGKgifSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVA 160
Cdd:PRK06920 78 --YPLVLLAENEIGYQNLLKISSS-----IMTK---SKEGIPKKWLAHYAKGLIAISPGKDGEIEQLLLEDKESQAEEVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 161 QWYKDVFGDdYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMRYSG 240
Cdd:PRK06920 148 RAYQNMFGN-FYMSLQHHAIQDELLLQEKLPEFSNRVNIPVVATNDVRYINQSDALVHECLLSVESGTKMTDPDRPRLKT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TE-YLKSGEEMRQLFRDHlpddviAEAVATTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDVAWNGLlerlnRKS 319
Cdd:PRK06920 227 DQyYLKSSDEMEALFSHV------PEAIYNTVEIAERCRVEIPFHVNQLPKFPVPSNETADMYLRRVCEEGL-----QKR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 320 RQEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLN 399
Cdd:PRK06920 296 YGTPKEVHINRLNHELNVISRMGFSDYFLIVWDFMKYAHENHILTGPGRGSAAGSLVSYVLEITDIDPIEYDLLFERFLN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 400 PERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIpvvrgkPTKL 479
Cdd:PRK06920 376 PERVTLPDIDIDFPDTRRDEMIRYVKDKYGQLRVAQIVTFGTLAAKAAIRDIARVMGLPPRDIDIFSKLI------PSKL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 480 KVMVSD-KTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGSVITQYFMEDLES 558
Cdd:PRK06920 450 GITLKDaYEESQSLREFIQGNLLHERVFEIAKRVEGLPRHTSIHAAGVIMSQEPLTGSVAIQEGHNDVYVTQYPADALEE 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 559 MGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRQErkaqkilakgehsslpkdvQKTYELLEAGELEGIFQLES 638
Cdd:PRK06920 530 LGLLKMDFLGLRNLTLLENIIKFIEQKTGKEIDIRNLPLQD-------------------EKTFQLLGRGDTTGVFQLES 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 639 SGMRQIVRDLKPSNIEDISSILALYRPGPLDAglIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMA 718
Cdd:PRK06920 591 SGMRNVLRGLKPNEFEDIVAVNSLYRPGPMEQ--IPTFIESKHGKRKIEYLHPDLKPILERTYGVIVYQEQIMQIASKLA 668
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1928662004 719 GYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK06920 669 GFSLGEADLLRRAVSKKNRDILDQERKHFVQGCLQNGYDETSAEKIYDLIVRFANY 724
|
|
| dnaE2 |
PRK05672 |
error-prone DNA polymerase; Validated |
3-774 |
1.21e-172 |
|
error-prone DNA polymerase; Validated
Pssm-ID: 235553 [Multi-domain] Cd Length: 1046 Bit Score: 527.89 E-value: 1.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEkqerrPK 82
Cdd:PRK05672 5 YAELHCHSNFSFLDGASHPEELVERAARLGLRALAITDECGLAGVVRAAEAAKELGLRLVIGAELSLGPDPDP-----GG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 83 YHQVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFSRPcinkDLLKQYHEGLIVTSACLGGEVPQAIL-SNRPDAARKVAQ 161
Cdd:PRK05672 80 PHLLVLARDREGYGRLSRLITRARLRAGKGEYRLDLD----DLAEPAGGHWAILTGCRKGFVILALPyGGDAAALAALAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 162 WYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIE-DKRMRYSG 240
Cdd:PRK05672 156 LLDAFFADRVWLELTLHGRPDDDRRNARLAALAARAGVPLVATGDVHMHHRSRRRLQDAMTAIRARRSLAEaGGWLAPNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 241 TEYLKSGEEMRQLFRDHlpDDVIAEAVATTEEVA---DKVEPyhimgepQIPTPPIPSGHTADTYAEDVAWNGLLERLNR 317
Cdd:PRK05672 236 ERHLRSGAEMARLFPDY--PEALAETVELAERCAfdlDLLAY-------EYPDEPVPAGHTPASWLRQLTEAGAARRYGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 318 KSRQEVdsvyKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIpVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERF 397
Cdd:PRK05672 307 GIPPKA----RAQIEHELALIAELGYEGYFLTVHDIVRFARSQGI-LCQGRGSAANSAVCYALGITEVDPVQSGLLFERF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 398 LNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLipvVRGKpt 477
Cdd:PRK05672 382 LSPERDEPPDIDVDFEHDRREEVIQYVYRRYGRDRAAQVANVITYRPRSAVRDVAKALGLSPGQVDAWAKQ---VSRW-- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 478 klkvmvSDKTPEPEFKEKYDKEPH---VRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQknN----DGSVItQ 550
Cdd:PRK05672 457 ------SGSADDLQRLRQAGLDPEspiPRRVVELAAQLIGFPRHLSQHSGGFVICDRPLARLVPVE--NaameGRSVI-Q 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 551 YFMEDLESMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDpdeiprqerkaqkiLAkgehsSLPKDVQKTYELLEAGEL 630
Cdd:PRK05672 528 WDKDDCAAVGLVKVDVLALGMLSALHRAFDLIAEHRGRRLT--------------LA-----SIPLDDPAVYDMLCRADS 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 631 EGIFQLESSG-MRQIVRdLKPSNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQ 709
Cdd:PRK05672 589 VGVFQVESRAqMAMLPR-LRPRTFYDLVVEVAIVRPGPIQGGMVHPYLRRRNGQEPVTYPHPELEKVLERTLGVPLFQEQ 667
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928662004 710 IMKIAQDMAGYSLGQADLLRRAMG-KKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK05672 668 VMQIAIDAAGFTPGEADQLRRAMAaWRRKGRLERLRERLYDGMLARGYTGEFADRIFEQIKGFGEY 733
|
|
| dnaE |
PRK07279 |
DNA polymerase III DnaE; Reviewed |
3-774 |
9.89e-163 |
|
DNA polymerase III DnaE; Reviewed
Pssm-ID: 180917 [Multi-domain] Cd Length: 1034 Bit Score: 501.49 E-value: 9.89e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMyvingDIEKQERrpK 82
Cdd:PRK07279 2 FAQLDTKTVYSFMDSLIDLEKYVERAKELGYQTIGIMDKDNLYGAYHFIEGAQKNGLQPILGLEL-----NIFVEEQ--E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 83 YHQVVLAKNTKGYKNLVKLTTishlQGVQGKGIFSrpcinkdLLKQYHEGLIVTsaclggeVPQAILSNRPDaarkvaqw 162
Cdd:PRK07279 75 VTLRLIAKNTQGYKNLLKIST----AKMSGKKQFS-------DLSQYLEGIAVI-------VPYFDWSETLE-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 163 ykdvFGDDYYLEIQDHGSQED---RIVNVEIVKIARELDIQIIATndSHFIScfdveahDALLCIQTGKLiiedkrmryS 239
Cdd:PRK07279 129 ----LPFDYYIGVDQETPGSDfkrPILPLRTVRYFESADRETLQM--LHAIR-------DNLSLREVPLV---------S 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 240 GTEYLKSGEEMRQLFRDHLPddviaEAVATTEEVADKVEpYHIMGEPQIP--TPPIPSGHTADTYAEdvawNGLlerlnr 317
Cdd:PRK07279 187 SDQELISCQSLETLFQERFP-----QALDNLEKLVSGIS-YDFDTDLKLPrfNRDRPAVEELRELAE----LGL------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 318 KSRQEVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERF 397
Cdd:PRK07279 251 KEKGLWSSPYQERLDKELSVIHDMGFDDYFLIVWDLLRFGRSQGYYMGMGRGSAAGSLVAYALDITGIDPVKHNLLFERF 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 398 LNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIpVVRGKPT 477
Cdd:PRK07279 331 LNKERYSMPDIDIDLPDIYRSEFLRYVRNRYGSDHSAQIVTFSTFGAKQAIRDVFKRFGVPEYELSNLTKKI-SFRDSLA 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 478 KlkvmVSDKTpePEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLqKNNDGSVITQYFMEDLE 557
Cdd:PRK07279 410 S----VYEKN--ISFRQIINSKLEYQKAFEIAKRIEGNPRQTSIHAAGVVMSDDDLTNHIPL-KYGDDMMITQYDAHAVE 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 558 SMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRQErkaqkilakgehsslpkdvQKTYELLEAGELEGIFQLE 637
Cdd:PRK07279 483 ANGLLKMDFLGLRNLTFVQKMQEKVAKDYGIHIDIEAIDLED-------------------KETLALFAAGDTKGIFQFE 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 638 SSGMRQIVRDLKPSNIEDISSILALYRPGPLDagLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDM 717
Cdd:PRK07279 544 QPGAINLLKRIKPVCFEDIVATTSLNRPGASD--YTDNFVKRRHGQEKVDLIDPVIAPILEPTYGIMLYQEQVMQIAQVF 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1928662004 718 AGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK07279 622 AGFSLGKADLLRRAMSKKNASEMQKMEEDFLQGALELGHSEEKARELFDRMEKFAGY 678
|
|
| dnaE |
PRK07135 |
DNA polymerase III DnaE; Validated |
1-774 |
7.60e-150 |
|
DNA polymerase III DnaE; Validated
Pssm-ID: 235944 [Multi-domain] Cd Length: 973 Bit Score: 466.09 E-value: 7.60e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 1 MSFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINgdiekqerr 80
Cdd:PRK07135 1 MKLINLHTNTEYSFLSSTIKLDSLIKYAKENNLKTLVLTDHNNMFGVPKFYKLCKKNNIKPIIGLDLEVEN--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 81 pkYHQVVLAKNTKGYKNLVKLTtishLQGVQGKGIFSRPCINKDLLkqyheglIVTSACLG-----GEVPQaiLSNrpda 155
Cdd:PRK07135 72 --FRFILLAKNYSGYKLLNELS----SKKSKNKEIELNDLDSDNII-------IIDHPKNGfyaknKEQLE--LKN---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 156 arkvaqwykdvfgddYYLEiqdhgSQEDRIVNVEIVKIARELDIqiiatndshfiscFDVEAHDALLCIQTGKliIEDKr 235
Cdd:PRK07135 133 ---------------YYIN-----SNDPKIENAVYVQERKLLFA-------------EDNEYLKILNKIGNNK--EENS- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 236 mrysGTEYLKSGEEMRQLfrdhlPDDVIAEavatTEEVADKVEPYHIMGEPQIPTPPIPSGHTADTYAEDvawngLLERL 315
Cdd:PRK07135 177 ----NFKFFDFEKWFEDI-----DEKILKR----TNYLVENINIEFPKKEFNLPDFDNNLGLESDLFLKK-----ILKES 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 316 NRKSRQEV--DSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLL 393
Cdd:PRK07135 239 VINKKAELkyYPNVKERINYEYSVIKKLKFSNYFLIIWDFIKWARKNKISIGPGRGSASGSLVSYLLNITSVNPLKYDLL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 394 FERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIP--- 470
Cdd:PRK07135 319 FERFLNPDRITMPDIDIDIQDDRRDEVIDYIFEKYGYEHCATISTFQTLGAKSAIRDVGRMLGIPESDVNAISKLIPnnq 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 471 ----VVRGKPTKLKVMVSDKtpEPEFKEKYdkephvrhwlDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGS 546
Cdd:PRK07135 399 sleeAYDKNKSFFRELISKG--DPIYKKLY----------KIAKKLEGLPRQSGTHAAGIIISNKPITNYVPTFESKDNY 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 547 VITQYFMEDLESMGLLKMDFLGLRNLTLIQKTVDLIQETR--GYRVDPDEIPRQErkaqkilakgehsslpkdvQKTYEL 624
Cdd:PRK07135 467 NQVQYSMEFLEDFGLLKIDLLGLKNLTIIKNIEEKINKELlfDHLINFNDLPIID-------------------KKTNNL 527
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 625 LEAGELEGIFQLESSGMRQIVRDLKPSNIEDISSILALYRPGPLDagLIPKFINRKHGRENIDYQHTVLEPILDETYGIM 704
Cdd:PRK07135 528 LSNGKTEGIFQLESPGMKSTIKKVGIDSFEDIVAIISLYRPGPIQ--YIPIYAKNKKNPKNIEKIHPEYDEIVAPTYGII 605
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 705 VYQEQIMKIAQDMAGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK07135 606 IYQEQIMQIAQKVAGFSFAQADLLRRAISKKDETKLDKIKDKFIEGGIKNGYSKKVLEKIYSLIEKFADY 675
|
|
| dnaE |
PRK05898 |
DNA polymerase III subunit alpha; |
3-774 |
2.69e-144 |
|
DNA polymerase III subunit alpha;
Pssm-ID: 135648 [Multi-domain] Cd Length: 971 Bit Score: 451.60 E-value: 2.69e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEmyvingdIEKQErrPK 82
Cdd:PRK05898 2 FINLNTHSHYSLLSSTLSIDDIIKFALDNNQPYVCLTDLNNLYGCIEFYDKAKAHNLIPIIGLE-------IEYQS--TN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 83 YHQVVLAKNTKGYKNLVKlttishlqgvqgkgIFSRPCINKDL-LKQYHEGLIVT--SACLGGEVPQAILSNRPDAARKV 159
Cdd:PRK05898 73 ATLVLYAKNYNGYLNLIK--------------ISSFIMTNKEFeIQDYLDDLFIVckKGTFVFKSPNFYQTHNQNAPNAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 160 AqwYKDVFgddYYleiqdhgSQEDRIVNVEIVKIARELDIQiiatndsHFISCFDVEAHdallciqtgkliiedkrmrys 239
Cdd:PRK05898 139 A--FNSVF---YA-------NKNDKIVFNAMLAIKNDLKID-------ELKNCQDFDNN--------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 240 gteYLKSGEEMRQLFRDHLPDDVIAEAVATTEEVADkvEPYHImgepqiPTPPIPSGHTADTYAEDVAWNGLLERLNRKS 319
Cdd:PRK05898 179 ---HFLNDNEAQSLFSPIQLDNLNKVLNELKVEIHD--LPINI------IKYDKQNSIISSEILKQLCISGLNKRLNAND 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 320 RQeVDSVYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMRITNIDPVHHGLLFERFLN 399
Cdd:PRK05898 248 GQ-VKKIYVKRLKYELDIINEKQFDDYFLIVYDFINFAKSNGIIIGPGRGSAAGSLIAYLLHITDIDPIKYNLIFERFLN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 400 PERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGEADKMAKLIPVVRGKPTKL 479
Cdd:PRK05898 327 PTRKSMPDIDTDIMDERRDEVVEYLFEKYGNDHVAHIITFQRIKAKMAIRDVGRILGIDLKVIDKICKNIKPDYEEDLDL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 480 KVMvsdktpepefKEKYDKEPHVRH--WLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQKNNDGSVITQYFMEDLE 557
Cdd:PRK05898 407 AIK----------KNTILKEMYVLHkeLFDLAKKIINAPRQIGTHAAGVVLSNSLLTNIIPIQLGINDRPLSQYSMEYLE 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 558 SMGLLKMDFLGLRNLTLIQKTVDLIQETRGYRVDPDEIPRQErkaqkilakgehsslpkdvQKTYELLEAGELEGIFQLE 637
Cdd:PRK05898 477 RFGLIKMDLLGLKNLTIIDNVLKLIKENQNKKIDLFNINLND-------------------KNVFEDLAKGRTNGIFQLE 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 638 SSGMRQIVRDLKPSNIEDISSILALYRPGPLDAglIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDM 717
Cdd:PRK05898 538 SPGMKKVLKKVKPQNIEDISIVSALFRPGPQQN--IKTFVERRFKREEFSYWNEATKKILEPTHGIIVYQEQVINLVKTI 615
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1928662004 718 AGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLKFAEY 774
Cdd:PRK05898 616 ANFDIATADNFRRAISKKDEKILIQLKKDFIEGALKNNYKQPLVNQIFEYIFSFADY 672
|
|
| PHP_PolIIIA_DnaE3 |
cd12113 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III ... |
2-289 |
4.23e-132 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE3; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, the PolIIIA PHP exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such an activity has not been found. It has been shown that the PHP of PolIIIA has a trinuclear metal complex and is capable of proofreading activity. Bacterial genome replication and DNA repair mechanisms is related to the GC content of its genomes. There is a correlation between GC content variations and the dimeric combinations of PolIIIA subunits. Eubacteria can be grouped into different GC variable groups: the full-spectrum or dnaE1 group, the high-GC or dnaE2-dnaE1 group, and the low GC or polC-dnaE3 group.
Pssm-ID: 213997 [Multi-domain] Cd Length: 283 Bit Score: 396.43 E-value: 4.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQERRP 81
Cdd:cd12113 1 DFVHLHVHTEYSLLDGAIRIKDLVKRAKELGMPALAITDHGNMFGAIEFYKAAKKAGIKPIIGCEVYVAPGSRFDKKDKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 K----YHQVVLAKNTKGYKNLVKLTTISHLQgvqgkGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAAR 157
Cdd:cd12113 81 GdkryYHLVLLAKNEEGYRNLMKLVSLAYLE-----GFYYKPRIDKELLAKYSEGLIALSACLAGEIPQLLLNGDEEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 158 KVAQWYKDVFG-DDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRM 236
Cdd:cd12113 156 EAALEYRDIFGkDNFYLELQDHGLPEQKKVNEGLIELAKELGIPLVATNDVHYLNKEDAEAHDVLLCIQTGKTLDDPNRM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 237 RYSGTE-YLKSGEEMRQLFRDhlpddvIAEAVATTEEVADKVEPYHIMGEPQIP 289
Cdd:cd12113 236 RFDTDEfYLKSPEEMRELFPD------VPEALENTLEIAERCNVELDFGKLHLP 283
|
|
| DNA_pol3_alpha |
pfam07733 |
Bacterial DNA polymerase III alpha NTPase domain; |
302-568 |
6.61e-125 |
|
Bacterial DNA polymerase III alpha NTPase domain;
Pssm-ID: 400196 [Multi-domain] Cd Length: 259 Bit Score: 376.84 E-value: 6.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 302 YAEDVAWNGLLERLNRKSRQEvdsvYKERLEYELKMIQQMGFSKYFLVVWDYIKFARDNNIPVGPGRGSAAGSLVAYAMR 381
Cdd:pfam07733 2 YLRKLVEEGLKERYGEGLPEE----YQERLEYELNVIIKMGFAGYFLIVWDLVKWAKDNGILVGPGRGSAAGSLVAYLLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 382 ITNIDPVHHGLLFERFLNPERKSMPDIDTDFCIEQRDKVIEYVTEKYGADRVAQIITFNRLTSKAVLKDVARVLNIPYGE 461
Cdd:pfam07733 78 ITEVDPLKHDLLFERFLNPERVSMPDIDIDFEDERREEVIDYVKEKYGRDRVAQIATFGTYAAKSAIRDVGRALGLPYDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 462 ADKMAKLIPVVRGKPTKLkvmvsdKTPEPEFKEKYDKEPHVRHWLDMAMRIEGTNKTFGVHAAGVVISDEPLDEIVPLQK 541
Cdd:pfam07733 158 IDRLAKLIPFELGILEKA------LEEEPELKELIESDPEVKRLIELAKKLEGLPRHTGQHAGGVVISPDPLTDFVPLYK 231
|
250 260
....*....|....*....|....*...
gi 1928662004 542 -NNDGSVITQYFMEDLESMGLLKMDFLG 568
Cdd:pfam07733 232 aDDDDRPVTQFDKDDLEDLGLLKMDFLG 259
|
|
| PHP_PolIIIA_DnaE1 |
cd07433 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III ... |
2-274 |
2.58e-85 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III DnaE1; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. PolIIIA core enzyme catalyzes the reaction for polymerizing both DNA strands. dnaE1 is the longest compared to dnaE2 and dnaE3. A unique motif was also identified in dnaE1 and dnaE3 genes.
Pssm-ID: 213988 [Multi-domain] Cd Length: 277 Bit Score: 273.97 E-value: 2.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 2 SFVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDiekqeRRP 81
Cdd:cd07433 1 SFVHLRVHSEYSLLDGAVRIKKLVKLAKEDGMPALAITDLSNLFGAVKFYKAASKAGIKPIIGADLNVANPD-----DAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 KYHQVVL-AKNTKGYKNLVKLTTISHLQGvQGKGifsRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDAARKVA 160
Cdd:cd07433 76 EPFRLTLlAQNEQGYKNLTELISRAYLEG-QRNG---GPHIKLEWLAEYSEGLIALSGGRDGDIGQLLLEGNPDLAEALL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 161 QWYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKLIIEDKRMR-YS 239
Cdd:cd07433 152 QFLKKIFPDRFYLELQRHGRPEEEAYEHALIDLAYELGLPLVATNDVRFLKPEDFEAHEARVCIAEGRTLDDPRRPRrYS 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1928662004 240 GTEYLKSGEEMRQLFRDhLPddviaEAVATTEEVA 274
Cdd:cd07433 232 PQQYFKSAEEMAELFAD-LP-----EAIENTVEIA 260
|
|
| DNA_pol3_finger |
pfam17657 |
Bacterial DNA polymerase III alpha subunit finger domain; |
571-755 |
8.27e-77 |
|
Bacterial DNA polymerase III alpha subunit finger domain;
Pssm-ID: 407553 [Multi-domain] Cd Length: 166 Bit Score: 246.68 E-value: 8.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 571 NLTLIQKTVDLIQETRGYRVDPDEIPrqerkaqkilakgehsslpKDVQKTYELLEAGELEGIFQLESSGMRQIVRDLKP 650
Cdd:pfam17657 1 TLTIIRDALDLIKENRGIGIDLATIP-------------------LDDPKTYKLLSSGDTLGVFQFESRGMRQMLKRLKP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 651 SNIEDISSILALYRPGPLDAGLIPKFINRKHGRENIDYQHTVLEPILDETYGIMVYQEQIMKIAQDMAGYSLGQADLLRR 730
Cdd:pfam17657 62 DTFEDLVALSALYRPGPMQGGNVDDYIKRKHGKEKIEYPHPDLEPILKETYGVIVYQEQVMQIAQILAGFSLGEADLLRR 141
|
170 180
....*....|....*....|....*
gi 1928662004 731 AMGKKKVSEMQKQREKFVDGAAKNG 755
Cdd:pfam17657 142 AMGKKKPEEMEKLREKFIEGAKENG 166
|
|
| PHP |
pfam02811 |
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative ... |
6-178 |
1.87e-59 |
|
PHP domain; The PHP (Polymerase and Histidinol Phosphatase) domain is a putative phosphoesterase domain.
Pssm-ID: 460705 [Multi-domain] Cd Length: 171 Bit Score: 200.08 E-value: 1.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 6 LHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINGDIEKQE--RRPKY 83
Cdd:pfam02811 2 LHVHSEYSLLDGAARIEELVKRAKELGMPAIAITDHGNLFGAVEFYKAAKKAGIKPIIGCEVYVAPGSREETEklLAKYF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 84 HQVVLAKNTKGYKNLVKLTTISHLQGvqgkgifSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILS-NRPDAARKVAQW 162
Cdd:pfam02811 82 DLVLLAVHEVGYKNLIKLSSRAYLEG-------FKPRIDKELLEEYFEGLIALSGCVLGHLDLILLApGDYEEAEELAEE 154
|
170
....*....|....*..
gi 1928662004 163 YKDVFGDD-YYLEIQDH 178
Cdd:pfam02811 155 YLEIFGEDgFYLEINTH 171
|
|
| PHP_PolIIIA_POLC |
cd07435 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ... |
4-279 |
1.64e-45 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at PolC gene; DNA polymerase III alphas (PolIIIAs) that contain a PHP domain have been classified into four basic groups based on phylogenetic and domain structural analyses: polC, dnaE1, dnaE2, and dnaE3. The PolC group is distinct from the other three and is clustered together. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. PolC PHP is located in different location compare to dnaE1, 2, and 3. The PHP domain has four conserved sequence motifs and and contains an invariant histidine that is involved in metal ion coordination.The PHP domain of PolC is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel. PHP domains found in dnaEs of thermophilic origin exhibit 3'-5' exonuclease activity. In contrast, PolC PHP lacks detectable nuclease activity.
Pssm-ID: 213990 [Multi-domain] Cd Length: 268 Bit Score: 164.57 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 4 VPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVINgdiekqerrpKY 83
Cdd:cd07435 2 VELHAHTKMSAMDGVTSVKELVKRAAEWGHKAIAITDHGVVQAFPEAYEAAKKNGIKVIYGVEAYLVD----------PY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 84 HQVVLAKNTKGYKNLVKLTTISHLqgvqgKGIFSRPCINKDLLKQYHEGLIVTSACLGGEVPQAILSNRPDA-ARKVAQW 162
Cdd:cd07435 72 HITILVKNQTGLKNLYKLVSLSHT-----KYFYRVPRIPKSELEKYREGLLIGSACENGELFEAALNKKSDEeLEEIASF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 163 YkDvfgddyYLEIQDHGSQEDRI-------------VNVEIVKIARELDIQIIATNDSHFISCFDVEAHDALLCIQTGKl 229
Cdd:cd07435 147 Y-D------YIEIQPLDNYQFLIekglikseeelkeINKRIIKLGKKLNKPVVATGDVHYLDPEDKIYREILLAGQGGG- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1928662004 230 iieDKRMRYSGTEYLKSGEEMRQLFrDHLPDDVIAEAVAT-TEEVADKVEP 279
Cdd:cd07435 219 ---DGRADEQPDLYFRTTDEMLDEF-SYLGEEKAYEVVVTnTNKIADMIED 265
|
|
| PHP_PolIIIA |
cd07431 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; ... |
4-233 |
2.21e-40 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III; PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that is responsible for the replication of the DNA duplex. The alpha subunit of DNA polymerase III core enzyme catalyzes the reaction for polymerizing both DNA strands. The PolIIIA PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination, and like other PHP structures, exhibits a distorted (beta/alpha) 7 barrel and coordinates up to 3 metals. Initially, it was proposed that PHP region might be involved in pyrophosphate hydrolysis, but such activity has not been found. It has been shown that the PHP domain of PolIIIA has a trinuclear metal complex and is capable of proofreading activity.
Pssm-ID: 213986 [Multi-domain] Cd Length: 179 Bit Score: 146.58 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 4 VPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVingdiekQERRPKY 83
Cdd:cd07431 1 AHLHVHSSYSLLDSAIRPEDLVARAKELGYSALALTDRNVLYGAVRFYKACKKAGIKPIIGLELTV-------EGDGEPY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 84 HQVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFsrpCINKDLLKQYHEGLIVTSACLggevpqailsnrpdaarkvaqwy 163
Cdd:cd07431 74 PLLLLAKNNEGYQNLLRLSTAAMLGEEKDGVPY---LDLEELAEAASGLLVVLLGPL----------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 164 kdvfgddyyleiqdhgsqedrivnveIVKIARELDIQIIATNDSHFISCFDVEAHDALLCiqtgKLIIED 233
Cdd:cd07431 128 --------------------------LLLLAAEQGLPLVATNDVHYLNPEDAFAADVLTA----FLAVAN 167
|
|
| PHP_PolIIIA_DnaE2 |
cd07434 |
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at ... |
3-275 |
2.41e-27 |
|
Polymerase and Histidinol Phosphatase domain of alpha-subunit of bacterial polymerase III at DnaE2 gene; PolIIIA DnaE2 plays a role in SOS mutagenesis/translesion synthesis and has dominant effects in determining GC variability in the bacterial genome. PolIIIAs that contain an N-terminal PHP domain have been classified into four basic groups based on genome composition, phylogenetic, and domain structural analysis: polC, dnaE1, dnaE2, and dnaE3. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. DNA polymerase III holoenzyme is one of the five eubacterial DNA polymerases that are responsible for the replication of the DNA duplex. PolIIIA core enzyme catalyzes the reaction for polymerizing both DNA strands. PolC PHP is located in a different location compared to dnaE1, 2, and 3. dnaE1 is the longest compared to dnaE2 and dnaE3. A unique motif was also identified in dnaE1 and dnaE3 genes. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP domains found in DnaEs of thermophilic origin exhibit 3'-5' exonuclease activity.
Pssm-ID: 213989 [Multi-domain] Cd Length: 260 Bit Score: 111.78 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 3 FVPLHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVING-DIekqerrp 81
Cdd:cd07434 1 YAELHCLSNFSFLRGASHPEELVARAAELGYRALAITDECSLAGVVRAHAAAKELGLKLIVGSELVLADGtRL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 82 kyhqVVLAKNTKGYKNLVKLTTISHLQGVQGKGIFSRpcinKDLLkQYHEGLIvtsACLGgeVPQAILSNRPDAARkvAQ 161
Cdd:cd07434 74 ----VLLARDRAGYGRLCRLITLGRRRAEKGEYRLTL----ADLL-AHAEGLL---LILL--PPDRLPAAAALLAQ--LR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 162 WYKDVFGDDYYLEIQDHGSQEDRIVNVEIVKIARELDIQIIATNDSHfiscFDVEA----HDALLCIQTGKLIIEDKRMR 237
Cdd:cd07434 138 WLARAFPGRLWLALELHLGGDDARRLARLAALAAALGLPLVATGDVL----MHSPSrrplQDVLTAIRLGTTVAEAGRRL 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 1928662004 238 YSGTE-YLKSGEEMRQLFRDHlpddviAEAVATTEEVAD 275
Cdd:cd07434 214 AANAErHLRSPAELARLFLYP------PEALAETLEIAA 246
|
|
| polC |
PRK00448 |
DNA polymerase III PolC; Validated |
65-387 |
1.45e-26 |
|
DNA polymerase III PolC; Validated
Pssm-ID: 234767 [Multi-domain] Cd Length: 1437 Bit Score: 117.25 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 65 NEMYVINGDIEKQerRPkYHQVVLAKNTKGYKNLVKLTTISHLqgvqgKGIFSRPCINKDLLKQYHEGLIVTSACLGGEV 144
Cdd:PRK00448 596 NKKLGSEDAYKKA--RP-KHATILVKNQVGLKNLFKLVSLSNT-----KYFYRVPRIPRSLLDKYREGLLIGSACEEGEV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 145 PQAILSNRPDAARKVAQWYkDvfgddyYLEIQ-----------DHGSQEDRI--VNVEIVKIARELDIQIIATNDSHFIS 211
Cdd:PRK00448 668 FDAVLQKGDEELEEIAKFY-D------YIEIQppanyqhlierELVKDEEELkeIIKNLIELGKKLNKPVVATGDVHYLD 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 212 CFDVEAHDALLCIQTGKliieDKRMRYSGTE-YLKSGEEMRQLFrDHLPDDVIAEAVAT-TEEVADKVEPYHimgepqip 289
Cdd:PRK00448 741 PEDKIYRKILVASQGGG----NPLNRHPLPElHFRTTDEMLDEF-AFLGEELAKEIVVEnTNKIADLIEEIE-------- 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 290 tpPIPSghtaDTYA---EDVAwngllERLNRKSRQEVDSVY--------KERLEYELKMIQQMGFSKYFLVVWDYIKFAR 358
Cdd:PRK00448 808 --PIKD----KLYTpkiEGAE-----EEIRELTYKKAHEIYgeplpeivEKRIEKELNSIIGNGFAVIYLISQKLVKKSL 876
|
330 340
....*....|....*....|....*....
gi 1928662004 359 DNNIPVGPgRGSAAGSLVAYAMRITNIDP 387
Cdd:PRK00448 877 EDGYLVGS-RGSVGSSFVATMIGITEVNP 904
|
|
| POLIIIAc |
smart00481 |
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family ... |
6-71 |
1.45e-23 |
|
DNA polymerase alpha chain like domain; DNA polymerase alpha chain like domain, incl. family of hypothetical proteins
Pssm-ID: 197753 [Multi-domain] Cd Length: 67 Bit Score: 94.64 E-value: 1.45e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1928662004 6 LHIHSDYSLLDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEMYVIN 71
Cdd:smart00481 2 LHVHSDYSLLDGALSPEELVKRAKELGLKAIAITDHGNLFGAVEFYKAAKKAGIKPIIGLEANIVD 67
|
|
| PHP_HisPPase |
cd07432 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase ... |
6-67 |
1.85e-12 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase; HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. HisPPase can be classified into two types: the bifunctional HisPPase found in proteobacteria that belongs to the DDDD superfamily and the monofunctional Bacillus subtilis type that is a member of the PHP family. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213987 [Multi-domain] Cd Length: 129 Bit Score: 64.95 E-value: 1.85e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1928662004 6 LHIHSDYSllDGASQLP-ELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEM 67
Cdd:cd07432 3 LHIHSVFS--PDSDMTPeEIVERAIELGLDGIAITDHNTIDGAEEALKEAYKDGLLVIPGVEV 63
|
|
| HintN |
smart00306 |
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ... |
774-857 |
9.29e-12 |
|
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.
Pssm-ID: 197642 [Multi-domain] Cd Length: 100 Bit Score: 62.29 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 774 YCLSYETEILTVEYGLLPIGKIvekRIECTVYSVDNNGNIYT--QPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTV 851
Cdd:smart00306 1 GCFPGDTLVLTEDGGIKKIEEL---EEGDKVLALDEGTLKYSpvKVFLVREPKGEKKFYRIKTENGREITLTPDHLLLVR 77
|
....*.
gi 1928662004 852 DGQMLQ 857
Cdd:smart00306 78 DGGKLV 83
|
|
| Hop |
COG1372 |
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ... |
691-853 |
1.08e-11 |
|
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];
Pssm-ID: 440983 [Multi-domain] Cd Length: 866 Bit Score: 68.77 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 691 TVLEPILDETYGIMVYQEQIMKIAQDMAGYSLGQADLLRRAMGKKKVSEMQKQREKFVDGAAKNGVPKKVADELFEQMLK 770
Cdd:COG1372 13 ATLVTDALRLKLLELKEEGIELLKLELDLEELGEVLAEALVRAIDGASLILLAAGGGVLLVALTGLGREAAAGLALAGGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 771 FAEY-CLSYETEILTVEYGLLPIGKIVEKRIECTVYSVDNNGN-IYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKF 848
Cdd:COG1372 93 TGTGvCLTGDTLVLTADGRLVPIGELVGSGEDVEVLSLDLDTGkLVWAPVTKVFKTGVKPVYRIRTRSGREIRATPDHPF 172
|
....*
gi 1928662004 849 MTVDG 853
Cdd:COG1372 173 LTLSG 177
|
|
| YciV |
COG0613 |
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and ... |
6-67 |
6.12e-11 |
|
5'-3' exoribonuclease TrpH/YciV (RNase AM), contains PHP domain [Nucleotide transport and metabolism];
Pssm-ID: 440378 [Multi-domain] Cd Length: 188 Bit Score: 62.23 E-value: 6.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKPIIGNEM 67
Cdd:COG0613 6 LHVHTTAS--DGSLSPEELVARAKAAGLDVLAITDHDTVAGYEEAAEAAKELGLLVIPGVEI 65
|
|
| intein_Nterm |
TIGR01445 |
intein N-terminal splicing region; This model is based on interated search results, starting ... |
776-850 |
9.19e-11 |
|
intein N-terminal splicing region; This model is based on interated search results, starting with a curated collection of intein N-terminal splicing regions from InBase, the New England Biolabs Intein Database, as presented on its web site. It is designed to recognize inteins but not the related region of the sonic hedgehog protein.
Pssm-ID: 273629 [Multi-domain] Cd Length: 81 Bit Score: 58.87 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 776 LSYETEILTVEYGLLPIGKIVEKRIEC------TVYSVDNNGNIYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFM 849
Cdd:TIGR01445 1 LTGDTKVLTEDGETVKIGELVEKEKDEkepikvKVLSLDGGKIVKARPVVVWKRRAEGKLIRIKTENGREIKATPDHPFL 80
|
.
gi 1928662004 850 T 850
Cdd:TIGR01445 81 T 81
|
|
| PHP |
cd07309 |
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2 ... |
4-69 |
1.98e-10 |
|
Polymerase and Histidinol Phosphatase domain; The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PHP in polymerases has trinuclear zinc/magnesium dependent proofreading activity. It has also been shown that the PHP domain functions in DNA repair. The PHP structures have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213985 [Multi-domain] Cd Length: 88 Bit Score: 57.82 E-value: 1.98e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1928662004 4 VPLHIHSDYSLLDGASqLPELVDQAIKLGMKAIALTDHGVMYGAVELIKI----CRSQ----NIKPIIGNEMYV 69
Cdd:cd07309 1 VDLHTHTVFSDGDHAK-LTELVDKAKELGPDALAITDHGNLRGLAEFNTAgk*nHIKAaeaaGIKIIIGSEVNL 73
|
|
| Hint |
cd00081 |
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ... |
775-866 |
3.35e-09 |
|
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.
Pssm-ID: 238035 [Multi-domain] Cd Length: 136 Bit Score: 56.12 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 775 CLSYETEILTVEYGLLPIGKIVEKRIEcTVYSVDNNGNI-YTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTVDG 853
Cdd:cd00081 1 CFTGDTLVLLEDGGRKKIEELVEKKGD-KVLALDETGKLvFSKVLKVLRRDYEKKFYKIKTESGREITLTPDHLLFVLED 79
|
90
....*....|...
gi 1928662004 854 QMLQidEIFERKL 866
Cdd:cd00081 80 GELK--WVFASDL 90
|
|
| PHP_HisPPase_AMP |
cd07438 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) ... |
6-75 |
8.10e-09 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase (HisPPase) AMP bound; The PHP domain of this HisPPase family has an unknown function. It has a second domain inserted in the middle that binds adenosine 5-monophosphate (AMP). The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to give histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to the other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213993 [Multi-domain] Cd Length: 155 Bit Score: 55.48 E-value: 8.10e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKICRSQNIKpiignemyVINGdIE 75
Cdd:cd07438 3 LHTHSTAS--DGTLSPEELVELAKEAGLKVLAITDHDTVAGLEEALAAAKELGIE--------LIPG-VE 61
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
6-42 |
1.79e-06 |
|
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]; Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 440997 [Multi-domain] Cd Length: 232 Bit Score: 50.15 E-value: 1.79e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDHG 42
Cdd:COG1387 5 LHTHTTYS--DGEGTIEEMVEAAIELGLEYIAITDHS 39
|
|
| PHP_PolX |
cd07436 |
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal ... |
6-41 |
3.12e-06 |
|
Polymerase and Histidinol Phosphatase domain of bacterial polymerase X; The bacterial/archaeal X-family DNA polymerases (PolXs) have a PHP domain at their C-terminus. The bacterial/archaeal PolX core domain and PHP domain interact with each other and together are involved in metal dependent 3'-5' exonuclease activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. PolX is found in all kingdoms, however bacterial PolXs have a completely different domain structure from eukaryotic PolXs. Bacterial PolX has an extended conformation in contrast to the common closed 'right hand' conformation for DNA polymerases. This extended conformation is stabilized by the PHP domain. The PHP domain of PolX is structurally homologous to other members of the PHP family that has a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213991 [Multi-domain] Cd Length: 237 Bit Score: 49.34 E-value: 3.12e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDH 41
Cdd:cd07436 9 LHVHTTWS--DGRNSIEEMAEAARALGYEYIAITDH 42
|
|
| CehA_McbA_metalo |
NF038032 |
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is ... |
6-53 |
5.85e-04 |
|
CehA/McbA family metallohydrolase domain; This domain, a branch of the PHP superfamily, is found in several partially characterized metallohydrolases, including McbA and CehA. Both were studied as hydrolases of carbaryl, a xenobiotic compound that does not contain a phosphate group, suggesting that presuming members of this family to be phosphoesterases (like many PHP domain-containing proteins) may be incorrect.
Pssm-ID: 468321 [Multi-domain] Cd Length: 315 Bit Score: 43.08 E-value: 5.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDHGVMYGAVELIKI 53
Cdd:NF038032 7 LHIHTNHS--DGPTTPEELARAALAEGLDVIALTDHNTISGRAYFAEL 52
|
|
| PRK07945 |
PRK07945 |
PHP domain-containing protein; |
6-41 |
5.94e-04 |
|
PHP domain-containing protein;
Pssm-ID: 236135 [Multi-domain] Cd Length: 335 Bit Score: 43.04 E-value: 5.94e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1928662004 6 LHIHSDYSllDGASQLPELVDQAIKLGMKAIALTDH 41
Cdd:PRK07945 100 LHTHSDWS--DGGSPIEEMARTAAALGHEYCALTDH 133
|
|
| recA |
PRK09519 |
intein-containing recombinase RecA; |
775-853 |
3.40e-03 |
|
intein-containing recombinase RecA;
Pssm-ID: 77219 [Multi-domain] Cd Length: 790 Bit Score: 41.23 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 775 CLSYETEILTVEYGLL-PIGKIVEKRIECTVYSVDNNGNIYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTVDG 853
Cdd:PRK09519 252 CLAEGTRIFDPVTGTThRIEDVVDGRKPIHVVAAAKDGTLHARPVVSWFDQGTRDVIGLRIAGGAIVWATPDHKVLTEYG 331
|
|
| PRK07773 |
PRK07773 |
replicative DNA helicase; Validated |
775-853 |
4.62e-03 |
|
replicative DNA helicase; Validated
Pssm-ID: 236093 [Multi-domain] Cd Length: 886 Bit Score: 40.89 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1928662004 775 CLSYETEILTVEYGL-LPIGKIVEKRiECTVYSVDNNG-NIYTQPIAQWHDRGQQEVFEYCLEDGSLIRATKDHKFMTVD 852
Cdd:PRK07773 398 CLTGDTLILRADTGAeVPIGELVGER-PFAVWALDERTlRLVAAPVSNVFPTGRKPVFRLRTRSGREIRATANHPFLTFE 476
|
.
gi 1928662004 853 G 853
Cdd:PRK07773 477 G 477
|
|
| |
