|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11061 |
PRK11061 |
phosphoenolpyruvate--protein phosphotransferase; |
1-747 |
0e+00 |
|
phosphoenolpyruvate--protein phosphotransferase;
Pssm-ID: 182937 [Multi-domain] Cd Length: 748 Bit Score: 1530.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 1 MLTRLREIVEKVASAPRLNEALNILVTDICLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVALAFDEGIVGLVGR 80
Cdd:PRK11061 1 MLTRLREIVEKVASAPRLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAFDEGIVGLVGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 81 LAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAILSQSQVT 160
Cdd:PRK11061 81 LAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQRELRQFDESEESFLVTLATQLAAILSQSQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 161 ALFGQYRQTRIRALPAAPGVAIATGWQDATMPLMEQVYEASTLDTSLERERLTGALEEAANEFRRYSKRFAAGAQKETAA 240
Cdd:PRK11061 161 ALFGQYRQTRIRALPASPGVAIAEGWQDATQPLLEQVYPASTLDPALERERLTGALEEAANEFRRYSKRFAAGAQKETAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 241 IFDLYSHLLSDARLRRELFAEVDKGAVAEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFHLDDSVQGPNAWP 320
Cdd:PRK11061 241 IFDLYSHLLNDPRLRRELFAEVDKGSVAEWAVKQVIEKFAEQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQGPNAWP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 321 ERFILVADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLVVDGYRGELLVDPEPV 400
Cdd:PRK11061 321 ERFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGADIQPSLLHQRLLIVDGYRGELLVDPEPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 401 LIQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFMLQSGFPSEEEQV 480
Cdd:PRK11061 401 LLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFPSEEEQV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 481 AQYQGMLQMFNDKPVTLRTLDVGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVT 560
Cdd:PRK11061 481 AQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 561 SIDEVDEARRLIERAGREVEEMIGYAIPKPRIGIMLEVPSMVFMLPHLANRIDFISVGTNDLTQYILAVDRNNTRVASIY 640
Cdd:PRK11061 561 SIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLY 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 641 DSLHPAMLRALSMIAQEAEKHGLDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARVKYLLRHIDFEDAQTLARRSLE 720
Cdd:PRK11061 641 DSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAEAENLAQRSLE 720
|
730 740
....*....|....*....|....*..
gi 446880627 721 AQMATEVRHQVAAFMERRGMGGLIRGG 747
Cdd:PRK11061 721 AQLATEVRHQVAAFMERRGLGGLIRGG 747
|
|
| PtsA |
COG1080 |
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ... |
171-738 |
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: 576.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 171 IRALPAAPGVAIATGW--QDATMPLMEQVYEASTLDTslERERLTGALEEAANEFRRYSKRFAAGAQKETAAIFDLYSHL 248
Cdd:COG1080 1 LKGIAASPGIAIGKAFllREEDLEVPEYTISPEDVEA--EIARLEAALAKAREELEALREKAPEDLGEEEAAIFDAHLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 249 LSDARLRRELFAEVDKGAV-AEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFHL-DDSVQGPNAWPERFILV 326
Cdd:COG1080 79 LEDPELIEEVEELIREGRYnAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLlGVEAPDLSDLPEPVILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 327 ADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGA-DIQPSVLHRRTLVVDGYRGELLVDPEPVLIQEY 405
Cdd:COG1080 159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLgDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 406 QRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQG 485
Cdd:COG1080 239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 486 MLQMFNDKPVTLRTLDVGADKQLPYMPIS-EENPCLGWRGIRITLDQPEIFLIQVRAMLRAnAATGNLSILLPMVTSIDE 564
Cdd:COG1080 319 VAEAMGGRPVTIRTLDIGGDKPLPYLPLPkEENPFLGLRAIRLCLDRPELFRTQLRAILRA-SAHGNLRIMFPMISSVEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 565 VDEARRLIERAGREV-EEMIGYAiPKPRIGIMLEVPSMVFMLPHLANRIDFISVGTNDLTQYILAVDRNNTRVASIYDSL 643
Cdd:COG1080 398 LRQAKALLEEAKAELrAEGIPFD-EDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 644 HPAMLRALSMIAQEAEKHGLDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARVKYLLRHIDFEDAQTLARRSLEAQM 723
Cdd:COG1080 477 HPAVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALALDT 556
|
570
....*....|....*
gi 446880627 724 ATEVRHQVAAFMERR 738
Cdd:COG1080 557 AEEVRALLEEFLAEL 571
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
416-708 |
7.81e-141 |
|
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: 415.17 E-value: 7.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 416 SRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFNDKPV 495
Cdd:pfam02896 1 KAELGKLKDLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 496 TLRTLDVGADKQLPYMPISEE-NPCLGWRGIRITLDQPEIFLIQVRAMLRAnAATGNLSILLPMVTSIDEVDEARRLIER 574
Cdd:pfam02896 81 TVRTLDIGGDKELPYLEEPEEmNPFLGWRGIRIGLDRPELFRTQLRAILRA-SAFGNLRIMFPMVASVEELREAKAIIEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 575 AGREVEEMIGYAiPKPRIGIMLEVPSMVFMLPHLANRIDFISVGTNDLTQYILAVDRNNTRVASIYDSLHPAMLRALSMI 654
Cdd:pfam02896 160 VKEELDAEVGFD-KDIKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446880627 655 AQEAEKHGLDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARVKYLLRHIDF 708
Cdd:pfam02896 239 IRAAHRHGKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
171-728 |
4.04e-117 |
|
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: 364.11 E-value: 4.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 171 IRALPAAPGVAIATGW--QDATMPLMEQVYEASTLDTslERERLTGALEEAANEFRRYSKRFAAGAQKETAAIFDLYSHL 248
Cdd:TIGR01417 1 ISGIGVSPGIAIGKALllKKPDLVIDRKKISASQVDQ--EISRFLSARAKAKEDLETIKTKAGKTFGQEKAAIFEAHILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 249 LSDARLRRELFAEVDKGAV-AEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFHL-DDSVQGPNAWPERFILV 326
Cdd:TIGR01417 79 LEDPELTEEVIELIKKDHKnAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLlGVKISDLSEIQDEVILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 327 ADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMG-ADIQPSVLHRRTLVVDGYRGELLVDPEPVLIQEY 405
Cdd:TIGR01417 159 AEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGtKSVTSQVKNGDTVIIDGVKGIVIFNPSSETIDKY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 406 QRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQG 485
Cdd:TIGR01417 239 EAKQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 486 MLQMFNDKPVTLRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLIQVRAMLRAnAATGNLSILLPMVTSIDE 564
Cdd:TIGR01417 319 VLEAMESDAVIVRTLDIGGDKELPYLNFpKEENPFLGYRAIRLALEREEILRTQLRAILRA-SAYGKLRIMFPMVATVEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 565 VDEARRLIERAGREVEEMIGYAIPKPRIGIMLEVPSMVFMLPHLANRIDFISVGTNDLTQYILAVDRNNTRVASIYDSLH 644
Cdd:TIGR01417 398 IRAVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 645 PAMLRALSMIAQEAEKHGLDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARVKYLLRHIDFEDAQTLARRSLEAQMA 724
Cdd:TIGR01417 478 PAVLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTT 557
|
....
gi 446880627 725 TEVR 728
Cdd:TIGR01417 558 EEVH 561
|
|
| PRK11177 |
PRK11177 |
phosphoenolpyruvate-protein phosphotransferase PtsI; |
236-736 |
7.56e-111 |
|
phosphoenolpyruvate-protein phosphotransferase PtsI;
Pssm-ID: 183017 [Multi-domain] Cd Length: 575 Bit Score: 348.15 E-value: 7.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 236 KETAAIFDLYSHLLSDARLRRELFAEV-DKGAVAEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFH-LDDSV 313
Cdd:PRK11177 67 EEKEAIFEGHIMLLEDEELEQEIIALIkDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLLKNiLGLKI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 314 QGPNAWPERFILVADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGA-DIQPSVLHRRTLVVDGYRGE 392
Cdd:PRK11177 147 IDLSAIQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTgNITKQVKNGDYLILDAVNNQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 393 LLVDPEPVLIQEYQRL----ISEEIELSRLAeddvNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFM 468
Cdd:PRK11177 227 IYVNPTNEVIEELKAVqeqyASEKAELAKLK----DLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 469 LQSGFPSEEEQVAQYQGMLQMFNDKPVTLRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLIQVRAMLRAnA 547
Cdd:PRK11177 303 DRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLpKEENPFLGWRAIRIAMDRKEILHDQLRAILRA-S 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 548 ATGNLSILLPMVTSIDEVDEARRLIE------RA-GREVEEMIgyaipkpRIGIMLEVPSMVFMLPHLANRIDFISVGTN 620
Cdd:PRK11177 382 AFGKLRIMFPMIISVEEVRELKAEIEilkqelRDeGKAFDESI-------EIGVMVETPAAAVIARHLAKEVDFFSIGTN 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 621 DLTQYILAVDRNNTRVASIYDSLHPAMLRALSMIAQEAEKHGLDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARVK 700
Cdd:PRK11177 455 DLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIK 534
|
490 500 510
....*....|....*....|....*....|....*.
gi 446880627 701 YLLRHIDFEDAQTLARRSLEAQMATEVRHQVAAFME 736
Cdd:PRK11177 535 KIIRNTNFEDAKALAEQALAQPTADELMTLVNKFIE 570
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
1-182 |
3.01e-66 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 217.46 E-value: 3.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 1 MLTRLREIVEKVASAPRLNEALNILVTDICLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVALAFDEGIVGLVGR 80
Cdd:COG3605 2 MLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVGKVRLPLGEGLVGLVAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 81 LAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAILSQSQVT 160
Cdd:COG3605 82 RGEPLNLADAASHPRFKYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAELL 161
|
170 180
....*....|....*....|....*.
gi 446880627 161 ALFGQYRQTRIRAL----PAAPGVAI 182
Cdd:COG3605 162 GELRAALAELSLAReeerEAAVEAAI 187
|
|
| PEP_synth |
TIGR01418 |
phosphoenolpyruvate synthase; Also called pyruvate,water dikinase and PEP synthase. The member ... |
342-699 |
2.41e-45 |
|
phosphoenolpyruvate synthase; Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273612 [Multi-domain] Cd Length: 786 Bit Score: 174.15 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 342 RLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDGYRGELLVdpepvliqEYQRLISEEIElsrlae 420
Cdd:TIGR01418 403 RASAIVTNEGGMTCHAAIVARELGIPAVVGTGDATKTLKDGMEVtVDCAEGDTGY--------VYAGKLEHEVK------ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 421 dDVNLPAQLKSGerIKVMLNAGlSPEHEEKLGSR-IDGIGLYRTEipFMLQSG----------FPSEEEQVAQ------- 482
Cdd:TIGR01418 469 -EVELSNMPVTA--TKIYMNVG-NPEVAFRFAALpNDGVGLARIE--FIILNWigkhplalidDDDLESVEKNeieelma 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 483 -----------YQGMLQM---FNDKPVTLRTLDVGAD--KQL----PYMPIsEENPCLGWRGIRITLDQ--PEIFLIQVR 540
Cdd:TIGR01418 543 gnprdffvdklAEGIAKVaaaFYPKPVIVRTSDFKSNeyRNLiggeEYEPD-EENPMLGWRGASRYYSEsyEEAFRLECR 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 541 AMLRANAATG--NLSILLPMVTSIDEVDEARRLIERAGREVEEmigyaiPKPRIGIMLEVPSMVFMLPHLANRIDFISVG 618
Cdd:TIGR01418 622 AIKRVREEMGltNVEVMIPFVRTPEEGKRALEIMAEEGLRRGK------NGLEVYVMCEVPSNALLADEFAKEFDGFSIG 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 619 TNDLTQYILAVDRNNTRVASIYDSLHPAMLRALSMIAQEAEKHGLDLRLCGEMAGD-PMCVAILIGLGYRHLSMNGRSVA 697
Cdd:TIGR01418 696 SNDLTQLTLGVDRDSGLVAHLFDERNPAVLRLIEMAIKAAKEHGKKVGICGQAPSDyPEVVEFLVEEGIDSISLNPDAVL 775
|
..
gi 446880627 698 RV 699
Cdd:TIGR01418 776 RT 777
|
|
| PRK06464 |
PRK06464 |
phosphoenolpyruvate synthase; Validated |
342-721 |
2.38e-43 |
|
phosphoenolpyruvate synthase; Validated
Pssm-ID: 235809 [Multi-domain] Cd Length: 795 Bit Score: 168.00 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 342 RLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV----VDGYRGelLVdpepvliqeYQRLISEEIELSR 417
Cdd:PRK06464 404 RASAIVTNRGGRTCHAAIIARELGIPAVVGTGNATEVLKDGQEVtvscAEGDTG--YV---------YEGLLEFEVEEVS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 418 LAEddvnLPAQlksgeRIKVMLNAGlSPEHEEKLgSRI--DGIGLYRTEipFM--------------------------- 468
Cdd:PRK06464 473 LEE----MPET-----PTKIMMNVG-NPERAFDF-AALpnDGVGLARLE--FIinnmigvhplallefdqqdadlkaeie 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 469 -LQSGFPSEEE----QVAQYQGML-QMFNDKPVTLRTLD---------VGADKqlpYMPIsEENPCLGWRGIRITLDQP- 532
Cdd:PRK06464 540 eLTAGYASPEEfyvdKLAEGIATVaAAFYPKPVIVRLSDfksneyanlIGGER---YEPE-EENPMLGFRGASRYLSESf 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 533 -EIFLIQVRAMLRANAATG--NLSILLPMVTSIDEVDEARRLIERAGREVEEmigyaiPKPRIGIMLEVPSMVFMLPHLA 609
Cdd:PRK06464 616 rEAFALECEAIKRVREEMGltNVEVMIPFVRTVEEAEKVIELLAENGLKRGE------NGLKVIMMCEIPSNALLAEEFL 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 610 NRIDFISVGTNDLTQYILAVDRNNTRVASIYDSLHPAMLRALSMIAQEAEKHGLDLRLCGEMAGD-PMCVAILIGLGYRH 688
Cdd:PRK06464 690 EYFDGFSIGSNDLTQLTLGLDRDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQAPSDhPDFAEWLVEEGIDS 769
|
410 420 430
....*....|....*....|....*....|...
gi 446880627 689 LSMNGRSVARVKYLLrhidfedAQTLARRSLEA 721
Cdd:PRK06464 770 ISLNPDAVVDTWLAV-------AEVEKKIILEA 795
|
|
| PEP-utilizers_N |
pfam05524 |
PEP-utilizing enzyme, N-terminal; |
172-294 |
7.20e-23 |
|
PEP-utilizing enzyme, N-terminal;
Pssm-ID: 461671 [Multi-domain] Cd Length: 125 Bit Score: 94.60 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 172 RALPAAPGVAIATGWQ-DATMPLMEQVYEASTLDTSLERERLTGALEEAANEFRRYSKRFAAGAQKETAAIFDLYSHLLS 250
Cdd:pfam05524 1 KGIGASPGIAIGKAVVlEEPELEVPDEREVPADDVEAEIARLEAALEAAREELEALAERAAGELGEEEAAIFEAHLMMLE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446880627 251 DARLRRELFAEVDKGAV-AEWAVKKIIEKFAEQFAALTDNYLKER 294
Cdd:pfam05524 81 DPELLEEVEELIREGGLnAEAAVKEVVDEFAAMFEAMDDPYLRER 125
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
17-158 |
1.08e-21 |
|
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: 92.06 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 17 RLNEALNILVTDICLAMDTEVCSVYLADHD-RRCYYLMATRGLKKPRGRtVALAFDEGIVGLVGRLAEPINLADAQKHPS 95
Cdd:smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVDENdRGELVLVAADGLTLPTLG-IRFPLDEGLAGRVAETGRPLNIPDVEADPL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446880627 96 FKYIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQREL-RQYDESEESFLVTLATQMAAILSQSQ 158
Cdd:smart00065 80 FAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQ 143
|
|
| PRK11377 |
PRK11377 |
dihydroxyacetone kinase subunit M; Provisional |
163-396 |
1.39e-21 |
|
dihydroxyacetone kinase subunit M; Provisional
Pssm-ID: 183108 [Multi-domain] Cd Length: 473 Bit Score: 98.67 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 163 FGQYRQTRIRALPAAPGVAIATGWQdaTMPLMEQVYEASTLDTSLERERLTGALEEAANEFRRYSKRFAAGAQKETAAIF 242
Cdd:PRK11377 239 FGETEEVAPPTLRPVPSPVSGKAFY--YQPVLCTVQAKSTLTVEEEQERLRQAIDFTLLDLMTLTAKAEASGLDDIAAIF 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 243 DLYSHLLSDArlrrELFAEVDK-----GAVAEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFHLddsvQGPN 317
Cdd:PRK11377 317 SGHHTLLDDP----ELLAAASErlqheHCTAEYAWQQVLKELSQQYQQLDDEYLQARYIDVDDLLHRTLVHL----TQTK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 318 AWPERF----ILVADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGAD-----IQPSvlhrRTLVVDG 388
Cdd:PRK11377 389 EELPQFnsptILLAENIYPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQGeklyaIQPE----ETLTLDV 464
|
....*...
gi 446880627 389 YRGELLVD 396
Cdd:PRK11377 465 KTQRLNRQ 472
|
|
| PEP-utilizers |
pfam00391 |
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain ... |
320-391 |
8.40e-16 |
|
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: 72.44 E-value: 8.40e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446880627 320 PERFILVADELSATTLAELpqDRLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHR-RTLVVDGYRG 391
Cdd:pfam00391 3 PEGVILVAPDTTPSDTAGL--DKAAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEgDLVTVDGSTG 73
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
18-154 |
1.26e-14 |
|
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: 71.36 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 18 LNEALNILVTDICLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTValafdEGIVGLVGRLAEPINLADAQKHPSF- 96
Cdd:pfam01590 2 LEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIP-----PGTGVTVLRTGRPLVVPDAAGDPRFl 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446880627 97 KYIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQRElRQYDESEESFLVTLATQMAAIL 154
Cdd:pfam01590 77 DPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPR-PPFTEEELELLEVLADQVAIAL 133
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2-467 |
7.42e-13 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 72.15 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 2 LTRLREIVEKVASAPRLNEALNILVTDICLAMDTEVCSVYLADHDRRCYYLMATRGLkkPRGRTVALAFDEGIVGLVGRL 81
Cdd:COG2203 192 LALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGL--PEEELGRLPLGEGLAGRALRT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 82 AEPINLADAQKHPSFK--YIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAILSQSQV 159
Cdd:COG2203 270 GEPVVVNDASTDPRFApsLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 160 TALFGQYRQTRIRALpaapgVAIATGWQDATMPLMEQVYEASTLDTSLERERLTGALEEAANEFRRYSKRFAAGAQKETA 239
Cdd:COG2203 350 YEALEAALAALLQEL-----ALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 240 AIFDLYSHLLSDARLRRELFAEVDKGAVAEWAVKKIIEKFAEQFAALTDNYLKERAGDLRTLGQRLLFHLDDSVQGPNAW 319
Cdd:COG2203 425 DLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 320 PERFILVADELSATTLAELPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLVVDGYRGELLVDPEP 399
Cdd:COG2203 505 VLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALI 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446880627 400 VLIQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPF 467
Cdd:COG2203 585 LALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALAS 652
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
18-154 |
6.79e-12 |
|
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: 63.64 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 18 LNEALNIlVTDICLAMD-TEVCSVYLADHDRRcyyLMATRGLKKPRGRTVALAFDEGIVGLVGRLAEPINLADAQKHPSF 96
Cdd:pfam13185 4 LEELLDA-VLEAAVELGaSAVGFILLVDDDGR---LAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446880627 97 KYIPSVkEERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAIL 154
Cdd:pfam13185 80 KGLPAG-HAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
|
|
| PykA2 |
COG3848 |
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms]; |
324-391 |
1.25e-05 |
|
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
Pssm-ID: 443058 Cd Length: 321 Bit Score: 47.97 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446880627 324 ILVADELSATTLAELpqDRLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDGYRG 391
Cdd:COG3848 245 ILVVPSTDAEFVPAI--EKAAGIITEEGGLTSHAAIVGLELGIPVIVGAEGATEILKDGQVVtVDAERG 311
|
|
| GAF_3 |
pfam13492 |
GAF domain; |
22-151 |
6.71e-05 |
|
GAF domain;
Pssm-ID: 433253 [Multi-domain] Cd Length: 129 Bit Score: 43.13 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 22 LNILVTDICLAMDTEVCSVYLADHDRRcyylmatrglkkprgRTVALAFDEGIVGLVGRLAEPINLAD-AQKHPSFKYIP 100
Cdd:pfam13492 6 LEALLKLLVRLLGAERAAVYLLDEDGN---------------KLQVAAGYDGEPDPSESLDADSPLARrALSSGEPISGL 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446880627 101 SVKEE---RFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMA 151
Cdd:pfam13492 71 GSAGEdglPDGPALVVPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIA 124
|
|
| PpsA |
COG0574 |
Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and ... |
324-392 |
9.66e-05 |
|
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: 45.59 E-value: 9.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446880627 324 ILVADELSattlaelPQD-----RLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDGYRGE 392
Cdd:COG0574 386 ILVRDETD-------PDDvpgmkAAAGIVTERGGMTSHAAIVARELGIPAVVGCGDATRVLKDGDEItVDGTTGE 453
|
|
| FhlA |
COG3604 |
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ... |
104-154 |
1.59e-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: 44.45 E-value: 1.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446880627 104 EERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAIL 154
Cdd:COG3604 70 ARERQLFLGVPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAI 120
|
|
| PRK05878 |
PRK05878 |
pyruvate phosphate dikinase; Provisional |
344-392 |
1.53e-03 |
|
pyruvate phosphate dikinase; Provisional
Pssm-ID: 235635 [Multi-domain] Cd Length: 530 Bit Score: 41.65 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446880627 344 AGVVVRDGAANSHAAIMVRALGIPTVM--GADIQPSvLHRRTLVVDGYRGE 392
Cdd:PRK05878 401 QGIVTEVGGATSHAAVVSRELGRVAVVgcGAGVAAA-LAGKEITVDGYEGE 450
|
|
| CitE |
COG2301 |
Citrate lyase beta subunit [Carbohydrate transport and metabolism]; |
523-664 |
4.12e-03 |
|
Citrate lyase beta subunit [Carbohydrate transport and metabolism];
Pssm-ID: 441876 Cd Length: 288 Bit Score: 39.75 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 523 RGIRI-TLDQPEiFLIQVRAMLRANAATgnlsILLPMVTSIDEVDEARRLIERAGREVEEMigyaipkpRIGIMLEVPSM 601
Cdd:COG2301 65 VFVRInALDTPW-GLDDLAALVGAGLDG----IVLPKVESAEDVRALAALLTELEAEGGSI--------PLMALIETARG 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446880627 602 VFMLPHLA---NRIDFISVGTNDLTqyilavdrNNTRVASIYDSlhPAMLRALSMIAQEAEKHGLD 664
Cdd:COG2301 132 LLNAAEIAaasPRVEALVFGAEDLA--------ADLGARRTRDG--DELLYARSRIVLAARAAGLA 187
|
|
| MsrC |
COG1956 |
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ... |
69-155 |
5.63e-03 |
|
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];
Pssm-ID: 441559 [Multi-domain] Cd Length: 156 Bit Score: 38.27 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446880627 69 AFDEGIVGLVGRLAEPINLADAQKHPsfKYI---PSVKEErfrafLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVT 145
Cdd:COG1956 73 PFGKGVCGTAAAEGETQLVPDVHAFP--GHIacdSASRSE-----IVVPIFKDGEVIGVLDIDSPTPGRFDEEDQAGLEA 145
|
90
....*....|
gi 446880627 146 LATQMAAILS 155
Cdd:COG1956 146 LAALLAEALD 155
|
|
| |
