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Conserved domains on  [gi|1769843723|ref|NP_001362322|]
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inactive ADP-ribosyltransferase ARH2 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
wall_bind_EntB super family cl48942
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1168-1393 1.48e-15

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


The actual alignment was detected with superfamily member NF040676:

Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 81.37  E-value: 1.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQWQ--TQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQ 1245
Cdd:NF040676   147 TEKKADEKTKQVAKVQKSVKAKEEAKTQkvAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVK 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:NF040676   227 PKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ 306

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTH 1393
Cdd:NF040676   307 EIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQ 374
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1239-1564 1.21e-04

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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:COG3064     56 EAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:COG3064    136 KAEEERKAAEAEAAAKAEAEAAR--AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPA 1478
Cdd:COG3064    214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1479 PRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPGAERALQDRMEA 1558
Cdd:COG3064    294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373


                   ....*.
gi 1769843723 1559 SEPERR 1564
Cdd:COG3064    374 ALLLGK 379
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 748-1142 4.28e-04

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  748 GAMAAAGSVASRATPAPAPGSTQSPGDRtAGEPETLGQWGSRALSESHPRGEALPRDPHSHGLLAPGGSLEPKSGAAGRS 827
Cdd:PRK07764   417 PAAAAAPAPAAAPQPAPAPAPAPAPPSP-AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  828 LLRGVALVQHPEDIATLARH-PEDAAALARHPEAarlyisnTSAASRHTAAVGG-RKDVAVegnlLGFSTES---GIPAS 902
Cdd:PRK07764   496 APAAPAAPAGADDAATLRERwPEILAAVPKRSRK-------TWAILLPEATVLGvRGDTLV----LGFSTGGlarRFASP 564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  903 DHPRPQARSVAE------SPSYGPGlpPSPPENPQAKGREGVRFPRGAEPDHLLPAVPPAEVDMGWVGGTHQRGPPHLQA 976
Cdd:PRK07764   565 GNAEVLVTALAEelggdwQVEAVVG--PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAA 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  977 HLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVAPSGskvvlnPAKEPQTWWAQ 1056
Cdd:PRK07764   643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAGQADD 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1057 DLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEGtrAARNPAVPPGEPEGPGSPAAQGQAQKQVQEWDRGQV 1136
Cdd:PRK07764   717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794


                   ....*.
gi 1769843723 1137 QGHAQE 1142
Cdd:PRK07764   795 DEDRRD 800
 
Name Accession Description Interval E-value
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1168-1393 1.48e-15

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 81.37  E-value: 1.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQWQ--TQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQ 1245
Cdd:NF040676   147 TEKKADEKTKQVAKVQKSVKAKEEAKTQkvAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVK 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:NF040676   227 PKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ 306

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTH 1393
Cdd:NF040676   307 EIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQ 374
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1239-1386 4.01e-14

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 76.74  E-value: 4.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:NF040676   232 KVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQEIAKA 311

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQE 1386
Cdd:NF040676   312 KEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1236-1374 6.81e-13

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 72.89  E-value: 6.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEqtqiEAQGQAQKGAQERAREQ 1315
Cdd:NF040676   245 VQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEE----KAQEIAKAKEEAKAREI 320

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1316 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE 1374
Cdd:NF040676   321 AKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1444 8.18e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.02  E-value: 8.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQG--QAQKGAQE-RAREQ 1315
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEaKKADE 1474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1316 AQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:PTZ00121  1475 AKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1392 THI----EAQGQAQKGAQEWARDRARDQGWEQTQIETQR-----------QTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1555 EELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeeeKKMKAEEAKKAEEAKIKA 1622
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1245-1480 3.10e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 3.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1324
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1325 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGA 1404
Cdd:COG1196    420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1405 QewARDRARDQGW--EQTQIETQRQTQKGAQERAWEQGREQALTSGMAprAWEQPISGIAEGVDAAGRSGGSRSPAPR 1480
Cdd:COG1196    500 E--ADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDDEVAAAAIEYLKAAKAGR 573
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1167-1431 1.27e-11

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 68.35  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1167 HSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE 1246
Cdd:pfam08017   25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1247 EAQGQAQWQTQIKAQKWAQ----EQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:pfam08017  105 RSQGNVLERRQRDAENKSQgnvlERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQTHI 1394
Cdd:pfam08017  185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRDAEN 264

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1769843723 1395 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKG 1431
Cdd:pfam08017  265 RSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVG 301
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1237-1441 1.37e-09

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: 61.79  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR02794   70 QKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERareQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1396
Cdd:TIGR02794  149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1769843723 1397 QGQAQKGAqewardrARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:TIGR02794  226 ERKADEAE-------LGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1239-1564 1.21e-04

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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:COG3064     56 EAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:COG3064    136 KAEEERKAAEAEAAAKAEAEAAR--AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPA 1478
Cdd:COG3064    214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1479 PRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPGAERALQDRMEA 1558
Cdd:COG3064    294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373


                   ....*.
gi 1769843723 1559 SEPERR 1564
Cdd:COG3064    374 ALLLGK 379
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1322-1391 1.30e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.58  E-value: 1.30e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1322 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAQ---ERAREQAQKgAQERAQEQGREQ 1391
Cdd:cd06503     43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEAErilEQAKAEIEQ-EKEKALAELRKE 118
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 748-1142 4.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  748 GAMAAAGSVASRATPAPAPGSTQSPGDRtAGEPETLGQWGSRALSESHPRGEALPRDPHSHGLLAPGGSLEPKSGAAGRS 827
Cdd:PRK07764   417 PAAAAAPAPAAAPQPAPAPAPAPAPPSP-AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  828 LLRGVALVQHPEDIATLARH-PEDAAALARHPEAarlyisnTSAASRHTAAVGG-RKDVAVegnlLGFSTES---GIPAS 902
Cdd:PRK07764   496 APAAPAAPAGADDAATLRERwPEILAAVPKRSRK-------TWAILLPEATVLGvRGDTLV----LGFSTGGlarRFASP 564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  903 DHPRPQARSVAE------SPSYGPGlpPSPPENPQAKGREGVRFPRGAEPDHLLPAVPPAEVDMGWVGGTHQRGPPHLQA 976
Cdd:PRK07764   565 GNAEVLVTALAEelggdwQVEAVVG--PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAA 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  977 HLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVAPSGskvvlnPAKEPQTWWAQ 1056
Cdd:PRK07764   643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAGQADD 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1057 DLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEGtrAARNPAVPPGEPEGPGSPAAQGQAQKQVQEWDRGQV 1136
Cdd:PRK07764   717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794


                   ....*.
gi 1769843723 1137 QGHAQE 1142
Cdd:PRK07764   795 DEDRRD 800
 
Name Accession Description Interval E-value
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1168-1393 1.48e-15

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 81.37  E-value: 1.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQWQ--TQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQ 1245
Cdd:NF040676   147 TEKKADEKTKQVAKVQKSVKAKEEAKTQkvAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVK 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:NF040676   227 PKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ 306

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTH 1393
Cdd:NF040676   307 EIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQ 374
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1239-1386 4.01e-14

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 76.74  E-value: 4.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:NF040676   232 KVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQEIAKA 311

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQE 1386
Cdd:NF040676   312 KEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1236-1374 6.81e-13

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 72.89  E-value: 6.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEqtqiEAQGQAQKGAQERAREQ 1315
Cdd:NF040676   245 VQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEE----KAQEIAKAKEEAKAREI 320

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1316 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE 1374
Cdd:NF040676   321 AKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1444 8.18e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.02  E-value: 8.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQG--QAQKGAQE-RAREQ 1315
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEaKKADE 1474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1316 AQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:PTZ00121  1475 AKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1392 THI----EAQGQAQKGAQEWARDRARDQGWEQTQIETQR-----------QTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1555 EELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeeeKKMKAEEAKKAEEAKIKA 1622
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1245-1480 3.10e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 3.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1324
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1325 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGA 1404
Cdd:COG1196    420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1405 QewARDRARDQGW--EQTQIETQRQTQKGAQERAWEQGREQALTSGMAprAWEQPISGIAEGVDAAGRSGGSRSPAPR 1480
Cdd:COG1196    500 E--ADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDDEVAAAAIEYLKAAKAGR 573
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1241-1406 4.33e-12

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 69.84  E-value: 4.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQAQWQTQIKAQKWA--QEQTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKgAQERAREQAQK 1318
Cdd:PRK09510    74 AKRAEEQRKKKEQQQAEELQQKQAaeQERLKQLEKERLAAQEQKKQAEEAAKQAA-----LKQKQAEE-AAAKAAAAAKA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQerAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:PRK09510   148 KAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225


                   ....*...
gi 1769843723 1399 QAQKGAQE 1406
Cdd:PRK09510   226 AAAKAAAE 233
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1167-1431 1.27e-11

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 68.35  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1167 HSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE 1246
Cdd:pfam08017   25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1247 EAQGQAQWQTQIKAQKWAQ----EQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:pfam08017  105 RSQGNVLERRQRDAENKSQgnvlERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQTHI 1394
Cdd:pfam08017  185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRDAEN 264

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1769843723 1395 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKG 1431
Cdd:pfam08017  265 RSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVG 301
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1445 9.53e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 9.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgaQERAREQAQK 1318
Cdd:PTZ00121  1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---EAKKADEAKK 1451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAQEQGREQT 1392
Cdd:PTZ00121  1452 KAEEaKKAEEAKKKAEEaKKADEAKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAE 1531

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1393 HIEAQGQAQKGAQEWARDRARdqgwEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELK----KAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1177-1388 9.81e-11

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 65.60  E-value: 9.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1177 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAqgqvqgqaqKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqt 1256
Cdd:PRK09510    62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQA---------AEQERLKQLEKERLAAQEQKKQAEEAAKQAAL--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1257 qikAQKWAQEQTQKGAQervQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1336
Cdd:PRK09510   130 ---KQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKA 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1337 REQAQKGAQERAREQAQKGAQERAREQA--QKGAQERAREQAQKGAQERAQEQG 1388
Cdd:PRK09510   204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAaeAKAAAEKAAAAKAAEKAAAAKAAA 257
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1245-1445 1.09e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQgQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtQIEAQGQAQKGAQERAR---EQAQKGAQ 1321
Cdd:COG1196    219 KEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA------ELEAELEELRLELEELElelEEAQAEEY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1322 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:COG1196    292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1769843723 1402 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:COG1196    372 AELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1244-1444 1.54e-10

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 66.08  E-value: 1.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQaqkgaqeR 1323
Cdd:PRK12678    54 AIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAA-------Q 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:PRK12678   127 ARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRR 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1769843723 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PRK12678   207 DRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDR 247
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1244-1441 1.75e-10

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 65.70  E-value: 1.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:PRK12678    71 AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGE 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGAqerareQAQKGAQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:PRK12678   151 QPATEARAD------AAERTEEEERDERRRRGDREDRQAEAERGERGR-REERGRDGDDRDRRDRREQGDRREERGRRDG 223

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1769843723 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:PRK12678   224 GDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGR 261
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1442 1.82e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAqEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQE-RAREQAQ 1317
Cdd:PTZ00121  1319 EAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAK 1397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE--RAQEQGR 1389
Cdd:PTZ00121  1398 KKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEaKKAEEAKKKAEEakKADEAKK 1477

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1390 EQTHIEAQGQAQKGAQEWAR--DRARDQGWEQTQIETQRQTQ---KGAQERAWEQGRE 1442
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEeakKADEAKKAEEAKK 1535
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1135-1403 2.61e-10

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 64.50  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1135 QVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQG 1214
Cdd:pfam08017   25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1215 QVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQE 1294
Cdd:pfam08017  105 RSQGNVLE----RRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1295 QTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKGAQERAR----EQAQK 1366
Cdd:pfam08017  181 DAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQgnvlERRQRDAENKSQgnvlERRQR 260

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1769843723 1367 GAQERAR----EQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam08017  261 DAENRSQgnvlERRQRDAENRSQGNVLERRQRDAENKSQVG 301
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1442 3.29e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121  1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQE-RAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAQ------- 1385
Cdd:PTZ00121  1386 KAEEkKKADEAKKKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEAKKaeeakkk 1465

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1386 -EQGREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQE-RAWEQGRE 1442
Cdd:PTZ00121  1466 aEEAKKADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1242-1444 7.64e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 7.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1242 KWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERaqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQ 1321
Cdd:COG1196    235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-----------LELEEAQAEEYELLAELARLEQD 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1322 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1769843723 1402 KGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:COG1196    383 ELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1237-1441 1.37e-09

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: 61.79  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR02794   70 QKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERareQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1396
Cdd:TIGR02794  149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1769843723 1397 QGQAQKGAqewardrARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:TIGR02794  226 ERKADEAE-------LGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1120-1394 2.78e-09

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 61.03  E-value: 2.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1120 AQGQAQKQVQEWDRGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIE 1199
Cdd:pfam08017   26 SQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1200 AQGQAQEPAQGGAQGQVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQ 1279
Cdd:pfam08017  106 SQGNVLERRQRDAENKSQGNVLE----RRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1280 AQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKG 1355
Cdd:pfam08017  182 AENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRD 261

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1769843723 1356 AQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:pfam08017  262 AENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQV 300
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1254-1473 3.05e-09

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: 60.63  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1254 WQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1333
Cdd:TIGR02794   43 VDPGAVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1334 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQAQKGAQ--EWA 1408
Cdd:TIGR02794  122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEakkKAEAEAKAKAEAEAKAKAEEAKAkaEAA 201

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843723 1409 RDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGG 1473
Cdd:TIGR02794  202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAA 266
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1237-1435 8.75e-09

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 59.49  E-value: 8.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:pfam08017   59 QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER----RQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDA 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQT 1392
Cdd:pfam08017  135 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQgnvlERRQRDA 214

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1769843723 1393 HIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1435
Cdd:pfam08017  215 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLER 257
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1247-1401 1.64e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 58.73  E-value: 1.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1247 EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKgAQERAREQAQkgaQERARE 1326
Cdd:COG2268    187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETARA 262

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1327 QAQKG---AQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAQEQGrEQTHIEAQGQAQ 1401
Cdd:COG2268    263 EAEAAyeiAEANAEREVQRQLEIAEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEA-EAEAIRAKGLAE 339
PTZ00121 PTZ00121
MAEBL; Provisional
 1244-1443 1.79e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQwqtqiKAQKwaqEQTQKGAQERVQGQAQKGAQE-RAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQE 1322
Cdd:PTZ00121  1092 ATEEAFGKAE-----EAKK---TETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1323 RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQThieaqgQAQK 1402
Cdd:PTZ00121  1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKK 1237

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1769843723 1403 GAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:PTZ00121  1238 DAEE-AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1298-1443 2.76e-08

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 58.76  E-value: 2.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1298 IEAQGQAQKGAQERAREQ-----AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1372
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATpaapaAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1373 R--EQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:PRK12678   132 ErgEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1445 2.97e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEqTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121  1474 EAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--------------EQAQKGAQERAR-EQAQKGAQER 1383
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklyeeekkmkaEEAKKAEEAKIKaEELKKAEEEK 1632

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843723 1384 AQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1444 3.52e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQaqeqtqieaqgQAQKGAQE-RAREQAQ 1317
Cdd:PTZ00121  1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-----------EAKKKAEEaKKADEAK 1321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR-EQAQKGAQE---------RAQ 1385
Cdd:PTZ00121  1322 KKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEkkkadeakkKAE 1401

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843723 1386 EQGREQTHIEAQGQAQKGAQEWAR--------DRARDQGWEQTQIETQRqtQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1402 EDKKKADELKKAAAAKKKADEAKKkaeekkkaDEAKKKAEEAKKADEAK--KKAEEAKKAEEAKKKA 1466
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1264-1470 3.64e-08

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 58.13  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1343
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1344 AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIE 1423
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1769843723 1424 TQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGR 1470
Cdd:COG3064    161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAA 207
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1272-1389 5.97e-08

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: 53.51  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1272 AQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQER 1347
Cdd:pfam05672   17 AEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQ 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1769843723 1348 AREQAQK-GAQERAREQAQKGAQERAReQAQKGAQERAQEQGR 1389
Cdd:pfam05672   97 ERLQKQKeEAEAKAREEAERQRQEREK-IMQQEEQERLERKKR 138
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1434 6.29e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 6.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:PTZ00121  1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKgaqERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQE--RAQEQGREQ 1391
Cdd:PTZ00121  1676 KAEEAKKAEEDE---KKAAEALKKEAEEaKKAEELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEdkKKAEEAKKD 1752

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1769843723 1392 THIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1434
Cdd:PTZ00121  1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1439 6.34e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 6.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQ 1315
Cdd:PTZ00121  1448 EAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADE 1526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1316 AQKGAQERAREQAQKGAQERAREQAQKG-----AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121  1527 AKKAEEAKKADEAKKAEEKKKADELKKAeelkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1769843723 1391 QTHIEAQG--QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:PTZ00121  1607 MKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1324-1435 8.19e-08

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: 53.12  E-value: 8.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1401
Cdd:pfam05672   23 AREQRER--EEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQ 100

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1769843723 1402 KGAQEwARDRARDQGwEQTQIETQRQTQKGAQER 1435
Cdd:pfam05672  101 KQKEE-AEAKAREEA-ERQRQEREKIMQQEEQER 132
Fibrinogen_BP pfam08017
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ...
 1241-1435 1.16e-07

Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.


Pssm-ID: 311808 [Multi-domain]  Cd Length: 393  Bit Score: 56.03  E-value: 1.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQA----QWQTQIKAQKWAQEQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1312
Cdd:pfam08017   35 QRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERR 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1313 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQG 1388
Cdd:pfam08017  115 QRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERR 194

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1769843723 1389 REQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1435
Cdd:pfam08017  195 QRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER 241
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1281-1474 2.20e-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: 54.85  E-value: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1281 QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAReqaQKGAQERAREQAQKGAQERAREQA--QKGAQE 1358
Cdd:TIGR02794   46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR---QKELEQRAAAEKAAKQAEQAAKQAeeKQKQAE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1359 RAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW-----ARDRARDQGWEQTQIETQRQTQKGAQ 1433
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAkkkaeAEAKAKAEAEAKAKAEEAKAKAEAAK 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1769843723 1434 ERAWEQGREQA-LTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1474
Cdd:TIGR02794  203 AKAAAEAAAKAeAEAAAAAAAEAERKADEAELGDIFGLASGS 244
PTZ00121 PTZ00121
MAEBL; Provisional
 1301-1475 2.67e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1301 QGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1379
Cdd:PTZ00121  1105 KTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1380 AQERAQEQGREQTHIEAQGQAQKGAQEWARDRARdQGWEQTQIETQRQTQKgAQERAWEQGREQALTSGMAPRAWEQPIS 1459
Cdd:PTZ00121  1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEE-AKKDAEEAKKAEEERNNEEIRKFEEARM 1262

                          170
                   ....*....|....*.
gi 1769843723 1460 GIAEGVDAAGRSGGSR 1475
Cdd:PTZ00121  1263 AHFARRQAAIKAEEAR 1278
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1257-1530 2.82e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 55.05  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1257 QIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1336
Cdd:COG3064      6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1337 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW--ARDRARD 1414
Cdd:COG3064     86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAarAAAAAAA 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1415 QGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPAPRDGGQSGGSGLGEPS 1494
Cdd:COG3064    166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1769843723 1495 AGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGG 1530
Cdd:COG3064    246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVV 281
PTZ00121 PTZ00121
MAEBL; Provisional
 1237-1444 3.19e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 3.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQ----KGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1312
Cdd:PTZ00121  1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1313 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1391 QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1177-1415 3.42e-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: 54.08  E-value: 3.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1177 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKwaqgqiqgqaqkqvqgEVQKWAQEEAQGQAQWQT 1256
Cdd:TIGR02794   50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE----------------QRAAAEKAAKQAEQAAKQ 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1257 QIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQER 1335
Cdd:TIGR02794  114 AEEKQKQAEEAKAKQAAEA----KAKAEAEAERKAKE-----EAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAE 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1336 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG---REQTHIEAQGQAQKGAQEWARDRA 1412
Cdd:TIGR02794  185 AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglASGSNAEKQGGARGAAAGSEVDKY 264


                   ...
gi 1769843723 1413 RDQ 1415
Cdd:TIGR02794  265 AAI 267
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1241-1444 4.15e-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: 4.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQER------------------VQGQAQKGAQERAQEQAQEQTQIEAQG 1302
Cdd:pfam13868  105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkelekeeereederiLEYLKEKAEREEEREAEREEIEEEKER 184

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG---AQERAREQAQKG 1379
Cdd:pfam13868  185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKErrlAEEAEREEEEFE 264

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843723 1380 AQERAQEQGREQTHIEAQGQAQKgAQEWARDRARdqgweqtQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:pfam13868  265 RMLRKQAEDEEIEQEEAEKRRMK-RLEHRRELEK-------QIEEREEQRAAEREEELEEGERLR 321
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1299-1391 4.25e-07

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: 51.19  E-value: 4.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQE-R 1371
Cdd:pfam05672   30 EEQERLEKEEEERLRkeELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaK 109

                           90       100
                   ....*....|....*....|
gi 1769843723 1372 AREQAQKGAQERAQEQGREQ 1391
Cdd:pfam05672  110 AREEAERQRQEREKIMQQEE 129
PTZ00121 PTZ00121
MAEBL; Provisional
 1246-1434 5.56e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 5.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQgQAQWQTQIKAQKWAQEqTQKGAQErvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERArEQAQKG-----A 1320
Cdd:PTZ00121  1215 EEAR-KAEDAKKAEAVKKAEE-AKKDAEE-----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKAdelkkA 1286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1321 QE-RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGREQThiEA 1396
Cdd:PTZ00121  1287 EEkKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--EE 1364

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1769843723 1397 QGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1434
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
PTZ00121 PTZ00121
MAEBL; Provisional
 1239-1444 6.98e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 6.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKwAQE----EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1314
Cdd:PTZ00121  1192 ELRK-AEDarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1315 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQErareqAQKGAQE---RAQEQGRE 1390
Cdd:PTZ00121  1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEE-----AKKKADAakkKAEEAKKA 1344

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843723 1391 QTHIEAQGQAQKGAQEWARDRAR--DQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1345 AEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 1123-1547 1.06e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 53.41  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1123 QAQKQVQEWDRGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQtqieaQG 1202
Cdd:pfam03157  171 QQSGQRQQPGQGQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQGQ-----QG 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1203 QAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQW---QTQIKAQKWAQEQTQKGAQERVQGQ 1279
Cdd:pfam03157  246 QQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYyptSQQQAGQLQQEQQLGQEQQDQQPGQ 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1280 AQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1359
Cdd:pfam03157  326 GRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQ 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1360 AREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWArdrarDQGWEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:pfam03157  406 QPGQGQPGYYPTSPQQSGQGQPGYYPTSPQQSGQGQQPGQGQQPGQEQP-----GQGQQPGQGQQGQQPGQPEQGQQPGQ 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1440 GREqaltsGMAPRAWEQPISGIAEGV-DAAGRSGGSRSPAPRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLG 1518
Cdd:pfam03157  481 GQP-----GYYPTSPQQSGQGQQLGQwQQQGQGQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQPTQGQQGQQ 555

                          410       420
                   ....*....|....*....|....*....
gi 1769843723 1519 KSPTEPKPEAGGCGTPQAPAQEGSPDHPG 1547
Cdd:pfam03157  556 SGQGQQGQQPGQGQQGQQPGQGQQGQQPG 584
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1128-1376 1.20e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1128 VQEWDRGQVQGHAQEQAQWQTQieaqgqaqeqAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEp 1207
Cdd:PRK09510    61 VEQYNRQQQQQKSAKRAEEQRK----------KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAL- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1208 aqggaqgqvqgqaqkwaqGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqtqiKAQKWAQEQTQKGAQErvqgQAQKGAQEr 1287
Cdd:PRK09510   130 ------------------KQKQAEEAAAKAAAAAKAKAEAEAKRAA-----AAAKKAAAEAKKKAEA----EAAKKAAA- 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1288 aqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaQKGAQERAREQAQKG 1367
Cdd:PRK09510   182 -----------EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE--AKAAAEKAAAAKAAE 248


                   ....*....
gi 1769843723 1368 AQERAREQA 1376
Cdd:PRK09510   249 KAAAAKAAA 257
PTZ00121 PTZ00121
MAEBL; Provisional
 1246-1442 1.46e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 1.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQiEAQGQAQKGAQE--RAREQAQKGAQER 1323
Cdd:PTZ00121  1173 EDAKKAEAARKAEEVRK--AEELRKAEDARKAEAARKAEEERKAEEARKAED-AKKAEAVKKAEEakKDAEEAKKAEEER 1249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGAQER----AREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---------RAQEQGR 1389
Cdd:PTZ00121  1250 NNEEIRKFEEARmahfARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadeakkKAEEAKK 1329

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1390 EQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1442
Cdd:PTZ00121  1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
PTZ00121 PTZ00121
MAEBL; Provisional
 1244-1444 2.57e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIK-AQKWAQ-----EQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1317
Cdd:PTZ00121  1103 AKKTETGKAEEARKAEeAKKKAEdarkaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA------REQAQKGAqerarEQAQKGAQERAQEQGREQ 1391
Cdd:PTZ00121  1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkkAEEAKKDA-----EEAKKAEEERNNEEIRKF 1257

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1392 THIEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:PTZ00121  1258 EEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
PTZ00121 PTZ00121
MAEBL; Provisional
 1246-1443 3.82e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQErar 1325
Cdd:PTZ00121  1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK---------KVEQLKKKEAEEKKKAEELKKAEE--- 1657

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1326 EQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAR--EQAQKGAQE--RAQEQGR---EQTHIEAQg 1398
Cdd:PTZ00121  1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEEAKkaEELKKKEAEekKKAEELKkaeEENKIKAE- 1733

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1769843723 1399 QAQKGAQEWAR--DRARDQGWEQTQIEtqrQTQKGAQERAWEQGREQ 1443
Cdd:PTZ00121  1734 EAKKEAEEDKKkaEEAKKDEEEKKKIA---HLKKEEEKKAEEIRKEK 1777
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1245-1381 4.63e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.03  E-value: 4.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKgaqERVQGQAQKGAQEraqeqaqeqTQIEAQgQAQKGAQERAREQAQKGAQERA 1324
Cdd:COG2268    221 REAEEAELEQEREIETARIAEAEAEL---AKKKAEERREAET---------ARAEAE-AAYEIAEANAEREVQRQLEIAE 287

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1325 REQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAREQAQKgaqERAREQAQKGAQ 1381
Cdd:COG2268    288 REREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEAEA---EAIRAKGLAEAE 341
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1298-1436 4.92e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.03  E-value: 4.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1298 IEAQGQAQ----KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQkgaQERAR 1373
Cdd:COG2268    186 LDALGRRKiaeiIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETAR 261

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1374 EQAQKGAQERAQEQGReqthiEAQGQAQKGAQEwardrardqgwEQTQIETQRQTQKGAQERA 1436
Cdd:COG2268    262 AEAEAAYEIAEANAER-----EVQRQLEIAERE-----------REIELQEKEAEREEAELEA 308
PTZ00121 PTZ00121
MAEBL; Provisional
 1246-1444 6.28e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1325
Cdd:PTZ00121  1143 EEARKAEDAKRVEIARK--AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1326 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQ 1405
Cdd:PTZ00121  1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1769843723 1406 EWARDRARDQGWEQTQIETQRQTQKGAQERAwEQGREQA 1444
Cdd:PTZ00121  1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKA-DAAKKKA 1338
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1298-1406 6.32e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.64  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1298 IEAQGQAQKGAQERAREQAQKgAQER-------AREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1370
Cdd:COG2268    208 AERETEIAIAQANREAEEAEL-EQEReietariAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEI 285

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1769843723 1371 RAREQAQKGAQ-ERAQEQGREQTHIEAQGQAQKGAQE 1406
Cdd:COG2268    286 AEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE 322
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1240-1456 6.80e-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: 51.21  E-value: 6.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1240 VQKWAQEEAQGQAQWQTQIKAQKWAQEQTQK--GAQERVQGQAQKGAQERAQEQaqeqtqieAQGQAQKGAQERAREQAQ 1317
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELE--------ELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1397
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1398 GQAQKGAQEwARDRARDQ----GWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQ 1456
Cdd:TIGR02168  467 REELEEAEQ-ALDAAERElaqlQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1239-1441 6.86e-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: 51.21  E-value: 6.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGA-QERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1317
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQKGAQERAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKgaqERAQEQGREQTHIEAQ 1397
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELEELIEELESELEALLN---ERASLEEALALLRSEL 896

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1398 GQAQKGAQEW--ARDRARDQGWEQTQIETQRQTQKGA--------QERAWEQGR 1441
Cdd:TIGR02168  897 EELSEELRELesKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYS 950
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1294-1417 1.02e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1294 EQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAR 1373
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDALREEL 325

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1769843723 1374 EQAQkgaQERAQEQGREQTHIEAQ-GQAQKGAQEWARDRARDQGW 1417
Cdd:COG4913    326 DELE---AQIRGNGGDRLEQLEREiERLERELEERERRRARLEAL 367
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1199-1416 1.04e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 50.29  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1199 EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQg 1278
Cdd:PRK12678    57 EARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE- 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1279 QAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGaqeRAREQAQ----KGAQERAREQAQKGAQERAREQAQK 1354
Cdd:PRK12678   136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG---DREDRQAeaerGERGRREERGRDGDDRDRRDRREQG 212

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1355 GAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI--EAQGQAQKGAQEWARDRARDQG 1416
Cdd:PRK12678   213 DRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGddGEGRGGRRGRRFRDRDRRGRRG 276
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1236-1481 1.66e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.27  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQ 1315
Cdd:COG3064      5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAR---------EAKAEAEQRAAELAAEA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1316 AQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:COG3064     76 AKKLAEaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1395 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1474
Cdd:COG3064    156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235


                   ....*..
gi 1769843723 1475 RSPAPRD 1481
Cdd:COG3064    236 AVEATEE 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1239-1445 1.72e-05

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: 49.74  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQwqtQIKAQKWAQEQTQKGAQERVQGQAQKG----AQERAQEQAQEQTQIEAQGQAQ--------- 1305
Cdd:pfam17380  349 ELERIRQEERKRELE---RIRQEEIAMEISRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQqqkvemeqi 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1306 KGAQERARE-QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1384
Cdd:pfam17380  426 RAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843723 1385 Q---EQGREQTHIEAQGQAQKGA--QEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1445
Cdd:pfam17380  506 QamiEEERKRKLLEKEMEERQKAiyEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
PTZ00121 PTZ00121
MAEBL; Provisional
 1236-1391 1.91e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1314
Cdd:PTZ00121  1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1315 QAQKGAQERAREQAQKgaqeRAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00121  1700 EAKKAEELKKKEAEEK----KKAEELKKAEEENKIkaEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775


                   .
gi 1769843723 1391 Q 1391
Cdd:PTZ00121  1776 E 1776
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1283-1426 2.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1283 GAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERARE 1362
Cdd:COG1196    634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEEALLAEEEEERELA 710

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1363 QAQkgaQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQR 1426
Cdd:COG1196    711 EAE---EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1264-1371 3.51e-05

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: 45.42  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQ 1341
Cdd:pfam05672   23 AREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQ 102

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1769843723 1342 K-GAQERAREQAQKGAQERAReQAQKGAQER 1371
Cdd:pfam05672  103 KeEAEAKAREEAERQRQEREK-IMQQEEQER 132
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1171-1448 4.16e-05

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: 48.43  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1171 QAQKQFQNWAQGQAQghAQEQA-QWQTQI-EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE-- 1246
Cdd:TIGR00618  236 QQTQQSHAYLTQKRE--AQEEQlKKQQLLkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRih 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1247 -EAQGQAQWQTQIKAQKWA-QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1324
Cdd:TIGR00618  314 tELQSKMRSRAKLLMKRAAhVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1325 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAQEQGREQTHieaqgqAQKGA 1404
Cdd:TIGR00618  394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELCAAAITCTAQCEKLEKIH------LQESA 465

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1769843723 1405 QewaRDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQALTSG 1448
Cdd:TIGR00618  466 Q---SLKEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCG 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1259-1441 4.61e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1259 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQkgAQERARE 1338
Cdd:COG4913    260 LAERYAAARERLAELEYLRAALRLWFAQRRLE--------LLEAELEELRAELARLEAELERLEARLDALR--EELDELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1339 QAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQK-----GAQERAQEQGREQTHIEAQGQAQKGAQEWARDRAR 1413
Cdd:COG4913    330 AQIRGNGGDRLEQLE---REIERLERELEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406

                          170       180
                   ....*....|....*....|....*...
gi 1769843723 1414 DQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:COG4913    407 LAEAEAALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 1259-1444 5.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1259 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR- 1337
Cdd:PTZ00121  1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKi 1620

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1338 --EQAQKGAQERAR-EQAQKGAQERAR--EQAQKGAQE---RAREQAQKGAQE--RAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:PTZ00121  1621 kaEELKKAEEEKKKvEQLKKKEAEEKKkaEELKKAEEEnkiKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEE 1700

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1769843723 1408 ARDRARDQGWEQTQIETQRQTQKGAQERAW--EQGREQA 1444
Cdd:PTZ00121  1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaEEAKKEA 1739
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 1259-1406 5.85e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 47.69  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1259 KAQKWAQEQTQKgaQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQaqKGAQERARE 1338
Cdd:pfam05262  214 RAQQLKEELDKK--QIDAD-KAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ--KREIEKAQI 288

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1339 QAQKGAQE--RAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQEQGREQTHIEAqgQAQKGAQE 1406
Cdd:pfam05262  289 EIKKNDEEalKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEDLQKTKPQVEA--QPTSLNED 354
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1244-1475 7.38e-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: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:COG3064     41 EERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:COG3064    121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAA 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843723 1404 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSR 1475
Cdd:COG3064    201 AALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAA 272
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1267-1438 8.20e-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: 47.25  E-value: 8.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1267 QTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaqkgaQE 1346
Cdd:pfam15709  339 RAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE------EE 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1347 RAREQAQKGAQERAREQAQ---KGAQERAREQAQKGAqERAQEQGREQTHIEAQ-GQAQKGAQEWArdrardqgwEQTQI 1422
Cdd:pfam15709  408 RKQRLQLQAAQERARQQQEefrRKLQELQRKKQQEEA-ERAEAEKQRQKELEMQlAEEQKRLMEMA---------EEERL 477

                          170
                   ....*....|....*.
gi 1769843723 1423 ETQRQTQKGAQERAWE 1438
Cdd:pfam15709  478 EYQRQKQEAEEKARLE 493
mukB PRK04863
chromosome partition protein MukB;
1303-1443 1.02e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.26  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKG 1379
Cdd:PRK04863   469 QAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSELEQRLRQQQR---AERLLAEFCKR 545

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1380 A----------QERAQEQGREQTHIEAQgQAQKGAQewaRDRARDQGwEQTQIETQRQTQKG-----AQERAwEQGREQ 1443
Cdd:PRK04863   546 LgknlddedelEQLQEELEARLESLSES-VSEARER---RMALRQQL-EQLQARIQRLAARApawlaAQDAL-ARLREQ 618
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1239-1564 1.21e-04

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: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1318
Cdd:COG3064     56 EAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:COG3064    136 KAEEERKAAEAEAAAKAEAEAAR--AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPA 1478
Cdd:COG3064    214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1479 PRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPGAERALQDRMEA 1558
Cdd:COG3064    294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373


                   ....*.
gi 1769843723 1559 SEPERR 1564
Cdd:COG3064    374 ALLLGK 379
DUF5384 pfam17358
Family of unknown function (DUF5384); This is a family of unknown function found in ...
 1299-1397 1.24e-04

Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.


Pssm-ID: 407453 [Multi-domain]  Cd Length: 145  Bit Score: 43.82  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE-QAQ 1377
Cdd:pfam17358    1 EQQGKEDRVAAERQAAYEREWEEEQARAEAAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRALEiEER 80

                           90       100
                   ....*....|....*....|.
gi 1769843723 1378 KGAQERAQEQG-REQTHIEAQ 1397
Cdd:pfam17358   81 KLALAAQKARAkRENDFIDQE 101
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1322-1391 1.30e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 43.58  E-value: 1.30e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1322 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAQ---ERAREQAQKgAQERAQEQGREQ 1391
Cdd:cd06503     43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEAErilEQAKAEIEQ-EKEKALAELRKE 118
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1244-1398 1.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQ------ERAREQAQ 1317
Cdd:COG4913    274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlerEIERLERE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQK-----GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaqERAQEQGREQT 1392
Cdd:COG4913    354 LEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR----RELRELEAEIA 429


                   ....*.
gi 1769843723 1393 HIEAQG 1398
Cdd:COG4913    430 SLERRK 435
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1270-1389 1.43e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.29  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1270 KGAQERVQGQAQKgaQERAQEQAQEQTQIEAQGQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAR 1349
Cdd:pfam11600    1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1769843723 1350 EQAQKGAQERAREQAQKGAQE----RAREQAQKGAQERAQEQGR 1389
Cdd:pfam11600   78 DEKEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEK 121
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1239-1409 1.44e-04

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: 46.48  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1239 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQ-KGAQERAREQAQ 1317
Cdd:pfam15709  349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFE--EIRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQQQE 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 ---KGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQK--GAQERAREQAQKGAQErAREQAQKGAQERAQEQgrEQ 1391
Cdd:pfam15709  427 efrRKLQELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQE-AEEKARLEAEERRQKE--EE 503

                          170
                   ....*....|....*...
gi 1769843723 1392 THIEAQGQAQKGAQEWAR 1409
Cdd:pfam15709  504 AARLALEEAMKQAQEQAR 521
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1310-1391 1.76e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 43.61  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1310 ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKGAQ---ERAREQAQKGAqERAREQAQKGAQ---ER 1383
Cdd:PRK05759    48 ERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKKRAAqiiEEAKAEAEAEA-ARIKAQAQAEIEqerKR 115


                   ....*...
gi 1769843723 1384 AQEQGREQ 1391
Cdd:PRK05759   116 AREELRKQ 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1322-1444 1.92e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1322 ERAREQAQK----GAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIE- 1395
Cdd:COG1196    206 ERQAEKAERyrelKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEe 285

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1396 AQGQAQKGAQEWARDRARDQGWEQTQIE-TQRQTQKGAQERAWEQGREQA 1444
Cdd:COG1196    286 AQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEEL 335
PTZ00121 PTZ00121
MAEBL; Provisional
 1183-1389 2.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1183 QAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQK 1262
Cdd:PTZ00121  1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1263 WAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEaqgQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR 1337
Cdd:PTZ00121  1668 KKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAE---ELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEDKK 1744

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1338 --EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGR 1389
Cdd:PTZ00121  1745 kaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 1294-1467 2.43e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 45.76  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1294 EQtqieaqgqaqkgaqERAREQAQKgAQERAREQAQKGaqERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR 1373
Cdd:pfam05262  214 RA--------------QQLKEELDK-KQIDADKAQQKA--DFAQDNADK--QRDEVRQKQQEAKNLPKPADTSSPKEDKQ 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1374 -EQAQKGAQERAQEQGREQTHiEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQ--ERAWEQGREQALTSGM 1449
Cdd:pfam05262  275 vAENQKREIEKAQIEIKKNDE-EALKAKDHKAFDLKQEsKASEKEAEDKELEAQKKREPVAEdlQKTKPQVEAQPTSLNE 353

                          170
                   ....*....|....*...
gi 1769843723 1450 APRAWEQPISGIaEGVDA 1467
Cdd:pfam05262  354 DAIDSSNPVYGL-KVVDP 370
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1241-1442 2.64e-04

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: 44.91  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQAQWQTQ-IKAQKWAQEQTQKGAQERVQGQAQkgaqeraqeqaqeqtqIEAQGQAQKGAQERAREQAQKG 1319
Cdd:pfam13868   36 AEEKEEERRLDEMMEEErERALEEEEEKEEERKEERKRYRQE----------------LEEQIEEREQKRQEEYEEKLQE 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1320 AQERaREQAQKGAQERAREQAQKGAQERA---------REQAQKGAQERARE----------QAQKGAQERAREQAQKgA 1380
Cdd:pfam13868  100 REQM-DEIVERIQEEDQAEAEEKLEKQRQlreeidefnEEQAEWKELEKEEEreederileyLKEKAEREEEREAERE-E 177

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1769843723 1381 QERAQEqgREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1442
Cdd:pfam13868  178 IEEEKE--REIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1252-1469 2.79e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1252 AQWQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqERAREQAQKG 1331
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVASAEREIAEL---EAELERLDAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1332 AQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKgAQERAQEQGREQTHIEAQGQAQKGAQEWAR-- 1409
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEE-ELDELQDRLEAAEDLARLELRALLEERFAAal 759

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1410 -DRARDQgwEQTQIETQRQTQKGAQERAweqgrEQALTSGMAP--RAWEQPISGIAEGVDAAG 1469
Cdd:COG4913    760 gDAVERE--LRENLEERIDALRARLNRA-----EEELERAMRAfnREWPAETADLDADLESLP 815
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 1236-1390 2.84e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQ--EQTQIEAQGQAQKGAQERAR 1313
Cdd:PTZ00341   979 VEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEydEENVEEIEENAEENVEENIE 1058

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1769843723 1314 EQAQKGAQERArEQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PTZ00341  1059 ENIEEYDEENV-EEIEENIEENIEENVEENVEENV-EEIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNEE 1133
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1244-1452 3.17e-04

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: 45.73  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQG---QAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGA----QERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR00618  251 AQEEQLKkqqLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QKGAQERAREQAQKG-------AQERAREQAQKGAQERAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQEQgR 1389
Cdd:TIGR00618  331 AAHVKQQSSIEEQRRllqtlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQ-R 407

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1769843723 1390 EQTHIEAQGQAQKGAQEwarDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPR 1452
Cdd:TIGR00618  408 EQATIDTRTSAFRDLQG---QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1303-1430 3.22e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 43.14  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1303 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKL 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1383 RAQEQGRE--QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQK 1430
Cdd:pfam11600   87 RLKEEKRKekQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1256-1458 3.56e-04

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: 45.34  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1256 TQIKAQKWAQEQTQKGAQERVQGQAQ---KGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER-AREQAQKG 1331
Cdd:TIGR00618  179 TQLALMEFAKKKSLHGKAELLTLRSQlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKReAQEEQLKK 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1332 AQERAREQAQKG---AQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQA-QKGA 1404
Cdd:TIGR00618  259 QQLLKQLRARIEelrAQEAVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRihtELQSKMRSRAKLLMKRAAhVKQQ 337

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1405 QEWARDRARDQGWEQTQIETQRQTQkgaQERAWEQGREQALTSGMAPRAWEQPI 1458
Cdd:TIGR00618  338 SSIEEQRRLLQTLHSQEIHIRDAHE---VATSIREISCQQHTLTQHIHTLQQQK 388
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1300-1422 4.16e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1300 AQGQAQKGAQERAREQAQKGA---QERAREQAQKGAQERAREQAQKgAQERAREQAQKGA-QERAREQAQKGAQE-RARE 1374
Cdd:COG1566     86 AQAEAQLAAAEAQLARLEAELgaeAEIAAAEAQLAAAQAQLDLAQR-ELERYQALYKKGAvSQQELDEARAALDAaQAQL 164

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1769843723 1375 QAQKGAQERAQEQGREQTHIEAQGQAQKGAQEwARDRARDQgWEQTQI 1422
Cdd:COG1566    165 EAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAELN-LARTTI 210
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1309-1414 4.18e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 42.46  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1309 QERAREQAQKGAQ-ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKgaqeRAREQAQKgAQERAQEq 1387
Cdd:PRK05759    34 EERQKKIADGLAAaERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKK----RAAQIIEE-AKAEAEA- 96

                           90       100
                   ....*....|....*....|....*..
gi 1769843723 1388 grEQTHIEAQGQAQKGAQewaRDRARD 1414
Cdd:PRK05759    97 --EAARIKAQAQAEIEQE---RKRARE 118
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 748-1142 4.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  748 GAMAAAGSVASRATPAPAPGSTQSPGDRtAGEPETLGQWGSRALSESHPRGEALPRDPHSHGLLAPGGSLEPKSGAAGRS 827
Cdd:PRK07764   417 PAAAAAPAPAAAPQPAPAPAPAPAPPSP-AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  828 LLRGVALVQHPEDIATLARH-PEDAAALARHPEAarlyisnTSAASRHTAAVGG-RKDVAVegnlLGFSTES---GIPAS 902
Cdd:PRK07764   496 APAAPAAPAGADDAATLRERwPEILAAVPKRSRK-------TWAILLPEATVLGvRGDTLV----LGFSTGGlarRFASP 564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  903 DHPRPQARSVAE------SPSYGPGlpPSPPENPQAKGREGVRFPRGAEPDHLLPAVPPAEVDMGWVGGTHQRGPPHLQA 976
Cdd:PRK07764   565 GNAEVLVTALAEelggdwQVEAVVG--PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAA 642

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723  977 HLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVAPSGskvvlnPAKEPQTWWAQ 1056
Cdd:PRK07764   643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAGQADD 716

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1057 DLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEGtrAARNPAVPPGEPEGPGSPAAQGQAQKQVQEWDRGQV 1136
Cdd:PRK07764   717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794


                   ....*.
gi 1769843723 1137 QGHAQE 1142
Cdd:PRK07764   795 DEDRRD 800
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1316-1401 5.05e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 41.91  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1316 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:pfam00430   38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115


                   ....*..
gi 1769843723 1395 EAQGQAQ 1401
Cdd:pfam00430  116 RQQVVAL 122
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1255-1436 5.28e-04

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: 44.73  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1255 QTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERA-------QEQAQEQTQIEAQGQAQkgaQERAREQAQKGAQERAREQ 1327
Cdd:pfam17380  412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAremervrLEEQERQQQVERLRQQE---EERKRKKLELEKEKRDRKR 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1328 aqkgAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:pfam17380  489 ----AEEQRRKILEKELEERKQAMIE---EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561

                          170       180
                   ....*....|....*....|....*....
gi 1769843723 1408 ARDRARDQGWEQTQiETQRQTQKGAQERA 1436
Cdd:pfam17380  562 TEERSRLEAMERER-EMMRQIVESEKARA 589
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 1253-1472 5.30e-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: 44.99  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1253 QWQTQIkaQKWAQEQTQKGAQERVQ--GQAQKGA---QERAQEQAQEQTQIEAQGQAQKGaQERAREQAQKGAQERAREQ 1327
Cdd:TIGR00927  603 KWNKQI--ELWVKEQLSRRPVAKVMalGDLSKGDvaeAEHTGERTGEEGERPTEAEGENG-EESGGEAEQEGETETKGEN 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1328 AQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKG-AQERAQEQGRE-QTHIEAQGQAQKGA 1404
Cdd:TIGR00927  680 ESEGEIPAERKGEQEGEGEiEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIeTGEEGEEVEDEgEGEAEGKHEVETEG 759

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1405 QEWARDRARDQGWEQTQIETQRQTQKGAQ-ERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSG 1472
Cdd:TIGR00927  760 DRKETEHEGETEAEGKEDEDEGEIQAGEDgEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEV 828
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1304-1390 5.49e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 5.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1304 AQKGAQERAREQAQKGAQERAREQAQKgaqeraREQAQKGAQERAREQAQKGAQERA--REQAQKGAQERAREQA---QK 1378
Cdd:cd16269    201 EAERAKAEAAEQERKLLEEQQRELEQK------LEDQERSYEEHLRQLKEKMEEEREnlLKEQERALESKLKEQEallEE 274

                           90
                   ....*....|..
gi 1769843723 1379 GAQERAQEQGRE 1390
Cdd:cd16269    275 GFKEQAELLQEE 286
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1310-1443 6.04e-04

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: 43.75  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1310 ERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERARE-QAQKGAQERAREQAQKGAQERAQEQG 1388
Cdd:pfam13868   50 EEERERALE--EEEEKEEERKEERKRYRQELEEQIEER-EQKRQEEYEEKLQErEQMDEIVERIQEEDQAEAEEKLEKQR 126

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1769843723 1389 REQTHIEAQGQAQKGAQEWARDRARDqgwEQTQIEtQRQTQKGAQERAWEQGREQ 1443
Cdd:pfam13868  127 QLREEIDEFNEEQAEWKELEKEEERE---EDERIL-EYLKEKAEREEEREAEREE 177
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1322-1444 6.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1322 ERAREQAQKgAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQ 1399
Cdd:COG4913    238 ERAHEALED-AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1769843723 1400 AQKGAQEwardrardqgwEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:COG4913    317 RLDALRE-----------ELDELEAQIRGNGGDRLEQLEREIERL 350
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 1324-1462 6.54e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 43.15  E-value: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQerareQAQKGAQERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam13904   62 AAKQRQRQ-KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKAR-----QQTKKREESHKQKAAESASKSLAKPERKV 135

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1404 AQEWARDRArdQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIA 1462
Cdd:pfam13904  136 SQEEAKEVL--QEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQKWMKNVK 192
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 1303-1385 7.22e-04

vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130217 [Multi-domain]  Cd Length: 113  Bit Score: 40.97  E-value: 7.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1303 QAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:TIGR01147   13 QAEKRAAEKVSE-ARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAKIREIKKAVQKN 91


                   ...
gi 1769843723 1383 RAQ 1385
Cdd:TIGR01147   92 KDA 94
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1241-1427 7.45e-04

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: 43.75  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGA--QERAQEqaqeqtqieaqgqaqkgaqERAREQAQK 1318
Cdd:pfam13868  163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-KAERDElrAKLYQE-------------------EQERKERQK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1319 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1398
Cdd:pfam13868  223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAE---REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI 299

                          170       180
                   ....*....|....*....|....*....
gi 1769843723 1399 QAQKGAQEWARDRARDQGWEQTQIETQRQ 1427
Cdd:pfam13868  300 EEREEQRAAEREEELEEGERLREEEAERR 328
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 1245-1443 7.85e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.87  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQGQAQWQTQIKAQKWAQEQTQkgaQERVQGQAQKGAQEraqeqaqeqtqiEAQGQAQKGAQERAR----EQAQKGA 1320
Cdd:pfam15558   54 LLLQQSQEQWQAEKEQRKARLGREE---RRRADRREKQVIEK------------ESRWREQAEDQENQRqeklERARQEA 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1321 QERAREQAQkgaqeraREQAQKGAQERAREQAQKGAQERAREQAQK---------------GAQERAREQAQKGA---QE 1382
Cdd:pfam15558  119 EQRKQCQEQ-------RLKEKEEELQALREQNSLQLQERLEEACHKrqlkereeqkkvqenNLSELLNHQARKVLvdcQA 191

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843723 1383 RAQEQGR----EQTHIEAQGQAQKGAQEWARD-RARDQGWEQtqietqrQTQKgAQERAWEQGREQ 1443
Cdd:pfam15558  192 KAEELLRrlslEQSLQRSQENYEQLVEERHRElREKAQKEEE-------QFQR-AKWRAEEKEEER 249
Caldesmon pfam02029
Caldesmon;
1308-1444 8.60e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 43.70  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1308 AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ------ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1381
Cdd:pfam02029    4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHnsyeedSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1382 ERAQEQGREQTHI------EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1444
Cdd:pfam02029   84 ERQKEFDPTIADEkesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA 152
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1304-1385 9.79e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 40.76  E-value: 9.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1304 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1382
Cdd:pfam00430   38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115


                   ...
gi 1769843723 1383 RAQ 1385
Cdd:pfam00430  116 RQQ 118
PRK06991 PRK06991
electron transport complex subunit RsxB;
1301-1415 9.97e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 42.86  E-value: 9.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1301 QGQAQkGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAReqaQKGA 1380
Cdd:PRK06991   149 QAQAD-AARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAA-ALERAR---KKKE 223

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1769843723 1381 QERAQEQG-REQTHIEAQGQAQKGAQEWARDRARDQ 1415
Cdd:PRK06991   224 ELAAQGAGpKNTEGVSAAVQAQIDAAEARRKRLAEQ 259
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1237-1374 1.14e-03

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: 43.40  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQEraqeqaqeqtqIEAQGQAQKGAQERAREQA 1316
Cdd:pfam15709  397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER-----------AEAEKQRQKELEMQLAEEQ 465

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QK--GAQERAREQAQKGAQErAREQAQKGAQERarEQAQKGAQERAREQAQKGAQERARE 1374
Cdd:pfam15709  466 KRlmEMAEEERLEYQRQKQE-AEEKARLEAEER--RQKEEEAARLALEEAMKQAQEQARQ 522
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 1309-1444 1.15e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 42.38  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1309 QERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQErAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG 1388
Cdd:pfam13904   70 KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ-QTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWE 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843723 1389 REQThieAQGQAQKgaQEWARDRARDQgweqtQIETQRQTQKgaqERAWEQGREQA 1444
Cdd:pfam13904  149 RKKL---EQQQRKR--EEEQREQLKKE-----EEEQERKQLA---EKAWQKWMKNV 191
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1299-1381 1.20e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.50  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQGQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAREQAQKGAqERAREQAQKGAQERA 1372
Cdd:cd06503     44 KAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAEI-EQEKEKALAELRKEV 119


                   ....*....
gi 1769843723 1373 REQAQKGAQ 1381
Cdd:cd06503    120 ADLAVEAAE 128
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 1237-1446 1.58e-03

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


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 43.45  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1237 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1316
Cdd:TIGR00927  682 EGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDR 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1317 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1396
Cdd:TIGR00927  762 KETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1769843723 1397 QGQAQKGAQ----EWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALT 1446
Cdd:TIGR00927  842 QGEAKQDEKgvdgGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1299-1382 1.60e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.54  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQgQAQKGAQER---AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQERAREQ 1375
Cdd:COG0711     49 EAE-AALAEYEEKlaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAEVADL 123


                   ....*..
gi 1769843723 1376 AQKGAQE 1382
Cdd:COG0711    124 AVAIAEK 130
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1310-1386 1.74e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.54  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1310 ERAREQAQKGAQER------AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQER 1383
Cdd:COG0711     44 ERAKEEAEAALAEYeeklaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAE 119


                   ...
gi 1769843723 1384 AQE 1386
Cdd:COG0711    120 VAD 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1236-1413 1.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1236 VQGEVQKWAQEEAQGQAQwQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIE-AQGQAQKGAQERARE 1314
Cdd:COG4372     43 LQEELEQLREELEQAREE-LEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELEsLQEEAEELQEELEEL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1315 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1394
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQELQALSEAEAEQALDELLKEANRNAEKE 199

                          170
                   ....*....|....*....
gi 1769843723 1395 EAQGQAQKGAQEWARDRAR 1413
Cdd:COG4372    200 EELAEAEKLIESLPRELAE 218
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1304-1409 1.96e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1304 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQaqkgaqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1383
Cdd:cd16269    177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQ------ERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEER 250

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1769843723 1384 AQ---EQGREQTHiEAQGQA---QKGAQEWAR 1409
Cdd:cd16269    251 ENllkEQERALES-KLKEQEallEEGFKEQAE 281
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 1244-1424 2.15e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.63  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1244 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1323
Cdd:PRK05035   463 EREKAAREARHKKAAEARAAKDKDAVAAALARVK--AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA 540

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1324 AREQAQKGAQE--RAREQAQKGAQerarEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAq 1401
Cdd:PRK05035   541 AAADPKKAAVAaaIARAKAKKAAQ----QAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA- 615

                          170       180
                   ....*....|....*....|...
gi 1769843723 1402 KGAQEWARDRARDQGWEQTQIET 1424
Cdd:PRK05035   616 AVAAAIARAKAKKAEQQANAEPE 638
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 1246-1445 2.39e-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: 42.65  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1246 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQAQKGAQE 1322
Cdd:TIGR00618  197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEELRAQE 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1323 RAREQAQKgAQERAREQAQKGAQERAREQAQKGAQER-AREQAQKGAQERAREQAQKGAQERAQEQgrEQTHIEAQGQAQ 1401
Cdd:TIGR00618  277 AVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRAAHVKQQSSIE--EQRRLLQTLHSQ 353

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1769843723 1402 KgaqewarDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQAL 1445
Cdd:TIGR00618  354 E-------IHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLT 392
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 1188-1390 2.60e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1188 AQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQ 1267
Cdd:PRK12678    73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1268 TQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQER 1347
Cdd:PRK12678   153 ATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRD-GDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1769843723 1348 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1390
Cdd:PRK12678   232 RRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGR 274
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1168-1377 2.74e-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: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1168 SQGQAQKQFQNWAQGQAQGHAQEQAQwQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEE 1247
Cdd:TIGR02794   65 KEQERQKKLEQQAEEAEKQRAAEQAR-QKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERK 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1248 AQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERARE 1326
Cdd:TIGR02794  144 AKEEAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1769843723 1327 QAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQ 1377
Cdd:TIGR02794  224 EAERKADEAELGDIFGLASGsNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1322-1391 2.90e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.77  E-value: 2.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1322 ERAREQAQKgAQERAREQAQKGAQERA--REQAQKGAQ---ERAREQAQKGAqERAREQAQK---GAQERAQEQGREQ 1391
Cdd:COG0711     44 ERAKEEAEA-ALAEYEEKLAEARAEAAeiIAEARKEAEaiaEEAKAEAEAEA-ERIIAQAEAeieQERAKALAELRAE 119
rne PRK10811
ribonuclease E; Reviewed
 1309-1439 3.65e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.95  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1309 QERaREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQK-GAQERAREQAQKGAQERAREQAQKgaQERAQEQ 1387
Cdd:PRK10811   604 QDR-RKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQqTAETRESQQAEVTEKARTQDEQQQ--APRRERQ 680

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1769843723 1388 GREQthiEAQGQAQKGAQEWARDRARDQgwEQTQIETQRQTQKGAQERAWEQ 1439
Cdd:PRK10811   681 RRRN---DEKRQAQQEAKALNVEEQSVQ--ETEQEERVQQVQPRRKQRQLNQ 727
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1334-1415 3.89e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.34  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1334 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAQEQGREQthIEAQGQAqkgaqew 1407
Cdd:cd06503     43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAE--IEQEKEK------- 110


                   ....*...
gi 1769843723 1408 ARDRARDQ 1415
Cdd:cd06503    111 ALAELRKE 118
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1260-1385 3.93e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 40.06  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1260 AQKWAQEQTQKgaqERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQ 1339
Cdd:pfam11600    3 SQKSVQSQEEK---EKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1340 AQKGAQERAREQAQKGAQE----RAREQAQKGAQERAREQAQKGAQERAQ 1385
Cdd:pfam11600   80 KEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 1241-1452 3.96e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.09  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAqgqAQKGAQERA---REQAQ 1317
Cdd:PRK10246   226 QVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSL---AQPARQLRPhweRIQEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGA----QERAREQAQKGAQERAQ--EQGREQ 1391
Cdd:PRK10246   303 SAALAHTRQQIE---EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwlaeHDRFRQWNNELAGWRAQfsQQTSDR 379

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1769843723 1392 THIEAQgQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQgREQALTSGMAPR 1452
Cdd:PRK10246   380 EQLRQW-QQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQ 438
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 1299-1381 4.05e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQ 1377
Cdd:PRK11448   141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQlEQLQEKAAETSQERKQKRKE 220


                   ....
gi 1769843723 1378 KGAQ 1381
Cdd:PRK11448   221 ITDQ 224
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1298-1407 4.06e-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: 41.29  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1298 IEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQ 1377
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                           90       100       110
                   ....*....|....*....|....*....|
gi 1769843723 1378 KGAQERAQEQGREQTHIEAQGQAQKGAQEW 1407
Cdd:COG4942    228 LIARLEAEAAAAAERTPAAGFAALKGKLPW 257
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 1323-1403 4.19e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 37.90  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1323 RAREQAQKGAQErAREQAQKGAQErAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQK 1402
Cdd:TIGR02926    6 KAEEDAEELIEE-AEEERKQRIAE-AREEARE-LLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIEAMKSKAK 82


                   .
gi 1769843723 1403 G 1403
Cdd:TIGR02926   83 E 83
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1264-1435 4.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1264 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQ-AQKGAQERAREQAQK 1342
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAElERLEARLDALREELD 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1343 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQA-QKGAQEWARDRARDQGWEQTQ 1421
Cdd:COG4913    327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAlRAEAAALLEALEEELEALEEA 406

                          170
                   ....*....|....
gi 1769843723 1422 IETQRQTQKGAQER 1435
Cdd:COG4913    407 LAEAEAALRDLRRE 420
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 1257-1467 4.62e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1257 QIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1335
Cdd:PRK05035   433 QAKAEIRAIEQEKKKAEEaKARFEARQARLEREKA--------AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQ 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1336 AREQAQKG--------AQERAREQAQKGAQERAREQA------QKGAQERAREQAQKGAQERAQEQGREqthiEAQGQAQ 1401
Cdd:PRK05035   505 PIVIKAGArpdnsaviAAREARKAQARARQAEKQAAAaadpkkAAVAAAIARAKAKKAAQQAANAEAEE----EVDPKKA 580

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1769843723 1402 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDA 1467
Cdd:PRK05035   581 AVAAAIARAKAKKA---AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 1188-1405 4.75e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.18  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1188 AQEQAQWQTQIEAQ----GQAQEPAQGGAQGQVQGQAQKWAQgqiqgqaqkqvQGEVQKWAQEEAQGQAQWQTQIKaqKW 1263
Cdd:pfam15558   57 QQSQEQWQAEKEQRkarlGREERRRADRREKQVIEKESRWRE-----------QAEDQENQRQEKLERARQEAEQR--KQ 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1264 AQEQTQKgAQERV----QGQAQKGAQERAQEQAQEQTQIEAQGQAQKGA---QERAREQAQKGA---QERAREQAQKGAQ 1333
Cdd:pfam15558  124 CQEQRLK-EKEEElqalREQNSLQLQERLEEACHKRQLKEREEQKKVQEnnlSELLNHQARKVLvdcQAKAEELLRRLSL 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1334 E----RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ------ERAQEQGREQTHIEAQGQAQKG 1403
Cdd:pfam15558  203 EqslqRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEalaelaDRKIQQARQVAHKTVQDKAQRA 282


                   ..
gi 1769843723 1404 AQ 1405
Cdd:pfam15558  283 RE 284
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1318-1441 4.88e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 39.67  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1318 KGAQERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1397
Cdd:pfam11600    1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1769843723 1398 GQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1441
Cdd:pfam11600   78 DEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEK 121
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1313-1443 5.51e-03

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: 41.09  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1313 REQaQKGAQERAREQAQKGAQ---ERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQ 1387
Cdd:pfam15709  328 REQ-EKASRDRLRAERAEMRRlevERKRreQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE 406

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1769843723 1388 GREQthiEAQGQAqkgaqewARDRARDQGWE--QTQIETQRQTQKGAQERAWEQGREQ 1443
Cdd:pfam15709  407 ERKQ---RLQLQA-------AQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQRQ 454
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
1310-1453 5.59e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 41.12  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1310 ERAREQAQKGAQERAREQAQKG-AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERaqEQG 1388
Cdd:PRK07735     4 EKDLEDLKKEAARRAKEEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQK--REG 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1769843723 1389 REQTHIEAQGQAQKGAQEWARDRARdqgweqtqiETQRQTQKGAQERAWEQGREQALTSGMAPRA 1453
Cdd:PRK07735    82 TEEVTEEEKAKAKAKAAAAAKAKAA---------ALAKQKREGTEEVTEEEKAAAKAKAAAAAKA 137
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1255-1448 5.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1255 QTQIKAQKWAQEQTQKGAQ-ERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQ---- 1329
Cdd:COG4372     42 KLQEELEQLREELEQAREElEQLEEELEQ-ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleel 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1330 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWAR 1409
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1769843723 1410 DRARDQgWEQTQIETQRQTQKGAQERAWEQGREQALTSG 1448
Cdd:COG4372    201 ELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
fliH PRK06669
flagellar assembly protein H; Validated
 1265-1394 6.28e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.38  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1265 QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqerAREQAqKGAQERAREQAqkga 1344
Cdd:PRK06669    32 IKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLK-----KTDEA-SSIIEKLQMQI---- 101

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1769843723 1345 qERAREQAQKgAQERAREQA-QKGAQErAREQAQKGAQERAQEQGREQTHI 1394
Cdd:PRK06669   102 -EREQEEWEE-ELERLIEEAkAEGYEE-GYEKGREEGLEEVRELIEQLNKI 149
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1299-1384 7.99e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1299 EAQGQAQ---KGAQERAREQAQKgAQERAREQAqkgaqERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQ 1375
Cdd:COG0711     63 EARAEAAeiiAEARKEAEAIAEE-AKAEAEAEA-----ERIIAQAEA-EIEQERAKALAELRAEVADLAVAIAEKILGKE 135


                   ....*....
gi 1769843723 1376 AQKGAQERA 1384
Cdd:COG0711    136 LDAAAQAAL 144
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1300-1381 8.79e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 38.06  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1300 AQGQAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQ 1377
Cdd:pfam00430   47 KDAAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQvvALAV 124


                   ....
gi 1769843723 1378 KGAQ 1381
Cdd:pfam00430  125 QIAE 128
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1241-1391 8.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 8.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1241 QKWAQEEAQgQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGA 1320
Cdd:COG4913    262 ERYAAARER-LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1321 QERAREQAQKGAQERAREQAQKGAQERAR---------EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:COG4913    341 EQLEREIERLERELEERERRRARLEALLAalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1245-1391 9.80e-03

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: 39.90  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1769843723 1245 QEEAQGQAQWQTQIKAQKWAQEQTQKgAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgAQERAREQAQKGAQERA 1324
Cdd:pfam13868  193 QEKAQDEKAERDELRAKLYQEEQERK-ERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRK 269

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1769843723 1325 REQAQKGAQERAREQAQKGAQERA--REQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQ 1391
Cdd:pfam13868  270 QAEDEEIEQEEAEKRRMKRLEHRRelEKQIEEREEQRAAEREEE-LEEGERLREEEAERRERIEEERQK 337
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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