|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11061 |
PRK11061 |
phosphoenolpyruvate--protein phosphotransferase; |
1-748 |
0e+00 |
|
phosphoenolpyruvate--protein phosphotransferase;
Pssm-ID: 182937 [Multi-domain] Cd Length: 748 Bit Score: 1528.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 1 MLTRLREIVEKVASAPRLNEALDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLKKPRGRTITLAFDEGIVGLVGR 80
Cdd:PRK11061 1 MLTRLREIVEKVASAPRLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAFDEGIVGLVGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 81 LAEPINLADAQKHPSFKYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAILSQSQLA 160
Cdd:PRK11061 81 LAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQRELRQFDESEESFLVTLATQLAAILSQSQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 161 ALFGQYRQTRIRALPASPGVAIAEGWMDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETAA 240
Cdd:PRK11061 161 ALFGQYRQTRIRALPASPGVAIAEGWQDATQPLLEQVYPASTLDPALERERLTGALEEAANEFRRYSKRFAAGAQKETAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 241 IFDLYSHLLTDARLRRELFDEVDKGSVAEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHLDDTIQSPNTWP 320
Cdd:PRK11061 241 IFDLYSHLLNDPRLRRELFAEVDKGSVAEWAVKQVIEKFAEQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQGPNAWP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 321 ERFVLVADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLVVDGYRGELLVDPETV 400
Cdd:PRK11061 321 ERFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGADIQPSLLHQRLLIVDGYRGELLVDPEPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 401 LLQEYQRLITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQV 480
Cdd:PRK11061 401 LLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFPSEEEQV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 481 AQYQGMLQMFNEKPVTLRTLDVGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLVQVRAMLRANAATGNLSILLPMIT 560
Cdd:PRK11061 481 AQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 561 SIDEIDEARRLIDRAGREVEEVLGYELPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLY 640
Cdd:PRK11061 561 SIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLY 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 641 DSLHPAMLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLE 720
Cdd:PRK11061 641 DSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAEAENLAQRSLE 720
|
730 740
....*....|....*....|....*...
gi 1445011758 721 AQLATEVRHQVASFMERRGMGGLIRGGR 748
Cdd:PRK11061 721 AQLATEVRHQVAAFMERRGLGGLIRGGK 748
|
|
| 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: 587.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 171 IRALPASPGVAIAEGWM--DSTLPLMEQVSEASTLDTilERERLTAALEEASNEFRRYSKRFAAGAQKETAAIFDLYSHL 248
Cdd:COG1080 1 LKGIAASPGIAIGKAFLlrEEDLEVPEYTISPEDVEA--EIARLEAALAKAREELEALREKAPEDLGEEEAAIFDAHLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 249 LTDARLRRELFDEVDKGSV-AEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHL-DDTIQSPNTWPERFVLV 326
Cdd:COG1080 79 LEDPELIEEVEELIREGRYnAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLlGVEAPDLSDLPEPVILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 327 ADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGA-DIQPSVLHRRTLVVDGYRGELLVDPETVLLQEY 405
Cdd:COG1080 159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLgDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 406 QRLITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQ--QLGGriDGIGLYRTEIPFMLQSGFPSEEEQVAQY 483
Cdd:COG1080 239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAalENGA--EGVGLFRTEFLFMDRDDLPTEEEQFEAY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 484 QGMLQMFNEKPVTLRTLDVGADKQLPYMPIS-EENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSI 562
Cdd:COG1080 317 RAVAEAMGGRPVTIRTLDIGGDKPLPYLPLPkEENPFLGLRAIRLCLDRPELFRTQLRAILRA-SAHGNLRIMFPMISSV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 563 DEIDEARRLIDRAGREVEEVlGYEL-PKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYD 641
Cdd:COG1080 396 EELRQAKALLEEAKAELRAE-GIPFdEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 642 SLHPAMLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLEA 721
Cdd:COG1080 475 PLHPAVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALAL 554
|
570
....*....|....*..
gi 1445011758 722 QLATEVRHQVASFMERR 738
Cdd:COG1080 555 DTAEEVRALLEEFLAEL 571
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
417-706 |
5.15e-134 |
|
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: 397.83 E-value: 5.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 417 RLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFNEKPVT 496
Cdd:pfam02896 2 AELGKLKDLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 497 LRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSIDEIDEARRLIDRA 575
Cdd:pfam02896 82 VRTLDIGGDKELPYLEEpEEMNPFLGWRGIRIGLDRPELFRTQLRAILRA-SAFGNLRIMFPMVASVEELREAKAIIEEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 576 GREVEEVLGYElPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYDSLHPAMLRALNHIA 655
Cdd:pfam02896 161 KEELDAEVGFD-KDIKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1445011758 656 KEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHI 706
Cdd:pfam02896 240 RAAHRHGKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQI 290
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
171-728 |
1.81e-119 |
|
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: 370.28 E-value: 1.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 171 IRALPASPGVAIAEGWMDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETAAIFDLYSHLLT 250
Cdd:TIGR01417 1 ISGIGVSPGIAIGKALLLKKPDLVIDRKKISASQVDQEISRFLSARAKAKEDLETIKTKAGKTFGQEKAAIFEAHILILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 251 DARLRRELFDEVDKGSV-AEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHL-DDTIQSPNTWPERFVLVAD 328
Cdd:TIGR01417 81 DPELTEEVIELIKKDHKnAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLlGVKISDLSEIQDEVILVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 329 ELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMG-ADIQPSVLHRRTLVVDGYRGELLVDPETVLLQEYQR 407
Cdd:TIGR01417 161 DLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGtKSVTSQVKNGDTVIIDGVKGIVIFNPSSETIDKYEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 408 LITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGML 487
Cdd:TIGR01417 241 KQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 488 QMFNEKPVTLRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSIDEID 566
Cdd:TIGR01417 321 EAMESDAVIVRTLDIGGDKELPYLNFpKEENPFLGYRAIRLALEREEILRTQLRAILRA-SAYGKLRIMFPMVATVEEIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 567 EARRLIDRAGREVEEVLGYELPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYDSLHPA 646
Cdd:TIGR01417 400 AVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 647 MLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLEAQLATE 726
Cdd:TIGR01417 480 VLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTTEE 559
|
..
gi 1445011758 727 VR 728
Cdd:TIGR01417 560 VH 561
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
17-163 |
2.81e-22 |
|
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: 93.60 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 17 RLNEALDILVTDICLAMDTEVCSVYLADHDRRCFY-LMATRGLKKPRGRtITLAFDEGIVGLVGRLAEPINLADAQKHPS 95
Cdd:smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPTLG-IRFPLDEGLAGRVAETGRPLNIPDVEADPL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1445011758 96 FKYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREH-RQYDESEESFLVTLATQMAAILSQSQLAALF 163
Cdd:smart00065 80 FAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQLYEEL 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11061 |
PRK11061 |
phosphoenolpyruvate--protein phosphotransferase; |
1-748 |
0e+00 |
|
phosphoenolpyruvate--protein phosphotransferase;
Pssm-ID: 182937 [Multi-domain] Cd Length: 748 Bit Score: 1528.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 1 MLTRLREIVEKVASAPRLNEALDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLKKPRGRTITLAFDEGIVGLVGR 80
Cdd:PRK11061 1 MLTRLREIVEKVASAPRLNEALDILVTETCLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAFDEGIVGLVGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 81 LAEPINLADAQKHPSFKYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAILSQSQLA 160
Cdd:PRK11061 81 LAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIYRRQLLGVLVVQQRELRQFDESEESFLVTLATQLAAILSQSQLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 161 ALFGQYRQTRIRALPASPGVAIAEGWMDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETAA 240
Cdd:PRK11061 161 ALFGQYRQTRIRALPASPGVAIAEGWQDATQPLLEQVYPASTLDPALERERLTGALEEAANEFRRYSKRFAAGAQKETAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 241 IFDLYSHLLTDARLRRELFDEVDKGSVAEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHLDDTIQSPNTWP 320
Cdd:PRK11061 241 IFDLYSHLLNDPRLRRELFAEVDKGSVAEWAVKQVIEKFAEQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQGPNAWP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 321 ERFVLVADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLVVDGYRGELLVDPETV 400
Cdd:PRK11061 321 ERFILVADELTATLLAELPQDRLAGVVVRDGAANSHAAILVRALGIPTVMGADIQPSLLHQRLLIVDGYRGELLVDPEPV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 401 LLQEYQRLITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQV 480
Cdd:PRK11061 401 LLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFPSEEEQV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 481 AQYQGMLQMFNEKPVTLRTLDVGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLVQVRAMLRANAATGNLSILLPMIT 560
Cdd:PRK11061 481 AQYQGMLQMFPDKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 561 SIDEIDEARRLIDRAGREVEEVLGYELPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLY 640
Cdd:PRK11061 561 SIDEVDEARRLIDRAGREVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLY 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 641 DSLHPAMLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLE 720
Cdd:PRK11061 641 DSLHPAMLRALKMIADEAEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAEAENLAQRSLE 720
|
730 740
....*....|....*....|....*...
gi 1445011758 721 AQLATEVRHQVASFMERRGMGGLIRGGR 748
Cdd:PRK11061 721 AQLATEVRHQVAAFMERRGLGGLIRGGK 748
|
|
| 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: 587.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 171 IRALPASPGVAIAEGWM--DSTLPLMEQVSEASTLDTilERERLTAALEEASNEFRRYSKRFAAGAQKETAAIFDLYSHL 248
Cdd:COG1080 1 LKGIAASPGIAIGKAFLlrEEDLEVPEYTISPEDVEA--EIARLEAALAKAREELEALREKAPEDLGEEEAAIFDAHLLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 249 LTDARLRRELFDEVDKGSV-AEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHL-DDTIQSPNTWPERFVLV 326
Cdd:COG1080 79 LEDPELIEEVEELIREGRYnAEWALKEVIEELAAQFEALDDEYLRERAADIRDVGRRVLRNLlGVEAPDLSDLPEPVILV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 327 ADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGA-DIQPSVLHRRTLVVDGYRGELLVDPETVLLQEY 405
Cdd:COG1080 159 AHDLTPSDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLgDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 406 QRLITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQ--QLGGriDGIGLYRTEIPFMLQSGFPSEEEQVAQY 483
Cdd:COG1080 239 RERQAEYAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAalENGA--EGVGLFRTEFLFMDRDDLPTEEEQFEAY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 484 QGMLQMFNEKPVTLRTLDVGADKQLPYMPIS-EENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSI 562
Cdd:COG1080 317 RAVAEAMGGRPVTIRTLDIGGDKPLPYLPLPkEENPFLGLRAIRLCLDRPELFRTQLRAILRA-SAHGNLRIMFPMISSV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 563 DEIDEARRLIDRAGREVEEVlGYEL-PKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYD 641
Cdd:COG1080 396 EELRQAKALLEEAKAELRAE-GIPFdEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 642 SLHPAMLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLEA 721
Cdd:COG1080 475 PLHPAVLRLIKMVIDAAHKAGKPVGVCGEMAGDPLATPLLLGLGLDELSMSPSSIPAVKAIIRRLDLAEARALAEKALAL 554
|
570
....*....|....*..
gi 1445011758 722 QLATEVRHQVASFMERR 738
Cdd:COG1080 555 DTAEEVRALLEEFLAEL 571
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
417-706 |
5.15e-134 |
|
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: 397.83 E-value: 5.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 417 RLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFNEKPVT 496
Cdd:pfam02896 2 AELGKLKDLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 497 LRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSIDEIDEARRLIDRA 575
Cdd:pfam02896 82 VRTLDIGGDKELPYLEEpEEMNPFLGWRGIRIGLDRPELFRTQLRAILRA-SAFGNLRIMFPMVASVEELREAKAIIEEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 576 GREVEEVLGYElPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYDSLHPAMLRALNHIA 655
Cdd:pfam02896 161 KEELDAEVGFD-KDIKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1445011758 656 KEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHI 706
Cdd:pfam02896 240 RAAHRHGKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQI 290
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
171-728 |
1.81e-119 |
|
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: 370.28 E-value: 1.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 171 IRALPASPGVAIAEGWMDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETAAIFDLYSHLLT 250
Cdd:TIGR01417 1 ISGIGVSPGIAIGKALLLKKPDLVIDRKKISASQVDQEISRFLSARAKAKEDLETIKTKAGKTFGQEKAAIFEAHILILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 251 DARLRRELFDEVDKGSV-AEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHL-DDTIQSPNTWPERFVLVAD 328
Cdd:TIGR01417 81 DPELTEEVIELIKKDHKnAEFAAHEVFEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLlGVKISDLSEIQDEVILVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 329 ELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMG-ADIQPSVLHRRTLVVDGYRGELLVDPETVLLQEYQR 407
Cdd:TIGR01417 161 DLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGtKSVTSQVKNGDTVIIDGVKGIVIFNPSSETIDKYEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 408 LITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGML 487
Cdd:TIGR01417 241 KQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPTEEEQFAAYKTVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 488 QMFNEKPVTLRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAATGNLSILLPMITSIDEID 566
Cdd:TIGR01417 321 EAMESDAVIVRTLDIGGDKELPYLNFpKEENPFLGYRAIRLALEREEILRTQLRAILRA-SAYGKLRIMFPMVATVEEIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 567 EARRLIDRAGREVEEVLGYELPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYDSLHPA 646
Cdd:TIGR01417 400 AVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDLISNLYQPYNPA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 647 MLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISLEEAQLLAQRSLEAQLATE 726
Cdd:TIGR01417 480 VLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLAEKALAQPTTEE 559
|
..
gi 1445011758 727 VR 728
Cdd:TIGR01417 560 VH 561
|
|
| PRK11177 |
PRK11177 |
phosphoenolpyruvate-protein phosphotransferase PtsI; |
171-736 |
1.28e-115 |
|
phosphoenolpyruvate-protein phosphotransferase PtsI;
Pssm-ID: 183017 [Multi-domain] Cd Length: 575 Bit Score: 360.48 E-value: 1.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 171 IRALPASPGVAIAEGwmdstLPLMEQvseastlDTILERERLTAALEEASNEfRRYSKRFAAGAQ-------------KE 237
Cdd:PRK11177 2 ISGILASPGIAFGKA-----LLLKED-------EIVINRKKISADQVDQEVE-RFLSGRAKASAQleaiktkagetfgEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 238 TAAIFDLYSHLLTDARLRRELFDEV-DKGSVAEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFH-LDDTIQS 315
Cdd:PRK11177 69 KEAIFEGHIMLLEDEELEQEIIALIkDKHMTADAAAHSVIEGQAKALEELDDEYLKERAADVRDIGKRLLKNiLGLKIID 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 316 PNTWPERFVLVADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGA-DIQPSVLHRRTLVVDGYRGELL 394
Cdd:PRK11177 149 LSAIQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTgNITKQVKNGDYLILDAVNNQIY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 395 VDPETVLLQEYQRL----ITEENELTRLVeddvDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPFMLQ 470
Cdd:PRK11177 229 VNPTNEVIEELKAVqeqyASEKAELAKLK----DLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 471 SGFPSEEEQVAQYQGMLQMFNEKPVTLRTLDVGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLVQVRAMLRAnAAT 549
Cdd:PRK11177 305 DALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLpKEENPFLGWRAIRIAMDRKEILHDQLRAILRA-SAF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 550 GNLSILLPMITSIDEIDEARRLIDRAGREV-EEVLGYElPKPRIGVMVEVPSMVFMLGHLASRVDFISVGTNDLTQYLLA 628
Cdd:PRK11177 384 GKLRIMFPMIISVEEVRELKAEIEILKQELrDEGKAFD-ESIEIGVMVETPAAAVIARHLAKEVDFFSIGTNDLTQYTLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 629 VDRNNTRVASLYDSLHPAMLRALNHIAKEAERNGIDLCLCGEMAGDPMCVALLVGMGYRHLSMNGRSVARVKYLLRHISL 708
Cdd:PRK11177 463 VDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNF 542
|
570 580
....*....|....*....|....*...
gi 1445011758 709 EEAQLLAQRSLEAQLATEVRHQVASFME 736
Cdd:PRK11177 543 EDAKALAEQALAQPTADELMTLVNKFIE 570
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
1-182 |
4.10e-67 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 219.77 E-value: 4.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 1 MLTRLREIVEKVASAPRLNEALDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLKKPRGRTITLAFDEGIVGLVGR 80
Cdd:COG3605 2 MLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAVGKVRLPLGEGLVGLVAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 81 LAEPINLADAQKHPSFKYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAILSQSQLA 160
Cdd:COG3605 82 RGEPLNLADAASHPRFKYFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAELL 161
|
170 180
....*....|....*....|....*.
gi 1445011758 161 ALFGQYRQTRIRAL----PASPGVAI 182
Cdd:COG3605 162 GELRAALAELSLAReeerEAAVEAAI 187
|
|
| PEP_synth |
TIGR01418 |
phosphoenolpyruvate synthase; Also called pyruvate,water dikinase and PEP synthase. The member ... |
345-699 |
8.68e-43 |
|
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: 166.45 E-value: 8.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 345 GVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDG--------YRGELLVDPETVLLQEYQRLITEenel 415
Cdd:TIGR01418 406 AIVTNEGGMTCHAAIVARELGIPAVVGTGDATKTLKDGMEVtVDCaegdtgyvYAGKLEHEVKEVELSNMPVTATK---- 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 416 trlveddvdspaalksgervqVMLNAGLSPEHEQQLGGRIDGIGLYRTEipFMLQSG----------FPSEEEQVAQ--- 482
Cdd:TIGR01418 482 ---------------------IYMNVGNPEVAFRFAALPNDGVGLARIE--FIILNWigkhplalidDDDLESVEKNeie 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 483 ---------------YQGMLQM---FNEKPVTLRTLDVGAD--KQL----PYMPIsEENPCLGWRGIRITLDQ--PEIFL 536
Cdd:TIGR01418 539 elmagnprdffvdklAEGIAKVaaaFYPKPVIVRTSDFKSNeyRNLiggeEYEPD-EENPMLGWRGASRYYSEsyEEAFR 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 537 VQVRAMLRANAATG--NLSILLPMITSIDEIDEARRLIDRAGREVEEVlGYElpkprIGVMVEVPSMVFMLGHLASRVDF 614
Cdd:TIGR01418 618 LECRAIKRVREEMGltNVEVMIPFVRTPEEGKRALEIMAEEGLRRGKN-GLE-----VYVMCEVPSNALLADEFAKEFDG 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 615 ISVGTNDLTQYLLAVDRNNTRVASLYDSLHPAMLRALNHIAKEAERNGIDLCLCGEMAGD-PMCVALLVGMGYRHLSMNG 693
Cdd:TIGR01418 692 FSIGSNDLTQLTLGVDRDSGLVAHLFDERNPAVLRLIEMAIKAAKEHGKKVGICGQAPSDyPEVVEFLVEEGIDSISLNP 771
|
....*.
gi 1445011758 694 RSVARV 699
Cdd:TIGR01418 772 DAVLRT 777
|
|
| PRK06464 |
PRK06464 |
phosphoenolpyruvate synthase; Validated |
355-717 |
2.37e-40 |
|
phosphoenolpyruvate synthase; Validated
Pssm-ID: 235809 [Multi-domain] Cd Length: 795 Bit Score: 159.14 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 355 SHAAIMVRALGIPTVMGADIQPSVLHRRTLV----VDG-----YRGELLVDPETVLLQEYQRLITEeneltrlveddvds 425
Cdd:PRK06464 417 CHAAIIARELGIPAVVGTGNATEVLKDGQEVtvscAEGdtgyvYEGLLEFEVEEVSLEEMPETPTK-------------- 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 426 paalksgervqVMLNAGlSPEHEQ---QLGGriDGIGLYRTEipFM----------------------------LQSGFP 474
Cdd:PRK06464 483 -----------IMMNVG-NPERAFdfaALPN--DGVGLARLE--FIinnmigvhplallefdqqdadlkaeieeLTAGYA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 475 SEEE----QVAQYQGML-QMFNEKPVTLRTLD---------VGADKqlpYMPIsEENPCLGWRGIRITLDQP--EIFLVQ 538
Cdd:PRK06464 547 SPEEfyvdKLAEGIATVaAAFYPKPVIVRLSDfksneyanlIGGER---YEPE-EENPMLGFRGASRYLSESfrEAFALE 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 539 VRAMLRANAATG--NLSILLPMITSIDEIDEARRLIDRAGREVEEVlgyelpKPRIGVMVEVPSMVFMLGHLASRVDFIS 616
Cdd:PRK06464 623 CEAIKRVREEMGltNVEVMIPFVRTVEEAEKVIELLAENGLKRGEN------GLKVIMMCEIPSNALLAEEFLEYFDGFS 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 617 VGTNDLTQYLLAVDRNNTRVASLYDSLHPAMLRALNHIAKEAERNGIDLCLCGEMAGD-PMCVALLVGMGYRHLSMNGRS 695
Cdd:PRK06464 697 IGSNDLTQLTLGLDRDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICGQAPSDhPDFAEWLVEEGIDSISLNPDA 776
|
410 420
....*....|....*....|..
gi 1445011758 696 VARVKYLLRHIsleEAQLLAQR 717
Cdd:PRK06464 777 VVDTWLAVAEV---EKKIILEA 795
|
|
| PEP-utilizers_N |
pfam05524 |
PEP-utilizing enzyme, N-terminal; |
172-294 |
3.92e-24 |
|
PEP-utilizing enzyme, N-terminal;
Pssm-ID: 461671 [Multi-domain] Cd Length: 125 Bit Score: 98.07 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 172 RALPASPGVAIAEGW-MDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETAAIFDLYSHLLT 250
Cdd:pfam05524 1 KGIGASPGIAIGKAVvLEEPELEVPDEREVPADDVEAEIARLEAALEAAREELEALAERAAGELGEEEAAIFEAHLMMLE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1445011758 251 DARLRRELFDEVDKGSV-AEWAVKKVIEKFAEQFASLSDSYLKER 294
Cdd:pfam05524 81 DPELLEEVEELIREGGLnAEAAVKEVVDEFAAMFEAMDDPYLRER 125
|
|
| PRK11377 |
PRK11377 |
dihydroxyacetone kinase subunit M; Provisional |
151-396 |
3.92e-23 |
|
dihydroxyacetone kinase subunit M; Provisional
Pssm-ID: 183108 [Multi-domain] Cd Length: 473 Bit Score: 103.29 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 151 AAILSQSQLAAL-FGQYRQTRIRALPASPGVAIAEGWMdsTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKR 229
Cdd:PRK11377 226 EALIAFRQLAEDnFGETEEVAPPTLRPVPSPVSGKAFY--YQPVLCTVQAKSTLTVEEEQERLRQAIDFTLLDLMTLTAK 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 230 FAAGAQKETAAIFDLYSHLLTDArlrrELFDEVDK-----GSVAEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQR 304
Cdd:PRK11377 304 AEASGLDDIAAIFSGHHTLLDDP----ELLAAASErlqheHCTAEYAWQQVLKELSQQYQQLDDEYLQARYIDVDDLLHR 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 305 LLFHLDDTIQSPNTWPERFVLVADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGAD-----IQPSvl 379
Cdd:PRK11377 380 TLVHLTQTKEELPQFNSPTILLAENIYPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQGeklyaIQPE-- 457
|
250
....*....|....*..
gi 1445011758 380 hrRTLVVDGYRGELLVD 396
Cdd:PRK11377 458 --ETLTLDVKTQRLNRQ 472
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
17-163 |
2.81e-22 |
|
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: 93.60 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 17 RLNEALDILVTDICLAMDTEVCSVYLADHDRRCFY-LMATRGLKKPRGRtITLAFDEGIVGLVGRLAEPINLADAQKHPS 95
Cdd:smart00065 1 DLEELLQTILEELRQLLGADRVLIYLVDENDRGELvLVAADGLTLPTLG-IRFPLDEGLAGRVAETGRPLNIPDVEADPL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1445011758 96 FKYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREH-RQYDESEESFLVTLATQMAAILSQSQLAALF 163
Cdd:smart00065 80 FAEDLLGRYQGVRSFLAVPLVADGELVGVLALHNKKSpRPFTEEDEELLQALANQLAIALANAQLYEEL 148
|
|
| PEP-utilizers |
pfam00391 |
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain ... |
320-391 |
1.34e-14 |
|
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: 68.98 E-value: 1.34e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1445011758 320 PERFVLVADELSATTLAELPqnRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHR-RTLVVDGYRG 391
Cdd:pfam00391 3 PEGVILVAPDTTPSDTAGLD--KAAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEgDLVTVDGSTG 73
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
18-154 |
1.65e-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: 70.97 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 18 LNEALDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLKKPRGRTItlafdEGIVGLVGRLAEPINLADAQKHPSF- 96
Cdd:pfam01590 2 LEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIP-----PGTGVTVLRTGRPLVVPDAAGDPRFl 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1445011758 97 KYVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQReHRQYDESEESFLVTLATQMAAIL 154
Cdd:pfam01590 77 DPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHP-RPPFTEEELELLEVLADQVAIAL 133
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
2-467 |
6.38e-14 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 75.62 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 2 LTRLREIVEKVASAPRLNEALDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLkkPRGRTITLAFDEGIVGLVGRL 81
Cdd:COG2203 192 LALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGL--PEEELGRLPLGEGLAGRALRT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 82 AEPINLADAQKHPSFK--YVPAVKEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAILSQSQL 159
Cdd:COG2203 270 GEPVVVNDASTDPRFApsLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 160 AALFGQYRQTRIRALpaspgVAIAEGWMDSTLPLMEQVSEASTLDTILERERLTAALEEASNEFRRYSKRFAAGAQKETA 239
Cdd:COG2203 350 YEALEAALAALLQEL-----ALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 240 AIFDLYSHLLTDARLRRELFDEVDKGSVAEWAVKKVIEKFAEQFASLSDSYLKERAGDLRTLGQRLLFHLDDTIQSPNTW 319
Cdd:COG2203 425 DLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 320 PERFVLVADELSATTLAELPQNRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLVVDGYRGELLVDPET 399
Cdd:COG2203 505 VLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALI 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1445011758 400 VLLQEYQRLITEENELTRLVEDDVDSPAALKSGERVQVMLNAGLSPEHEQQLGGRIDGIGLYRTEIPF 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 |
6.42e-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: 66.34 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 18 LNEALDIlVTDICLAMD-TEVCSVYLADHDRRcfyLMATRGLKKPRGRTITLAFDEGIVGLVGRLAEPINLADAQKHPSF 96
Cdd:pfam13185 4 LEELLDA-VLEAAVELGaSAVGFILLVDDDGR---LAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1445011758 97 KYVPAVkEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAIL 154
Cdd:pfam13185 80 KGLPAG-HAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
|
|
| GAF_3 |
pfam13492 |
GAF domain; |
22-151 |
1.48e-05 |
|
GAF domain;
Pssm-ID: 433253 [Multi-domain] Cd Length: 129 Bit Score: 45.05 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445011758 22 LDILVTDICLAMDTEVCSVYLADHDRRCFYLMATRGLKKPRGRTITLAFDegivgLVGRLAEPINLADAQKhpsfkyVPA 101
Cdd:pfam13492 6 LEALLKLLVRLLGAERAAVYLLDEDGNKLQVAAGYDGEPDPSESLDADSP-----LARRALSSGEPISGLG------SAG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1445011758 102 VKEERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMA 151
Cdd:pfam13492 75 EDGLPDGPALVVPLVAGRRVIGVLALASSKPRAFDAEDLRLLESLAAQIA 124
|
|
| FhlA |
COG3604 |
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ... |
104-154 |
7.75e-05 |
|
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: 45.61 E-value: 7.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1445011758 104 EERFRAFLGVPIIQRRQLLGVLVVQQREHRQYDESEESFLVTLATQMAAIL 154
Cdd:COG3604 70 ARERQLFLGVPLRVGGEVLGVLTLDSRRPGAFSEEDLRLLETLASLAAVAI 120
|
|
| PykA2 |
COG3848 |
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms]; |
324-391 |
3.06e-04 |
|
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
Pssm-ID: 443058 Cd Length: 321 Bit Score: 43.74 E-value: 3.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1445011758 324 VLVADELSATTLAELPqnRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDGYRG 391
Cdd:COG3848 245 ILVVPSTDAEFVPAIE--KAAGIITEEGGLTSHAAIVGLELGIPVIVGAEGATEILKDGQVVtVDAERG 311
|
|
| PpsA |
COG0574 |
Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and ... |
324-392 |
2.07e-03 |
|
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: 41.35 E-value: 2.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1445011758 324 VLVADELSattlaelPQ-----NRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLV-VDGYRGE 392
Cdd:COG0574 386 ILVRDETD-------PDdvpgmKAAAGIVTERGGMTSHAAIVARELGIPAVVGCGDATRVLKDGDEItVDGTTGE 453
|
|
| PRK05878 |
PRK05878 |
pyruvate phosphate dikinase; Provisional |
344-392 |
2.36e-03 |
|
pyruvate phosphate dikinase; Provisional
Pssm-ID: 235635 [Multi-domain] Cd Length: 530 Bit Score: 41.27 E-value: 2.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1445011758 344 VGVVVRDGAANSHAAIMVRALGIPTVM--GADIQPSvLHRRTLVVDGYRGE 392
Cdd:PRK05878 401 QGIVTEVGGATSHAAVVSRELGRVAVVgcGAGVAAA-LAGKEITVDGYEGE 450
|
|
| |
