|
Name |
Accession |
Description |
Interval |
E-value |
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
568-677 |
1.22e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] :
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 568 TNPNTPEAQQAMQQRAEaEAKPKPddikaQADAQRAQTDAGDKQAQAALRQVEAQvklAQVELAKQEAVVKQREISLKEQ 647
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAE-EAEKQR-----AAEQARQKELEQRAAAEKAAKQAEQA---AKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110
....*....|....*....|....*....|..
gi 496838653 648 ELQLE--RERFVWERARNEAEyhLEATQQRAA 677
Cdd:TIGR02794 133 KAKAEaeAERKAKEEAAKQAE--EEAKAKAAA 162
|
|
| P22_portal super family |
cl24922 |
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ... |
334-652 |
7.65e-03 |
|
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure. The actual alignment was detected with superfamily member pfam16510:
Pssm-ID: 293119 Cd Length: 668 Bit Score: 39.57 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 334 KIKDIQEIRTFLTRSILDSVTRNNQGRTVVLDGQV--------NLDD----LL--TNEAAGVVRVKQMAAIQPlptPPLP 399
Cdd:pfam16510 310 LAKDAQRLRNLIVSMLADSVAQDPKKKPFFGKEQIaglehmyaGNDDypyyLLnrTDENSGDLPPTPVGYTEN---PELN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 400 GDVYNMLDRLENDrAKRTGvsdrSRGLDENTLHSNQAATSVNQLMTAAEQQ----------------------------I 451
Cdd:pfam16510 387 QAMAAMLQAATAA-IKEVA----SQGVDPMASNGQVAFDTVNQLNHRSDLEtyvfqdnlakamrrdgeiylsiareiydS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 452 DLIARMFAETGVKRLFQLLHEHAIKYQDQKE-MFRLRGKW---VEVNPTnWRERSDLIVTVgIGNMNKdqQLLHLQRMWE 527
Cdd:pfam16510 462 DRQVRITNEDGTESDVALMSVVVDNQTGQVVaMNDIRGRYevyTDVGPS-FQSRKDATRAE-ITNLLA--KMPPQDPMRQ 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 528 MAQTVIAGGGMGILVSEQNIYNILQEVTEnaGYKdvdrfwtNPNTPE-------AQQAMQQRAEAE-AKPKPDDIKAQAD 599
Cdd:pfam16510 538 VLQLIYLDNMEGKGVEEFRDYANKQLITQ--GVK-------KPETTEeqqwlmeAQQAQQGQQDPEmVAAQGVLMQGQAE 608
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 600 AQRAQTDAGDKQAQAALRQVEAQVK-------LAQVELAKQEAVVKQREISLKEQELQLE 652
Cdd:pfam16510 609 LQKAQNEELAIQIKAFQAQTEARVAeakmvqiLASADSAKQAEIREALKMLHQFQKEQGD 668
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
568-677 |
1.22e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 568 TNPNTPEAQQAMQQRAEaEAKPKPddikaQADAQRAQTDAGDKQAQAALRQVEAQvklAQVELAKQEAVVKQREISLKEQ 647
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAE-EAEKQR-----AAEQARQKELEQRAAAEKAAKQAEQA---AKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110
....*....|....*....|....*....|..
gi 496838653 648 ELQLE--RERFVWERARNEAEyhLEATQQRAA 677
Cdd:TIGR02794 133 KAKAEaeAERKAKEEAAKQAE--EEAKAKAAA 162
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
574-677 |
1.01e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKpkpddiKAQADAQRAQTDAGD------KQAQAALRQVEAQVKLAQVELAKQEAVVKQREISlKEQ 647
Cdd:COG1566 77 DPTDLQAALAQAEAQ------LAAAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVS-QQE 149
|
90 100 110
....*....|....*....|....*....|
gi 496838653 648 ELQLERERFVWERARNEAEYHLEATQQRAA 677
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLR 179
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
597-684 |
3.59e-04 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 43.94 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 597 QADAQRAQTDAGDKQAQAALRQVEAQVKLAQVELAkqEAVVKQReiSLKEQELQLERERFVWERArnEAEYHLEATQQRA 676
Cdd:PRK06975 361 ANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLA--DAQSAQQ--ALEQQYQDLSRNRDDWMIA--EVEQMLSSASQQL 434
|
....*...
gi 496838653 677 AYIGDGKV 684
Cdd:PRK06975 435 QLTGNVQL 442
|
|
| P22_portal |
pfam16510 |
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ... |
334-652 |
7.65e-03 |
|
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure.
Pssm-ID: 293119 Cd Length: 668 Bit Score: 39.57 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 334 KIKDIQEIRTFLTRSILDSVTRNNQGRTVVLDGQV--------NLDD----LL--TNEAAGVVRVKQMAAIQPlptPPLP 399
Cdd:pfam16510 310 LAKDAQRLRNLIVSMLADSVAQDPKKKPFFGKEQIaglehmyaGNDDypyyLLnrTDENSGDLPPTPVGYTEN---PELN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 400 GDVYNMLDRLENDrAKRTGvsdrSRGLDENTLHSNQAATSVNQLMTAAEQQ----------------------------I 451
Cdd:pfam16510 387 QAMAAMLQAATAA-IKEVA----SQGVDPMASNGQVAFDTVNQLNHRSDLEtyvfqdnlakamrrdgeiylsiareiydS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 452 DLIARMFAETGVKRLFQLLHEHAIKYQDQKE-MFRLRGKW---VEVNPTnWRERSDLIVTVgIGNMNKdqQLLHLQRMWE 527
Cdd:pfam16510 462 DRQVRITNEDGTESDVALMSVVVDNQTGQVVaMNDIRGRYevyTDVGPS-FQSRKDATRAE-ITNLLA--KMPPQDPMRQ 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 528 MAQTVIAGGGMGILVSEQNIYNILQEVTEnaGYKdvdrfwtNPNTPE-------AQQAMQQRAEAE-AKPKPDDIKAQAD 599
Cdd:pfam16510 538 VLQLIYLDNMEGKGVEEFRDYANKQLITQ--GVK-------KPETTEeqqwlmeAQQAQQGQQDPEmVAAQGVLMQGQAE 608
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 600 AQRAQTDAGDKQAQAALRQVEAQVK-------LAQVELAKQEAVVKQREISLKEQELQLE 652
Cdd:pfam16510 609 LQKAQNEELAIQIKAFQAQTEARVAeakmvqiLASADSAKQAEIREALKMLHQFQKEQGD 668
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
568-677 |
1.22e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 568 TNPNTPEAQQAMQQRAEaEAKPKPddikaQADAQRAQTDAGDKQAQAALRQVEAQvklAQVELAKQEAVVKQREISLKEQ 647
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAE-EAEKQR-----AAEQARQKELEQRAAAEKAAKQAEQA---AKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110
....*....|....*....|....*....|..
gi 496838653 648 ELQLE--RERFVWERARNEAEyhLEATQQRAA 677
Cdd:TIGR02794 133 KAKAEaeAERKAKEEAAKQAE--EEAKAKAAA 162
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
574-677 |
1.01e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.04 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKpkpddiKAQADAQRAQTDAGD------KQAQAALRQVEAQVKLAQVELAKQEAVVKQREISlKEQ 647
Cdd:COG1566 77 DPTDLQAALAQAEAQ------LAAAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVS-QQE 149
|
90 100 110
....*....|....*....|....*....|
gi 496838653 648 ELQLERERFVWERARNEAEYHLEATQQRAA 677
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLR 179
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
597-684 |
3.59e-04 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 43.94 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 597 QADAQRAQTDAGDKQAQAALRQVEAQVKLAQVELAkqEAVVKQReiSLKEQELQLERERFVWERArnEAEYHLEATQQRA 676
Cdd:PRK06975 361 ANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLA--DAQSAQQ--ALEQQYQDLSRNRDDWMIA--EVEQMLSSASQQL 434
|
....*...
gi 496838653 677 AYIGDGKV 684
Cdd:PRK06975 435 QLTGNVQL 442
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
574-682 |
3.80e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKPKPD-DIKAQADAQR-AQTDAGDK-QAQAALRQVEAQVKLAQVELAKQEAVVKQREISLKEQELQ 650
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEaERKAKEEAAKqAEEEAKAKaAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEA 200
|
90 100 110
....*....|....*....|....*....|....
gi 496838653 651 LE--RERFVWERARNEAEYHLEATQQRAAYIGDG 682
Cdd:TIGR02794 201 AKakAAAEAAAKAEAEAAAAAAAEAERKADEAEL 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
574-677 |
1.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAkpkpddikAQADAQRAQTDAGDKQAQAALRQVEAQVKLAQVELAKQEAVVKQREislkEQELQLER 653
Cdd:COG1196 305 ARLEERRRELEERL--------EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE----EALLEAEA 372
|
90 100
....*....|....*....|....
gi 496838653 654 ERFVWERARNEAEYHLEATQQRAA 677
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAA 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
574-696 |
1.38e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKPKPDDiKAQADAQRAQTDAGDKQAQAALRQVEAQVKLAQVELAKQEAVVKQREISLKEQ---ELQ 650
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaEKK 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 496838653 651 LERERFVWERARNEAEyhleatQQRAAYIGDGKVPETAKPSKSVRK 696
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAE------EKKKADEAKKKAEEDKKKADELKK 1412
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
597-662 |
2.88e-03 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 40.33 E-value: 2.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496838653 597 QADAQRAQTDAGDKQAQAALRQVEA-----QVKLAQVELAKQEAVVKQREISLKEQELQLERERFVWERAR 662
Cdd:PRK03598 149 NARSSRDQAQATLKSAQDKLSQYREgnrpqDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAV 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
574-696 |
5.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKPKPDDIKAQADaQRAQTDAGDKQAQAALRQVEAQVKLAQVELAKQEAVVKQREISLKEQElqlER 653
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE---ED 1686
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496838653 654 ERFVWERARNEAEYHLEATQQRAAYIGDGKVPETAKPSKSVRK 696
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
574-677 |
6.37e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKPKpddiKAQADAQRAQtDAGDKQAQAALRQVEAQVKLAQVELAKQEAVVKQREIS----LKEQEL 649
Cdd:PRK09510 109 ERLAAQEQKKQAEEAAK----QAALKQKQAE-EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAeaakKAAAEA 183
|
90 100
....*....|....*....|....*...
gi 496838653 650 QLERERFVWERARNEAEYHLEATQQRAA 677
Cdd:PRK09510 184 KKKAEAEAAAKAAAEAKKKAEAEAKKKA 211
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
611-678 |
7.31e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 39.16 E-value: 7.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496838653 611 QAQAALRQVEAQVKLAQVELAKQEAVVKQREISlkEQEL-QLERERFVWERARNEAEYHLEATQQRAAY 678
Cdd:COG0845 65 QAQAQLAAAQAQLELAKAELERYKALLKKGAVS--QQELdQAKAALDQAQAALAAAQAALEQARANLAY 131
|
|
| P22_portal |
pfam16510 |
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages ... |
334-652 |
7.65e-03 |
|
Phage P22-like portal protein; The portal protein of P22 and similar Podoviridae tail phages is a dodecameric structure consisting of a hip (2), a leg(1) and a barrel(3). DNA viruses such as bacteriophages and herpesviruses deliver their genome into and out of the capsid through large proteinaceous assemblies, known as portal proteins. Domains 1 and 3 are mostly helical and form the majority of the DNA-translocating channel. Domain 2 adopts an alpha-beta-fold characterized by two sheets of eight beta-strands, which cross each other to form a beta-barrel-like structure.
Pssm-ID: 293119 Cd Length: 668 Bit Score: 39.57 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 334 KIKDIQEIRTFLTRSILDSVTRNNQGRTVVLDGQV--------NLDD----LL--TNEAAGVVRVKQMAAIQPlptPPLP 399
Cdd:pfam16510 310 LAKDAQRLRNLIVSMLADSVAQDPKKKPFFGKEQIaglehmyaGNDDypyyLLnrTDENSGDLPPTPVGYTEN---PELN 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 400 GDVYNMLDRLENDrAKRTGvsdrSRGLDENTLHSNQAATSVNQLMTAAEQQ----------------------------I 451
Cdd:pfam16510 387 QAMAAMLQAATAA-IKEVA----SQGVDPMASNGQVAFDTVNQLNHRSDLEtyvfqdnlakamrrdgeiylsiareiydS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 452 DLIARMFAETGVKRLFQLLHEHAIKYQDQKE-MFRLRGKW---VEVNPTnWRERSDLIVTVgIGNMNKdqQLLHLQRMWE 527
Cdd:pfam16510 462 DRQVRITNEDGTESDVALMSVVVDNQTGQVVaMNDIRGRYevyTDVGPS-FQSRKDATRAE-ITNLLA--KMPPQDPMRQ 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 528 MAQTVIAGGGMGILVSEQNIYNILQEVTEnaGYKdvdrfwtNPNTPE-------AQQAMQQRAEAE-AKPKPDDIKAQAD 599
Cdd:pfam16510 538 VLQLIYLDNMEGKGVEEFRDYANKQLITQ--GVK-------KPETTEeqqwlmeAQQAQQGQQDPEmVAAQGVLMQGQAE 608
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 600 AQRAQTDAGDKQAQAALRQVEAQVK-------LAQVELAKQEAVVKQREISLKEQELQLE 652
Cdd:pfam16510 609 LQKAQNEELAIQIKAFQAQTEARVAeakmvqiLASADSAKQAEIREALKMLHQFQKEQGD 668
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
574-677 |
8.79e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.09 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 574 EAQQAMQQRAEAEAKPKPDDIKAQADAQRAQTD-AGDKQAQAALRQV---------EAQVKLAQVE----LAKQEAVVKQ 639
Cdd:COG2268 233 EIETARIAEAEAELAKKKAEERREAETARAEAEaAYEIAEANAEREVqrqleiaerEREIELQEKEaereEAELEADVRK 312
|
90 100 110
....*....|....*....|....*....|....*...
gi 496838653 640 REISLKEQELQLERERFVWERARNEAEyhLEATQQRAA 677
Cdd:COG2268 313 PAEAEKQAAEAEAEAEAEAIRAKGLAE--AEGKRALAE 348
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
597-681 |
8.88e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496838653 597 QADAQRAQTDAGDK------------QAQAALRQVEA--------QVKLAQV------ELAKQEAVVKQREISLKEQELQ 650
Cdd:PRK10929 146 QTEARRQLNEIERRlqtlgtpntplaQAQLTALQAESaalkalvdELELAQLsannrqELARLRSELAKKRSQQLDAYLQ 225
|
90 100 110
....*....|....*....|....*....|.
gi 496838653 651 LERERFVWERARnEAEYHLEATQQRAAYIGD 681
Cdd:PRK10929 226 ALRNQLNSQRQR-EAERALESTELLAEQSGD 255
|
|
|