NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1952201083|ref|WP_199529493|]
View 

signal recognition particle-docking protein FtsY [Pseudoalteromonas sp. bablab_jr010]

Protein Classification

signal recognition particle-docking protein FtsY( domain architecture ID 11484700)

signal recognition particle-docking protein FtsY is a GTPase involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane; acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC)

Gene Symbol:  ftsY
Gene Ontology:  GO:0005047|GO:0005525|GO:0006614

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
392-694 0e+00

Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 529.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 392 FFARLKKGLLKTRVNIGSGFASIFSG-KKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ 470
Cdd:COG0552     1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 471 EMASMLKTAEQPLVVSnDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVI 550
Cdd:COG0552    81 ELLEILDPVDKPLAIE-EKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 551 AQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVK 630
Cdd:COG0552   160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 631 LFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQD 694
Cdd:COG0552   240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
17-392 1.16e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 103.86  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG1196   546 AAL-QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG1196   625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:COG1196   705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
 
Name Accession Description Interval E-value
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
392-694 0e+00

Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 529.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 392 FFARLKKGLLKTRVNIGSGFASIFSG-KKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ 470
Cdd:COG0552     1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 471 EMASMLKTAEQPLVVSnDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVI 550
Cdd:COG0552    81 ELLEILDPVDKPLAIE-EKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 551 AQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVK 630
Cdd:COG0552   160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 631 LFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQD 694
Cdd:COG0552   240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
385-695 0e+00

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 529.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 385 EKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDAL 464
Cdd:PRK10416    9 KKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 465 YELMKQEMASMLKTAEQPLVVsNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGER 544
Cdd:PRK10416   89 KELLKEELAEILEPVEKPLNI-EEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGER 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 545 NSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQN 624
Cdd:PRK10416  168 VGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQN 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 625 AISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQDE 695
Cdd:PRK10416  248 ALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
419-691 4.51e-128

signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 380.45  E-value: 4.51e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 419 KIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQEMASMLKTAE----QPLVVSNDKKPFVI 494
Cdd:TIGR00064   1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 495 LMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNV 574
Cdd:TIGR00064  81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 575 DVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGV 654
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1952201083 655 IFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
FtsY cd17874
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ...
492-690 4.52e-110

signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.


Pssm-ID: 349783  Cd Length: 199  Bit Score: 331.07  E-value: 4.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17874     1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd17874    81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd17874   161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
491-691 1.98e-97

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 298.17  E-value: 1.98e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  491 PFVILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAA 569
Cdd:smart00962   1 PGVILLVGPNGVGKTTTIAKLAARLKlKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  570 KARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGT 649
Cdd:smart00962  81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1952201083  650 AKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
492-690 1.37e-91

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 282.89  E-value: 1.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:pfam00448   1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:pfam00448  81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
17-392 1.16e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 103.86  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG1196   546 AAL-QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG1196   625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:COG1196   705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
PTZ00121 PTZ00121
MAEBL; Provisional
15-399 2.49e-19

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 93.28  E-value: 2.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERI---AAEKAEAERLEQEriAAEKAE 91
Cdd:PTZ00121  1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKK--AEEKKK 1432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   92 AERLEQEriAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:PTZ00121  1433 ADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  172 EKAEAERLEQERIAAEKAEAE---RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAE 247
Cdd:PTZ00121  1511 KADEAKKAEEAKKADEAKKAEeakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdKNMALRKAEEAKKAE 1590
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  248 KAEAERLEQERIAAEKAEAERL---EQERIAAE---KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVA 321
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  322 E----KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAA--AEKPKKEGFFAR 395
Cdd:PTZ00121  1671 EedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEEAK 1750

                   ....
gi 1952201083  396 LKKG 399
Cdd:PTZ00121  1751 KDEE 1754
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
30-387 1.11e-13

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 74.39  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  30 NQKQIEEQQRIEaekaEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQERIAAEKAEAERL------EQERIAA 102
Cdd:pfam17380 280 HQKAVSERQQQE----KFEKMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMamererELERIRQ 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 103 E--RRDAERVEQERIAAEkaeAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAaeqaqreaeqaaaekaeaerlE 180
Cdd:pfam17380 356 EerKRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELEAARKVKILEEE---------------------R 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERiaaeKAEAERLEQEriaaEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEER----AREMERVRLE----EQERQQQVERLRQQEEERKRKKLELEKEK 483
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAErlEQERIAAEKAEAERleQERIAAEKAEADRLEQERIAAEKAEAErlEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:pfam17380 484 RDRKRAE--EQRRKILEKELEER--KQAMIEEERKRKLLEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQ 557
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1952201083 341 ADRLEQERIAAEKAEAERLEQERIAEeqAEAERLEQEKVAQAAAEKP 387
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQIVE--SEKARAEYEATTPITTIKP 602
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
63-388 2.55e-08

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 57.33  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  63 ERLEQERIAAEKAEAErLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQAR 142
Cdd:NF033838   99 EYLYELNVLKEKSEAE-LTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 143 LAEQEAAMKLEQERAAAEQAQREAEQAAAEKAeaerleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:NF033838  178 IAESDVEVKKAELELVKEEAKEPRDEEKIKQA------KAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 223 RLEQERIAAEKAEAER--LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEADRLE 300
Cdd:NF033838  252 NVATSEQDKPKRRAKRgvLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRN 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 301 QERIAAEKAEAERLEQERIVAEkAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE----QERIAEEQAEAERLEQ 376
Cdd:NF033838  331 YPTNTYKTLELEIAESDVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEkiktDRKKAEEEAKRKAAEE 409
                         330
                  ....*....|..
gi 1952201083 377 EKVAQAAAEKPK 388
Cdd:NF033838  410 DKVKEKPAEQPQ 421
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
200-410 2.26e-07

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: 53.31  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 279
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 280 EaeRLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERL 359
Cdd:TIGR02794 126 A--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 360 EQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSG 410
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
182-391 1.27e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 48.68  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  182 ERIAAEKAEAERLEQEriaaEKAEA--ERLEQER------IAAEKAEAERLEQERIAAeKAEAER----LEQERIAAEKA 249
Cdd:NF012221  1549 KHAKQDDAAQNALADK----ERAEAdrQRLEQEKqqqlaaISGSQSQLESTDQNALET-NGQAQRdailEESRAVTKELT 1623
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  250 E-AERLEQERIAAEKAE----------AERLeQERIAAEKAEAERLEQERIAAEK-AEADRLEQERIAAEKAEA--ERLE 315
Cdd:NF012221  1624 TlAQGLDALDSQATYAGesgdqwrnpfAGGL-LDRVQEQLDDAKKISGKQLADAKqRHVDNQQKVKDAVAKSEAgvAQGE 1702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  316 QERIVAE------KAEAERLEQERIAAEKAEADRLEQERIAAEKAEaERLEQE-RIAEEQAEAERLEQEKVAQAAAEKPK 388
Cdd:NF012221  1703 QNQANAEqdiddaKADAEKRKDDALAKQNEAQQAESDANAAANDAQ-SRGEQDaSAAENKANQAQADAKGAKQDESDKPN 1781

                   ...
gi 1952201083  389 KEG 391
Cdd:NF012221  1782 RQG 1784
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
181-366 1.40e-05

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 48.55  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER-IAAEKAEAERLEQ-ERIAAEKAEAERL---- 254
Cdd:NF033875    80 QKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQpVVSPETTNEPLGQpTEVAPAENEANKStsip 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  255 -EQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEADRLEQEriaaekaeaerleQERIVAEKAEAERLE 330
Cdd:NF033875   160 kEFETPDVDKAVDEAKKDPNITVVEKPAEDLgnvSSKDLAAKEKEVDQLQKE-------------QAKKIAQQAAELKAK 226
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1952201083  331 QERIAAEKAEadrleqerIAAE-KAEAERLEQErIAE 366
Cdd:NF033875   227 NEKIAKENAE--------IAAKnKAEKERYEKE-VAE 254
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
18-347 1.12e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.39  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKqiEEQQR------------------IEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 79
Cdd:NF033838  145 TKKVEEAEKKAKDQK--EEDRRnyptntyktleleiaesdVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATR 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  80 LEQERIAAEKAEAErleqeriaaerrdaerveqeriAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAA 159
Cdd:NF033838  223 LEKIKTDREKAEEE----------------------AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 160 EQAQREAEQAAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERL 239
Cdd:NF033838  281 NDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESD-VKVKEAELELV 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 240 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAerlEQERIAAE--KAEADRLEQERIAAEKAEAERLEQE 317
Cdd:NF033838  359 KEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEE---EAKRKAAEedKVKEKPAEQPQPAPAPQPEKPAPKP 435
                         330       340       350
                  ....*....|....*....|....*....|
gi 1952201083 318 RIVAEKAEAERLEQERiaAEKAEADRLEQE 347
Cdd:NF033838  436 EKPAEQPKAEKPADQQ--AEEDYARRSEEE 463
growth_prot_Scy NF041483
polarized growth protein Scy;
181-395 4.53e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERL----EQERIAAEKAEAE-RL 254
Cdd:NF041483   523 EETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEALADaRA 600
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  255 EQERIAAEKAEaerlEQERIAAEKAEAERLEQeriAAEKAEADRLEQEriAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:NF041483   601 EAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTE--AAADASAARAEGENVAVRLRSEAAAEAERL 671
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083  335 AAEKAE-ADRLEQE-RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFAR 395
Cdd:NF041483   672 KSEAQEsADRVRAEaAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
growth_prot_Scy NF041483
polarized growth protein Scy;
20-397 1.21e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   20 QAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQE 98
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTAKEEIARLVGE--ATKEAEALKAEAEQALADaRAEAEKLVAEAAEKARTVAAEDTAA 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   99 RIAAERRDAERV-------EQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:NF041483   365 QLAKAARTAEEVltkasedAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARR 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  172 EKAEAERLEQEriAAEKAEAERLEQERIAAEK-AEAERLEQERIAAEKAEAERLEQeriaAEKAEAERLEQEriAAEKAE 250
Cdd:NF041483   445 LRGEAEQLRAE--AVAEGERIRGEARREAVQQiEEAARTAEELLTKAKADADELRS----TATAESERVRTE--AIERAT 516
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  251 AERLE-QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERL----EQERIVAEKA 324
Cdd:NF041483   517 TLRRQaEETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEA 594
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083  325 EAE-RLEQERIAAEKAEadrlEQERIAAEKAEAERLEQeriAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLK 397
Cdd:NF041483   595 LADaRAEAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTEAAADASAARAEGENVAVRLR 661
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
277-364 2.07e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 40.74  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 277 EKAEAER------LEQERIAAEKAEADRLEQeRIAAEK-AEAERLEQERIVAEKaEAERLEQE-----RIAAEKAEAD-- 342
Cdd:cd03406   169 EAMEAEKtklliaEQHQKVVEKEAETERKRA-VIEAEKdAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARADae 246
                          90       100
                  ....*....|....*....|....*
gi 1952201083 343 --RLEQERIAAE-KAEAERLEQERI 364
Cdd:cd03406   247 yyRALREAEANKlKLTPEYLELKKY 271
growth_prot_Scy NF041483
polarized growth protein Scy;
17-382 3.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:NF041483   527 ERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIR 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   97 QEriAAERRDAERVE-QERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:NF041483   607 RE--AAEETERLRTEaAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRA 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERL--------EQERIAAEKAEAERLEQERIAAEKAEAERL----EQER 243
Cdd:NF041483   685 EAAAAAERVGTEAAEALAAAQEEAARRRREAEETlgsaraeaDQERERAREQSEELLASARKRVEEAQAEAQrlveEADR 764
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  244 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRL------EQERIAAEKAEAERLEQE 317
Cdd:NF041483   765 RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVrsdayaERERASEDANRLRREAQE 844
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  318 RIVAEKAEAERL------EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:NF041483   845 ETEAAKALAERTvseaiaEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQA 915
 
Name Accession Description Interval E-value
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
392-694 0e+00

Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 529.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 392 FFARLKKGLLKTRVNIGSGFASIFSG-KKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ 470
Cdd:COG0552     1 FFERLKEGLSKTRSGLGEKLKSLFSGkKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKDPEELKEALKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 471 EMASMLKTAEQPLVVSnDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVI 550
Cdd:COG0552    81 ELLEILDPVDKPLAIE-EKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGERVGVPVI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 551 AQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVK 630
Cdd:COG0552   160 AQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKKLDPDAPHEVLLVLDATTGQNALSQAK 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 631 LFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQD 694
Cdd:COG0552   240 VFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDALFGEE 303
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
385-695 0e+00

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 529.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 385 EKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDAL 464
Cdd:PRK10416    9 KKEKKEGWFERLKKGLSKTRENFGEGINGLFAKKKIDEDLLEELEELLIEADVGVETTEEIIEELRERVKRKNLKDPEEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 465 YELMKQEMASMLKTAEQPLVVsNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGER 544
Cdd:PRK10416   89 KELLKEELAEILEPVEKPLNI-EEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGER 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 545 NSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQN 624
Cdd:PRK10416  168 VGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKKADPDAPHEVLLVLDATTGQN 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 625 AISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALFSQDE 695
Cdd:PRK10416  248 ALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLGGED 318
ftsY TIGR00064
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ...
419-691 4.51e-128

signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 272883 [Multi-domain]  Cd Length: 277  Bit Score: 380.45  E-value: 4.51e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 419 KIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQEMASMLKTAE----QPLVVSNDKKPFVI 494
Cdd:TIGR00064   1 KDDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLlkntDLELIVEENKPNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 495 LMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNV 574
Cdd:TIGR00064  81 LFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGADPAAVAFDAIQKAKARNI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 575 DVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGV 654
Cdd:TIGR00064 161 DVVLIDTAGRLQNKVNLMDELKKIKRVIKKVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGI 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1952201083 655 IFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:TIGR00064 241 ILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
FtsY cd17874
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ...
492-690 4.52e-110

signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.


Pssm-ID: 349783  Cd Length: 199  Bit Score: 331.07  E-value: 4.52e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17874     1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGADPAAVAFDAIQAAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd17874    81 RGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKKKDPEAPHEVLLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGTAK 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd17874   161 GGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
491-691 1.98e-97

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 298.17  E-value: 1.98e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  491 PFVILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAA 569
Cdd:smart00962   1 PGVILLVGPNGVGKTTTIAKLAARLKlKGGKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGADPVAVAKDAVELA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  570 KARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGT 649
Cdd:smart00962  81 KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIK------PDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILTKLDGT 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1952201083  650 AKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDALF 691
Cdd:smart00962 155 AKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLL 196
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
492-690 1.37e-91

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 282.89  E-value: 1.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:pfam00448   1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGADPAAVAFDAVEKAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:pfam00448  81 ENYDVVLVDTAGRLQNDKNLMDELKKIKRVVA------PDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:pfam00448 155 GGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
492-690 1.61e-82

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 259.23  E-value: 1.61e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd03115     1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd03115    81 EGYDVLLVDTAGRLQKDEPLMEELKKVKEV------ESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd03115   155 GGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
PRK14974 PRK14974
signal recognition particle-docking protein FtsY;
357-692 2.00e-75

signal recognition particle-docking protein FtsY;


Pssm-ID: 237875 [Multi-domain]  Cd Length: 336  Bit Score: 246.04  E-value: 2.00e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 357 ERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKkgllktrvnigsgfASIFSGKKIDDELfEELETQLLTAD 436
Cdd:PRK14974   14 EKVEEKIEEEEEEEAPEAEEEEEEEDEEEKKEKPGFFDKAK--------------ITEIKEKDIEDLL-EELELELLESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 437 LGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ-------EMASMLKTAEQPLVVSNDKKPFVILMVGVNGVGKTTTIG 509
Cdd:PRK14974   79 VALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNalkeallEVLSVGDLFDLIEEIKSKGKPVVIVFVGVNGTGKTTTIA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 510 KLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKD 589
Cdd:PRK14974  159 KLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 590 NLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYI 669
Cdd:PRK14974  239 NLMDELKKIVRVTK------PDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFL 312
                         330       340
                  ....*....|....*....|...
gi 1952201083 670 GVGEGIDDLRTFNSSDFIDALFS 692
Cdd:PRK14974  313 GVGQGYDDLIPFDPDWFVDKLLG 335
Ffh COG0541
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ...
406-682 2.62e-63

Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440307 [Multi-domain]  Cd Length: 423  Bit Score: 216.43  E-value: 2.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 406 NIGSGFASIF---SGK-KID----DELFEELETQLLTADLGVDTTMKLIDNLTDAA----DRKQLKDGDALYELMKQEMA 473
Cdd:COG0541     4 NLSERLQGAFkklRGKgRLTeeniKEALREVRRALLEADVNLKVVKDFIERVKERAlgeeVLKSLTPGQQVIKIVHDELV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 474 SMLKTAEQPLVVSNdKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQH 553
Cdd:COG0541    84 ELLGGENEELNLAK-KPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 554 TGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFN 633
Cdd:COG0541   163 DGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVN------PDETLLVVDAMTGQDAVNVAKAFN 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1952201083 634 ECVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFN 682
Cdd:COG0541   237 EALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFH 285
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
493-681 1.07e-59

GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349786  Cd Length: 193  Bit Score: 198.98  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKAR 572
Cdd:cd18539     2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRALEKAKEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 573 NVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKG 652
Cdd:cd18539    82 GFDVVIVDTAGRLHIDEELMDELKEIKEVLN------PDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKLDGDARG 155
                         170       180
                  ....*....|....*....|....*....
gi 1952201083 653 GVIFAVADKFNIPIRYIGVGEGIDDLRTF 681
Cdd:cd18539   156 GAALSIRHVTGKPIKFIGVGEKIEDLEPF 184
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
406-687 2.43e-53

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 190.03  E-value: 2.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 406 NIGSGFASIFSGKKIDDELFEE----LETQLLTADLGVDTTMKLIDNLTDAADRKQLKDG----DALYELMKQEMASMLK 477
Cdd:PRK00771    4 SLRDALKKLAGKSRIDEKTVKEvvkdIQRALLQADVNVKLVKELSKSIKERALEEEPPKGltprEHVIKIVYEELVKLLG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 478 TAEQPLVvsNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGAD 557
Cdd:PRK00771   84 EETEPLV--LPLKPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGDPDNKD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 558 SASVVFDAFQAAKarNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVG 637
Cdd:PRK00771  162 AVEIAKEGLEKFK--KADVIIVDTAGRHALEEDLIEEMKEIKEAVK------PDEVLLVIDATIGQQAKNQAKAFHEAVG 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952201083 638 LTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFI 687
Cdd:PRK00771  234 IGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFI 283
SRalpha_C cd17876
C-terminal domain of signal recognition particle receptor alpha subunit; The ...
492-690 2.62e-47

C-terminal domain of signal recognition particle receptor alpha subunit; The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins.


Pssm-ID: 349785  Cd Length: 204  Bit Score: 165.87  E-value: 2.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17876     1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELYEKGYGKDPAAVAKEAIKYARD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidPDApheVMLTIDAGTGQNAISQVKLFNECV----------GLTGI 641
Cdd:cd17876    81 QGFDVVLIDTAGRMQNNEPLMRALAKLIKENN---PDL---VLFVGEALVGNDAVDQLKKFNQALadyspsdnprLIDGI 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 642 TLSKLDgTA--KGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:cd17876   155 VLTKFD-TIddKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
492-687 1.07e-46

GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349784  Cd Length: 193  Bit Score: 163.90  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKA 571
Cdd:cd17875     1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEGVEKFKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:cd17875    81 EKFDIIIVDTSGRHKQEEELFEEMKQISDAVK------PDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLDGHAK 154
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1952201083 652 -GGVIFAVAdKFNIPIRYIGVGEGIDDLRTFNSSDFI 687
Cdd:cd17875   155 gGGALSAVA-ATGAPIIFIGTGEHIDDLEPFDPKRFV 190
SRP54_euk TIGR01425
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ...
407-690 4.02e-37

signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.


Pssm-ID: 273615 [Multi-domain]  Cd Length: 428  Bit Score: 144.21  E-value: 4.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 407 IGSGFASIFSGKKIDDE----LFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMKQ----EMASMLKT 478
Cdd:TIGR01425   9 LVTALRSMSSATVIDEEvintMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDavfeELCNLVDP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 479 AEQPLVVSNDKkPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADS 558
Cdd:TIGR01425  89 GVEAFTPKKGK-TCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYEESDP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 559 ASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKkidpdaPHEVMLTIDAGTGQNAISQVKLFNECVGL 638
Cdd:TIGR01425 168 VKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIK------PDSIIFVMDGSIGQAAFGQAKAFKDSVEV 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 639 TGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDDLRTFNSSDFIDAL 690
Cdd:TIGR01425 242 GSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
367-691 3.45e-33

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 131.14  E-value: 3.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 367 EQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLI 446
Cdd:COG1419    50 DEDEAEKAPAAAAAPAAASAAAEEEELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 447 DNLtdaadrKQLKDGDALYELMKQEMASMLKTAEQPLVvsndKKPFVILMVGVNGVGKTTTIGKLAKQF-QNEGKSVMLA 525
Cdd:COG1419   130 EKL------PEDLSAEEAWRALLEALARRLPVAEDPLL----DEGGVIALVGPTGVGKTTTIAKLAARFvLRGKKKVALI 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 526 AGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKI 605
Cdd:COG1419   200 TTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEAL------ERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPI 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 606 dpdaphEVMLTIDAGT-GQNAISQVKLFNEcVGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNS 683
Cdd:COG1419   274 ------EVYLVLSATTkYEDLKEIVEAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADP 346

                  ....*...
gi 1952201083 684 SDFIDALF 691
Cdd:COG1419   347 ERLARLLL 354
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
493-678 1.25e-28

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 113.03  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQ-NEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSAsvvfDAFQAAKA 571
Cdd:cd17873     2 VIALVGPTGVGKTTTLAKLAARYVlKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEV----AEDP----EDLADALE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 R--NVDVLIADTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGT-GQNAISQVKLFnECVGLTGITLSKLDG 648
Cdd:cd17873    74 RlsDRDLILIDTAGRSPRDKEQLEELKELLGAGEDI------EVHLVLSATTkAKDLKEIIERF-SPLGYRGLILTKLDE 146
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1952201083 649 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDL 678
Cdd:cd17873   147 TTSLGSVLSVLAESQLPVSYVTTGQRVpEDI 177
flhF PRK05703
flagellar biosynthesis protein FlhF;
315-679 3.66e-23

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 102.66  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 315 EQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFA 394
Cdd:PRK05703   55 ETPKKNPVLREEKRKPAKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELDE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 395 RLK-----KGLLKTRVnigsgfASIFSGKKIDDElFEELETQLLTADLG---VDTTMKLIDNLTDAADRkqlkdgdALYE 466
Cdd:PRK05703  135 LRDelkelKNLLEDQL------SGLRQVERIPPE-FAELYKRLKRSGLSpeiAEKLLKLLLEHMPPRER-------TAWR 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 467 LMKQEMASMLKTAEQPLVvsndKKPFVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGER 544
Cdd:PRK05703  201 YLLELLANMIPVRVEDIL----KQGGVVALVGPTGVGKTTTLAKLAARYalLYGKKKVALITLDTYRIGAVEQLKTYAKI 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 545 NSIPVIaqhtgadsasVVFDAFQAAKA----RNVDVLIADTAGRLQNKDNLMQELEKIARvmkkiDPDAPHEVMLTIDAg 620
Cdd:PRK05703  277 MGIPVE----------VVYDPKELAKAleqlRDCDVILIDTAGRSQRDKRLIEELKALIE-----FSGEPIDVYLVLSA- 340
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 621 TGQN----AIsqVKLFNECvGLTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLR 679
Cdd:PRK05703  341 TTKYedlkDI--YKHFSRL-PLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIK 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
17-392 1.16e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 103.86  E-value: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG1196   546 AAL-QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG1196   625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:COG1196   705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-377 2.75e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 102.32  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRlELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  94 RLEQERIAAERRDAERvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG1196   320 ELEEELAELEEELEEL-EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAE--------KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAE 325
Cdd:COG1196   479 LAELLEELAEAAARLLLLLEAEADyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 326 AERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG1196   559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
18-390 5.70e-22

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 101.55  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQ------RIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--- 88
Cdd:COG1196   206 ERQAEKAERYRELKEELKELEaellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElee 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  89 KAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 169 AAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 248
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE------KAEAERLEQERIVAE 322
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvKAALLLAGLRGLAGA 525
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 323 KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG1196   526 VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
PTZ00121 PTZ00121
MAEBL; Provisional
15-399 2.49e-19

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 93.28  E-value: 2.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERI---AAEKAEAERLEQEriAAEKAE 91
Cdd:PTZ00121  1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKK--AEEKKK 1432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   92 AERLEQEriAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:PTZ00121  1433 ADEAKKK--AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  172 EKAEAERLEQERIAAEKAEAE---RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAE 247
Cdd:PTZ00121  1511 KADEAKKAEEAKKADEAKKAEeakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdKNMALRKAEEAKKAE 1590
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  248 KAEAERLEQERIAAEKAEAERL---EQERIAAE---KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVA 321
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAkkaEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  322 E----KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAA--AEKPKKEGFFAR 395
Cdd:PTZ00121  1671 EedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEEAK 1750

                   ....
gi 1952201083  396 LKKG 399
Cdd:PTZ00121  1751 KDEE 1754
PTZ00121 PTZ00121
MAEBL; Provisional
17-422 3.51e-19

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 92.90  E-value: 3.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEAD-NQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAERL 95
Cdd:PTZ00121  1389 EKKKADEAKKKAEeDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKAEEA 1462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   96 EQEriAAERRDAErvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:PTZ00121  1463 KKK--AEEAKKAD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---KAEAE 252
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEA 1618
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  253 RLEQERIAAEKAEAERLEQ--ERIAAEKAEAERL---EQERIAAEKAEADRLEQERIAAEKA----EAERLEQERIVAEK 323
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQlkKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKEA 1698
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  324 AEAERLEQERIAAE----KAEADRLEQE--RIAAEKAEAERLEQERIAEEqAEAERLEQEKVAQAAAEKPKKEGFFARLK 397
Cdd:PTZ00121  1699 EEAKKAEELKKKEAeekkKAEELKKAEEenKIKAEEAKKEAEEDKKKAEE-AKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
                          410       420
                   ....*....|....*....|....*
gi 1952201083  398 KGLLKTRVNIGSGFASIFSGKKIDD 422
Cdd:PTZ00121  1778 EAVIEEELDEEDEKRRMEVDKKIKD 1802
PTZ00121 PTZ00121
MAEBL; Provisional
26-390 3.26e-18

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 89.82  E-value: 3.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   26 KEADNQKQIEEQQRIEAEK--AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 103
Cdd:PTZ00121  1194 RKAEDARKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  104 RRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQER 183
Cdd:PTZ00121  1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  184 IAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEK 263
Cdd:PTZ00121  1354 AAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEK 1430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  264 AEAERLEQEriAAEKAEAERLEQERIAAEKAEadrlEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:PTZ00121  1431 KKADEAKKK--AEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1952201083  344 LEQERIAAEkaEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1505 AAEAKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
PTZ00121 PTZ00121
MAEBL; Provisional
15-390 4.48e-18

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 89.43  E-value: 4.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEaekaEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAaekAEAER 94
Cdd:PTZ00121  1147 KAEDAKRVEIARKAEDARKAEEARKAE----DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA---EEARK 1219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   95 LEQERIAAERRDAERVEQERIAAEKAEAERlaqEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PTZ00121  1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEER---NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  175 EAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:PTZ00121  1297 KAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  254 LEQERIAAEKAEAERLEQE-RIAAEKAEAERLEQERIAAEKAEADRLEQEriAAEKAEAERLEQERIVAEKA-EAERLEQ 331
Cdd:PTZ00121  1377 KKKADAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKAdEAKKKAE 1454
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083  332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
PTZ00121 PTZ00121
MAEBL; Provisional
18-390 7.55e-18

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 88.66  E-value: 7.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   18 KQQAEQAAKEADNQKQIEEQQRIEAEKA--EAERLEQERIAAEKAEAERLEQERIAAEKAEAER--------LEQERIAA 87
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeakkkAEEDKKKA 1407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   88 EKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:PTZ00121  1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  168 QAAAEKAEAERLEQERIAAEkaEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  248 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaEADRLEQERIAAE---KAEAERLEQERIVAEKA 324
Cdd:PTZ00121  1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEA 1643
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083  325 EAERLEQERIAAEKAEADRLEQERIAAE--KAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1644 EEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
PTZ00121 PTZ00121
MAEBL; Provisional
15-390 8.44e-18

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 88.66  E-value: 8.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAeAER 94
Cdd:PTZ00121  1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA-AIK 1273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PTZ00121  1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  175 EAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERI---AAEKA 249
Cdd:PTZ00121  1354 AAA--DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkKAAAAKKKADEAkkkAEEKK 1431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  250 EAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PTZ00121  1432 KADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083  329 LEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
PTZ00121 PTZ00121
MAEBL; Provisional
17-390 1.07e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 88.27  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErlE 96
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--A 1376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQ-EAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:PTZ00121  1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA----EAERLEQERIAAEKAEA 251
Cdd:PTZ00121  1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKA 1536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERleqeriaAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ 331
Cdd:PTZ00121  1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEE-------AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083  332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERL---EQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAE 1671
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-377 2.00e-17

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 86.91  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAEr 94
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE- 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  95 leqeriaAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA-MKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG1196   499 -------AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKA 571
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG1196   572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQER 333
Cdd:COG1196   652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG1196   732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
PTZ00121 PTZ00121
MAEBL; Provisional
11-402 2.40e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 87.12  E-value: 2.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   11 FGFGKSDKQQAEQAAKEAdnQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERleqeriaaEKAEAERLEQERIAAEKA 90
Cdd:PTZ00121  1079 FDFDAKEDNRADEATEEA--FGKAEEAKKTETGKAEEARKAEE--AKKKAEDAR--------KAEEARKAEDARKAEEAR 1146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   91 EAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:PTZ00121  1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  171 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL----EQERIAA 246
Cdd:PTZ00121  1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaeEKKKADE 1306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  247 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAE-KAE 325
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKK 1386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  326 AERLEQERIAAEKAEADRLEQERI---AAEKAEAERLEQEriAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLK 402
Cdd:PTZ00121  1387 AEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
PTZ00121 PTZ00121
MAEBL; Provisional
15-404 1.23e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 84.81  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAE---RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 91
Cdd:PTZ00121  1279 KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   92 AERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEqaaa 171
Cdd:PTZ00121  1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD---- 1434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  172 ekaeaerlEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:PTZ00121  1435 --------EAKKKAEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  252 ERLEQERIAAEKA----EAERLEQERIAAEKAEAERLeqeRIAAEKAEADRL---EQERIAAE--KAEAERLEQERIVAE 322
Cdd:PTZ00121  1503 KKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEA---KKAEEKKKADELkkaEELKKAEEkkKAEEAKKAEEDKNMA 1579
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  323 KAEAERLEQ-ERIAAEKAEADRLEQERIAAE---KAEAERLEQERIAEEQAEAERLEQEKVAQA----AAEKPKKEGFFA 394
Cdd:PTZ00121  1580 LRKAEEAKKaEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEEN 1659
                          410
                   ....*....|
gi 1952201083  395 RLKKGLLKTR 404
Cdd:PTZ00121  1660 KIKAAEEAKK 1669
PTZ00121 PTZ00121
MAEBL; Provisional
17-402 2.20e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 84.04  E-value: 2.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEK--AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:PTZ00121  1113 EARKAEEAKKKAEDARKAEEARKAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE 1192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   95 L---EQERIAAERRDAE---RVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:PTZ00121  1193 LrkaEDARKAEAARKAEeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  169 AAAEKAEAERL---EQERIAAEKAEAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 244
Cdd:PTZ00121  1273 KAEEARKADELkkaEEKKKADEAKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  245 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEKAEADRLEQERI---AAEKAEAERLEQERIVA 321
Cdd:PTZ00121  1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELkkaAAAKKKADEAKKKAEEK 1430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  322 EKAEaerlEQERIAAEKAEADRLEQERIAAEKAEaerlEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLL 401
Cdd:PTZ00121  1431 KKAD----EAKKKAEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502

                   .
gi 1952201083  402 K 402
Cdd:PTZ00121  1503 K 1503
PTZ00121 PTZ00121
MAEBL; Provisional
15-390 6.74e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 82.50  E-value: 6.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQE-RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:PTZ00121  1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQ----EAAMKLEQERAAAEQAQREAEQA 169
Cdd:PTZ00121  1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADEAKKKAEED 1403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE--RIAAEKAEAERLEQERIAAE 247
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEAKKKAEEAK 1483
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  248 KAEAERLEQERIAAEKAEAERLEQERIAAEKA----EAERLEQERIAAEKAEADRLeqeRIAAEKAEAERLEQERIVAEK 323
Cdd:PTZ00121  1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEA---KKAEEKKKADELKKAEELKKA 1560
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083  324 AEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEdKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
334-583 1.19e-15

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 77.76  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFfARLKKGLLKTRVNIGSGFAS 413
Cdd:TIGR03499  48 AAIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPE-EELRKELEALRELLERLLAG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 414 IfsGKKIDDELFEELETQLLTADLGVDTTMKLIDNLtdaadrKQLKDGDALYELMKQEMASML--KTAEQPLvvsnDKKP 491
Cdd:TIGR03499 127 L--AWLQRPPERAKLYERLLEAGVSEELARELLEKL------PEDADAEDAWRWLREALEGMLpvKPEEDPI----LEQG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 492 FVILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvvfdaFQAA 569
Cdd:TIGR03499 195 GVIALVGPTGVGKTTTLAKLAARFalEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKVARDPKE--------LREA 266
                         250
                  ....*....|....*.
gi 1952201083 570 KA--RNVDVLIADTAG 583
Cdd:TIGR03499 267 LDrlRDKDLILIDTAG 282
PTZ00121 PTZ00121
MAEBL; Provisional
17-390 4.54e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 76.33  E-value: 4.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:PTZ00121  1051 DIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA 1130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   97 QERIAAErrDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKleqERAAAEQAQREAEQAAAEKAEA 176
Cdd:PTZ00121  1131 EEARKAE--DARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK---AEEVRKAEELRKAEDARKAEAA 1205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  177 ERLEQERIAaekAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:PTZ00121  1206 RKAEEERKA---EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE-KAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:PTZ00121  1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083  336 AEKAEADRL----EQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00121  1363 EEKAEAAEKkkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
30-387 1.11e-13

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 74.39  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  30 NQKQIEEQQRIEaekaEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQERIAAEKAEAERL------EQERIAA 102
Cdd:pfam17380 280 HQKAVSERQQQE----KFEKMEQERLRQEKEEKAReVERRRKLEEAEKARQAEMDRQAAIYAEQERMamererELERIRQ 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 103 E--RRDAERVEQERIAAEkaeAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAaeqaqreaeqaaaekaeaerlE 180
Cdd:pfam17380 356 EerKRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELEAARKVKILEEE---------------------R 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERiaaeKAEAERLEQEriaaEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEER----AREMERVRLE----EQERQQQVERLRQQEEERKRKKLELEKEK 483
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAErlEQERIAAEKAEAERleQERIAAEKAEADRLEQERIAAEKAEAErlEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:pfam17380 484 RDRKRAE--EQRRKILEKELEER--KQAMIEEERKRKLLEKEMEERQKAIYE--EERRREAEEERRKQQEMEERRRIQEQ 557
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1952201083 341 ADRLEQERIAAEKAEAERLEQERIAEeqAEAERLEQEKVAQAAAEKP 387
Cdd:pfam17380 558 MRKATEERSRLEAMEREREMMRQIVE--SEKARAEYEATTPITTIKP 602
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
186-390 2.69e-13

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 73.44  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 186 AEKAEAERLEQERIAAEKAEaERLE--QERIAAEKAE-AERLEQ--ERIAAEKAEAERLEQERIAAEKAEAerleqERIA 260
Cdd:PRK05035  433 QAKAEIRAIEQEKKKAEEAK-ARFEarQARLEREKAArEARHKKaaEARAAKDKDAVAAALARVKAKKAAA-----TQPI 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAA--EKAEAERLEQERIVAEKAEAERLEQERIAA-- 336
Cdd:PRK05035  507 VIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAai 586
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK05035  587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP 640
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
57-317 1.24e-12

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 71.13  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  57 AEKAEAERLEQERIAAEKAeaerleQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQR 136
Cdd:PRK05035  433 QAKAEIRAIEQEKKKAEEA------KARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 137 QEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAaeKAEAERLEQERIAAEKAEAERLEQERIAA 216
Cdd:PRK05035  507 VIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA--RAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 217 --EKAEAERLEQERIAAEKAEAERLEQERIAA-----EKAEAERLEQERiAAEKAEAERLEQERIAAE--KAEAERLEQE 287
Cdd:PRK05035  585 aiARAKAKKAAQQAASAEPEEQVAEVDPKKAAvaaaiARAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQ 663
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1952201083 288 RIAAEKAEADRLEQERIAAE--KAEAERLEQE 317
Cdd:PRK05035  664 QANAEPEEAEDPKKAAVAAAiaRAKAKKAAQQ 695
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
490-616 3.42e-12

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 64.70  E-value: 3.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  490 KPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVwgernsIPVIAQHTGADSASVVFDAFQAA 569
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL------IIVGGKKASGSGELRLRLALALA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1952201083  570 KARNVDVLIADTAGRLQNKDNLMQELEKI-ARVMKKIDPDAPHEVMLT 616
Cdd:smart00382  75 RKLKPDVLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILT 122
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
88-390 4.50e-12

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 69.38  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  88 EKAEAERLEQERIaaerrdaERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:pfam17380 281 QKAVSERQQQEKF-------EKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEKA---EAERLEQERiaaeKAEAERLEQERIAAEKAEAERLEQER-IAAEKAEAERLEQER 243
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISrmrELERLQMER----QQKNERVRQELEAARKVKILEEERQRkIQQQKVEMEQIRAEQ 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 244 IAAEKAEAERLEQERiaaeKAEAERLEQEriaaEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErlEQERIVAEK 323
Cdd:pfam17380 430 EEARQREVRRLEEER----AREMERVRLE----EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE--EQRRKILEK 499
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 324 AEAER----LEQERiAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam17380 500 ELEERkqamIEEER-KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
SRP54_N smart00963
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ...
406-476 7.67e-12

SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.


Pssm-ID: 214941 [Multi-domain]  Cd Length: 77  Bit Score: 61.41  E-value: 7.67e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083  406 NIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADR---KQLKDGDALYELMKQEMASML 476
Cdd:smart00963   4 ALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGevlKGLTPKQEVKKILKEELVKIL 77
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
228-333 9.64e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 68.61  E-value: 9.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  228 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEADRLEQERIaa 306
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
                           90       100
                   ....*....|....*....|....*..
gi 1952201083  307 ekaeaERLEQERIvaEKAEAERLEQER 333
Cdd:PTZ00266   505 -----DRLERERV--DRLERDRLEKAR 524
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
183-288 1.17e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 68.23  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  183 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEAERLEQERIaa 261
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
                           90       100
                   ....*....|....*....|....*..
gi 1952201083  262 ekaeaERLEQERIaaEKAEAERLEQER 288
Cdd:PTZ00266   505 -----DRLERERV--DRLERDRLEKAR 524
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
76-386 1.18e-11

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 66.48  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  76 EAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQE 155
Cdd:pfam13868  25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 156 RAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA- 234
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEr 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 235 EAERL--EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAE 312
Cdd:pfam13868 185 EIARLraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFE 264
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 313 RLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEK 386
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
258-363 1.45e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 67.84  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  258 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEADRLEQERIaaEKAEAERLEQERIVAEKAEAERLEQERIaa 336
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-- 504
                           90       100
                   ....*....|....*....|....*..
gi 1952201083  337 ekaeaDRLEQERIaaEKAEAERLEQER 363
Cdd:PTZ00266   505 -----DRLERERV--DRLERDRLEKAR 524
PTZ00121 PTZ00121
MAEBL; Provisional
89-398 5.85e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 5.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   89 KAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQ 168
Cdd:PTZ00121  1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  169 AAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEk 248
Cdd:PTZ00121  1141 KAEEARKAEDAKRVEIARKAEDARKAEEARKAED---AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE- 1216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  249 aeAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PTZ00121  1217 --ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  329 LeqeRIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKK 398
Cdd:PTZ00121  1295 A---KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
flhF PRK14722
flagellar biosynthesis regulator FlhF; Provisional
326-677 7.55e-11

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 173185 [Multi-domain]  Cd Length: 374  Bit Score: 64.36  E-value: 7.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 326 AERLEQERIAAEKAeADRLEQERIAAE----KAEAERLEQERIAEEQAEAERLEQEKVAQAA-AEKPKKEGFFARLKKGL 400
Cdd:PRK14722    5 ARRLPADEPAAAKP-ALRLPEDTAAAVadavKARIERIVNDTVMQELGSLRELMEEQFAGLMwNERQRRNPVHGALTKYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 401 lktrvnigsgFASIFSGKKIddelfeeletqlltadlgvdttMKLIDNLTDAADRKQLkdgDALYELMKQEMASMLktae 480
Cdd:PRK14722   84 ----------FAAGFSAQLV----------------------RMIVDNLPEGEGYDTL---DAAADWAQSVLAANL---- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 481 qPLVVSND---KKPFVILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTG 555
Cdd:PRK14722  125 -PVLDSEDalmERGGVFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDG 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 556 ADSASVVfdafqaAKARNVDVLIADTAGRLQNKDNLMQELEKIArvmkkiDPDAPHEVMLTIDAGTGQNAISQV-KLFNE 634
Cdd:PRK14722  204 GDLQLAL------AELRNKHMVLIDTIGMSQRDRTVSDQIAMLH------GADTPVQRLLLLNATSHGDTLNEVvQAYRS 271
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 635 CVG--------LTGITLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGIDD 677
Cdd:PRK14722  272 AAGqpkaalpdLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
14-114 1.28e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 64.76  E-value: 1.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   14 GKSDKQQAEQAAKEADN------QKQIEEQQRIE-AEKAEAERLEQERIaaekaeaERLEQERIAAEKAEAERLEQERIa 86
Cdd:PTZ00266   428 GRVDKDHAERARIEKENahrkalEMKILEKKRIErLEREERERLERERM-------ERIERERLERERLERERLERDRL- 499
                           90       100
                   ....*....|....*....|....*...
gi 1952201083   87 aEKAEAERLEQERIaaERRDAERVEQER 114
Cdd:PTZ00266   500 -ERDRLDRLERERV--DRLERDRLEKAR 524
PRK12726 PRK12726
flagellar biosynthesis regulator FlhF; Provisional
493-677 1.70e-10

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183704 [Multi-domain]  Cd Length: 407  Bit Score: 63.60  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAqhtgADSASVVFDAFQAAKAR 572
Cdd:PRK12726  208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIV----ATSPAELEEAVQYMTYV 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 573 N-VDVLIADTAGRlqnkdNLMQElEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAK 651
Cdd:PRK12726  284 NcVDHILIDTVGR-----NYLAE-ESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITKMDETTR 357
                         170       180
                  ....*....|....*....|....*.
gi 1952201083 652 GGVIFAVADKFNIPIRYIGVGEGIDD 677
Cdd:PRK12726  358 IGDLYTVMQETNLPVLYMTDGQNITE 383
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
187-389 1.98e-10

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 63.82  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaekaEAERLEQERIAAEKAEA 266
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELE-------QQRRFEEIRLRKQRLEE 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 267 ERLEQERIAAEKAEAERLEQERIAAEKAEADR-LEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLE 345
Cdd:pfam15709 399 ERQRQEEEERKQRLQLQAAQERARQQQEEFRRkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 478
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952201083 346 QERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:pfam15709 479 YQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
288-395 2.98e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 63.60  E-value: 2.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  288 RIAAEKAEADRLEQERIAAEKAEAERLEQERIV-AEKAEAERLEQERIaaEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRLDR 506
                           90       100       110
                   ....*....|....*....|....*....|
gi 1952201083  367 -EQAEAERLEQEKVaqaaaEKPKKEGFFAR 395
Cdd:PTZ00266   507 lERERVDRLERDRL-----EKARRNSYFLK 531
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
493-687 3.24e-10

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 63.09  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQF--QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTgADSASVVFDAFQaaK 570
Cdd:PRK12727  352 VIALVGPTGAGKTTTIAKLAQRFaaQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAESLLDLLE--R 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVDVLIADTAGRLQNKDNLMQELE--KIARVMKKidpdaphevMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDG 648
Cdd:PRK12727  426 LRDYKLVLIDTAGMGQRDRALAAQLNwlRAARQVTS---------LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDE 496
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1952201083 649 TAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFI 687
Cdd:PRK12727  497 TGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLV 536
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
72-382 4.49e-10

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 63.04  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  72 AEKAEAERLEQERIAAEKAEaERLE--QERIaaerrdaERVEQERIAAEKAEAERLAQEQQAAEQqrqeqqarlaeqeAA 149
Cdd:PRK05035  433 QAKAEIRAIEQEKKKAEEAK-ARFEarQARL-------EREKAAREARHKKAAEARAAKDKDAVA-------------AA 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 150 MkleqeraaaeqaqreaeqaaaEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 229
Cdd:PRK05035  492 L---------------------ARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAV 550
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AA--EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleqeriaAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:PRK05035  551 AAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK--------AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA 622
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 308 KAEAERLEQERiVAEKAEAERLEQERIAAE--KAEADRLEQERIAAEKAEAERLEQERIAeeqAEAERLEQEKVAQA 382
Cdd:PRK05035  623 RAKAKKAEQQA-NAEPEEPVDPRKAAVAAAiaRAKARKAAQQQANAEPEEAEDPKKAAVA---AAIARAKAKKAAQQ 695
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
28-362 5.55e-10

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 61.47  E-value: 5.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  28 ADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERiaaEKAEAERLEQERIAAEKAEAERLEQERIAAERRDA 107
Cdd:pfam13868  22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK---EEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 108 ERVEQERIAAEKAEAERlaqeqqaaeqqrQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAE 187
Cdd:pfam13868  99 EREQMDEIVERIQEEDQ------------AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 188 KAEAERLEQERIAAEKAEaeRLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 267
Cdd:pfam13868 167 REEEREAEREEIEEEKER--EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 268 RLEQERIAAEKAEAERLEQERIAAEKAEADRLEQEriAAEKAEAERL----EQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:pfam13868 245 IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE--EAEKRRMKRLehrrELEKQIEEREEQRAAEREEELEEGERLRE 322
                         330
                  ....*....|....*....
gi 1952201083 344 LEQERIAAEKAEAERLEQE 362
Cdd:pfam13868 323 EEAERRERIEEERQKKLKE 341
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
17-317 1.73e-09

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 59.93  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:pfam13868  40 EEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:pfam13868 120 EKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:pfam13868 200 KA---ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 255 EQERIA--AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQE 317
Cdd:pfam13868 277 EQEEAEkrRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
PTZ00121 PTZ00121
MAEBL; Provisional
15-297 1.90e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 1.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRI-EAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIaaekAEAE 93
Cdd:PTZ00121  1523 KADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVM 1598
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  174 AEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:PTZ00121  1679 EAKKAEEDEKKAAEALKKE--AEEAKKAEELKKKEAEEKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1952201083  252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAD 297
Cdd:PTZ00121  1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
PTZ00121 PTZ00121
MAEBL; Provisional
185-404 2.35e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  185 AAEKAEAERLEQERIAAEkaEAERLEQERIAAEKAEAE---RLEQER---IAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:PTZ00121  1120 AKKKAEDARKAEEARKAE--DARKAEEARKAEDAKRVEiarKAEDARkaeEARKAEDAKKAEAARKAEEVRKAEELRKAE 1197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  259 IAAEKAEAERLEQERIAaekAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEK 338
Cdd:PTZ00121  1198 DARKAEAARKAEEERKA---EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083  339 AEADRLEQERIAAEKAEAERLeqeRIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTR 404
Cdd:PTZ00121  1275 EEARKADELKKAEEKKKADEA---KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
39-125 5.74e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 59.75  E-value: 5.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   39 RIEAEKAEAERLEQERIAAEKAEAERLEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAERRDAERVEQERI-A 116
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRLdR 506

                   ....*....
gi 1952201083  117 AEKAEAERL 125
Cdd:PTZ00266   507 LERERVDRL 515
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
174-389 8.13e-09

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 58.81  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:PRK05035  465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAAD 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAA--EKAEADRLEQERIAAEKAEAERLEQERIVA-----EKA 324
Cdd:PRK05035  545 PKKAAVAAaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAaiARAKAKKAAQQAASAEPEEQVAEVDPKKAAvaaaiARA 624
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 325 EAERLEQERIAAEKAEAD-RLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE-KPKK 389
Cdd:PRK05035  625 KAKKAEQQANAEPEEPVDpRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARaKAKK 691
SRP54_N pfam02881
SRP54-type protein, helical bundle domain;
407-472 9.74e-09

SRP54-type protein, helical bundle domain;


Pssm-ID: 460734 [Multi-domain]  Cd Length: 75  Bit Score: 52.47  E-value: 9.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 407 IGSGFASIFSGKKIDDELFEE----LETQLLTADLGVDTTMKLIDNLTDAA-DRKQLKDGDALYELMKQEM 472
Cdd:pfam02881   5 LSSLFKGLRGKGKIDEEDLEEalkeLEEALLEADVGVEVVKKIIERLREKAvGEKKLKPPQEVKKILKEEL 75
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
179-258 1.02e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 58.60  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  179 LEQERIA-AEKAEAERLEQERIaaEKAEAERLEQERIAAEKAEAERLEQERIaaekaeaERLEQERIaaEKAEAERLEQE 257
Cdd:PTZ00266   455 LEKKRIErLEREERERLERERM--ERIERERLERERLERERLERDRLERDRL-------DRLERERV--DRLERDRLEKA 523

                   .
gi 1952201083  258 R 258
Cdd:PTZ00266   524 R 524
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
18-325 1.03e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 57.62  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEAER 94
Cdd:pfam13868  35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEED 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAeka 174
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRA--- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 eaerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:pfam13868 192 -----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 255 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAE 325
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
flhF PRK06731
flagellar biosynthesis regulator FlhF; Validated
488-675 1.38e-08

flagellar biosynthesis regulator FlhF; Validated


Pssm-ID: 75717 [Multi-domain]  Cd Length: 270  Bit Score: 56.68  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 488 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 567
Cdd:PRK06731   72 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 568 AAKARNVDVLIADTAGRLQNKDnlmQELEKIARVMKKIDPDApheVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLD 647
Cdd:PRK06731  149 FKEEARVDYILIDTAGKNYRAS---ETVEEMIETMGQVEPDY---ICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFD 222
                         170       180
                  ....*....|....*....|....*...
gi 1952201083 648 GTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK06731  223 ETASSGELLKIPAVSSAPIVLMTDGQDV 250
PRK12724 PRK12724
flagellar biosynthesis regulator FlhF; Provisional
493-675 1.62e-08

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183703 [Multi-domain]  Cd Length: 432  Bit Score: 57.28  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLA-KQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTgadsasvvFDAFQAAKA 571
Cdd:PRK12724  225 VVFFVGPTGSGKTTSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKD--------IKKFKETLA 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 572 RNVDVLI-ADTAGRLQNKdnlMQELEKIARVMKKIDPDAPHEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTA 650
Cdd:PRK12724  297 RDGSELIlIDTAGYSHRN---LEQLERMQSFYSCFGEKDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEAD 373
                         170       180
                  ....*....|....*....|....*
gi 1952201083 651 KGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK12724  374 FLGSFLELADTYSKSFTYLSVGQEV 398
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
63-388 2.55e-08

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 57.33  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  63 ERLEQERIAAEKAEAErLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQAR 142
Cdd:NF033838   99 EYLYELNVLKEKSEAE-LTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 143 LAEQEAAMKLEQERAAAEQAQREAEQAAAEKAeaerleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:NF033838  178 IAESDVEVKKAELELVKEEAKEPRDEEKIKQA------KAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 223 RLEQERIAAEKAEAER--LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEADRLE 300
Cdd:NF033838  252 NVATSEQDKPKRRAKRgvLGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRN 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 301 QERIAAEKAEAERLEQERIVAEkAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE----QERIAEEQAEAERLEQ 376
Cdd:NF033838  331 YPTNTYKTLELEIAESDVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEkiktDRKKAEEEAKRKAAEE 409
                         330
                  ....*....|..
gi 1952201083 377 EKVAQAAAEKPK 388
Cdd:NF033838  410 DKVKEKPAEQPQ 421
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
15-257 3.22e-08

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 56.88  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEE--QQRIEAEKAE-AERLEQ--ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE- 88
Cdd:PRK05035  435 KAEIRAIEQEKKKAEEAKARFEarQARLEREKAArEARHKKaaEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARp 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  89 ------KAEAERLEQERIAAERRDAERVEQERIAA-----EKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERA 157
Cdd:PRK05035  515 dnsaviAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKA 594
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 158 AAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 237
Cdd:PRK05035  595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEE-PVDPRKAAVAAAIARAKARKAAQQQANAEPEEAE 673
                         250       260
                  ....*....|....*....|..
gi 1952201083 238 RLEQERIAAE--KAEAERLEQE 257
Cdd:PRK05035  674 DPKKAAVAAAiaRAKAKKAAQQ 695
flhF PRK11889
flagellar biosynthesis protein FlhF;
488-675 3.32e-08

flagellar biosynthesis protein FlhF;


Pssm-ID: 183360 [Multi-domain]  Cd Length: 436  Bit Score: 56.61  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 488 DKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHtgaDSASVVFDAFQ 567
Cdd:PRK11889  238 EKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR---DEAAMTRALTY 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 568 AAKARNVDVLIADTAGRlqnKDNLMQELEKIARVMKKIDPDApheVMLTIDAG-TGQNAISQVKLFNEcVGLTGITLSKL 646
Cdd:PRK11889  315 FKEEARVDYILIDTAGK---NYRASETVEEMIETMGQVEPDY---ICLTLSASmKSKDMIEIITNFKD-IHIDGIVFTKF 387
                         170       180
                  ....*....|....*....|....*....
gi 1952201083 647 DGTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK11889  388 DETASSGELLKIPAVSSAPIVLMTDGQDV 416
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
233-390 5.04e-08

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 56.03  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 233 KAEAERLEQERIAaeKAEAERLEQERIA-----AEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:COG2268   192 RKIAEIIRDARIA--EAEAERETEIAIAqanreAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAETARAEAEAAY 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 308 KAEAERLEQERI----VAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErleqeriAEEQAEAERLEQEKVAQAA 383
Cdd:COG2268   269 EIAEANAEREVQrqleIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE-------AEAEAEAEAIRAKGLAEAE 341

                  ....*..
gi 1952201083 384 AEKPKKE 390
Cdd:COG2268   342 GKRALAE 348
valS PRK14900
valyl-tRNA synthetase; Provisional
189-390 1.05e-07

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 55.38  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  189 AEAERLEQE--RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERL----EQERIA 260
Cdd:PRK14900   842 AETARVDKEigKVDQDLAVLERKLQNPSFVQNAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEANSArrdtMEIQNE 921
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:PRK14900   922 QKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAP 1001
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1952201083  341 ADRLEQERIAAEKAEAerleqERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK14900  1002 AKKAAAKKAAAKKAAA-----KKKVAKKAPAKKVARKPAAKKAAKKPARK 1046
PRK12723 PRK12723
flagellar biosynthesis regulator FlhF; Provisional
490-675 1.32e-07

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183702 [Multi-domain]  Cd Length: 388  Bit Score: 54.52  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 490 KPFVILMVGVNGVGKTTTIGKLAKQF----QNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVFDa 565
Cdd:PRK12723  173 KKRVFILVGPTGVGKTTTIAKLAAIYginsDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQ- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 566 fqaakARNVDVLIADTAGRlQNKDNLmqELEKIARVMKKIDPDAphEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSK 645
Cdd:PRK12723  252 -----SKDFDLVLVDTIGK-SPKDFM--KLAEMKELLNACGRDA--EFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTK 321
                         170       180       190
                  ....*....|....*....|....*....|
gi 1952201083 646 LDGTAKGGVIFAVADKFNIPIRYIGVGEGI 675
Cdd:PRK12723  322 LDETTCVGNLISLIYEMRKEVSYVTDGQIV 351
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
180-409 1.33e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 54.66  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 256
Cdd:COG3064    15 QERLEQAEAEKRAAAEAEQKAKEEAEEERLaelEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG3064    95 AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 337 EKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGS 409
Cdd:COG3064   175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
212-660 1.49e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 54.66  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 212 ERIAAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 291
Cdd:COG3064     6 EEKAAEAAAQERLEQAE-AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 292 EKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:COG3064    85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 372 ERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTD 451
Cdd:COG3064   165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 452 AADRKQLKDGDALYELMKQEMASMLKTAEQPLVVSNDKkpfVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFR 531
Cdd:COG3064   245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVA---AALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 532 AAAVEQLQVWGERNSIPVIAQHTGADSASVVFDAFQAAKARNVDVLIADTAGRLQNKDNLMQELEKIARVMKKIDPDAPH 611
Cdd:COG3064   322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1952201083 612 EVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTAKGGVIFAVAD 660
Cdd:COG3064   402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVG 450
flhF PRK14723
flagellar biosynthesis regulator FlhF; Provisional
493-691 1.69e-07

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 237802 [Multi-domain]  Cd Length: 767  Bit Score: 54.81  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADsasvVFDAFQAAK 570
Cdd:PRK14723  187 VLALVGPTGVGKTTTTAKLAARCvAREGADqLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAAD----LRFALAALG 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVmkkidpDAPHEVMLTIdagtgqNAISQVKLFNECV---------GLTGI 641
Cdd:PRK14723  263 DKHL-VLI-DTVGMSQRDRNVSEQIAMLCGV------GRPVRRLLLL------NAASHGDTLNEVVhayrhgageDVDGC 328
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 642 TLSKLDGTAKGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFIDALF 691
Cdd:PRK14723  329 IITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVpEHLELAQADELVDRAF 379
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
187-390 1.93e-07

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 53.77  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 266
Cdd:pfam13868  83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 267 ERLEQERIAAEKAEAERLEQERIAAEKAEadrlEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQ 346
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRA----QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ 238
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1952201083 347 ERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
200-410 2.26e-07

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: 53.31  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 279
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 280 EaeRLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERL 359
Cdd:TIGR02794 126 A--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 360 EQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSG 410
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
179-376 2.78e-07

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 54.23  E-value: 2.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  179 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-------KAEAER---LEQERIAAEKAEAErlEQERIAAEK 248
Cdd:TIGR00927  630 LSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEqegetetKGENESegeIPAERKGEQEGEGE--IEAKEADHK 707
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA----AEKAEADRLEQERIAAEKAEAERLEQE-RIVAEK 323
Cdd:TIGR00927  708 GETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAegkhEVETEGDRKETEHEGETEAEGKEDEDEgEIQAGE 787
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083  324 ----------AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQ 376
Cdd:TIGR00927  788 dgemkgdegaEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEK 850
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
10-366 4.06e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.44  E-value: 4.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   10 WFGFGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 89
Cdd:pfam02463  657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAE--RLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAE 167
Cdd:pfam02463  737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSlkEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAEL 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  168 QAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:pfam02463  817 LEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK 896
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  248 KAEAERLEQERIAAEKAEAERLEQERIAAEK-------AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIV 320
Cdd:pfam02463  897 EEKKELEEESQKLNLLEEKENEIEERIKEEAeillkyeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1952201083  321 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:pfam02463  977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
COG3899 COG3899
Predicted ATPase [General function prediction only];
19-385 4.48e-07

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 53.32  E-value: 4.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   19 QQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE 98
Cdd:COG3899    726 RYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGD 805
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   99 RIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAER 178
Cdd:COG3899    806 YEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAA 885
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  179 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:COG3899    886 LAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAA 965
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  259 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEK 338
Cdd:COG3899    966 AAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALAL 1045
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1952201083  339 AEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3899   1046 LAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAAL 1092
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
180-375 5.84e-07

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.08  E-value: 5.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  180 EQERIAAEKAEAErLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:TIGR00927  672 ETETKGENESEGE-IPAERKGEQEGEGE--IEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGE 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  260 A----AEKAEAERLEQERIAAEKAEAERLEQE-RIAAEK----------AEADRLEQERIAAEKAEAERLEQERIVAEKA 324
Cdd:TIGR00927  749 AegkhEVETEGDRKETEHEGETEAEGKEDEDEgEIQAGEdgemkgdegaEGKVEHEGETEAGEKDEHEGQSETQADDTEV 828
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083  325 EAERLEQERIAAEKAEA-------------DRLEQERIAAEKAEAERLEQERIAEEQAEAERLE 375
Cdd:TIGR00927  829 KDETGEQELNAENQGEAkqdekgvdggggsDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
15-371 5.95e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 52.73  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 94
Cdd:COG3064    12 AAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:COG3064    92 KAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:COG3064   172 ARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:COG3064   252 ADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRG 331
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:COG3064   332 GGAASLEAALSLLAAGAAAAAAGAGALATGALGDALA 368
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
183-372 7.90e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 51.73  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 183 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 262
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 263 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEAD 342
Cdd:PRK09510  145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
                         170       180       190
                  ....*....|....*....|....*....|
gi 1952201083 343 RLEQERIAAEKAEAERLEQERIAEEQAEAE 372
Cdd:PRK09510  225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
13-405 9.85e-07

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 52.28  E-value: 9.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:pfam02463  625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   93 ERLEQERIAAERRDAERVEQERI--AAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:pfam02463  705 EQREKEELKKLKLEAEELLADRVqeAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  171 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 250
Cdd:pfam02463  785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  251 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA--EAERLEQERIVAEKAEAER 328
Cdd:pfam02463  865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIkeEAEILLKYEEEPEELLLEE 944
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083  329 LEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRV 405
Cdd:pfam02463  945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
17-385 1.20e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.58  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERL-------EQERIAAEKAEAERLEQERIAAEK 89
Cdd:COG3064    37 EEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAaaeaekkAAAEKAKAAKEAEAAAAAEKAAAA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQA 169
Cdd:COG3064   117 AEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 249
Cdd:COG3064   197 AAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSS 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:COG3064   277 GLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAG 356
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 330 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3064   357 ALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALL 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
143-396 1.29e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  143 LAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  223 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEADRLEQe 302
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE--AANLRERLESLERRIAATERRLEDLEE- 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  303 RIAAEKAEAERLEQErIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:TIGR02168  846 QIEELSEDIESLAAE-IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          250
                   ....*....|....
gi 1952201083  383 AAEKPKKEGFFARL 396
Cdd:TIGR02168  925 AQLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
186-411 1.30e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  186 AEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAERLEQERIAA--EKAEAERLEQERIAAEKAEAERLEQERIAAE 262
Cdd:TIGR02168  277 SELEEEIEELQKELYALANEISRLEQQkQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEELESL 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  263 KAEAERLEQERIAAEKAEAErLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEA-ERLEQERIAAEKAEA 341
Cdd:TIGR02168  357 EAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAEL 435
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  342 DRLeQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGF 411
Cdd:TIGR02168  436 KEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
180-390 1.69e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 50.69  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER---------IAAEKAEAERLEQERIAAEKAE 250
Cdd:pfam13868  52 ERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEReqmdeiverIQEEDQAEAEEKLEKQRQLREE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAA------EKAEAERLEQERIVAEKA 324
Cdd:pfam13868 132 IDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArlraqqEKAQDEKAERDELRAKLY 211
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 325 EAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:pfam13868 212 QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
11-344 1.70e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   11 FGFGKSDKQQAEQAAKEADNQKQIEEQQRIEAE--------KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 82
Cdd:TIGR02168  663 GGSAKTNSSILERRREIEELEEKIEELEEKIAElekalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   83 ERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQqrqeqqarlaeQEAAMKLEQERAAAEQA 162
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------KEELKALREALDELRAE 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  163 QREAEQAAAEKAEAERLEQERIAAEKAEAERLEQeRIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEAERLEQE 242
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLE 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  243 RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAE 322
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
                          330       340
                   ....*....|....*....|..
gi 1952201083  323 KAEAERLEQERIAAEKAEADRL 344
Cdd:TIGR02168  963 IEDDEEEARRRLKRLENKIKEL 984
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
17-267 1.90e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAE--KAEAERLEQERIAAEKA---EAERLEQERiaaeKAEAERLEQERIAAEKAE 91
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELERIRQEerKRELERIRQEEIAMEISrmrELERLQMER----QQKNERVRQELEAARKVK 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  92 AERLEQER-IAAERRDAERVEQERIAAEKAEAERLAQEQQ-------AAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQ 163
Cdd:pfam17380 406 ILEEERQRkIQQQKVEMEQIRAEQEEARQREVRRLEEERAremervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 164 REAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 243
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER 565
                         250       260
                  ....*....|....*....|....*
gi 1952201083 244 IAAEKAEAER-LEQERIAAEKAEAE 267
Cdd:pfam17380 566 SRLEAMEREReMMRQIVESEKARAE 590
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
181-400 2.19e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKaEAERLEQERIAAEKAEAERleQERIAAEKAEAERLEQERIAAEKAEAERleQERIA 260
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLK-QLAALERRIAALARRIRAL--EQELAALEAELAELEKEIAELRAELEAQ--KEELA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQ----ERIAAEKAEADRLEQERIAAEKAEAERLEQErIVAEKAEAERLEQERIAA 336
Cdd:COG4942   108 ELLRALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRAE-LEAERAELEALLAELEEE 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 337 EKA-EADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE----KVAQAAAEKPKKEGFFARLKKGL 400
Cdd:COG4942   187 RAAlEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiarlEAEAAAAAERTPAAGFAALKGKL 255
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
194-391 2.64e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 50.76  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  194 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErLEQERIAAEKAEAErlEQER 273
Cdd:TIGR00927  630 LSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQEGEGE--IEAK 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  274 IAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQER----IVAEKAEAERLEQERIAAEKAEADRLEQE-- 347
Cdd:TIGR00927  703 EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGeaegKHEVETEGDRKETEHEGETEAEGKEDEDEge 782
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  348 -------RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:TIGR00927  783 iqagedgEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETG 833
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
198-385 4.13e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 198 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAE 277
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE-EAAAKAAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 278 KAEAERLEQERIAAE-----KAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAE 352
Cdd:PRK09510  144 AAKAKAEAEAKRAAAaakkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1952201083 353 KAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK09510  224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
180-356 6.68e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.03  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK---AEAERLEQERIAAEKAEAERLEQ 256
Cdd:PRK09510   78 EEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAAAKAKAEAEAKRA 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 257 ERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAD-RLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:PRK09510  157 AAAAKKaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
                         170       180
                  ....*....|....*....|..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEA 356
Cdd:PRK09510  237 AAEKAAAAKAAEKAAAAKAAAE 258
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
23-396 8.75e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  23 QAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAA------EKAEAERLEQERIAAEKAEAE---RLEQERIAAEKA--E 91
Cdd:PRK02224  264 RETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglDDADAEAVEARREELEDRDEElrdRLEECRVAAQAHneE 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  92 AERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:PRK02224  344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQERIAAEK--AEAERL-------EQERIAAEKAEAERLEQERIAAEKAEAE----RLEQERIAAEKAEAER 238
Cdd:PRK02224  424 LREREAELEATLRTARErvEEAEALleagkcpECGQPVEGSPHVETIEEDRERVEELEAEledlEEEVEEVEERLERAED 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 239 L-EQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQEriaAEKAEADRLEQERIAAEKAEAERLEQE 317
Cdd:PRK02224  504 LvEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAELNS 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 318 RIVAEKAEAERLE-----QERIAAEKAEADRLEQERiaAEKAEAERLEQERIAEE----QAEAERLEQEKVAQAAAEKPK 388
Cdd:PRK02224  580 KLAELKERIESLErirtlLAAIADAEDEIERLREKR--EALAELNDERRERLAEKrerkRELEAEFDEARIEEAREDKER 657

                  ....*...
gi 1952201083 389 KEGFFARL 396
Cdd:PRK02224  658 AEEYLEQV 665
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
15-372 9.00e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.88  E-value: 9.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEE-QQRIEAEKA----EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 89
Cdd:COG3064    67 RAAELAAEAAKKLAEAEKAAAEaEKKAAAEKAkaakEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  90 AEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQA 169
Cdd:COG3064   147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAA 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 170 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 249
Cdd:COG3064   227 AASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:COG3064   307 LLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEA 386
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1952201083 330 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAE 372
Cdd:COG3064   387 AGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGA 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-390 9.78e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLE-QERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAeKAEAERLE 96
Cdd:PRK02224  229 REQARETRDEADEVLEEHEERREELETLEAEIEDlRETIAETEREREEL-AEEVRDLRERLEELEEERDDL-LAEAGLDD 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  97 QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEA 176
Cdd:PRK02224  307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 177 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAE-------------------- 235
Cdd:PRK02224  387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEalleagkcpecgqpvegsph 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 236 AERLEQERIAAEKAEAE----RLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAAEKAEADRlEQERIAAEKAE 310
Cdd:PRK02224  467 VETIEEDRERVEELEAEledlEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRER 545
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 311 AERLEQErivAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE-----QERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK02224  546 AAELEAE---AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtlLAAIADAEDEIERLREKREALAELN 622

                  ....*
gi 1952201083 386 KPKKE 390
Cdd:PRK02224  623 DERRE 627
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
180-356 1.16e-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: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:TIGR02794  87 EQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA---AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA 339
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASG 243
                         170
                  ....*....|....*..
gi 1952201083 340 EADRLEQERIAAEKAEA 356
Cdd:TIGR02794 244 SNAEKQGGARGAAAGSE 260
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
46-382 1.17e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 48.68  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   46 EAERLEQERIAAEKAEAERLEqeRIAAEKAEAERLEQERIAAEKAEAE--RLEQERIAAERRDAERvEQERIAAEKAEAE 123
Cdd:pfam12128  214 PKSRLNRQQVEHWIRDIQAIA--GIMKIRPEFTKLQQEFNTLESAELRlsHLHFGYKSDETLIASR-QEERQETSAELNQ 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  124 RLAQEQQAAEQQRQEQQARLAEQEAAMKleqeraaaeqaqREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 203
Cdd:pfam12128  291 LLRTLDDQWKEKRDELNGELSAADAAVA------------KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  204 AEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEA 281
Cdd:pfam12128  359 LEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEE 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  282 ERLEQERIAAEKAeadrleqeRIAAEKAEAERLEQERIVAEKAEAERLEQEriaAEKAEADRLEQERIAAEKA-----EA 356
Cdd:pfam12128  439 EYRLKSRLGELKL--------RLNQATATPELLLQLENFDERIERAREEQE---AANAEVERLQSELRQARKRrdqasEA 507
                          330       340
                   ....*....|....*....|....*.
gi 1952201083  357 ERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:pfam12128  508 LRQASRRLEERQSALDELELQLFPQA 533
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
17-377 1.26e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG4717   120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  97 -----QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMkLEQERAAAEQAQREAEQAAA 171
Cdd:COG4717   200 eleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGV 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 172 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 251
Cdd:COG4717   279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 252 ERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ 331
Cdd:COG4717   359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE 438
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1952201083 332 ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQE 377
Cdd:COG4717   439 EELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
182-391 1.27e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 48.68  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  182 ERIAAEKAEAERLEQEriaaEKAEA--ERLEQER------IAAEKAEAERLEQERIAAeKAEAER----LEQERIAAEKA 249
Cdd:NF012221  1549 KHAKQDDAAQNALADK----ERAEAdrQRLEQEKqqqlaaISGSQSQLESTDQNALET-NGQAQRdailEESRAVTKELT 1623
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  250 E-AERLEQERIAAEKAE----------AERLeQERIAAEKAEAERLEQERIAAEK-AEADRLEQERIAAEKAEA--ERLE 315
Cdd:NF012221  1624 TlAQGLDALDSQATYAGesgdqwrnpfAGGL-LDRVQEQLDDAKKISGKQLADAKqRHVDNQQKVKDAVAKSEAgvAQGE 1702
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  316 QERIVAE------KAEAERLEQERIAAEKAEADRLEQERIAAEKAEaERLEQE-RIAEEQAEAERLEQEKVAQAAAEKPK 388
Cdd:NF012221  1703 QNQANAEqdiddaKADAEKRKDDALAKQNEAQQAESDANAAANDAQ-SRGEQDaSAAENKANQAQADAKGAKQDESDKPN 1781

                   ...
gi 1952201083  389 KEG 391
Cdd:NF012221  1782 RQG 1784
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
181-366 1.40e-05

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 48.55  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER-IAAEKAEAERLEQ-ERIAAEKAEAERL---- 254
Cdd:NF033875    80 QKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQpVVSPETTNEPLGQpTEVAPAENEANKStsip 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  255 -EQERIAAEKAEAERLEQERIAAEKAEAERL---EQERIAAEKAEADRLEQEriaaekaeaerleQERIVAEKAEAERLE 330
Cdd:NF033875   160 kEFETPDVDKAVDEAKKDPNITVVEKPAEDLgnvSSKDLAAKEKEVDQLQKE-------------QAKKIAQQAAELKAK 226
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1952201083  331 QERIAAEKAEadrleqerIAAE-KAEAERLEQErIAE 366
Cdd:NF033875   227 NEKIAKENAE--------IAAKnKAEKERYEKE-VAE 254
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
261-391 1.58e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.95  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAE----RLEQERI--AAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQErI 334
Cdd:COG2268   201 ARIAEAEAERETEIAIAQANREaeeaELEQEREieTARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE-V 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 335 AAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:COG2268   280 QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKG 336
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
228-389 1.79e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.49  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 228 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK---AEADRLEQERI 304
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 305 AAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:PRK09510  145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224

                  ....*
gi 1952201083 385 EKPKK 389
Cdd:PRK09510  225 AAAAK 229
PRK12678 PRK12678
transcription termination factor Rho; Provisional
168-328 1.79e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 47.98  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 168 QAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 247
Cdd:PRK12678   64 AAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEA-APAARAAAAAAAEAASAPEAAQARERRERGEAARRGAA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 248 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiaaekaEADRLEQERIAAEKAEAERLEQERIVAEKAEAE 327
Cdd:PRK12678  143 RKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQA------EAERGERGRREERGRDGDDRDRRDRREQGDRRE 216

                  .
gi 1952201083 328 R 328
Cdd:PRK12678  217 E 217
COG3899 COG3899
Predicted ATPase [General function prediction only];
45-385 2.37e-05

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 47.93  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   45 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAER 124
Cdd:COG3899    722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  125 LAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 204
Cdd:COG3899    802 LLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAA 881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  205 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 284
Cdd:COG3899    882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  285 EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERI 364
Cdd:COG3899    962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
                          330       340
                   ....*....|....*....|.
gi 1952201083  365 AEEQAEAERLEQEKVAQAAAE 385
Cdd:COG3899   1042 ALALLAALAAAAAAAAAAAAL 1062
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
18-463 2.47e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 47.34  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERI----AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:COG3064     7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaeleAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:COG3064    87 AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG3064   167 AAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV-AARAAAASREAALAAVEATEEAAL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQER 333
Cdd:COG3064   246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 334 IAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSGFAS 413
Cdd:COG3064   326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952201083 414 IFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDA 463
Cdd:COG3064   406 DLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKAL 455
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
42-284 2.89e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  42 AEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAE 121
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 122 AERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQerIAAEKAEAERLEQERIAA 201
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE--LRADLAELAALRAELEAE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 202 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 281
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252

                  ...
gi 1952201083 282 ERL 284
Cdd:COG4942   253 GKL 255
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
282-392 3.45e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.13  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 282 ERLEQERIAAEK--AEADRLEQEriaAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERL 359
Cdd:PRK00409  523 ASLEELERELEQkaEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1952201083 360 EQERIAEEQAEAERLEQEKVAQAAAEKPKKEGF 392
Cdd:PRK00409  600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-287 3.52e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAERL 95
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTA-ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   96 EQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAerleQERIAAEKAEAERLEQERIAAEKAEAERLE 255
Cdd:TIGR02168  397 SLNNEIERLEARLERLED----RRERLQQEIEELLKKLEEAELKEL----QAELEELEEELEELQEELERLEEALEELRE 468
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1952201083  256 QERIAAEKAEAERLEQERIAAEKAEAERLEQE 287
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDSLERLQEN 500
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
101-390 3.84e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.96  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 101 AAERRDAERVEQERIaaEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLE 180
Cdd:COG3064     4 ALEEKAAEAAAQERL--EQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERiaaEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG3064    82 AEK---AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAE 340
Cdd:COG3064   159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952201083 341 ADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG3064   239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGL 288
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
43-238 3.93e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  43 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---KAEAERLEQERIAAERRDAERVEQERIAAEK 119
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAekmREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 120 AEAERLAQEQQAAEQQRQEQQARlaeQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERI 199
Cdd:pfam15709 406 EERKQRLQLQAAQERARQQQEEF---RRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 238
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
28-396 3.98e-05

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 46.82  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  28 ADNQKQIEE----QQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 103
Cdd:COG5278   100 ADNPEQQARldelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLL 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 104 RRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQER 183
Cdd:COG5278   180 LALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALAL 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 184 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 263
Cdd:COG5278   260 AALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAA 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 264 AEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:COG5278   340 AAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAA 419
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 344 LEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARL 396
Cdd:COG5278   420 EALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVA 472
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
15-364 4.34e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.57  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEEQQRIE--AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:COG3064    85 AAAEAEKKAAAEKAKAAKEAEAAAAAEkaAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:COG3064   165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:COG3064   245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:COG3064   325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1952201083 333 RIAAEKAEADRLEQERIAAEKAEAERLEQERI 364
Cdd:COG3064   405 LDLGAALLEAASAVELRVLLALAGAAGAVVAL 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
34-379 4.74e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 4.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   34 IEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERlEQERIAAERRDAERVEQE 113
Cdd:TIGR02169  192 IIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER-QKEAIERQLASLEE-ELEKLTEEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  114 RIAAEKAEAERLAQEQQAAEqqrqeqqarLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAER 193
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQ---------LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  194 LEqERIAAEKAEAERLeQERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQER 273
Cdd:TIGR02169  341 LE-REIEEERKRRDKL-TEEYAELKEELEDLRAE--LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  274 IAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAErleqerIAAEKAEADRLEQERIAAEK 353
Cdd:TIGR02169  417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------LYDLKEEYDRVEKELSKLQR 490
                          330       340
                   ....*....|....*....|....*.
gi 1952201083  354 aEAERLEQERIAEEQAEAERLEQEKV 379
Cdd:TIGR02169  491 -ELAEAEAQARASEERVRGGRAVEEV 515
mukB PRK04863
chromosome partition protein MukB;
16-361 5.05e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 5.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE--RIAAEKAEAe 93
Cdd:PRK04863   324 SDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEvdELKSQLADY- 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   94 rleQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEK 173
Cdd:PRK04863   403 ---QQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAY 479
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  174 AEAERL--EQERIAAEKAEAERLEQERiaAEKAEAERLEQ--------ERIAAEKAEAERLEQE---RIAAEKAEAERLE 240
Cdd:PRK04863   480 QLVRKIagEVSRSEAWDVARELLRRLR--EQRHLAEQLQQlrmrlselEQRLRQQQRAERLLAEfckRLGKNLDDEDELE 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  241 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAeADRLeQERIAAEKAEAERLEQERI- 319
Cdd:PRK04863   558 QLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA-LARL-REQSGEEFEDSQDVTEYMQq 635
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1952201083  320 VAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQ 361
Cdd:PRK04863   636 LLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNA 677
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
14-270 5.49e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 46.53  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   14 GKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:TIGR00927  649 GERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGE--IEAKEADHKGETEAEEVEHEGETEAEGT 726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   94 RLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKleqeraaaeQAQREAEQAAAEK 173
Cdd:TIGR00927  727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQ---------AGEDGEMKGDEGA 797
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  174 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ---ERIAAEKAEAERLEQERIAAEKAE 250
Cdd:TIGR00927  798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKgvdGGGGSDGGDSEEEEEEEEEEEEEE 877
                          250       260
                   ....*....|....*....|
gi 1952201083  251 AERLEQERIAAEKAEAERLE 270
Cdd:TIGR00927  878 EEEEEEEEEEEENEEPLSLE 897
valS PRK14900
valyl-tRNA synthetase; Provisional
188-358 5.60e-05

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 46.52  E-value: 5.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  188 KAEAERLEQERIAAE--KAEAERLEQERIAAEKAEAERL----EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK14900   873 NAPPAVVEKDRARAEelREKRGKLEAHRAMLSGSEANSArrdtMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAV 952
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA-- 339
Cdd:PRK14900   953 SEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVar 1032
                          170
                   ....*....|....*....
gi 1952201083  340 EADRLEQERIAAEKAEAER 358
Cdd:PRK14900  1033 KPAAKKAAKKPARKAAGRK 1051
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
23-269 5.71e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  23 QAAKEADNQKQIEE-QQRIEAEKAEAERLEQERIAAEKaEAERLEQERIAAEKAEAERleQERIAAEKAEAERLEQERIA 101
Cdd:COG4942    18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLK-QLAALERRIAALARRIRAL--EQELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 102 AERRDAERveQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAeaerleQ 181
Cdd:COG4942    95 LRAELEAQ--KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL------R 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG4942   167 AELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

                  ....*....
gi 1952201083 261 AEKAEAERL 269
Cdd:COG4942   247 GFAALKGKL 255
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
234-302 5.87e-05

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 44.66  E-value: 5.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 234 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEADRLEQE 302
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
219-287 6.39e-05

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 44.66  E-value: 6.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 219 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 287
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
204-272 6.39e-05

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 44.66  E-value: 6.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 204 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 272
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
189-257 6.39e-05

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 44.66  E-value: 6.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 189 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 257
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
66-313 7.43e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  66 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAE 145
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRK 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 146 QEaamkleqeraaaeqaqreaeqaaaekaeaerLEQERIAAEKAEAERLEQERIAAEKAeaeRLEQERIAAEKAEAERLE 225
Cdd:pfam15709 394 QR-------------------------------LEEERQRQEEEERKQRLQLQAAQERA---RQQQEEFRRKLQELQRKK 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 226 QERiAAEKAEAERLEQERIAAEKAEaerlEQERIaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIA 305
Cdd:pfam15709 440 QQE-EAERAEAEKQRQKELEMQLAE----EQKRL-MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAM 513

                  ....*...
gi 1952201083 306 AEKAEAER 313
Cdd:pfam15709 514 KQAQEQAR 521
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
39-315 9.63e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 45.76  E-value: 9.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   39 RIEAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErleqerIAAERRDAERVEQErIAAE 118
Cdd:TIGR00927  635 VAEAE-HTGERTGEEGERPTEAEGENGEESGGEAEQEG----ETETKGENESEGE------IPAERKGEQEGEGE-IEAK 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  119 KAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKlEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQE- 197
Cdd:TIGR00927  703 EADHKGETEAEEVEHEGETEAEGTEDEGEIETG-EEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEg 781
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  198 RIAAEKAEAERLEQERIAAEKAEAERLEqeriaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErlEQERIAAE 277
Cdd:TIGR00927  782 EIQAGEDGEMKGDEGAEGKVEHEGETEA-----GEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAK--QDEKGVDG 854
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1952201083  278 KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLE 315
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
243-390 1.04e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.18  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 243 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEK---AEAERLEQERI 319
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAA 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 320 VAEKAEAERlEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK09510  145 AKAKAEAEA-KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
181-432 1.07e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEkaeaERLEQERIAAEKAEAERLEQERia 260
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEI-- 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  261 aekaEAERLEQERIAAEKAEAER-LEQERIAAEKAEAD----RLEQERIAAEKAEAERLEQERIVAE-KAEAERLEQERI 334
Cdd:TIGR02169  754 ----ENVKSELKELEARIEELEEdLHKLEEALNDLEARlshsRIPEIQAELSKLEEEVSRIEARLREiEQKLNRLTLEKE 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  335 AAEKAEADRLEQERIAAEKAEAERLEQE----RIAEEQAEAERLEQEkVAQAAAEKPKKEGFFARLKKGLLKTRVNIGSG 410
Cdd:TIGR02169  830 YLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEELEAA-LRDLESRLGDLKKERDELEAQLRELERKIEEL 908
                          250       260
                   ....*....|....*....|..
gi 1952201083  411 FASIFSGKKIDDELFEELETQL 432
Cdd:TIGR02169  909 EAQIEKKRKRLSELKAKLEALE 930
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
249-317 1.08e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 43.89  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 249 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA-DRLEQERIAAEKAEAERLEQE 317
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELkHLLEERKEALEKLRAEAREEA 70
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
187-313 1.11e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 187 EKAEAERLEQERiAAEKAEAERLEQERIAAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEAerleqERIAAEKAE 265
Cdd:PRK00409  523 ASLEELERELEQ-KAEEAEALLKEAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-----DEIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952201083 266 AERLEQERIAAEKAEaERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:PRK00409  596 LQKGGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
18-347 1.12e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.39  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKqiEEQQR------------------IEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER 79
Cdd:NF033838  145 TKKVEEAEKKAKDQK--EEDRRnyptntyktleleiaesdVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATR 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  80 LEQERIAAEKAEAErleqeriaaerrdaerveqeriAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAA 159
Cdd:NF033838  223 LEKIKTDREKAEEE----------------------AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 160 EQAQREAEQAAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERL 239
Cdd:NF033838  281 NDAKSSDSSVGEETLPSPSLKPEKKVAE-AEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESD-VKVKEAELELV 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 240 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAerlEQERIAAE--KAEADRLEQERIAAEKAEAERLEQE 317
Cdd:NF033838  359 KEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEE---EAKRKAAEedKVKEKPAEQPQPAPAPQPEKPAPKP 435
                         330       340       350
                  ....*....|....*....|....*....|
gi 1952201083 318 RIVAEKAEAERLEQERiaAEKAEADRLEQE 347
Cdd:NF033838  436 EKPAEQPKAEKPADQQ--AEEDYARRSEEE 463
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
232-358 1.17e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 232 EKAEAERLEQERiAAEKAEAERLEQERIAAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEADrleqeRIAAEKAE 310
Cdd:PRK00409  523 ASLEELERELEQ-KAEEAEALLKEAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEAD-----EIIKELRQ 595
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952201083 311 AERLEQERIVAEKAEaERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:PRK00409  596 LQKGGYASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
215-371 1.35e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 44.97  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 215 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 294
Cdd:PRK13108  287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 295 EADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEA 371
Cdd:PRK13108  365 ETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDP 441
PTZ00491 PTZ00491
major vault protein; Provisional
196-346 1.36e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 45.39  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 196 QEriAAEKAEAERLEQEriaaekaEAERLEQERIAaEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 275
Cdd:PTZ00491  664 QE--AAARHQAELLEQE-------ARGRLERQKMH-DKAKAE---EQRTKLLELQAESAAVESSGQSRAEALAEAEARLI 730
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 276 aeKAEAErLEQERIaaeKAEADRLEQEriaaekAEAERLEQERIVAEKAEAERLEQERI---AAEKAEADRLEQ 346
Cdd:PTZ00491  731 --EAEAE-VEQAEL---RAKALRIEAE------AELEKLRKRQELELEYEQAQNELEIAkakELADIEATKFER 792
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
15-389 1.49e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEA 92
Cdd:PRK03918  196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleERIEELKKEI 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:PRK03918  276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQER--IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 250
Cdd:PRK03918  356 ELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 251 AE-----RLEQERIAAEKAEAERLEQERIAAEKAEA-ERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKA 324
Cdd:PRK03918  436 GKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY 515
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 325 EAERLEqeriaaEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:PRK03918  516 NLEELE------KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
rne PRK10811
ribonuclease E; Reviewed
240-390 1.61e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.03  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  240 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErleqERIAAEKAEADRLEQERIAAEKAEAERLEQERI 319
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEE----PVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV 930
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083  320 VAEKAEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK10811   931 ITESDVAVAQEVAEHAEPvVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVA 1002
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
35-98 1.82e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 43.12  E-value: 1.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083  35 EEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 98
Cdd:pfam15927   6 EEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
235-367 1.90e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.34  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 235 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEaERL 314
Cdd:pfam05672  11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-ERE 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 315 EQERIVAEKAEAERLEQERIAAEKAEADRLEQERIaAEKAEAERLEQERIAEE 367
Cdd:pfam05672  90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKI-MQQEEQERLERKKRIEE 141
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
45-113 1.92e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 43.12  E-value: 1.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  45 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAERRDAERVEQE 113
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
31-332 2.39e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   31 QKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERLEqeriaaERRDAERV 110
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-ELEELQEELKEAEEELEELTAELQELEEKLE------ELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  111 EQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLE-QERIAAEKA 189
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEA 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  190 EAERLEQERIAAEKAEAErLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA-ERLEQERIAAEKAEAER 268
Cdd:TIGR02168  359 ELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqQEIEELLKKLEEAELKE 437
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083  269 LeQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:TIGR02168  438 L-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
83-298 2.57e-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: 43.68  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  83 ERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAErlaqeqqAAEQQRQEQQARLAEQEAAMKLEQERAAAEQA 162
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKE-------LEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 163 QREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 241
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 242 ERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEADR 298
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAErKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
294-362 2.86e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 42.73  E-value: 2.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 294 AEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEA-DRLEQERIAAEKAEAERLEQE 362
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELkHLLEERKEALEKLRAEAREEA 70
PLN02316 PLN02316
synthase/transferase
264-310 3.12e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 44.09  E-value: 3.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  264 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EADRLEQERIAAEKAE 310
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
201-296 3.27e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 44.17  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  201 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAEKAE 280
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETS 211
                           90
                   ....*....|....*.
gi 1952201083  281 AERLEQERIAAEKAEA 296
Cdd:PRK11448   212 QERKQKRKEITDQAAK 227
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
182-384 3.31e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:COG4717    49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQ-ERIAAEK 338
Cdd:COG4717   129 PLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRL 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1952201083 339 AEADR-LEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:COG4717   209 AELEEeLEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
181-270 3.53e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 44.17  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:PRK11448   148 QQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221
                           90
                   ....*....|
gi 1952201083  261 AEKAeAERLE 270
Cdd:PRK11448   222 TDQA-AKRLE 230
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
238-366 3.54e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.92  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 238 RLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEADRLEqeriaaEKAEAERLEQE 317
Cdd:COG0542   403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIE 471
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1952201083 318 RIVAEKAEAERLEQERIAAEKaEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:COG0542   472 EIQELKEELEQRYGKIPELEK-ELAELEEELAELAPLLREEVTEEDIAE 519
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
18-385 3.70e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLeQERIAAEKAEAERLEQ 97
Cdd:COG4717   156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA-QEELEELEEELEQLEN 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  98 ERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAE 177
Cdd:COG4717   235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 178 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQE 257
Cdd:COG4717   315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 258 RIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAE 337
Cdd:COG4717   395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1952201083 338 KAEADRLEQE-RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAE 385
Cdd:COG4717   475 LQELEELKAElRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
180-242 3.71e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 42.35  E-value: 3.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAER-LEQERIAAEKAEAERLEQE 242
Cdd:pfam15927   7 EEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
PLN02316 PLN02316
synthase/transferase
60-106 3.73e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 44.09  E-value: 3.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083   60 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAERRD 106
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
17-124 4.01e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKA--EAERLEQERiaaeKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAer 94
Cdd:PRK00409  514 DKEKLNELIASLEELERELEQKAEEAEALlkEAEKLKEEL----EEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-- 586
                          90       100       110
                  ....*....|....*....|....*....|
gi 1952201083  95 leqERIAAERRDAERVEQERIAAEKAEAER 124
Cdd:PRK00409  587 ---DEIIKELRQLQKGGYASVKAHELIEAR 613
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
179-298 4.29e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAE--KAEAERLEQERiaaeKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAerleqERIAAEKAEAERLEQ 256
Cdd:PRK00409  532 LEQKAEEAEalLKEAEKLKEEL----EEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEA-----DEIIKELRQLQKGGY 601
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1952201083 257 ERIAAEKAEaERLEQERIAAEKAEAERLEQERIAAEKAEADR 298
Cdd:PRK00409  602 ASVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVGDE 642
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
279-347 4.30e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.96  E-value: 4.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 279 AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER-LEQERIAAEKAEADRLEQE 347
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
growth_prot_Scy NF041483
polarized growth protein Scy;
181-395 4.53e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  181 QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERL----EQERIAAEKAEAE-RL 254
Cdd:NF041483   523 EETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEALADaRA 600
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  255 EQERIAAEKAEaerlEQERIAAEKAEAERLEQeriAAEKAEADRLEQEriAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:NF041483   601 EAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTE--AAADASAARAEGENVAVRLRSEAAAEAERL 671
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952201083  335 AAEKAE-ADRLEQE-RIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFAR 395
Cdd:NF041483   672 KSEAQEsADRVRAEaAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR 734
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
86-311 4.75e-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: 42.91  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  86 AAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERlaqeqqaaeqqRQEQQARLAEQEAAMKLEQERAAAEQAQRE 165
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR-----------AAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 166 AEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 245
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEA 311
Cdd:TIGR02794 195 KAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
174-388 5.12e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 174 AEAerlEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAEKAEAER 253
Cdd:COG2268   228 LEQ---EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE-VQRQLEIAEREREIELQEKEAEREE 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEADRLEQERIAAEKAEAERLEQ------ERIVAEKAEA- 326
Cdd:COG2268   304 AELEADVRKPAEAEKQAAEAEAEAEAEAIR------AKGLAEAEGKRALAEAWNKLGDAAILLmlieklPEIAEAAAKPl 377
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 327 ERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPK 388
Cdd:COG2268   378 EKIDKITIIDGGNGGNGAGSAVAEALAPLLESLLEETGLDLPGLLKGLTGAGAAAPAGEPAE 439
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
17-361 5.24e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:COG3096    316 EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   97 ------QERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAA 170
Cdd:COG3096    396 sqladyQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFE 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  171 AEKAEAERL--EQERIAAEKAEAERLEQERiaAEKAEAERLEQerIAAEKAEAERLEQERiaaekAEAERLEQE---RIA 245
Cdd:COG3096    476 KAYELVCKIagEVERSQAWQTARELLRRYR--SQQALAQRLQQ--LRAQLAELEQRLRQQ-----QNAERLLEEfcqRIG 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAeAERLEQE--RIVAEK 323
Cdd:COG3096    547 QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDA-LERLREQsgEALADS 625
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1952201083  324 AE-----AERLEQERIAaeKAEADRLEQERIAAEKaEAERLEQ 361
Cdd:COG3096    626 QEvtaamQQLLEREREA--TVERDELAARKQALES-QIERLSQ 665
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
69-228 5.39e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.57  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   69 RIAAEKAEAERLEQERIAAEKAEAERLEQERIA-AERRDAERVEQERIaaekaeaerlaqeqqaaeqqrqeqqarlaeqe 147
Cdd:PTZ00266   429 RVDKDHAERARIEKENAHRKALEMKILEKKRIErLEREERERLERERM-------------------------------- 476
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  148 aamkleqeraaaeqaqreaeqaaaekaeaerleqERIAAEKAEAERLEQERIAAEKAEAERLEQ-ERIAAEKAEAERLEQ 226
Cdd:PTZ00266   477 ----------------------------------ERIERERLERERLERERLERDRLERDRLDRlERERVDRLERDRLEK 522

                   ..
gi 1952201083  227 ER 228
Cdd:PTZ00266   523 AR 524
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-360 5.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAER 94
Cdd:PRK02224  370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEALL 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  95 LEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:PRK02224  450 EAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERR 529
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 175 EAERLEQERIAAEKAEAERLEQEriaAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE-----QERIAAEKA 249
Cdd:PRK02224  530 ETIEEKRERAEELRERAAELEAE---AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtlLAAIADAED 606
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 250 EAERLEQERiaAEKAEAERLEQERIAaekaeaERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERL 329
Cdd:PRK02224  607 EIERLREKR--EALAELNDERRERLA------EKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1952201083 330 EQERIAAEKAEADRLE--QERIAAEKAEAERLE 360
Cdd:PRK02224  679 LQAEIGAVENELEELEelRERREALENRVEALE 711
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
230-391 5.86e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 309
Cdd:PRK13108  287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 310 EAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:PRK13108  365 ETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEP 444

                  ..
gi 1952201083 390 EG 391
Cdd:PRK13108  445 DG 446
PLN02316 PLN02316
synthase/transferase
279-325 6.11e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 43.32  E-value: 6.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  279 AEAERLEQERIAAEKAEADRL--EQERIAAEKA--EAERLEQERIVAEKAE 325
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
185-373 6.39e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 42.66  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 185 AAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA 264
Cdd:PRK13108  287 GSEYVVDEALERE--PAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 265 EAERLEQERIAAEKaeaerleqerIAAEKAEADRLEQERIAAEKAEAERLEqerivAEKAEAERLEQERIAAEKAEADRL 344
Cdd:PRK13108  365 ETSEADIEREQPGD----------LAGQAPAAHQVDAEAASAAPEEPAALA-----SEAHDETEPEVPEKAAPIPDPAKP 429
                         170       180
                  ....*....|....*....|....*....
gi 1952201083 345 EQERIAAEKAEAERLEQERIAEEQAEAER 373
Cdd:PRK13108  430 DELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
15-300 7.18e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.06  E-value: 7.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQqrieaekAEAERLEQERIAAEKAEaerlEQERIAAEKAEAErLEQERIAAEKAEAER 94
Cdd:TIGR00927  632 KGDVAEAEHTGERTGEEGERPTE-------AEGENGEESGGEAEQEG----ETETKGENESEGE-IPAERKGEQEGEGEI 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   95 LEQERIAAERRDAERVEQEriaaEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKA 174
Cdd:TIGR00927  700 EAKEADHKGETEAEEVEHE----GETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGK 775
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  175 EAERlEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 254
Cdd:TIGR00927  776 EDED-EGEIQAGEDGEMKGDEGAEGKVEHEGETE------AGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQD 848
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1952201083  255 EQ---ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLE 300
Cdd:TIGR00927  849 EKgvdGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLE 897
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
226-358 7.22e-04

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 41.30  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 226 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIA 305
Cdd:pfam07382   5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 306 AEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:pfam07382  85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
268-379 7.51e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 268 RLEQERIAAEKAEAER----LEQERIAAEKaEADRLEQERIAAEKAEAERLEQERIVAEKA-EAERLEQERIAAEKAEAD 342
Cdd:COG0542   403 RMEIDSKPEELDELERrleqLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARwEAEKELIEEIQELKEELE 481
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1952201083 343 RLEQERIAAEKAEAERLEQEriaeeqAEAERLEQEKV 379
Cdd:COG0542   482 QRYGKIPELEKELAELEEEL------AELAPLLREEV 512
PRK12472 PRK12472
hypothetical protein; Provisional
230-383 7.55e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 42.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEADRLEQERIAAEK 308
Cdd:PRK12472  181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKT 253
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 309 AEAerleqerivaeKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErLEQERIAEEQAEAERLEQEKVAQAA 383
Cdd:PRK12472  254 DEA-----------KARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA-AAATKEAAKAAAAKKAETAKAATDA 316
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
47-348 7.60e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 7.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   47 AERLEQERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAE-KAEAERL 125
Cdd:TIGR02169  661 APRGGILFSRSEPAELQRL-RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeEKLKERL 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  126 AQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAE-KA 204
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREiEQ 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  205 EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 284
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083  285 EQERIAAEKAEADRLEQERIAAEKAEAERLEQE--RIVAEKAEAERLEQERIAAEKAEADRLEQER 348
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEElsEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
208-336 7.77e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 208 RLEQERIAAEKAEAERleqeRIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqeriaaEKAEAERLEQE 287
Cdd:COG0542   403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIE 471
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1952201083 288 RIAAEKAEADRLEQERIAAEKAEAErLEQERIVAEKAEAERLEQERIAA 336
Cdd:COG0542   472 EIQELKEELEQRYGKIPELEKELAE-LEEELAELAPLLREEVTEEDIAE 519
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
264-332 7.83e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 41.19  E-value: 7.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 264 AEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER-LEQERIVAEKAEAERLEQE 332
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEA 70
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
71-536 8.37e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  71 AAEKAEAERLEQERIA-AEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA 149
Cdd:COG3064     4 ALEEKAAEAAAQERLEqAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 150 MKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 229
Cdd:COG3064    84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 230 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 309
Cdd:COG3064   164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 310 EAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKK 389
Cdd:COG3064   244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 390 EGFFARLKKGLLKTRVNIGSGFASIFSGKKIDDELFEELETQLLTADLGVDTTMKLIDNLTDAADRKQLKDGDALYELMK 469
Cdd:COG3064   324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 470 QEMASMLKTAEQPLVVSNDKKPFVILMVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAGDTFRAAAVE 536
Cdd:COG3064   404 RLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
181-313 8.62e-04

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 40.92  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:pfam07382   5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:pfam07382  85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
186-313 1.02e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 42.15  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 186 AEKAEAERLEQERIAAEKAEAERLEQERIA------------AEKAEAERLEQERIAAEKAEAERLEQERIAAEKaeaeR 253
Cdd:PRK00247  285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRmiitpwrapelhAENAEIKKTRTAEKNEAKARKKEIAQKRRAAER----E 360
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 254 LEQERIAAEKAEAERLEQERIAAEKA-----EAERLEQERIAAEKAEADRLEQERIAAEKAEAER 313
Cdd:PRK00247  361 INREARQERAAAMARARARRAAVKAKkkgliDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
flhF PRK14721
flagellar biosynthesis regulator FlhF; Provisional
493-691 1.11e-03

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 173184 [Multi-domain]  Cd Length: 420  Bit Score: 41.86  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 493 VILMVGVNGVGKTTTIGKLAKQ--FQNEGKSVMLAAGDTFRAAAVEQLQVWGERNSIPViaqHTGADSASVVFdAFQAAK 570
Cdd:PRK14721  193 VYALIGPTGVGKTTTTAKLAARavIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSV---RSIKDIADLQL-MLHELR 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 571 ARNVdVLIaDTAGRLQNKDNLMQELEKIARVMKKIdpdaphEVMLTIDAGTGQNAISQVKLFNECVGLTGITLSKLDGTA 650
Cdd:PRK14721  269 GKHM-VLI-DTVGMSQRDQMLAEQIAMLSQCGTQV------KHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAA 340
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1952201083 651 KGGVIFAVADKFNIPIRYIGVGEGI-DDLRTFNSSDFIDALF 691
Cdd:PRK14721  341 SLGIALDAVIRRKLVLHYVTNGQKVpEDLHEANSRYLLHRIF 382
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
42-266 1.13e-03

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: 41.75  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  42 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAE 121
Cdd:TIGR02794  47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 122 AERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAaaekaeaerleQERIAAEKAEAERLEQERIAA 201
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKK-----------AEAEAKAKAEAEAKAKAEEAK 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083 202 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 266
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
growth_prot_Scy NF041483
polarized growth protein Scy;
20-397 1.21e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   20 QAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQE 98
Cdd:NF041483   287 EAKEAAAKQLASAESANEQRTRTAKEEIARLVGE--ATKEAEALKAEAEQALADaRAEAEKLVAEAAEKARTVAAEDTAA 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   99 RIAAERRDAERV-------EQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAA 171
Cdd:NF041483   365 QLAKAARTAEEVltkasedAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARR 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  172 EKAEAERLEQEriAAEKAEAERLEQERIAAEK-AEAERLEQERIAAEKAEAERLEQeriaAEKAEAERLEQEriAAEKAE 250
Cdd:NF041483   445 LRGEAEQLRAE--AVAEGERIRGEARREAVQQiEEAARTAEELLTKAKADADELRS----TATAESERVRTE--AIERAT 516
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  251 AERLE-QERIAAEKAEAERLEQEriAAEKAEAERLEQERIAAE-KAEADRLEQERIAAEKAEAERL----EQERIVAEKA 324
Cdd:NF041483   517 TLRRQaEETLERTRAEAERLRAE--AEEQAEEVRAAAERAARElREETERAIAARQAEAAEELTRLhteaEERLTAAEEA 594
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083  325 EAE-RLEQERIAAEKAEadrlEQERIAAEKAEAERLEQeriAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLK 397
Cdd:NF041483   595 LADaRAEAERIRREAAE----ETERLRTEAAERIRTLQ---AQAEQEAERLRTEAAADASAARAEGENVAVRLR 661
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
189-300 1.22e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 189 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaERLEQERIAAEKAEAER 268
Cdd:pfam05672  25 EQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE-EREQREQEEQERLQKQK 103
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1952201083 269 LEQERIAAEKAEAERLEQERIaAEKAEADRLE 300
Cdd:pfam05672 104 EEAEAKAREEAERQRQEREKI-MQQEEQERLE 134
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
196-328 1.33e-03

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 40.53  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 196 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 275
Cdd:pfam07382   5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 276 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:pfam07382  85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
265-381 1.38e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 265 EAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRl 344
Cdd:pfam05672  11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE- 89
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1952201083 345 EQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQ 381
Cdd:pfam05672  90 QREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQ 126
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
231-330 1.49e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  231 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEADRLEQERIAAEKAE 310
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETS 211
                           90       100
                   ....*....|....*....|
gi 1952201083  311 AERLEQERIVAEKAeAERLE 330
Cdd:PRK11448   212 QERKQKRKEITDQA-AKRLE 230
PLN02316 PLN02316
synthase/transferase
189-235 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  189 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 235
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PLN02316 PLN02316
synthase/transferase
45-91 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083   45 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 91
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PLN02316 PLN02316
synthase/transferase
204-250 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  204 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 250
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PLN02316 PLN02316
synthase/transferase
219-265 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  219 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 265
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PLN02316 PLN02316
synthase/transferase
234-280 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  234 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 280
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
PLN02316 PLN02316
synthase/transferase
249-295 1.56e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  249 AEAERLEQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 295
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
309-378 1.56e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 40.42  E-value: 1.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 309 AEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAER-LEQERIAEEQAEAERLEQEK 378
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHlLEERKEALEKLRAEAREEAE 71
PRK12704 PRK12704
phosphodiesterase; Provisional
212-382 1.62e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 212 ERIAAEKA-EAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaekAEAERLEQERIAAEKAEAERLEQERIA 290
Cdd:PRK12704   26 KKIAEAKIkEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNE------FEKELRERRNELQKLEKRLLQKEENLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 291 AEKAEADRLEQERIAAEKAEAER---LEQERIVAEKAEAERLEQ-ERIAAEKAEADRLEQERIAAEKAEAERLEQERIAE 366
Cdd:PRK12704  100 RKLELLEKREEELEKKEKELEQKqqeLEKKEEELEELIEEQLQElERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIE 179
                         170
                  ....*....|....*...
gi 1952201083 367 EQA--EAERLEQEKVAQA 382
Cdd:PRK12704  180 EEAkeEADKKAKEILAQA 197
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
283-391 1.62e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 283 RLEQERIAAEKAEADRleqeRIAAEKAEAERLEQERIVAEKAEAERLEQErIAAEKAEADRLEqERIAAEKAEAERLEQE 362
Cdd:COG0542   403 RMEIDSKPEELDELER----RLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK-ARWEAEKELIEEIQEL 476
                          90       100
                  ....*....|....*....|....*....
gi 1952201083 363 RIAEEQAEAERLEQEKVAQAAAEKPKKEG 391
Cdd:COG0542   477 KEELEQRYGKIPELEKELAELEEELAELA 505
PLN02316 PLN02316
synthase/transferase
324-370 1.71e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 41.78  E-value: 1.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  324 AEAERLEQERIAAEKAEADRL--EQERIAAEKA--EAERLEQERIAEEQAE 370
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
17-362 1.82e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.88  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQ-ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL 95
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   96 EQERIAAERrdaeRVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR00618  313 HTELQSKMR----SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKaeAERLEQERIAAEKAEAERLEQERIAaekaeAERLE 255
Cdd:TIGR00618  389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK--QQELQQRYAELCAAAITCTAQCEKL-----EKIHL 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  256 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAaeKAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:TIGR00618  462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI--HPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1952201083  336 AEKAEAD-----RLEQERIAAEKAEAERLEQE 362
Cdd:TIGR00618  540 LETSEEDvyhqlTSERKQRASLKEQMQEIQQS 571
PRK12472 PRK12472
hypothetical protein; Provisional
200-347 1.85e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.39  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 200 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEAERLEQERIAAE- 277
Cdd:PRK12472  181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKt 253
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 278 ---KAEAERLEQERIAAEKAEADRLEQERIAAEKAEAErleqerIVAEKAEAERLEQERIAAEKAEAD-RLEQE 347
Cdd:PRK12472  254 deaKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA------AAATKEAAKAAAAKKAETAKAATDaKLALE 321
valS PRK14900
valyl-tRNA synthetase; Provisional
180-313 1.90e-03

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 41.52  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERI 259
Cdd:PRK14900   916 MEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGIEKVAEAVRKTVRRSVKKAAATRAAMKKK 995
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083  260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKA--EADRLEQERIAAEKAEAER 313
Cdd:PRK14900   996 VAKKAPAKKAAAKKAAAKKAAAKKKVAKKAPAKKVarKPAAKKAAKKPARKAAGRK 1051
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
15-404 1.98e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   15 KSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAERLEQERIAAEKAEAE 93
Cdd:pfam12128  314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   94 RLEQERIAAERRDAERVEQERIAAEKAEAE-RLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:pfam12128  394 GIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:pfam12128  474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE---------KAEADRLEqERIAAEKAEAERLEQERIVAEK 323
Cdd:pfam12128  554 VISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPewaaseeelRERLDKAE-EALQSAREKQAAAEEQLVQANG 632
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  324 AEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKEGFFARLKKGLLKT 403
Cdd:pfam12128  633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712

                   .
gi 1952201083  404 R 404
Cdd:pfam12128  713 R 713
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
277-364 2.07e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 40.74  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 277 EKAEAER------LEQERIAAEKAEADRLEQeRIAAEK-AEAERLEQERIVAEKaEAERLEQE-----RIAAEKAEAD-- 342
Cdd:cd03406   169 EAMEAEKtklliaEQHQKVVEKEAETERKRA-VIEAEKdAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARADae 246
                          90       100
                  ....*....|....*....|....*
gi 1952201083 343 --RLEQERIAAE-KAEAERLEQERI 364
Cdd:cd03406   247 yyRALREAEANKlKLTPEYLELKKY 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-271 2.13e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   68 ERIAAEKAEAERLEQERIAAEKAEA--ERLEQ-----ERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQ 140
Cdd:COG4913    225 EAADALVEHFDDLERAHEALEDAREqiELLEPirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  141 ARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAE 220
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  221 AERLEQERIAAEKAEAERLEQERIAAEKAEAErlEQERIAAEKAEAERLEQ 271
Cdd:COG4913    385 LRAEAAALLEALEEELEALEEALAEAEAALRD--LRRELRELEAEIASLER 433
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
211-343 2.18e-03

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 39.76  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 211 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIA 290
Cdd:pfam07382   5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 291 AEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADR 343
Cdd:pfam07382  85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
181-291 2.22e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 181 QERIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqeriaaEKAEAERLEQERIAAEKAEAERLEQERIA 260
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK------ARWEAEKELIEEIQELKEELEQRYGKIPE 489
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1952201083 261 AEKAEAErLEQERIAAEKAEAERLEQERIAA 291
Cdd:COG0542   490 LEKELAE-LEEELAELAPLLREEVTEEDIAE 519
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
200-285 2.26e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  200 AAEKAEAERLEQ--ERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAE 277
Cdd:PRK11448   145 HALQQEVLTLKQqlELQAREKAQSQAL-AEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITD 223

                   ....*...
gi 1952201083  278 KAeAERLE 285
Cdd:PRK11448   224 QA-AKRLE 230
PTZ00121 PTZ00121
MAEBL; Provisional
13-218 2.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEA 92
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   93 ERLEQERiaaERRDAERVEQERIAAEKAEAERlaqeQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:PTZ00121  1680 AKKAEED---EKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1952201083  173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEK 218
Cdd:PTZ00121  1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-385 2.35e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  35 EEQQRIEAEKAEAERLEQEriAAEKAEAERLEQERIAAEKAEAERLeQERIAAEKAEAERLeQERIAAERRDAERVEQER 114
Cdd:PRK02224  220 EEIERYEEQREQARETRDE--ADEVLEEHEERREELETLEAEIEDL-RETIAETEREREEL-AEEVRDLRERLEELEEER 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 115 IAAeKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERL 194
Cdd:PRK02224  296 DDL-LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEE 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 195 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE-RLEQERIAAEKAEAERLE--- 270
Cdd:PRK02224  375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEaTLRTARERVEEAEALLEAgkc 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 271 -------QERIAAEKAEAERLEQERIAAEKAEAdRLEQERIAAEKAEAERL-EQERIVAEKAEAERLEQERIAAEKAEAD 342
Cdd:PRK02224  455 pecgqpvEGSPHVETIEEDRERVEELEAELEDL-EEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIE 533
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1952201083 343 RlEQERIAAEKAEAERLEQE-RIAEEQAEAERLEQEKVAQAAAE 385
Cdd:PRK02224  534 E-KRERAEELRERAAELEAEaEEKREAAAEAEEEAEEAREEVAE 576
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
179-337 2.35e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 179 LEQERIAAEKAEAERLEQERIAAEK---AEAERLEQERIAAEKAEAERLEQERIAAE-KAEAERLEQERIAAEKAEAERL 254
Cdd:PRK09510  106 LEKERLAAQEQKKQAEEAAKQAALKqkqAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAAEAKK 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 255 EQERIAAEKAEAErleqeriAAEKAEAERLEQeriAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERI 334
Cdd:PRK09510  186 KAEAEAAAKAAAE-------AKKKAEAEAKKK---AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255

                  ...
gi 1952201083 335 AAE 337
Cdd:PRK09510  256 AAE 258
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
216-358 2.36e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 40.99  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 216 AEKAEAERLEQERIAAEKAEAERLEQERIAAekaeaeRLEQERIAAEKAEAERLEQER---IAAEKAEAERLEQERIAAE 292
Cdd:PRK00247  285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRtaeKNEAKARKKEIAQKRRAAE 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 293 KaEADRleqERIAAEKAEAERLEQERIVAEKA-----EAERLEQERIAAEKAEADRLEQERIAAEKAEAER 358
Cdd:PRK00247  359 R-EINR---EARQERAAAMARARARRAAVKAKkkgliDASPNEDTPSENEESKGSPPQVEATTTAEPNREP 425
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
23-115 2.46e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 40.59  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  23 QAAKEADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAERLEQEriaaekAEAERleQERIAAEKAEAERLEQerIAA 102
Cdd:COG0330   167 EEVQDAMEDRMKAERER-EAAILEAEGYREAAIIRAEGEAQRAIIE------AEAYR--EAQILRAEGEAEAFRI--VAE 235
                          90
                  ....*....|...
gi 1952201083 103 ERRDAERVEQERI 115
Cdd:COG0330   236 AYSAAPFVLFYRS 248
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
246-390 2.57e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 40.99  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAekaeaeRLEQERIAAEKAEADRLEQER---IAAEKAEAERLEQERIVAE 322
Cdd:PRK00247  285 EHHAEQRAQYREKQKEKKAFLWTLRRNRLRM------IITPWRAPELHAENAEIKKTRtaeKNEAKARKKEIAQKRRAAE 358
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201083 323 KaEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEqAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PRK00247  359 R-EINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSE-NEESKGSPPQVEATTTAEPNRE 424
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
35-390 2.70e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  35 EEQQRIEAEKAEAERLEQERiAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQEriaaERRDAERVEQER 114
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAE-AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAE----QRAAELAAEAAK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 115 IAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAERLEQERIAAEKAEAERL 194
Cdd:COG3064    78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 195 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiAAEKAEAERLEQERI 274
Cdd:COG3064   158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV-AARAAAASREAALAA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 275 AAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADRLEQERIAAEKA 354
Cdd:COG3064   237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1952201083 355 EAERLEQERIAEEQAEAERLEQEKVAQAAAEKPKKE 390
Cdd:COG3064   317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAA 352
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
182-328 2.73e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK13108  312 ASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDA 391
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAER 328
Cdd:PRK13108  392 EAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSSRRR 458
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
182-337 2.80e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 182 ERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAA 261
Cdd:PRK13108  297 EREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQP 376
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083 262 EKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQerIVAEKAEAERLEQERIAAE 337
Cdd:PRK13108  377 GDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDE--LAVAGPGDDPAEPDGIRRQ 450
growth_prot_Scy NF041483
polarized growth protein Scy;
17-382 3.07e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLE 96
Cdd:NF041483   527 ERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIR 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   97 QEriAAERRDAERVE-QERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:NF041483   607 RE--AAEETERLRTEaAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRA 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  176 AERLEQERIAAEKAEAERLEQERIAAEKAEAERL--------EQERIAAEKAEAERLEQERIAAEKAEAERL----EQER 243
Cdd:NF041483   685 EAAAAAERVGTEAAEALAAAQEEAARRRREAEETlgsaraeaDQERERAREQSEELLASARKRVEEAQAEAQrlveEADR 764
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  244 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRL------EQERIAAEKAEAERLEQE 317
Cdd:NF041483   765 RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVrsdayaERERASEDANRLRREAQE 844
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  318 RIVAEKAEAERL------EQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQA 382
Cdd:NF041483   845 ETEAAKALAERTvseaiaEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQA 915
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
37-122 3.12e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   37 QQRIEAEKAEAERLEQERIAAEkAEAERLEQERIAAEKaeaerLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIA 116
Cdd:PRK11448   148 QQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEG-----LAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221

                   ....*.
gi 1952201083  117 AEKAEA 122
Cdd:PRK11448   222 TDQAAK 227
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
232-321 3.16e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 39.97  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 232 EKAEAER------LEQERIAAEKAEAERLEQeRIAAEK-AEAERLEQERIAAEKaEAERLEQE-----RIAAEKAEAD-- 297
Cdd:cd03406   169 EAMEAEKtklliaEQHQKVVEKEAETERKRA-VIEAEKdAEVAKIQMQQKIMEK-EAEKKISEiedemHLAREKARADae 246
                          90       100
                  ....*....|....*....|....*..
gi 1952201083 298 --RLEQERIAAE-KAEAERLEQERIVA 321
Cdd:cd03406   247 yyRALREAEANKlKLTPEYLELKKYQA 273
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
37-124 3.18e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  37 QQRIEAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEqERIAAEKAEAERLEQERIAAERRDAERVEQERIA 116
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQDEASFERLAELRDE-LAELEEELEALK-ARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494

                  ....*...
gi 1952201083 117 AEKAEAER 124
Cdd:COG0542   495 AELEEELA 502
rne PRK10811
ribonuclease E; Reviewed
225-386 3.63e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  225 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAA---EKAEADRLE 300
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVvVAEPQPEEVVVVETTHPEVIAApvtEQPQVITES 934
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  301 QERIAAEKAEaerlEQERIVAEKAEAERLEQeriAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVA 380
Cdd:PRK10811   935 DVAVAQEVAE----HAEPVVEPQDETADIEE---AAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVP 1007

                   ....*.
gi 1952201083  381 QAAAEK 386
Cdd:PRK10811  1008 EATVEH 1013
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
261-360 3.70e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  261 AEKAEAERLEQERIAAEKAEAERLEQERIAAEkAEADRLEQERIAAEKAEAErLEQERivaeKAEAERLEQERIAAEKAE 340
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAE-LEEKQ----QELEAQLEQLQEKAAETS 211
                           90       100
                   ....*....|....*....|
gi 1952201083  341 ADRLEQERIAAEKAeAERLE 360
Cdd:PRK11448   212 QERKQKRKEITDQA-AKRLE 230
rne PRK10811
ribonuclease E; Reviewed
180-335 4.06e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL-EQERIAAEKAEAERLEQERIAAEKAEAERLEQER 258
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVvVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITES 934
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201083  259 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIA 335
Cdd:PRK10811   935 DVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATV 1011
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
276-375 4.24e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  276 AEKAEAERLEQERIAAEKAEADRLEQERIAAEkAEAERLEQERivaekAEAERLEQERIAAEKAEADRLEQERIAAEKAE 355
Cdd:PRK11448   138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQEL-----VALEGLAAELEEKQQELEAQLEQLQEKAAETS 211
                           90       100
                   ....*....|....*....|
gi 1952201083  356 AERLEQERIAEEQAeAERLE 375
Cdd:PRK11448   212 QERKQKRKEITDQA-AKRLE 230
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
17-123 4.30e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  17 DKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQE--RIAAEKA-EAERLEQERIAAEKAEAERLEQErIAAEKAEAE 93
Cdd:COG2268   222 EAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaRAEAEAAyEIAEANAEREVQRQLEIAERERE-IELQEKEAE 300
                          90       100       110
                  ....*....|....*....|....*....|
gi 1952201083  94 RLEQERIAAERRDAERVEQERIAAEKAEAE 123
Cdd:COG2268   301 REEAELEADVRKPAEAEKQAAEAEAEAEAE 330
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
489-601 4.31e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 38.30  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 489 KKPFVILmVGVNGVGKTTTIGKLAKQFQNEGKSVMLAAgDTFRAAAVeqLqvwGERNSIPV--IAQHTGADSASVVFDaF 566
Cdd:cd17933    11 RNRVSVL-TGGAGTGKTTTLKALLAALEAEGKRVVLAA-PTGKAAKR--L---SESTGIEAstIHRLLGINPGGGGFY-Y 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952201083 567 QAAKARNVDVLIADTAG----RLQNKdnLMQELEKIARV 601
Cdd:cd17933    83 NEENPLDADLLIVDEASmvdtRLMAA--LLSAIPAGARL 119
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
75-125 4.33e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 38.88  E-value: 4.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  75 AEAERLEQERIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERL 125
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHL 51
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
18-111 4.35e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQieEQQRIEAE-KAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERL- 95
Cdd:PRK00409  529 ERELEQKAEEAEALLK--EAEKLKEElEEKKEKL-QEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVk 605
                          90
                  ....*....|....*.
gi 1952201083  96 EQERIAAERRDAERVE 111
Cdd:PRK00409  606 AHELIEARKRLNKANE 621
PLN02316 PLN02316
synthase/transferase
339-389 4.60e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 40.24  E-value: 4.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1952201083  339 AEADRLEQERIAAEKAEAERL--EQERIAEEQA--EAERleqekvAQAAAEKPKK 389
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQaeEQRRREEEKAamEADR------AQAKAEVEKR 299
PRK12472 PRK12472
hypothetical protein; Provisional
215-367 4.93e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 39.85  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 215 AAEKAEAERLEQERIAAEKAEAERLEQE-RIAAEKAEAErleqerIAAEKAEAERLEQERIAAEkAEAERLEQERIAAEK 293
Cdd:PRK12472  181 KAEALAAAPARAETLAREAEDAARAADEaKTAAAAAARE------AAPLKASLRKLERAKARAD-AELKRADKALAAAKT 253
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201083 294 AEAdrleqeriaaeKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADrLEQERIAAEKAEAERLEQERIAEE 367
Cdd:PRK12472  254 DEA-----------KARAEERQQKAAQQAAEAATQLDTAKADAEAKRAA-AAATKEAAKAAAAKKAETAKAATD 315
flhF PRK06995
flagellar biosynthesis protein FlhF;
275-672 5.15e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 39.95  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 275 AAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERleqeRIAAEKAEADRLeQERIAAEKA 354
Cdd:PRK06995   79 PAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRL----ARAAAAAPRPRV-PADAAAAVA 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 355 EAERLEQERIAEEQAEAE------RLEQEKVAQAAAEKPKKEGFFARLKKGLLktrvniGSGFASIFSGKKIDDelfeel 428
Cdd:PRK06995  154 DAVKARIERIVNDTVMQElrslrgMLEEQLASLAWGERQRRDPVRAALLKHLL------AAGFSAQLVRMLVDN------ 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 429 etqlLTADLGVDTTMK-----LIDNLTDAADRKQLKDGDALYELMkqemasmlktaeqplvvsndkkpfvilmvGVNGVG 503
Cdd:PRK06995  222 ----LPEGDDAEAALDwvqsaLAKNLPVLDSEDALLDRGGVFALM-----------------------------GPTGVG 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 504 KTTTIGKLAKQF-QNEGKS-VMLAAGDTFRAAAVEQLQVWGERNSIPVIAQHTGADSASVVfdafqaAKARNVDVLIADT 581
Cdd:PRK06995  269 KTTTTAKLAARCvMRHGASkVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRLAL------SELRNKHIVLIDT 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 582 AGRLQnKDNLMqeLEKIArvmkkidpdaphevMLtidAGTGQ--------NAISQVKLFNECV------GLTGITLSKLD 647
Cdd:PRK06995  343 IGMSQ-RDRMV--SEQIA--------------ML---HGAGApvkrllllNATSHGDTLNEVVqayrgpGLAGCILTKLD 402
                         410       420
                  ....*....|....*....|....*
gi 1952201083 648 GTAKGGVIFAVADKFNIPIRYIGVG 672
Cdd:PRK06995  403 EAASLGGALDVVIRYKLPLHYVSNG 427
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
22-149 5.39e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  22 EQAAKEADNQKQIEEQQRiEAEKAEAERlEQERIAAEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAErLEQERIA 101
Cdd:COG2268   204 AEAEAERETEIAIAQANR-EAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAET------ARAEAEAA-YEIAEAN 274
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1952201083 102 AER---RDAERVEQER-IAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAA 149
Cdd:COG2268   275 AERevqRQLEIAEREReIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
230-315 5.51e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  230 AAEKAEAERLEQ--ERIAAEKAEAERLeQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAE 307
Cdd:PRK11448   145 HALQQEVLTLKQqlELQAREKAQSQAL-AEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITD 223

                   ....*...
gi 1952201083  308 KAeAERLE 315
Cdd:PRK11448   224 QA-AKRLE 230
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
18-222 6.01e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  18 KQQAEQAAKEADNQKQIEEQQRIEAEKAEAErleQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQ 97
Cdd:PRK09510   62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEEL---QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  98 ERIAAERRDAERVEQERIAAEKAEAErlaqeqQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAEAE 177
Cdd:PRK09510  139 AKAAAAAKAKAEAEAKRAAAAAKKAA------AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1952201083 178 RLEQERIAAE-KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 222
Cdd:PRK09510  213 AEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-367 6.25e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  13 FGKSDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEaERLEQERIAAEKAEA 92
Cdd:COG4372    16 FGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE-EELEELNEQLQAAQA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  93 ERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAE 172
Cdd:COG4372    95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 173 KAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 252
Cdd:COG4372   175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 253 RLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQE 332
Cdd:COG4372   255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1952201083 333 RIAAEKAEADRLEQERIAAEKAEAERLEQERIAEE 367
Cdd:COG4372   335 LLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
60-124 6.55e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 38.50  E-value: 6.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201083  60 AEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAERRDAERV-EQERIAAEKAEAER 124
Cdd:pfam15927   1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHLlEERKEALEKLRAEA 66
PTZ00491 PTZ00491
major vault protein; Provisional
271-390 6.88e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 39.62  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 271 QEriAAEKAEAERLEQEriaaekaEADRLEQERIAAE-KAEAERLEQERIVAEKAEAERLEQERIAAE-KAEADRLEQE- 347
Cdd:PTZ00491  664 QE--AAARHQAELLEQE-------ARGRLERQKMHDKaKAEEQRTKLLELQAESAAVESSGQSRAEALaEAEARLIEAEa 734
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1952201083 348 --RIAAEKAEAERLEQEriaeeqAEAERLEQEKVAQAAAEKPKKE 390
Cdd:PTZ00491  735 evEQAELRAKALRIEAE------AELEKLRKRQELELEYEQAQNE 773
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
86-316 7.06e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  86 AAEKAEAERLEQERIAAERRDAErvEQERIAAEKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQRE 165
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 166 AEQAAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQerIAAEKAEAERLEQERIAAEKAEAERLEQERIA 245
Cdd:COG4942    94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ--YLKYLAPARREQAEELRADLAELAALRAELEA 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201083 246 AEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQ 316
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PLN02316 PLN02316
synthase/transferase
294-355 7.29e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.85  E-value: 7.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201083  294 AEADRLEQERIAAEKAEAERleqerivaEKAEAERLEQERIAaekAEADRLEQERIAAEKAE 355
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERER--------QAEEQRRREEEKAA---MEADRAQAKAEVEKRRE 301
PRK12705 PRK12705
hypothetical protein; Provisional
193-350 7.33e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.31  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 193 RLEQERIAAEKAEAERLEQERIAAEKAEAERLE-QERIAAEKAEAERLEQERIAAEKAEAERLEQ--ERIAAEKAEAERL 269
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQkeEQLDARAEKLDNL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 270 EQERIAAEKAEAERlEQERIAAEKAEADRLEQeriaAEKAEAERLEQERIVAEKAEAERLEQERIAAEKAEADrLEQERI 349
Cdd:PRK12705  104 ENQLEEREKALSAR-ELELEELEKQLDNELYR----VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEAD-LEAERK 177

                  .
gi 1952201083 350 A 350
Cdd:PRK12705  178 A 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
16-224 7.90e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   16 SDKQQAEQAAKEADNQKQIEEQQRIEAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAErLEQERIAAEKAEAERL 95
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLE 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083   96 EQERIAAERRDAERVEQERIAAEKaeaERLAQEQQAAEQQRQEQQARLAEQEAAMKLEQERAAAEQAQREAEQAAAEKAE 175
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1952201083  176 AERLEQERIAAEKAEAERleQERIAAEKAEAERLE--QERIAAEKAEAERL 224
Cdd:TIGR02168  470 LEEAEQALDAAERELAQL--QARLDSLERLQENLEgfSEGVKALLKNQSGL 518
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
27-244 7.95e-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: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  27 EADNQKQIEEQQRiEAEKAEAERLEQERIAAEKAEAErleqeriaAEKAEAERlEQERIAAEKAEAERLEQERIAAERRD 106
Cdd:COG2268   187 DALGRRKIAEIIR-DARIAEAEAERETEIAIAQANRE--------AEEAELEQ-EREIETARIAEAEAELAKKKAEERRE 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 107 AERVEQERIAA-EKAEAERLAQEQQAAEQQRQEQQARLAEQEAAMKLEqeraaaeqaqreaeqaaaekaeaerlEQERIA 185
Cdd:COG2268   257 AETARAEAEAAyEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA--------------------------ELEADV 310
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 186 AEKAEAERLEQERIAAEKAEAERleqeriAAEKAEAERLEQERIAAEKAEAERLEQERI 244
Cdd:COG2268   311 RKPAEAEKQAAEAEAEAEAEAIR------AKGLAEAEGKRALAEAWNKLGDAAILLMLI 363
PLN02316 PLN02316
synthase/transferase
180-220 9.25e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 39.47  E-value: 9.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1952201083  180 EQERIAAEKAEAERL--EQERIAAEKA--EAERLEQERIAAEKAE 220
Cdd:PLN02316   257 ELEKLAKEEAERERQaeEQRRREEEKAamEADRAQAKAEVEKRRE 301
HC2 pfam07382
Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like ...
241-373 9.30e-03

Histone H1-like nucleoprotein HC2; This family contains the bacterial histone H1-like nucleoprotein HC2 (approximately 200 residues long), which seems to be found mostly in Chlamydia. HC2 functions in DNA condensation, although it has been suggested that it also has other roles.


Pssm-ID: 369339 [Multi-domain]  Cd Length: 187  Bit Score: 37.84  E-value: 9.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 241 QERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIV 320
Cdd:pfam07382   5 QKKRSSKKTAAKKAAVRKPAAKKAAAKKTVVRKVAAKKPAARKTVAKKTVAAKKPAAKKAAKKAVAKKVVAKKPVAKKAV 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1952201083 321 AEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIAEEQAEAER 373
Cdd:pfam07382  85 AKKATAKKVAAKKVVAKKTVAKKAAAKKPAAKKAVAKKAVARKPAAKKAVAKK 137
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
54-282 9.52e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083  54 RIAAEKAEAERLEQERIAAEKAEAERLEQErIAAEKAEAERLEQERIAAERRDAERVEQERIAAEKAEAERLAQEQQAAE 133
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 134 QQRQEQQARLAEQEAAMKLeqeraaaeqaqreaeqaaaekaeaerleqeriaaeKAEAERLEQERIAAEKAEAERLEQER 213
Cdd:PRK09510  145 AKAKAEAEAKRAAAAAKKA-----------------------------------AAEAKKKAEAEAAKKAAAEAKKKAEA 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201083 214 IAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAE 282
Cdd:PRK09510  190 EAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
180-384 9.56e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 39.19  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 180 EQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEAERLEQERiaAEKAEAERLEQERI 259
Cdd:PRK07735   13 EAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAK--QKREGTEEVTEEEK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201083 260 AAEKAEAERLEQERIAAEKAEAERLEQERIAAEKAEADRLEQERIAAEKAEAERLEQERIVAEKAEAERLEQERIAAEKA 339
Cdd:PRK07735   91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAA 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952201083 340 EADRLEQERIAAEKAEAERLEQERIAEEQAEAERLEQEKVAQAAA 384
Cdd:PRK07735  171 AAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKA 215
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH