|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11061 |
PRK11061 |
phosphoenolpyruvate--protein phosphotransferase; |
6-760 |
0e+00 |
|
phosphoenolpyruvate--protein phosphotransferase;
Pssm-ID: 182937 [Multi-domain] Cd Length: 748 Bit Score: 742.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 6 LDTLRRIVQEVNASVSLHESLDIMVNQVAEAMKVDVCSIYLLDERNQRYVLMASKGLNPESVGHVSLQLGEGLVGLVGQR 85
Cdd:PRK11061 2 LTRLREIVEKVASAPRLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAFDEGIVGLVGRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 86 EEIVNLDNAPKHERFLYLPETGEEIYNSFLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIAHAHAVG 165
Cdd:PRK11061 82 AEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQRELRQFDESEESFLVTLATQLAAILSQSQLTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 166 NIDVFRKPSngpayktFQGASGAGGVALGRAIILYPPADLGSVPDREAEDISDELRILDQAISSVRSEIRSLDEKMHDSL 245
Cdd:PRK11061 162 LFGQYRQTR-------IRALPASPGVAIAEGWQDATQPLLEQVYPASTLDPALERERLTGALEEAANEFRRYSKRFAAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 246 MAEERALFSVFLRMLDENALPAEIKELIRDGHWAQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRILASLQEEDS 325
Cdd:PRK11061 235 QKETAAIFDLYSHLLNDPRLRRELFAEVDKGSVAEWAVKQVIEKFAEQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 326 SHRDLSPDSILIGEEISTAALVELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVtELPVNTLDDAEMIVDAYQGRV 405
Cdd:PRK11061 315 GPNAWPERFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGA-DIQPSLLHQRLLIVDGYRGEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 406 FVNPPRRLRQRYKEIQKEDEQIAKDLKQYETKEAITPDGVSVQLYVNTGLMIDVVRGVQRGAQGVGLYRSEIPFMLRERF 485
Cdd:PRK11061 394 LVDPEPVLLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 486 PGEEEQRAIYRQQLSHFANKPVVMRTLDIGADKDLPYFSIEEENSALGWRGIRFTLDHPEIFSSQIRAMLKASIGLNNLH 565
Cdd:PRK11061 474 PSEEEQVAQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 566 ILLPMVTTVSEVEEVLYLLERDWIAVQEEEQVKITKPKIGIMVEVPSVLLQIDEFAELVDFFSVGSNDLTQYLLAVDRNN 645
Cdd:PRK11061 554 ILLPMVTSIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVDRNN 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 646 PHVANVYSHFHPSILRALTRLVKECHEYKKPISICGEMAGDPLSAILLMAMGFNTLSMSSSNILRVRKAICHVPMTDAQK 725
Cdd:PRK11061 634 TRVASLYDSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAEAEN 713
|
730 740 750
....*....|....*....|....*....|....*
gi 491207686 726 LLDDVMKMNNPLIVKSWLEYYFKTHGLADMVKSNR 760
Cdd:PRK11061 714 LAQRSLEAQLATEVRHQVAAFMERRGLGGLIRGGK 748
|
|
| PtsA |
COG1080 |
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ... |
182-750 |
0e+00 |
|
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];
Pssm-ID: 440698 [Multi-domain] Cd Length: 571 Bit Score: 604.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 182 FQGASGAGGVALGRAIILYPPADlgSVPDR--EAEDISDELRILDQAISSVRSEIRSLDEKMHDSLMAEERALFSVFLRM 259
Cdd:COG1080 1 LKGIAASPGIAIGKAFLLREEDL--EVPEYtiSPEDVEAEIARLEAALAKAREELEALREKAPEDLGEEEAAIFDAHLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 260 LDENALPAEIKELIRDGHW-AQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRILASLQ-EEDSSHRDLSPDSILI 337
Cdd:COG1080 79 LEDPELIEEVEELIREGRYnAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLgVEAPDLSDLPEPVILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 338 GEEISTAALVELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQGRVFVNPPRRLRQRY 417
Cdd:COG1080 159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 418 KEIQKEDEQIAKDLKQYETKEAITPDGVSVQLYVNTGLMIDVVRGVQRGAQGVGLYRSEIPFMLRERFPGEEEQRAIYRQ 497
Cdd:COG1080 239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 498 QLSHFANKPVVMRTLDIGADKDLPYFSI-EEENSALGWRGIRFTLDHPEIFSSQIRAMLKASIgLNNLHILLPMVTTVSE 576
Cdd:COG1080 319 VAEAMGGRPVTIRTLDIGGDKPLPYLPLpKEENPFLGLRAIRLCLDRPELFRTQLRAILRASA-HGNLRIMFPMISSVEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 577 VEEVLYLLERdwiaVQEE---EQVKI-TKPKIGIMVEVPSVLLQIDEFAELVDFFSVGSNDLTQYLLAVDRNNPHVANVY 652
Cdd:COG1080 398 LRQAKALLEE----AKAElraEGIPFdEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 653 SHFHPSILRALTRLVKECHEYKKPISICGEMAGDPLSAILLMAMGFNTLSMSSSNILRVRKAICHVPMTDAQKLLDDVMK 732
Cdd:COG1080 474 DPLHPAVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALA 553
|
570
....*....|....*...
gi 491207686 733 MNNPLIVKSWLEYYFKTH 750
Cdd:COG1080 554 LDTAEEVRALLEEFLAEL 571
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
190-733 |
1.31e-116 |
|
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.
Pssm-ID: 273611 [Multi-domain] Cd Length: 565 Bit Score: 363.34 E-value: 1.31e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 190 GVALGRAIILYPPADLGSVPDREAEDISDELRILDQAISSVRSEIRSLDEKMHDSLMAEERALFSVFLRMLDENALPAEI 269
Cdd:TIGR01417 9 GIAIGKALLLKKPDLVIDRKKISASQVDQEISRFLSARAKAKEDLETIKTKAGKTFGQEKAAIFEAHILILEDPELTEEV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 270 KELIRDGHW-AQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRILASLQ-EEDSSHRDLSPDSILIGEEISTAALV 347
Cdd:TIGR01417 89 IELIKKDHKnAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLLgVKISDLSEIQDEVILVAEDLTPSETA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 348 ELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQGRVFVNPPRRLRQRYKEIQKEDEQI 427
Cdd:TIGR01417 169 QLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIFNPSSETIDKYEAKQEAVSSE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 428 AKDLKQYETKEAITPDGVSVQLYVNTGLMIDVVRGVQRGAQGVGLYRSEIPFMLRERFPGEEEQRAIYRQQLSHFANKPV 507
Cdd:TIGR01417 249 KAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVLEAMESDAV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 508 VMRTLDIGADKDLPYF-SIEEENSALGWRGIRFTLDHPEIFSSQIRAMLKASiGLNNLHILLPMVTTVSEVEEVLYLLER 586
Cdd:TIGR01417 329 IVRTLDIGGDKELPYLnFPKEENPFLGYRAIRLALEREEILRTQLRAILRAS-AYGKLRIMFPMVATVEEIRAVKQELEE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 587 DWIAVQEEEQVKITKPKIGIMVEVPSVLLQIDEFAELVDFFSVGSNDLTQYLLAVDRNNPHVANVYSHFHPSILRALTRL 666
Cdd:TIGR01417 408 EKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPAVLRLIKLV 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491207686 667 VKECHEYKKPISICGEMAGDPLSAILLMAMGFNTLSMSSSNILRVRKAICHVPMTDAQKLLDDVMKM 733
Cdd:TIGR01417 488 IDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQ 554
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
436-718 |
7.95e-109 |
|
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilizing proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain.
Pssm-ID: 397163 [Multi-domain] Cd Length: 292 Bit Score: 333.51 E-value: 7.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 436 TKEAITPDGVSVQLYVNTGLMIDVVRGVQRGAQGVGLYRSEIPFMLRERFPGEEEQRAIYRQQLSHFANKPVVMRTLDIG 515
Cdd:pfam02896 9 DLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVTVRTLDIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 516 ADKDLPYFSI-EEENSALGWRGIRFTLDHPEIFSSQIRAMLKASIGlNNLHILLPMVTTVSEVEEVLYLLERdwIAVQEE 594
Cdd:pfam02896 89 GDKELPYLEEpEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAF-GNLRIMFPMVASVEELREAKAIIEE--VKEELD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 595 EQVKITKP-KIGIMVEVPSVLLQIDEFAELVDFFSVGSNDLTQYLLAVDRNNPHVANVYSHFHPSILRALTRLVKECHEY 673
Cdd:pfam02896 166 AEVGFDKDiKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVIRAAHRH 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491207686 674 KKPISICGEMAGDPLSAILLMAMGFNTLSMSSSNILRVRKAICHV 718
Cdd:pfam02896 246 GKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQI 290
|
|
| PRK11177 |
PRK11177 |
phosphoenolpyruvate-protein phosphotransferase PtsI; |
239-733 |
1.14e-106 |
|
phosphoenolpyruvate-protein phosphotransferase PtsI;
Pssm-ID: 183017 [Multi-domain] Cd Length: 575 Bit Score: 337.75 E-value: 1.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 239 EKMHDSLMAEERALFSVFLRMLDENALPAEIKELIRDGHW-AQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRI- 316
Cdd:PRK11177 59 TKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMtADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 317 ----------LASLQEEdsshrdlspdSILIGEEISTAALVELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTEL 386
Cdd:PRK11177 139 knilglkiidLSAIQEE----------VILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTGNI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 387 PVNTLDDAEMIVDAYQGRVFVNPPRRLRQRYKEIQKEDEQIAKDLKQYETKEAITPDGVSVQLYVNTGLMIDVVRGVQRG 466
Cdd:PRK11177 209 TKQVKNGDYLILDAVNNQIYVNPTNEVIEELKAVQEQYASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 467 AQGVGLYRSEIPFMLRERFPGEEEQRAIYRQQLSHFANKPVVMRTLDIGADKDLPYFSI-EEENSALGWRGIRFTLDHPE 545
Cdd:PRK11177 289 AEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLpKEENPFLGWRAIRIAMDRKE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 546 IFSSQIRAMLKASiGLNNLHILLPMVTTVSEVEEVLYLLERDWIAVQEEEQVKITKPKIGIMVEVPSVLLQIDEFAELVD 625
Cdd:PRK11177 369 ILHDQLRAILRAS-AFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVIARHLAKEVD 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 626 FFSVGSNDLTQYLLAVDRNNPHVANVYSHFHPSILRALTRLVKECHEYKKPISICGEMAGDPLSAILLMAMGFNTLSMSS 705
Cdd:PRK11177 448 FFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSA 527
|
490 500
....*....|....*....|....*...
gi 491207686 706 SNILRVRKAICHVPMTDAQKLLDDVMKM 733
Cdd:PRK11177 528 ISIPRIKKIIRNTNFEDAKALAEQALAQ 555
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
5-185 |
6.88e-69 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 224.78 E-value: 6.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 5 QLDTLRRIVQEVNASVSLHESLDIMVNQVAEAMKVDVCSIYLLDERNQRYVLMASKGLNPESVGHVSLQLGEGLVGLVGQ 84
Cdd:COG3605 2 MLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVGKVRLPLGEGLVGLVAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 85 REEIVNLDNAPKHERFLYLPETGEEIYNSFLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIAHAHAV 164
Cdd:COG3605 82 RGEPLNLADAASHPRFKYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAELL 161
|
170 180
....*....|....*....|.
gi 491207686 165 GNIDVFRKPSNGPAYKTFQGA 185
Cdd:COG3605 162 GELRAALAELSLAREEEREAA 182
|
|
| PRK06464 |
PRK06464 |
phosphoenolpyruvate synthase; Validated |
355-715 |
4.69e-56 |
|
phosphoenolpyruvate synthase; Validated
Pssm-ID: 235809 [Multi-domain] Cd Length: 795 Bit Score: 205.75 E-value: 4.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 355 AAIVTSEGAANSHMVIVARALGIPTVVG---VTElpvnTLDDAEMI----VDAYQGRVfvnpprrlrqrYK-EIQKEDEQ 426
Cdd:PRK06464 406 SAIVTNRGGRTCHAAIIARELGIPAVVGtgnATE----VLKDGQEVtvscAEGDTGYV-----------YEgLLEFEVEE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 427 IAKDlkqyetKEAITPdgvsVQLYVNTGlMIDVV-RGVQRGAQGVGLYRSEipFM------------------------- 480
Cdd:PRK06464 471 VSLE------EMPETP----TKIMMNVG-NPERAfDFAALPNDGVGLARLE--FIinnmigvhplallefdqqdadlkae 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 481 LRERFPGEEEQRAIYRQQLSH--------FANKPVVMRTLD---------IGADKDLPyfsiEEENSALGWRGIRFTLDH 543
Cdd:PRK06464 538 IEELTAGYASPEEFYVDKLAEgiatvaaaFYPKPVIVRLSDfksneyanlIGGERYEP----EEENPMLGFRGASRYLSE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 544 P--EIFSSQIRAMLKA--SIGLNNLHILLPMVTTVSEVEEVLYLLERDWIAVQEEEQvkitkpKIGIMVEVPSVLLQIDE 619
Cdd:PRK06464 614 SfrEAFALECEAIKRVreEMGLTNVEVMIPFVRTVEEAEKVIELLAENGLKRGENGL------KVIMMCEIPSNALLAEE 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 620 FAELVDFFSVGSNDLTQYLLAVDRNNPHVANVYSHFHPSILRALTRLVKECHEYKKPISICGEMAGD-PLSAILLMAMGF 698
Cdd:PRK06464 688 FLEYFDGFSIGSNDLTQLTLGLDRDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQAPSDhPDFAEWLVEEGI 767
|
410
....*....|....*..
gi 491207686 699 NTLSMSSSNILRVRKAI 715
Cdd:PRK06464 768 DSISLNPDAVVDTWLAV 784
|
|
| PEP-utilizers_N |
pfam05524 |
PEP-utilizing enzyme, N-terminal; |
183-305 |
7.44e-26 |
|
PEP-utilizing enzyme, N-terminal;
Pssm-ID: 461671 [Multi-domain] Cd Length: 125 Bit Score: 103.08 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 183 QGASGAGGVALGRAIILYPPA-DLGSVPDREAEDISDELRILDQAISSVRSEIRSLDEKMHDSLMAEERALFSVFLRMLD 261
Cdd:pfam05524 1 KGIGASPGIAIGKAVVLEEPElEVPDEREVPADDVEAEIARLEAALEAAREELEALAERAAGELGEEEAAIFEAHLMMLE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 491207686 262 ENALPAEIKELIRDGH-WAQGAVRRVIEKHTALFAQMEDDYLRER 305
Cdd:pfam05524 81 DPELLEEVEELIREGGlNAEAAVKEVVDEFAAMFEAMDDPYLRER 125
|
|
| PRK11377 |
PRK11377 |
dihydroxyacetone kinase subunit M; Provisional |
183-405 |
9.23e-22 |
|
dihydroxyacetone kinase subunit M; Provisional
Pssm-ID: 183108 [Multi-domain] Cd Length: 473 Bit Score: 99.44 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 183 QGASGAGGVALGRAIIlYPPAdLGSVPDREAEDISDELRILDQAISSVRSEIRSLDEKMHDSLMAEERALFSVFLRMLDE 262
Cdd:PRK11377 248 PTLRPVPSPVSGKAFY-YQPV-LCTVQAKSTLTVEEEQERLRQAIDFTLLDLMTLTAKAEASGLDDIAAIFSGHHTLLDD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 263 NALPAEIKELIRDGHW-AQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRILASLQEEDSSHRDLSPDSILIGEEI 341
Cdd:PRK11377 326 PELLAAASERLQHEHCtAEYAWQQVLKELSQQYQQLDDEYLQARYIDVDDLLHRTLVHLTQTKEELPQFNSPTILLAENI 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491207686 342 STAALVELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQGRV 405
Cdd:PRK11377 406 YPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQGEKLYAIQPEETLTLDVKTQRL 469
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
22-164 |
1.64e-20 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 88.59 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 22 LHESLDIMVNQVAEAMKVDVCSIYLLDERN-QRYVLMASKGLNPESVGHVSLqLGEGLVGLVGQREEIVNLDNAPKHERF 100
Cdd:smart00065 2 LEELLQTILEELRQLLGADRVLIYLVDENDrGELVLVAADGLTLPTLGIRFP-LDEGLAGRVAETGRPLNIPDVEADPLF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491207686 101 LYLPETGEEIYNSFLGVPVMYRRKVMGVLVVQNKL-PQDFSEAAESFLVTLCAQLSGVIAHAHAV 164
Cdd:smart00065 81 AEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKsPRPFTEEDEELLQALANQLAIALANAQLY 145
|
|
| PEP-utilizers |
pfam00391 |
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain ... |
329-403 |
5.81e-19 |
|
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it.
Pssm-ID: 459796 [Multi-domain] Cd Length: 73 Bit Score: 81.69 E-value: 5.81e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491207686 329 DLSPDSILIGEEISTAALVELpvDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQG 403
Cdd:pfam00391 1 KLPEGVILVAPDTTPSDTAGL--DKAAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEGDLVTVDGSTG 73
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
5-501 |
3.78e-18 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 89.10 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 5 QLDTLRRIVQEVNASVSLHESLDIMVNQVAEAMKVDVCSIYLLDERNQRYVLMASKGLNPESVGHvsLQLGEGLVGLVGQ 84
Cdd:COG2203 191 RLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGR--LPLGEGLAGRALR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 85 REEIVNLDNAPKHERF--LYLPETGEEIYNSFLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIAHAH 162
Cdd:COG2203 269 TGEPVVVNDASTDPRFapSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERAR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 163 AVGNIDVFRKPSNGPAYKTFQGASGAGGVALGRAIILYPPADLGSVPDREAEDISDELRILDQAISSVRSEIRSLDEKMH 242
Cdd:COG2203 349 LYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 243 DSLMAEERALFSVFLRMLDENALPAEIKELIRDGHWAQGAVRRVIEKHTALFAQMEDDYLRERVSDLKDLGRRILASLQE 322
Cdd:COG2203 429 LLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLAS 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 323 EDSSHRDLSPDSILIGEEISTAALVELPVDNIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQ 402
Cdd:COG2203 509 LLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALA 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 403 GRVFVNPPRRLRQRYKEIQKEDEQIAKDLkqyETKEAITPDGVSVQLYVNTGLMIDVVRGVQRGAQGVGLYRSEIPFMLR 482
Cdd:COG2203 589 LLELLLVAVGDLLLLERDLLLLLVLLVRL---LLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELD 665
|
490
....*....|....*....
gi 491207686 483 ERFPGEEEQRAIYRQQLSH 501
Cdd:COG2203 666 LILDSSLLLGLLLLGALLL 684
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
21-158 |
9.24e-16 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 74.44 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 21 SLHESLDIMVNQVAEAMKVDVCSIYLLDERNQRYVlmaSKGLNPESVGHVSLQLGEGlvGLVGQREEIVNLDNAPKHERF 100
Cdd:pfam01590 1 DLEEILQTILEELRELLGADRCALYLPDADGLEYL---PPGARWLKAAGLEIPPGTG--VTVLRTGRPLVVPDAAGDPRF 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491207686 101 LYLPETGEEI-YNSFLGVPVMYRRKVMGVLVVQNKLPQdFSEAAESFLVTLCAQLSGVI 158
Cdd:pfam01590 76 LDPLLLLRNFgIRSLLAVPIIDDGELLGVLVLHHPRPP-FTEEELELLEVLADQVAIAL 133
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
19-159 |
9.49e-13 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 65.95 E-value: 9.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 19 SVSLHESLDIMVNQVAEAMKVDVCSIYLLDERNQryvLMASKGLNPESVGHVSLQLGEGLVGLVGQREEIVNLDNAPKHE 98
Cdd:pfam13185 1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGR---LAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADP 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207686 99 RFLYLPEtGEEIYNSFLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIA 159
Cdd:pfam13185 78 AKKGLPA-GHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
|
|
| GAF_3 |
pfam13492 |
GAF domain; |
21-160 |
4.36e-08 |
|
GAF domain;
Pssm-ID: 433253 [Multi-domain] Cd Length: 129 Bit Score: 52.37 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 21 SLHESLDIMVNQVAEAMKVDVCSIYLLDERNQRYVLMASKGLNPESVGHVSLQlgEGLVGLVGQREEIVNLDNAPKherf 100
Cdd:pfam13492 1 SLDEILEALLKLLVRLLGAERAAVYLLDEDGNKLQVAAGYDGEPDPSESLDAD--SPLARRALSSGEPISGLGSAG---- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 101 lylpETGEEIYNSFLgVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIAH 160
Cdd:pfam13492 75 ----EDGLPDGPALV-VPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIATAIEN 129
|
|
| PykA2 |
COG3848 |
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms]; |
353-406 |
7.22e-08 |
|
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
Pssm-ID: 443058 Cd Length: 321 Bit Score: 54.91 E-value: 7.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491207686 353 NIAAIVTSEGAANSHMVIVARALGIPTVVGVtELPVNTLDDAEMI-VDAYQGRVF 406
Cdd:COG3848 261 KAAGIITEEGGLTSHAAIVGLELGIPVIVGA-EGATEILKDGQVVtVDAERGVVY 314
|
|
| PpsA |
COG0574 |
Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and ... |
354-405 |
7.58e-08 |
|
Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and metabolism]; Phosphoenolpyruvate synthase/pyruvate phosphate dikinase is part of the Pathway/BioSystem: Gluconeogenesis
Pssm-ID: 440339 [Multi-domain] Cd Length: 455 Bit Score: 55.61 E-value: 7.58e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491207686 354 IAAIVTSEGAANSHMVIVARALGIPTVVGV---TElpvnTLDDAEMI-VDAYQGRV 405
Cdd:COG0574 403 AAGIVTERGGMTSHAAIVARELGIPAVVGCgdaTR----VLKDGDEItVDGTTGEV 454
|
|
| PRK05878 |
PRK05878 |
pyruvate phosphate dikinase; Provisional |
355-406 |
4.46e-06 |
|
pyruvate phosphate dikinase; Provisional
Pssm-ID: 235635 [Multi-domain] Cd Length: 530 Bit Score: 50.13 E-value: 4.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 491207686 355 AAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQGRVF 406
Cdd:PRK05878 401 QGIVTEVGGATSHAAVVSRELGRVAVVGCGAGVAAALAGKEITVDGYEGEVR 452
|
|
| MsrC |
COG1956 |
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ... |
17-159 |
5.34e-06 |
|
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];
Pssm-ID: 441559 [Multi-domain] Cd Length: 156 Bit Score: 47.13 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 17 NASVSLHESLDimvnqvaeamKVDVCSIYLLDERNQrYVLMASKGLnpesVGHVSLQLGEGLVGLVGQREEIVNLDNAPK 96
Cdd:COG1956 32 NISALLFEALP----------DYNWVGFYLVDGGGE-LVLGPFQGP----PACTRIPFGKGVCGTAAAEGETQLVPDVHA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491207686 97 HERFLYL-PETgeeiyNSFLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVIA 159
Cdd:COG1956 97 FPGHIACdSAS-----RSEIVVPIFKDGEVIGVLDIDSPTPGRFDEEDQAGLEALAALLAEALD 155
|
|
| PRK05849 |
PRK05849 |
hypothetical protein; Provisional |
353-407 |
4.90e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235623 [Multi-domain] Cd Length: 783 Bit Score: 46.90 E-value: 4.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491207686 353 NIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIV-DAYQGRVFV 407
Cdd:PRK05849 727 GIAGLITCYGGANSHMAIRAAELGLPAVIGVGEELFEKWLKAKRILlDCASQRIEI 782
|
|
| PRK06354 |
PRK06354 |
pyruvate kinase; Provisional |
353-406 |
2.14e-04 |
|
pyruvate kinase; Provisional
Pssm-ID: 235784 [Multi-domain] Cd Length: 590 Bit Score: 44.53 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491207686 353 NIAAIVTSEGAANSHMVIVARALGIPTVVGVTELPVNTLDDAEMIVDAYQGRVF 406
Cdd:PRK06354 530 KAAAIITEEGGLTSHAAVVGLRLGIPVIVGVKNATSLIKDGQIITVDAARGVVY 583
|
|
| FhlA |
COG3604 |
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ... |
114-158 |
5.53e-04 |
|
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 442823 [Multi-domain] Cd Length: 338 Bit Score: 42.91 E-value: 5.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 491207686 114 FLGVPVMYRRKVMGVLVVQNKLPQDFSEAAESFLVTLCAQLSGVI 158
Cdd:COG3604 76 FLGVPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAI 120
|
|
| PRK08296 |
PRK08296 |
hypothetical protein; Provisional |
354-405 |
1.04e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181362 Cd Length: 603 Bit Score: 42.33 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491207686 354 IAAIVTSEGAANSHMVIVARALGIPTVVGvTELPVNTLDDAEMI-VDAYQGRV 405
Cdd:PRK08296 548 IKATVTDIGGVMSHAAIVCREYGLPAVVG-TGNATKRIKTGQRLrVDGTKGVV 599
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-438 |
5.78e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 186 SGA--GGVALGRAIILYPPADLGSVP---------DREAEDISDELRILDQAISSVRSEI----RSLDEKMHD-SLMAEE 249
Cdd:TIGR02169 652 SGAmtGGSRAPRGGILFSRSEPAELQrlrerleglKRELSSLQSELRRIENRLDELSQELsdasRKIGEIEKEiEQLEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 250 RALFS-------VFLRMLDEN--ALPAEIKELIRDghwaQGAVRRVIEKHTALFAQMEDDYLRERV-------SDLKDLG 313
Cdd:TIGR02169 732 EEKLKerleeleEDLSSLEQEieNVKSELKELEAR----IEELEEDLHKLEEALNDLEARLSHSRIpeiqaelSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207686 314 RRILASLQEEDSSHRDLSPDSILIGEEISTA-ALVELPVDNIAAIVTSEGAANSHmvivaralgiptvvgvtelpvntLD 392
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELqEQRIDLKEQIKSIEKEIENLNGK-----------------------KE 864
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 491207686 393 DAEMIVDAYQGRVfvnppRRLRQRYKEIQKEDEQIAKDLKQYETKE 438
Cdd:TIGR02169 865 ELEEELEELEAAL-----RDLESRLGDLKKERDELEAQLRELERKI 905
|
|
| |
