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Conserved domains on  [gi|496838653|ref|YP_006907046|]
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portal protein [Pseudomonas phage UFV-P2]

Protein Classification

Graphical summary

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List of domain hits

 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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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