|
Name |
Accession |
Description |
Interval |
E-value |
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1-1908 |
0e+00 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 3349.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1 MGKPFWRSVEYFFTGNYSADDGNNNIVAIGFGGQIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLKVEDSTGHLIV 80
Cdd:NF012221 1 MGKSFWRSTEYFFTGNYSADDGNNDIVAIGFGGIIHAYGGDDTITVGSIGATVYTGSGNDTVVGGAGYLKVVDTSGNLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 81 KGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNHGDVSYGGAAAYNGITRKGLSGNVTFAGAGGYNALWHETNQGNLSFT 160
Cdd:NF012221 81 KGAAGYADINKSGDGNVSFTGAAGGVKIDHTGDHGDINYSGAAAYNGITRKGLSGNVSFEGAGGYNKLWHETNQGNLSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 161 GAGAGNKLDRTWSNRYQGSHGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTHQA 240
Cdd:NF012221 161 GAGAGNKLDRTWFNQYQGSHGDVTFDGAGAANIISSRVESGNITFTGAGADNHLIRKGKEGDITLQGAGASNRIERIRNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 241 EDVYTQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTIIRKGSGNDFAKEGMTNAKADEIVLTKAVMSGSWIGQDH 320
Cdd:NF012221 241 QDVYSETRGNIRFEGVGGYNSLYSDVAHGDIHFSGAGAYNEITRKGSGNDSNSEGLEYAKADEIVLTTAYMGGSWIDQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 321 HVTAVKSASEPNTYLFAFADSTYTKINKVQLRNDPQTGELKYYSTAWYKEVNHLSNLANQDISDNGGFTAVNINGaytls 400
Cdd:NF012221 321 QVTAIKSTREPNTYLFAFADGMYTKINKVQLRNDPETGKLKYYSTSWYKEGNHLSNLAGQDISSGNGFESTPTDG----- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 401 dlkvehqqsvtvhavekslteyewvtyangavidakevslsdakmgghaiyadgtkvDVKAVKSNRQPNTYIYAKVLGPY 480
Cdd:NF012221 396 ---------------------------------------------------------DVNAVKSNRKPNTYIYAKLLGTY 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 481 TKIVVVELANDPETGALKYQARSWYKEGDHTANIANQDISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTD 560
Cdd:NF012221 419 TKIVVVELANDAETGALKYQARAWYKEGDHTANLANEDISESNGYTAMGKGGYSLSDLHYSVNTVRIVSERVADIREYSD 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 561 QTLFKPANDSGESSGDVRFNGAGGGNVIKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFR 640
Cdd:NF012221 499 QELFKSSADSGESSGDINFNGAGGGNVIKSNVTRGNVYFNGAGIANVILHSSQFGNTEFNGAGAANVIVKKGEEGDLTFR 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 641 GAGLANVLVHQSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAG 720
Cdd:NF012221 579 GAGLANVLVHQSKQGKMDVYAGGAANVLVRIGDGQYLAHLLAYGNISVHKGNGDSRVVMLGGYNTHTQIGNGNGLWLAAG 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 721 GFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGG 800
Cdd:NF012221 659 GFNVMTQVGKGDVTSVLAGGANVLTKMGEGDLTSGMLGGANIITHISNDEETSNTTAVALGGANILTKKGKGNVLAVMGG 738
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 801 GANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNI 880
Cdd:NF012221 739 GANVLTHIGDGSTTGVMLGGANILTKVGNGDTTGIMLGLGNVLTHVGNGQTLGVMGAAGNIFTKVGDGTTIAAMIGAGNI 818
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 881 FTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHI 960
Cdd:NF012221 819 FTHVGEGDAWALMGGLGNVFTKVGNGNALALMVAKANVFTHIGDGMSVALMLAKGNIATKVGNGMTLAAMVGNANIFTHI 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 961 GHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGL 1040
Cdd:NF012221 899 GHGSTFAAMIGQANILTKVGNDLTAALMVGKANIYTHVGDGTSIGLFAGEANVMTKVGNGTTLAAMFGKANIMTHVGDGL 978
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1041 TGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIG 1120
Cdd:NF012221 979 TGVLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDGTTAAVLAGKGNILTKVGDGTTVGLLISDVGNIMTHVGDGTTIG 1058
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1121 IAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWG 1200
Cdd:NF012221 1059 FAKGKANIITKVGDGLGVNAAWGKANILTHVGDGDRYNFAKGEANIITKVGDGQEVSVVQGDANIITHVGNGDDYTGAWG 1138
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1201 KANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANI 1280
Cdd:NF012221 1139 KANVITKVGDGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGEANITTTVGDGLSVTATYGDANI 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1281 NTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNK 1360
Cdd:NF012221 1219 NTKVGDGVSVNVAWGKYNVNTKVGDGLNVAVMKGKANANIHVGDGLGINASYARNNVAIKIGNGDFYSLAVASSNTSSNK 1298
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1361 LSALFDNIKQTVLGVGGSQAINYLVQGDEASSSGTHKGRGAIATPEITKLDGFQMDAIKEVSSDLGDSLTGSVTKVDTPD 1440
Cdd:NF012221 1299 LSALFDNIKQTVLGVAGSQAINYLVQGDEASTSGTHKGRGAIALPEVSKLDGFQMNEIDEVGSDLGDSLTGSVTQVETPD 1378
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1441 LNKMQHALNVDDS--SVQAPNLIVNGDFELGEHGWQSTHGVEASYAGSVYGVEGEGHGARVTELDTYTNTSLYQDLANLA 1518
Cdd:NF012221 1379 LNAMQNALNIDESvlSTQAPNLIVNGDFEQGAEGWNSTYGVEASHSASVYGLRAEGHGARVSELDTYTNTSLYQDLSNLT 1458
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1519 QGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDESAWQQKNLKLTAQAGSNRIEFKGTGHNDGLGYILDNVVATS 1598
Cdd:NF012221 1459 AGEVIALSFDFARRAGLSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAKAGSNRLEFKGTGHNDGLGYILDNVVATS 1538
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1599 ESSQQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALENNGQAQRDAVKEESEAV 1678
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAV 1618
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1679 TAELAKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGV 1758
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1759 AQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGD 1838
Cdd:NF012221 1699 AQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
1850 1860 1870 1880 1890 1900 1910
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1839 RPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQINAGIR 1908
Cdd:NF012221 1779 KPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAADGRFSEGLTEQEQEALEGATNAVNRLQINAGSR 1848
|
|
| ACD |
pfam16671 |
Actin cross-linking domain; This domain is found in Vibrio cholerae RtxA toxin and VgrG1 ... |
1973-2358 |
0e+00 |
|
Actin cross-linking domain; This domain is found in Vibrio cholerae RtxA toxin and VgrG1 protein. This domain cross-links to G-actin leading to cytoskeletal changes.
Pssm-ID: 293276 Cd Length: 386 Bit Score: 791.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1973 KSVPGFKSHFASTSIGIENELSGLVVVLPKNSAQTFGYVHDSQGNPLFMLTKDMNQGGYSNPVGINDIQGVNNWQTHTIE 2052
Cdd:pfam16671 1 KAVPDFPSHFPKSSIGIENELAGLVVALPKNSAQKFGYVHDAQGNPLFMLTKDMNQGGYQNPPGIQDGKGYNNWQTHTIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2053 LVTYPSEISDTAAVESRKEAMLWLAKEFTDHINQSNHQSLPHLVSDDGRFTLVISNSKHLIAAGNGTSIDAQGKTIGMTP 2132
Cdd:pfam16671 81 LVTYPSEMDDKAAVETRKEAMLWLATEFTTHIDQSNHQPLAPLVSEDGRFTLVISNAKHVIAAGNGISADSQGQTIGMTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2133 SGQQATMAISAKEFGTSSSPEVRLLESAPWYQAGLRDEFLANAKNTTLDDPATAQNVYAYLTSVYSKTADLAKEYGIYIN 2212
Cdd:pfam16671 161 SGQQATVAVSAKGFGTSSSPELRLLESAPWYQKSLKDQFLSNTSNENLDDKATAQNVFAYLTSIYLKTADLAKEYGIYIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2213 DWDPASEGFSPNAQGLTDPKVKNAWSILPRTKPVRMLELLSAEDSRYVRQQIAEKLKGTYSESLAKNVFEYFQYGGEVAG 2292
Cdd:pfam16671 241 DWDPMSEGITPNAQGLTDPKVKNAWEILPRTKPVKMLELLSASDAKAVMKQIKPQLKSRYSESLAKNVFQYFQDGGEVAG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 903393592 2293 HGINNATTGSVQQPEPAILFEFRSVPSALSDFVPKTASTVKVDVKALDHFDSASRKAIITEVNALV 2358
Cdd:pfam16671 321 HGINNATTGDKHSPEPAILFEFRTVPNELSSFVPKTESTTKVEVKLLDQFDPMSRKTIIQQVNSLV 386
|
|
| C80_RtxA-like |
cd20501 |
peptidase C80 cysteine binding domain of RTX toxin RtxA and related proteins; This peptidase ... |
3442-3634 |
3.21e-100 |
|
peptidase C80 cysteine binding domain of RTX toxin RtxA and related proteins; This peptidase C80 family includes the autoproteolytic cysteine protease domain (CPD) of Vibrio cholerae multifunctional autoprocessing repeats-in-toxin (MARTX) toxin that causes disassembly of the actin cytoskeleton and enhances V. cholerae colonization of the small intestine, possibly by facilitating evasion of phagocytic cells. The central region of this toxin is composed of several domains, including the actin cross-linking domain (ACD) that introduces lysine-glutamate cross-links between actin protomers, the Rho-inactivating domain (RID) that disables small Rho GTPases, and an autoprocessing cysteine protease domain (CPD). Within the cell, the CPD is activated by the binding of inositol hexakisphosphate to release individual effector domains of the toxin into the cytosol. The CPD contains the characteristic Cys/His residues in the active site.
Pssm-ID: 410974 Cd Length: 194 Bit Score: 321.12 E-value: 3.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3442 WGPITVTPTTDGGETRFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGR 3521
Cdd:cd20501 1 WDKPTVTPLNKGTDSRYDGQIIIQLENDPTVAEAAARLAGKHPDNSVLVQLDADGNYRVVYGDPSLLKGKLRWQLVGHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3522 DHSET-NNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRS 3600
Cdd:cd20501 81 GGENEaNHQTLAGYSAEQLAEQLAQFSQKLGKDYGINSSPEYISLVGCSLAGEDKQQGFAHQFAQALDKQGIRTDVSARS 160
|
170 180 190
....*....|....*....|....*....|....
gi 903393592 3601 SELAVDEAGRKHTKDANGDWVQKAENNKVSLSWD 3634
Cdd:cd20501 161 TEVAVDEEGRKVTLDEDGNWLHKASEDKVVLSWN 194
|
|
| Peptidase_C80 |
pfam11713 |
Peptidase C80 family; This family belongs to cysteine peptidase family C80. |
3457-3613 |
8.58e-64 |
|
Peptidase C80 family; This family belongs to cysteine peptidase family C80.
Pssm-ID: 288550 Cd Length: 152 Bit Score: 214.91 E-value: 8.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3457 RFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDhsETNNTRLSGYSA 3536
Cdd:pfam11713 1 RYDKQVIVQLEDDDISARAARNLASKHPANSVVYQQDADGSLRVVYGDPAPLAGKLKIQFVGHGRD--EFNNPRLGGYSA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 3537 DELAVKLakfqQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDAN-GLRVDVSVRSSELAVDEAGRKHT 3613
Cdd:pfam11713 79 DSLATEI----QALKQTIPADAKPDKISLVGCSTASNDSRTSLAGKFIQSLDQEiGLSIAVSAYQGEVDVDAAGRKET 152
|
|
| MLD |
pfam11647 |
Membrane Localization Domain; This is a membrane localization domain found in multiple ... |
2561-2646 |
5.10e-33 |
|
Membrane Localization Domain; This is a membrane localization domain found in multiple families of bacterial toxins including all of the clostridial glucosyltransferase toxins and various MARTX toxins (multifunctional-autoprocessing RTX toxins). In the Pasteurella multocida toxin (PMT) C-terminal fragment, structural analysis have indicated that the C1 domain possesses a signal that leads the toxin to the cell membrane. Furthermore, the C1 domain was found to structurally resemble the phospholipid-binding domain of C. difficile toxin B. Functional studies in Vibrio cholera indicate that the subdomain at the N terminus of RID (Rho-inactivation domain), homologous to the membrane targeting C1 domain of Pasteurella multocida toxin, is a conserved membrane localization domain essential for proper localization. The Rho-inactivation domain (RID) of MARTX (Multifunctional Autoprocessing RTX toxin) is responsible for inactivating the Rho-family of small GTPases in Vibrio cholerae. It is a bacterial toxin that self-process by a cysteine peptidase mechanism. The Vibrio cholerae RTX toxin is an autoprocessing cysteine protease whose activity is stimulated by the intracellular environment. This cysteine peptidase belongs to MEROPS peptidase family G6.
Pssm-ID: 431977 Cd Length: 81 Bit Score: 124.01 E-value: 5.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2561 ELMSVTELLDAANVTGKIRGESYQQVIDALTDYHASITEHadyepESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQ 2640
Cdd:pfam11647 1 DLMSVDELRKAAAVFGKRIGESYQNILDALAHYHTASGND-----EKLEALFELRQQITGYLLGHPDSGRNPALKSLQSQ 75
|
....*.
gi 903393592 2641 VNTRLD 2646
Cdd:pfam11647 76 LEDRLF 81
|
|
| toxin_MLD |
cd16840 |
toxin effector region membrane localization domain; This MLD domain functions as a ... |
2563-2646 |
4.59e-28 |
|
toxin effector region membrane localization domain; This MLD domain functions as a membrane-targeting domain for toxin effectors such as the Rho-inactivation domain of Vibrio MARTX, Pasteurella mitogenic toxin (PMT), where it has been termed PMT C1 domain, and clostridial glycosylating cytotoxins including Clostridium difficile toxins A (TcdA) and B (TcdB), Clostridium novyi alpha-toxin (TcnA), and Clostridium sordellii lethal toxin (TcsL). During infection, the C. difficile homologous exotoxins, TcdA and TcdB, target and disrupt the colonic epithelium, leading to diarrhea and colitis. They disrupt host cell function through a multistep process involving receptor binding, endocytosis, low pH-induced pore formation, and the translocation and delivery of a C-terminal glucosyltransferase domain (GTD) that inactivates host GTPases. Their N-terminal MLD domains confer membrane localization of adjacent effector domains via the 4-helix-bundle motif.
Pssm-ID: 411037 Cd Length: 78 Bit Score: 109.63 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2563 MSVTELLDAANVTGKIRGESYQQVIDALTDYHASITEhadyepESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQVN 2642
Cdd:cd16840 1 MSRDELKKAASVFGKPIGESYQAILDALDRYHNTSGD------EKIEKLFELNNQIDGYLEKHPDSGRNPALKKLKQQLN 74
|
....
gi 903393592 2643 TRLD 2646
Cdd:cd16840 75 SALF 78
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
3141-3311 |
1.77e-19 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 91.13 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3141 HAVEKGESQKITLQGEAG-RLTGYYHqgtAPSEGETSSPsgkVVLFLHGSGSSAEeQASAIRNHYQKQGIDMLAVNLRGY 3219
Cdd:COG1073 3 PPSDKVNKEDVTFKSRDGiKLAGDLY---LPAGASKKYP---AVVVAHGNGGVKE-QRALYAQRLAELGFNVLAFDYRGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3220 GESDGGPSEKGLY--QDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADlaryAAQNGQAVSGLLLDRPMPSMTKAITA 3297
Cdd:COG1073 76 GESEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALN----AAATDPRVKAVILDSPFTSLEDLAAQ 151
|
170
....*....|....
gi 903393592 3298 HEVANPAGIVGAIA 3311
Cdd:COG1073 152 RAKEARGAYLPGVP 165
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
701-1223 |
1.75e-11 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 70.96 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 701 GGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVAL 780
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 781 GGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGN 860
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 861 IFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATK 940
Cdd:COG4625 163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 941 VGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNG 1020
Cdd:COG4625 243 GGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1021 TTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFmGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVG 1100
Cdd:COG4625 323 GGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGG-GTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1101 LLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQ 1180
Cdd:COG4625 402 GGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGN 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 903393592 1181 GEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANI 1223
Cdd:COG4625 482 NTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATL 524
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
3181-3297 |
3.25e-10 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 63.68 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3181 KVVLFLHGSGSSAEEQASAIRnHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDA-RTMFNYLVNDKGIDPSNIIihGYS 3259
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAP-ALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDlAEDLEYILEALGLEKVNLV--GHS 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 903393592 3260 MGGPIAadlARYAAQNGQAVSGLLLDRPMPSMTKAITA 3297
Cdd:pfam00561 78 MGGLIA---LAYAAKYPDRVKALVLLGALDPPHELDEA 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1594-1842 |
3.48e-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: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1594 VVATSESSQQANAIR-EHATQNPAAQNALSDKERAEAD---RQRLEQEKQKQLDAVAGSQS---QLESTDQQALENNGQA 1666
Cdd:TIGR02794 42 LVDPGAVAQQANRIQqQKKPAAKKEQERQKKLEQQAEEaekQRAAEQARQKELEQRAAAEKaakQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1667 QRDAVKEESEAVTAELAKLAQgldvldgqathtgesgdqwrndfagglldgvQSQLDDAKQLANDKIAAAKQtlsDNNSK 1746
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAER-------------------------------KAKEEAAKQAEEEAKAKAAA---EAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1747 VKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAES-DAHHAVNNAQSRGDRDVQLAENKANQA 1825
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAaAAAEAERKADEAELGDIFGLASGSNAE 247
|
250
....*....|....*..
gi 903393592 1826 QAdAQGAKQNEGDRPDR 1842
Cdd:TIGR02794 248 KQ-GGARGAAAGSEVDK 263
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1602-1861 |
9.43e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1602 QQANAIR-EHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAgSQSQLESTDQQALENNGQAqrdavkEESEAVTA 1680
Cdd:PRK09510 70 QQKSAKRaEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQE-QKKQAEEAAKQAALKQKQA------EEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1681 ELAKLAQGldvldgqathtgesgdqwrndfagglldgvqsqlDDAKQLAndkiAAAKQTLSDNNSKVKESVAKSEAGVAQ 1760
Cdd:PRK09510 143 AAAKAKAE----------------------------------AEAKRAA----AAAKKAAAEAKKKAEAEAAKKAAAEAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1761 GEQNRAgveqdiADAQADAE-KRKADALAKGKDAQQAE--SDAHHAVNNAQSRGDRDVQlAENKANQAQADAQGAKQNEG 1837
Cdd:PRK09510 185 KKAEAE------AAAKAAAEaKKKAEAEAKKKAAAEAKkkAAAEAKAAAAKAAAEAKAA-AEKAAAAKAAEKAAAAKAAA 257
|
250 260 270
....*....|....*....|....*....|...
gi 903393592 1838 DRPDRQG---------VTGSGLSGNAHSVEGAG 1861
Cdd:PRK09510 258 EVDDLFGgldsgknapKTGGGAKGNGAQGAGAG 290
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
3179-3284 |
1.11e-07 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 56.07 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3179 SGKVVLFLHG-SGSSAEEQASAirnHYQKQGIDMLAVNLRGYGESDGgPSEKGLY-------QDARTMFNYLvndkGIDP 3250
Cdd:TIGR03695 1 AKPVLVFLHGfLGSGADWQALI---EALGPHFRCLAIDLPGHGSSQS-PSDIERYdfeeaaqLLLATLLDQL----GIEP 72
|
90 100 110
....*....|....*....|....*....|....
gi 903393592 3251 snIIIHGYSMGGPIAADLARYAAQNgqaVSGLLL 3284
Cdd:TIGR03695 73 --FFLVGYSMGGRIALYYALQYPER---VQGLIL 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1547-1941 |
3.80e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 56.76 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1547 GEVVFSSSGDESAWQQKNLKLTAQAGSNRIEFKGTGHNDGLGyildnvvatSESSQQANAIREHATQNPAAQNALSDKER 1626
Cdd:NF041483 653 GENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG---------TEAAEALAAAQEEAARRRREAEETLGSAR 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1627 AEADRQR-LEQEKQKQL---------DAVAGSQSQLESTDQQA------LENNGQAQRDAVKEESEAVTAELAKLAQGLD 1690
Cdd:NF041483 724 AEADQEReRAREQSEELlasarkrveEAQAEAQRLVEEADRRAtelvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1691 -VLDGQATHTGESGDQWRNDF----------AGGLLDGVQSQLDDAKQLA----NDKIAAAKQTLSDNNSKVKESVAKSE 1755
Cdd:NF041483 804 hAAERTRTEAQEEADRVRSDAyaererasedANRLRREAQEETEAAKALAertvSEAIAEAERLRSDASEYAQRVRTEAS 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1756 AGVAQGEQNRAgveQDIADAQADAEKRKADALAKG------------KDAQQAESDAHHAVNNAQSRGDRDVQLAENKAN 1823
Cdd:NF041483 884 DTLASAEQDAA---RTRADAREDANRIRSDAAAQAdrligeatseaeRLTAEARAEAERLRDEARAEAERVRADAAAQAE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1824 QAQADAQGakqnEGDRPDRQGVTGSGlSGNAHSVEGAGETDsHVNTDSQTNADGRFSEGLTEQEQeALEGATNAVNRLQI 1903
Cdd:NF041483 961 QLIAEATG----EAERLRAEAAETVG-SAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADR-TLDEARKDANKRRS 1033
|
410 420 430
....*....|....*....|....*....|....*...
gi 903393592 1904 NAGIRAKNSVSSMTSMFSETNSKSIVVPTKVSPEPERQ 1941
Cdd:NF041483 1034 EAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQ 1071
|
|
| 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 ... |
1769-1843 |
4.40e-06 |
|
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: 48.85 E-value: 4.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 903393592 1769 EQDIADAQADAEKRKADALAKGKDAQ----QAESDAHHAVNNAQSRGdrdVQLAENKANQAQADAQGAKQNEGDRPDRQ 1843
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEAEqqlkEARAEAQEIIENAKKRA---EKLKEEIVAAAEAEAERIIEQAAAEIEQE 107
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1598-1865 |
4.78e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.29 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1598 SESSQQANAIREHATQ--NPAAQNALSDKE--RAEADR--QRLEQEKQKQLDAvAGSQSQlESTDQ-QALENNGQAQRDA 1670
Cdd:NF041483 174 AEAEQALAAARAEAERlaEEARQRLGSEAEsaRAEAEAilRRARKDAERLLNA-ASTQAQ-EATDHaEQLRSSTAAESDQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1671 VKEESeavtAELAKLAQgldvldgQATHtgESGDQWRNDFAGGlldgvQSQLDDAKQLANDKIAAAKQTLSDNNSKVKES 1750
Cdd:NF041483 252 ARRQA----AELSRAAE-------QRMQ--EAEEALREARAEA-----EKVVAEAKEAAAKQLASAESANEQRTRTAKEE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1751 VAK--SEAgVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAvnnaqsrgdRDVQLAENKANQAQAD 1828
Cdd:NF041483 314 IARlvGEA-TKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLA---------KAARTAEEVLTKASED 383
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 903393592 1829 AQG---AKQNEGDRPDRQGVT-GSGLSGNAH----SVEGAGETDS 1865
Cdd:NF041483 384 AKAttrAAAEEAERIRREAEAeADRLRGEAAdqaeQLKGAAKDDT 428
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1627-1833 |
6.98e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1627 AEADRQRLEQEKQKQLD--------AVAGSQSQLESTDQQALENNGqAQRDAVKEESEAVTAELAKLAQGLdvLDGQATH 1698
Cdd:NF041483 154 AEQLRARTESQARRLLDesraeaeqALAAARAEAERLAEEARQRLG-SEAESARAEAEAILRRARKDAERL--LNAASTQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1699 TGESGDQwrndfAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAgveQDIADAQAD 1778
Cdd:NF041483 231 AQEATDH-----AEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAA---KQLASAESA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 903393592 1779 AEKRKADALAK--------GKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQAD---AQGAK 1833
Cdd:NF041483 303 NEQRTRTAKEEiarlvgeaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEdtaAQLAK 368
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1569-1830 |
5.31e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1569 AQAGSNRIEFKGTGHNDGLgyildnvvaTSESSQQANAIREHATqnpAAQNALSDKERAEADRQRLEQ-EKQKQLDAVAG 1647
Cdd:NF041483 900 AREDANRIRSDAAAQADRL---------IGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAaAQAEQLIAEAT 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1648 SQSqlESTDQQALENNGQAQRDA--VKEESEAVTAELAKLAQGL---------DVLDgqatHTGESGDQWRNDFAGGLLD 1716
Cdd:NF041483 968 GEA--ERLRAEAAETVGSAQQHAerIRTEAERVKAEAAAEAERLrteareeadRTLD----EARKDANKRRSEAAEQADT 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1717 GVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESV--AKSEAGVAQGEQNRAG---VEQDIADAQ---------ADAEKR 1782
Cdd:NF041483 1042 LITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaARKEAERIVAEATVEGnslVEKARTDADellvgarrdATAIRE 1121
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 903393592 1783 KADALakgKDAQQAESDAHH---------AVNNAQSRGDRDVQLAENKANQAQADAQ 1830
Cdd:NF041483 1122 RAEEL---RDRITGEIEELHerarresaeQMKSAGERCDALVKAAEEQLAEAEAKAK 1175
|
|
| auto_AIDA-I |
NF033176 |
autotransporter adhesin AIDA-I; |
574-1034 |
2.24e-03 |
|
autotransporter adhesin AIDA-I;
Pssm-ID: 380183 [Multi-domain] Cd Length: 1287 Bit Score: 44.26 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 574 SGDVRFNG---AGGGNVIKSNVTRGNVHFNGGGIANVilhssqfgnteFNGGGAANVIVKSGEEGDLTFRGAGLANVLvh 650
Cdd:NF033176 53 SSGVVSGGvvsSGETQVVYSNGQTSNATVNSGGIQNV-----------NNGGKTTSTTVNSSGAQNVGNSGTAISTIV-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 651 qSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSgdSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGK 730
Cdd:NF033176 120 -NSGGVQRVSSGGVTSATSLSGGAQNIYNLGHASNTVIFNGG--NQTIFSGGISDDTNISSGGQQRVSSGGVASNTTINS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 731 GDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISN-------------DDQLS-NTTAVALGGANILTKKGKGNTLA 796
Cdd:NF033176 197 SGTQNILSGGSTVSTHISSGGNQYISAGGNASATVVSSggfqrvssggtatGTVLSgGTQNVSSGGSAISTSVYSSGVQT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 797 VMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNifTKVGDGTSIAVM-- 874
Cdd:NF033176 277 VYAGATVTDTTVNSGGKQNISSGGIVSGTIVNSSGTQNIYSGGSALSANIKGSQIVNSDGTAIN--TLVNDGGYQHIRng 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 875 -IGAGNIFTHVGE------GNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTL 947
Cdd:NF033176 355 gVASGTIINQSGRvnissgGYAESTIINSGGTQSVLSGGYASGTLINNSGRENVSNGGSAYNTIINAGGNQYIYSNGEAS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 948 AAMVgNVNIFTHIGHGSTFAA--MIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLF-AGEVNVMTKVGNGTTLa 1024
Cdd:NF033176 435 GTTV-NTSGFQRVNSGGTATGtkLSGGNQNVSSGGKAIAAEVYSGGKQTVYAGGEASGTQIFdGGVVNVSGGSVSGASV- 512
|
490
....*....|
gi 903393592 1025 AMFGKANIMT 1034
Cdd:NF033176 513 NLNGRLNVFA 522
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1769-1834 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 1769 EQDIADAQADAEKRKADALAKGKDAQQ----AESDAHHAVNNAQSRGDRDVQLAENKAN--------QAQADAQGAKQ 1834
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEklaeARAEAQEIIEEARKEAEKIKEEILAEAKeeaerileQAKAEIEQEKE 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1-1908 |
0e+00 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 3349.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1 MGKPFWRSVEYFFTGNYSADDGNNNIVAIGFGGQIHAYGGDDHVTVGSIGATVYTGSGNDTVVGGSAYLKVEDSTGHLIV 80
Cdd:NF012221 1 MGKSFWRSTEYFFTGNYSADDGNNDIVAIGFGGIIHAYGGDDTITVGSIGATVYTGSGNDTVVGGAGYLKVVDTSGNLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 81 KGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNHGDVSYGGAAAYNGITRKGLSGNVTFAGAGGYNALWHETNQGNLSFT 160
Cdd:NF012221 81 KGAAGYADINKSGDGNVSFTGAAGGVKIDHTGDHGDINYSGAAAYNGITRKGLSGNVSFEGAGGYNKLWHETNQGNLSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 161 GAGAGNKLDRTWSNRYQGSHGDVTFDGAGAANSISSRVETGNITFRGAGADNHLVRKGKVGDITLQGAGASNRIERTHQA 240
Cdd:NF012221 161 GAGAGNKLDRTWFNQYQGSHGDVTFDGAGAANIISSRVESGNITFTGAGADNHLIRKGKEGDITLQGAGASNRIERIRNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 241 EDVYTQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTIIRKGSGNDFAKEGMTNAKADEIVLTKAVMSGSWIGQDH 320
Cdd:NF012221 241 QDVYSETRGNIRFEGVGGYNSLYSDVAHGDIHFSGAGAYNEITRKGSGNDSNSEGLEYAKADEIVLTTAYMGGSWIDQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 321 HVTAVKSASEPNTYLFAFADSTYTKINKVQLRNDPQTGELKYYSTAWYKEVNHLSNLANQDISDNGGFTAVNINGaytls 400
Cdd:NF012221 321 QVTAIKSTREPNTYLFAFADGMYTKINKVQLRNDPETGKLKYYSTSWYKEGNHLSNLAGQDISSGNGFESTPTDG----- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 401 dlkvehqqsvtvhavekslteyewvtyangavidakevslsdakmgghaiyadgtkvDVKAVKSNRQPNTYIYAKVLGPY 480
Cdd:NF012221 396 ---------------------------------------------------------DVNAVKSNRKPNTYIYAKLLGTY 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 481 TKIVVVELANDPETGALKYQARSWYKEGDHTANIANQDISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTD 560
Cdd:NF012221 419 TKIVVVELANDAETGALKYQARAWYKEGDHTANLANEDISESNGYTAMGKGGYSLSDLHYSVNTVRIVSERVADIREYSD 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 561 QTLFKPANDSGESSGDVRFNGAGGGNVIKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFR 640
Cdd:NF012221 499 QELFKSSADSGESSGDINFNGAGGGNVIKSNVTRGNVYFNGAGIANVILHSSQFGNTEFNGAGAANVIVKKGEEGDLTFR 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 641 GAGLANVLVHQSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAG 720
Cdd:NF012221 579 GAGLANVLVHQSKQGKMDVYAGGAANVLVRIGDGQYLAHLLAYGNISVHKGNGDSRVVMLGGYNTHTQIGNGNGLWLAAG 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 721 GFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGG 800
Cdd:NF012221 659 GFNVMTQVGKGDVTSVLAGGANVLTKMGEGDLTSGMLGGANIITHISNDEETSNTTAVALGGANILTKKGKGNVLAVMGG 738
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 801 GANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNI 880
Cdd:NF012221 739 GANVLTHIGDGSTTGVMLGGANILTKVGNGDTTGIMLGLGNVLTHVGNGQTLGVMGAAGNIFTKVGDGTTIAAMIGAGNI 818
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 881 FTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHI 960
Cdd:NF012221 819 FTHVGEGDAWALMGGLGNVFTKVGNGNALALMVAKANVFTHIGDGMSVALMLAKGNIATKVGNGMTLAAMVGNANIFTHI 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 961 GHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGL 1040
Cdd:NF012221 899 GHGSTFAAMIGQANILTKVGNDLTAALMVGKANIYTHVGDGTSIGLFAGEANVMTKVGNGTTLAAMFGKANIMTHVGDGL 978
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1041 TGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIG 1120
Cdd:NF012221 979 TGVLALGEANIVTKVGDDFMGVVAAAKANVVTHVGDGTTAAVLAGKGNILTKVGDGTTVGLLISDVGNIMTHVGDGTTIG 1058
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1121 IAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWG 1200
Cdd:NF012221 1059 FAKGKANIITKVGDGLGVNAAWGKANILTHVGDGDRYNFAKGEANIITKVGDGQEVSVVQGDANIITHVGNGDDYTGAWG 1138
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1201 KANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANI 1280
Cdd:NF012221 1139 KANVITKVGDGRNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGEANITTTVGDGLSVTATYGDANI 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1281 NTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNK 1360
Cdd:NF012221 1219 NTKVGDGVSVNVAWGKYNVNTKVGDGLNVAVMKGKANANIHVGDGLGINASYARNNVAIKIGNGDFYSLAVASSNTSSNK 1298
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1361 LSALFDNIKQTVLGVGGSQAINYLVQGDEASSSGTHKGRGAIATPEITKLDGFQMDAIKEVSSDLGDSLTGSVTKVDTPD 1440
Cdd:NF012221 1299 LSALFDNIKQTVLGVAGSQAINYLVQGDEASTSGTHKGRGAIALPEVSKLDGFQMNEIDEVGSDLGDSLTGSVTQVETPD 1378
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1441 LNKMQHALNVDDS--SVQAPNLIVNGDFELGEHGWQSTHGVEASYAGSVYGVEGEGHGARVTELDTYTNTSLYQDLANLA 1518
Cdd:NF012221 1379 LNAMQNALNIDESvlSTQAPNLIVNGDFEQGAEGWNSTYGVEASHSASVYGLRAEGHGARVSELDTYTNTSLYQDLSNLT 1458
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1519 QGEVIAVSFDFAKRAGLSNNEGIEVLWNGEVVFSSSGDESAWQQKNLKLTAQAGSNRIEFKGTGHNDGLGYILDNVVATS 1598
Cdd:NF012221 1459 AGEVIALSFDFARRAGLSTNNGIEVLWNGEVVFASSGDASAWQQKTLKLTAKAGSNRLEFKGTGHNDGLGYILDNVVATS 1538
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1599 ESSQQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALENNGQAQRDAVKEESEAV 1678
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAV 1618
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1679 TAELAKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGV 1758
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1759 AQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGD 1838
Cdd:NF012221 1699 AQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
1850 1860 1870 1880 1890 1900 1910
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1839 RPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQINAGIR 1908
Cdd:NF012221 1779 KPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAADGRFSEGLTEQEQEALEGATNAVNRLQINAGSR 1848
|
|
| ACD |
pfam16671 |
Actin cross-linking domain; This domain is found in Vibrio cholerae RtxA toxin and VgrG1 ... |
1973-2358 |
0e+00 |
|
Actin cross-linking domain; This domain is found in Vibrio cholerae RtxA toxin and VgrG1 protein. This domain cross-links to G-actin leading to cytoskeletal changes.
Pssm-ID: 293276 Cd Length: 386 Bit Score: 791.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1973 KSVPGFKSHFASTSIGIENELSGLVVVLPKNSAQTFGYVHDSQGNPLFMLTKDMNQGGYSNPVGINDIQGVNNWQTHTIE 2052
Cdd:pfam16671 1 KAVPDFPSHFPKSSIGIENELAGLVVALPKNSAQKFGYVHDAQGNPLFMLTKDMNQGGYQNPPGIQDGKGYNNWQTHTIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2053 LVTYPSEISDTAAVESRKEAMLWLAKEFTDHINQSNHQSLPHLVSDDGRFTLVISNSKHLIAAGNGTSIDAQGKTIGMTP 2132
Cdd:pfam16671 81 LVTYPSEMDDKAAVETRKEAMLWLATEFTTHIDQSNHQPLAPLVSEDGRFTLVISNAKHVIAAGNGISADSQGQTIGMTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2133 SGQQATMAISAKEFGTSSSPEVRLLESAPWYQAGLRDEFLANAKNTTLDDPATAQNVYAYLTSVYSKTADLAKEYGIYIN 2212
Cdd:pfam16671 161 SGQQATVAVSAKGFGTSSSPELRLLESAPWYQKSLKDQFLSNTSNENLDDKATAQNVFAYLTSIYLKTADLAKEYGIYIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2213 DWDPASEGFSPNAQGLTDPKVKNAWSILPRTKPVRMLELLSAEDSRYVRQQIAEKLKGTYSESLAKNVFEYFQYGGEVAG 2292
Cdd:pfam16671 241 DWDPMSEGITPNAQGLTDPKVKNAWEILPRTKPVKMLELLSASDAKAVMKQIKPQLKSRYSESLAKNVFQYFQDGGEVAG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 903393592 2293 HGINNATTGSVQQPEPAILFEFRSVPSALSDFVPKTASTVKVDVKALDHFDSASRKAIITEVNALV 2358
Cdd:pfam16671 321 HGINNATTGDKHSPEPAILFEFRTVPNELSSFVPKTESTTKVEVKLLDQFDPMSRKTIIQQVNSLV 386
|
|
| C80_RtxA-like |
cd20501 |
peptidase C80 cysteine binding domain of RTX toxin RtxA and related proteins; This peptidase ... |
3442-3634 |
3.21e-100 |
|
peptidase C80 cysteine binding domain of RTX toxin RtxA and related proteins; This peptidase C80 family includes the autoproteolytic cysteine protease domain (CPD) of Vibrio cholerae multifunctional autoprocessing repeats-in-toxin (MARTX) toxin that causes disassembly of the actin cytoskeleton and enhances V. cholerae colonization of the small intestine, possibly by facilitating evasion of phagocytic cells. The central region of this toxin is composed of several domains, including the actin cross-linking domain (ACD) that introduces lysine-glutamate cross-links between actin protomers, the Rho-inactivating domain (RID) that disables small Rho GTPases, and an autoprocessing cysteine protease domain (CPD). Within the cell, the CPD is activated by the binding of inositol hexakisphosphate to release individual effector domains of the toxin into the cytosol. The CPD contains the characteristic Cys/His residues in the active site.
Pssm-ID: 410974 Cd Length: 194 Bit Score: 321.12 E-value: 3.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3442 WGPITVTPTTDGGETRFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGR 3521
Cdd:cd20501 1 WDKPTVTPLNKGTDSRYDGQIIIQLENDPTVAEAAARLAGKHPDNSVLVQLDADGNYRVVYGDPSLLKGKLRWQLVGHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3522 DHSET-NNTRLSGYSADELAVKLAKFQQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRS 3600
Cdd:cd20501 81 GGENEaNHQTLAGYSAEQLAEQLAQFSQKLGKDYGINSSPEYISLVGCSLAGEDKQQGFAHQFAQALDKQGIRTDVSARS 160
|
170 180 190
....*....|....*....|....*....|....
gi 903393592 3601 SELAVDEAGRKHTKDANGDWVQKAENNKVSLSWD 3634
Cdd:cd20501 161 TEVAVDEEGRKVTLDEDGNWLHKASEDKVVLSWN 194
|
|
| Peptidase_C80 |
pfam11713 |
Peptidase C80 family; This family belongs to cysteine peptidase family C80. |
3457-3613 |
8.58e-64 |
|
Peptidase C80 family; This family belongs to cysteine peptidase family C80.
Pssm-ID: 288550 Cd Length: 152 Bit Score: 214.91 E-value: 8.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3457 RFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDhsETNNTRLSGYSA 3536
Cdd:pfam11713 1 RYDKQVIVQLEDDDISARAARNLASKHPANSVVYQQDADGSLRVVYGDPAPLAGKLKIQFVGHGRD--EFNNPRLGGYSA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 3537 DELAVKLakfqQSFNQAENINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDAN-GLRVDVSVRSSELAVDEAGRKHT 3613
Cdd:pfam11713 79 DSLATEI----QALKQTIPADAKPDKISLVGCSTASNDSRTSLAGKFIQSLDQEiGLSIAVSAYQGEVDVDAAGRKET 152
|
|
| Peptidase_C80 |
cd20500 |
peptidase C80 family; The peptidase C80 family includes self-cleaving proteins that are ... |
3461-3613 |
3.72e-53 |
|
peptidase C80 family; The peptidase C80 family includes self-cleaving proteins that are precursors of bacterial toxins such as the Vibrio cholerae RTX self-cleaving toxin, as well as the major virulence factors of Clostridium difficile multidomain toxins, TcdA and TcdB. These toxins contain a cysteine protease domain (CPD) that autoproteolytically releases a cytotoxic effector domain upon binding intracellular inositol hexakisphosphate. This family also contains filamentous hemagglutinin family cysteine protease C80 domains, that are located at the C-terminus. All domains in this family contain the characteristic Cys/His residues in the active site. Site-directed mutagenesis has identified functional residues Asp/His/Cys in Clostridium toxin B and His/Cys in cholera RTX toxin.
Pssm-ID: 410973 Cd Length: 150 Bit Score: 184.43 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3461 QIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSK-LDGKLRWQLVGHGRDhSETNNTRLSGYSADEL 3539
Cdd:cd20500 2 QIIVQLEDDPVVLEAALRLASKHPDNSVLIQLDKDGNYRVVYGDALLgLTGNVRLVLVGHGST-DGGGRTTLAGYTAEEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 903393592 3540 AVKLAKFQQSFnqaeNINNKPDHISIVGCSLVSDDKQKGFGHQFINAMDANGLRVDVSVRSSELAVDEAGRKHT 3613
Cdd:cd20500 81 AERISTLKQKL----GPNSRIEKISLVGCNLGSPGVDESFALDFLQALHKNGINAEVTAYTGEVQVNDSGRKIT 150
|
|
| MLD |
pfam11647 |
Membrane Localization Domain; This is a membrane localization domain found in multiple ... |
2561-2646 |
5.10e-33 |
|
Membrane Localization Domain; This is a membrane localization domain found in multiple families of bacterial toxins including all of the clostridial glucosyltransferase toxins and various MARTX toxins (multifunctional-autoprocessing RTX toxins). In the Pasteurella multocida toxin (PMT) C-terminal fragment, structural analysis have indicated that the C1 domain possesses a signal that leads the toxin to the cell membrane. Furthermore, the C1 domain was found to structurally resemble the phospholipid-binding domain of C. difficile toxin B. Functional studies in Vibrio cholera indicate that the subdomain at the N terminus of RID (Rho-inactivation domain), homologous to the membrane targeting C1 domain of Pasteurella multocida toxin, is a conserved membrane localization domain essential for proper localization. The Rho-inactivation domain (RID) of MARTX (Multifunctional Autoprocessing RTX toxin) is responsible for inactivating the Rho-family of small GTPases in Vibrio cholerae. It is a bacterial toxin that self-process by a cysteine peptidase mechanism. The Vibrio cholerae RTX toxin is an autoprocessing cysteine protease whose activity is stimulated by the intracellular environment. This cysteine peptidase belongs to MEROPS peptidase family G6.
Pssm-ID: 431977 Cd Length: 81 Bit Score: 124.01 E-value: 5.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2561 ELMSVTELLDAANVTGKIRGESYQQVIDALTDYHASITEHadyepESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQ 2640
Cdd:pfam11647 1 DLMSVDELRKAAAVFGKRIGESYQNILDALAHYHTASGND-----EKLEALFELRQQITGYLLGHPDSGRNPALKSLQSQ 75
|
....*.
gi 903393592 2641 VNTRLD 2646
Cdd:pfam11647 76 LEDRLF 81
|
|
| toxin_MLD |
cd16840 |
toxin effector region membrane localization domain; This MLD domain functions as a ... |
2563-2646 |
4.59e-28 |
|
toxin effector region membrane localization domain; This MLD domain functions as a membrane-targeting domain for toxin effectors such as the Rho-inactivation domain of Vibrio MARTX, Pasteurella mitogenic toxin (PMT), where it has been termed PMT C1 domain, and clostridial glycosylating cytotoxins including Clostridium difficile toxins A (TcdA) and B (TcdB), Clostridium novyi alpha-toxin (TcnA), and Clostridium sordellii lethal toxin (TcsL). During infection, the C. difficile homologous exotoxins, TcdA and TcdB, target and disrupt the colonic epithelium, leading to diarrhea and colitis. They disrupt host cell function through a multistep process involving receptor binding, endocytosis, low pH-induced pore formation, and the translocation and delivery of a C-terminal glucosyltransferase domain (GTD) that inactivates host GTPases. Their N-terminal MLD domains confer membrane localization of adjacent effector domains via the 4-helix-bundle motif.
Pssm-ID: 411037 Cd Length: 78 Bit Score: 109.63 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2563 MSVTELLDAANVTGKIRGESYQQVIDALTDYHASITEhadyepESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQVN 2642
Cdd:cd16840 1 MSRDELKKAASVFGKPIGESYQAILDALDRYHNTSGD------EKIEKLFELNNQIDGYLEKHPDSGRNPALKKLKQQLN 74
|
....
gi 903393592 2643 TRLD 2646
Cdd:cd16840 75 SALF 78
|
|
| C80_adhesin-like |
cd20503 |
peptidase C80 domains found in filamentous hemagglutinin or adhesin, and other similar ... |
3457-3612 |
3.83e-26 |
|
peptidase C80 domains found in filamentous hemagglutinin or adhesin, and other similar proteins; This peptidase C80 family includes the cysteine-binding domain (CPD) of several large, repetitive bacterial exoproteins involved in heme utilization or adhesion and many typically having CPD repeats as well as regions rich in repeats. Many members of this family have been designated adhesins or filamentous haemagglutinins. The CPD contains the characteristic Asp/Cys/His residues found in Clostridium toxin B active site.
Pssm-ID: 410976 Cd Length: 156 Bit Score: 107.39 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3457 RFDGQIIVQMENDPVVAKAAANLAGKHAESSVVVQLDSDGNYRVVYGDPSKLDGKLRWQLVGHGRDHSETNntRLSGYSA 3536
Cdd:cd20503 1 KYDSRVIVQLGDDEATRQAARRLAGKHPDNTVLVKRDADGELQVLQGGPKNAKGPYKVQVVGHGDGDKGVP--TLGGNDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3537 DELAVKLAKFQQSFNQAEninnkPDHISIVGC--------SLVSDdkqkgFGHQFinamDANGLRVDVSVRSSELAVDEA 3608
Cdd:cd20503 79 AQLAEDLKTLLPQLPGAS-----LAKVTLVGCdsgacngaSLASD-----LRSAL----QAQGPAPEVKGYDGRVDVDAD 144
|
....
gi 903393592 3609 GRKH 3612
Cdd:cd20503 145 GRKL 148
|
|
| toxin_MLD_like |
cd21058 |
membrane localization domain (MLD) of Vibrio MARTX, Pasteurella PMT, clostridial glycosylating ... |
2564-2645 |
6.21e-25 |
|
membrane localization domain (MLD) of Vibrio MARTX, Pasteurella PMT, clostridial glycosylating cytotoxins, toxin effectors BteA (Bordetella T3SS effector A) and related proteins; This family includes membrane localization domains (MLDs) for toxin effectors such as the Rho-inactivation domain of Vibrio MARTX, Pasteurella mitogenic toxin (PMT), where it has been termed PMT C1 domain, and clostridial glycosylating cytotoxins including Clostridium difficile toxins A (TcdA) and B (TcdB), Clostridium novyi alpha-toxin (TcnA), and Clostridium sordellii lethal toxin (TcsL). It also includes the MLD located in the N-terminal minimal membrane-binding fragment of BteA, a type III secretion system (T3SS) effector protein from Bordetella pertussis, the causative agent of whooping cough.
Pssm-ID: 411038 Cd Length: 78 Bit Score: 100.73 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2564 SVTELLDAANVTGKIRGESYQQVIDALTDYHASITEHadyepESVEKLLNLRKKIEGYVLGHPDSGRVEAMNSLLNQVNT 2643
Cdd:cd21058 1 NNDELVRSAAVRGKHSGESYREVLDALREYHASGDRT-----ESLQKLRDLEVLLDHYEASQPFSGRGGAVAELRTQLDA 75
|
..
gi 903393592 2644 RL 2645
Cdd:cd21058 76 YL 77
|
|
| C80_toxinA_B-like |
cd20502 |
Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related ... |
3461-3642 |
4.58e-22 |
|
Peptidase C80 cysteine binding domain of Clostridium difficile toxins A and B, and related proteins; This peptidase C80 family includes the major virulence factors of Clostridium difficile multidomain toxins TcdA and TcdB. These large homologous toxins contain several distinct domains including a cysteine protease domain (CPD) that autoproteolytically releases a cytotoxic effector domain upon binding of intracellular inositol hexakisphosphate. C. difficile is a major cause of intestinal tissue damage and inflammation, and TcdA is generally more inflammatory whereas TcdB is more cytotoxic; studies show that the CPD is an internal regulator of the proinflammatory activity. Site-directed mutagenesis has identified functional residues Asp/His/Cys in Clostridium toxin B.
Pssm-ID: 410975 Cd Length: 209 Bit Score: 97.40 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3461 QIIVQMENDPVVAKAAANLAGKHAESSVVVQL----------DSDGNYRVVYGDPSKLD--GKLRWQLVGHGRDhsETNN 3528
Cdd:cd20502 3 QLIIQLQGDDISFEAACNLFSKHPKNSEWLQLndgeiadvltWDGGSIQEVYTIPLRLDdeGKVKLTLVGHGED--EFGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3529 TRLSGYSADELAVKLAKFQQsfNQAENINNKPDHISIVGCSLVSDDK-----------QKGFGHqfINAMDANGLRVDVS 3597
Cdd:cd20502 81 TTFGGLNAEQLSTELSSLFD--QIKLDIKPKSIKINLLGCNLFDYSQnleetlpgqlaLWLKSK--SDALGISKEQISVS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 903393592 3598 VRSSELAVDEAGRKHTKDANGDWVQKAEN------NKVSLSWDAQ-GEVVAK 3642
Cdd:cd20502 157 ARQYPVRVNSNGKKEVLTHEGGWINKEEAiikdlsHKVELVWDAVeGKLTEK 208
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
3141-3311 |
1.77e-19 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 91.13 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3141 HAVEKGESQKITLQGEAG-RLTGYYHqgtAPSEGETSSPsgkVVLFLHGSGSSAEeQASAIRNHYQKQGIDMLAVNLRGY 3219
Cdd:COG1073 3 PPSDKVNKEDVTFKSRDGiKLAGDLY---LPAGASKKYP---AVVVAHGNGGVKE-QRALYAQRLAELGFNVLAFDYRGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3220 GESDGGPSEKGLY--QDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADlaryAAQNGQAVSGLLLDRPMPSMTKAITA 3297
Cdd:COG1073 76 GESEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALN----AAATDPRVKAVILDSPFTSLEDLAAQ 151
|
170
....*....|....
gi 903393592 3298 HEVANPAGIVGAIA 3311
Cdd:COG1073 152 RAKEARGAYLPGVP 165
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
3182-3292 |
4.71e-14 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 74.67 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3182 VVLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKgLYQDARTMFNYLVNDKGIDPSNIIIHGYSMG 3261
Cdd:COG1506 25 VVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGD-EVDDVLAAIDYLAARPYVDPDRIGIYGHSYG 103
|
90 100 110
....*....|....*....|....*....|.
gi 903393592 3262 GPIAADLaryAAQNGQAVSGLLLDRPMPSMT 3292
Cdd:COG1506 104 GYMALLA---AARHPDRFKAAVALAGVSDLR 131
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
3174-3284 |
9.41e-13 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 70.42 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3174 ETSSPSGKVVLFLHGSGSSAEEQASAIRnHYQKQGIDMLAVNLRGYGESDG----GPSEKGLYQDARTMFNYLVNDKGID 3249
Cdd:COG2267 22 RPAGSPRGTVVLVHGLGEHSGRYAELAE-ALAAAGYAVLAFDLRGHGRSDGprghVDSFDDYVDDLRAALDALRARPGLP 100
|
90 100 110
....*....|....*....|....*....|....*
gi 903393592 3250 psnIIIHGYSMGGPIAadlARYAAQNGQAVSGLLL 3284
Cdd:COG2267 101 ---VVLLGHSMGGLIA---LLYAARYPDRVAGLVL 129
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
3174-3284 |
4.43e-12 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 68.49 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3174 ETSSPSGKVVLFLHGSGSSA---EEQASAIRNHYQkqgidMLAVNLRGYGESDGGPSEKGLYQDARTMfNYLVNDKGIDP 3250
Cdd:COG0596 17 REAGPDGPPVVLLHGLPGSSyewRPLIPALAAGYR-----VIAPDLRGHGRSDKPAGGYTLDDLADDL-AALLDALGLER 90
|
90 100 110
....*....|....*....|....*....|....
gi 903393592 3251 snIIIHGYSMGGPIAadlARYAAQNGQAVSGLLL 3284
Cdd:COG0596 91 --VVLVGHSMGGMVA---LELAARHPERVAGLVL 119
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
701-1223 |
1.75e-11 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 70.96 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 701 GGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVAL 780
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 781 GGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGN 860
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 861 IFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATK 940
Cdd:COG4625 163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 941 VGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNG 1020
Cdd:COG4625 243 GGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1021 TTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFmGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVG 1100
Cdd:COG4625 323 GGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGG-GTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1101 LLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQ 1180
Cdd:COG4625 402 GGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGN 481
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 903393592 1181 GEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANI 1223
Cdd:COG4625 482 NTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATL 524
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
773-1276 |
3.32e-11 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 69.81 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 773 SNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTL 852
Cdd:COG4625 3 GGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 853 GVMGAAGNIFTKVGDGTSIAvmIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALML 932
Cdd:COG4625 83 GGGGGGGTGGVGGGGGGGGG--GGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 933 AKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVN 1012
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1013 VMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVvthVGDATTAAVLAGKGNILTK 1092
Cdd:COG4625 241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGG---GGGGGGGGGGGGGGGGGGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1093 VGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGD 1172
Cdd:COG4625 318 GGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1173 GQEVSVVQGEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQV 1252
Cdd:COG4625 398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477
|
490 500
....*....|....*....|....
gi 903393592 1253 TAAKGQANITTTVGNGLNVTAAYG 1276
Cdd:COG4625 478 LTGNNTYTGTTTVNGGGNYTQSAG 501
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
658-1222 |
1.31e-10 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 67.88 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 658 DVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVL 737
Cdd:COG4625 5 GGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 738 AGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVM 817
Cdd:COG4625 85 GGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 818 VGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLG 897
Cdd:COG4625 165 GGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 898 NVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMT 977
Cdd:COG4625 245 GGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 978 KVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGD 1057
Cdd:COG4625 325 GGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1058 DFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLG 1137
Cdd:COG4625 405 AGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTY 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1138 VNVTwgqanvftQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLA 1217
Cdd:COG4625 485 TGTT--------TVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVAAALDALAG 556
|
....*
gi 903393592 1218 KGEAN 1222
Cdd:COG4625 557 NGDLS 561
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1618-1834 |
1.42e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1618 QNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALENngQAQRDAVKEESEAVTAELAKLAQGLDVLDGQAT 1697
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL--ELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1698 HTGESGDQwrndfagglLDGVQSQLDDAKQLANDKIAAAKQTLSDnnskVKESVAKSEAGVAQGEQNRAGVEQDIADAQA 1777
Cdd:COG1196 313 ELEERLEE---------LEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 903393592 1778 DAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQ 1834
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
582-1408 |
2.05e-10 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 67.48 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 582 AGGGNVIKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYA 661
Cdd:COG3210 799 TADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASIT 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 662 GGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLG-----GYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAV 736
Cdd:COG3210 879 VGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVTAtgtggGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAAS 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 737 LAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGV 816
Cdd:COG3210 959 ASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAA 1038
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 817 MVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGL 896
Cdd:COG3210 1039 TAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTA 1118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 897 GNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIM 976
Cdd:COG3210 1119 SKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDL 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 977 TKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLG 1056
Cdd:COG3210 1199 KGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAG 1278
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1057 DDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGL 1136
Cdd:COG3210 1279 ATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGA 1358
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1137 GVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVL 1216
Cdd:COG3210 1359 TDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTG 1438
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1217 AKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANINTKVGDGVSVNVAWGK 1296
Cdd:COG3210 1439 NTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAE 1518
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1297 YNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTVLGVG 1376
Cdd:COG3210 1519 VAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLT 1598
|
810 820 830
....*....|....*....|....*....|..
gi 903393592 1377 GSQAINYLVQGDEASSSGTHKGRGAIATPEIT 1408
Cdd:COG3210 1599 LSLAEGTNAEYGGTTNVTSGTAGNAGATGANS 1630
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
766-1200 |
2.64e-10 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 66.89 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 766 ISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTH 845
Cdd:COG3468 4 GGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 846 VGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFThvGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDG 925
Cdd:COG3468 84 TGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGG--GGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 926 MSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLG 1005
Cdd:COG3468 162 GSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1006 LFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAG 1085
Cdd:COG3468 242 GGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1086 KGNILTKVGEGTTVGLLISDVGNVMThvGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEAN 1165
Cdd:COG3468 322 AGGGSGGGGGGGGGGGGGGTTLNGAG--SAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGG 399
|
410 420 430
....*....|....*....|....*....|....*
gi 903393592 1166 LITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWG 1200
Cdd:COG3468 400 TGNNGGGGVGGGGGGGLTLTGGTLTVNGNYTGNNG 434
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
3181-3297 |
3.25e-10 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 63.68 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3181 KVVLFLHGSGSSAEEQASAIRnHYQKQGIDMLAVNLRGYGESDGGPSEKGLYQDA-RTMFNYLVNDKGIDPSNIIihGYS 3259
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAP-ALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDlAEDLEYILEALGLEKVNLV--GHS 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 903393592 3260 MGGPIAadlARYAAQNGQAVSGLLLDRPMPSMTKAITA 3297
Cdd:pfam00561 78 MGGLIA---LAYAAKYPDRVKALVLLGALDPPHELDEA 112
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
3181-3288 |
1.76e-09 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 61.46 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3181 KVVLFLHGSGSSA---EEQASAIrnhyQKQGIDMLAVNLRGYGESDGG----PSEKGLYQDARTMFNYLVNDKGIDPsnI 3253
Cdd:pfam12146 5 AVVVLVHGLGEHSgryAHLADAL----AAQGFAVYAYDHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEHPGLP--L 78
|
90 100 110
....*....|....*....|....*....|....*
gi 903393592 3254 IIHGYSMGGPIAadlARYAAQNGQAVSGLLLDRPM 3288
Cdd:pfam12146 79 FLLGHSMGGLIA---ALYALRYPDKVDGLILSAPA 110
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1594-1842 |
3.48e-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: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1594 VVATSESSQQANAIR-EHATQNPAAQNALSDKERAEAD---RQRLEQEKQKQLDAVAGSQS---QLESTDQQALENNGQA 1666
Cdd:TIGR02794 42 LVDPGAVAQQANRIQqQKKPAAKKEQERQKKLEQQAEEaekQRAAEQARQKELEQRAAAEKaakQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1667 QRDAVKEESEAVTAELAKLAQgldvldgqathtgesgdqwrndfagglldgvQSQLDDAKQLANDKIAAAKQtlsDNNSK 1746
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAER-------------------------------KAKEEAAKQAEEEAKAKAAA---EAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1747 VKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAES-DAHHAVNNAQSRGDRDVQLAENKANQA 1825
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAaAAAEAERKADEAELGDIFGLASGSNAE 247
|
250
....*....|....*..
gi 903393592 1826 QAdAQGAKQNEGDRPDR 1842
Cdd:TIGR02794 248 KQ-GGARGAAAGSEVDK 263
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
844-1290 |
9.47e-09 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 61.89 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 844 THVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIG 923
Cdd:COG3468 4 GGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 924 DGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTS 1003
Cdd:COG3468 84 TGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1004 LGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVL 1083
Cdd:COG3468 164 GGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1084 AGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGE 1163
Cdd:COG3468 244 SAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1164 ANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWGKANVITkvGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIV 1243
Cdd:COG3468 324 GGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSG--GGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTG 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 903393592 1244 TKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANINTKVGDGVSV 1290
Cdd:COG3468 402 NNGGGGVGGGGGGGLTLTGGTLTVNGNYTGNNGTLVLNTVLGDDNSP 448
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
705-1130 |
1.35e-08 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 61.50 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 705 THTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGAN 784
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 785 ILTkkGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVlthVGDGQTLGVMGAAGNIFTK 864
Cdd:COG3468 81 SGG--TGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSA---GGGGGGGGGGTGVGGTGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 865 VGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNG 944
Cdd:COG3468 156 AAGGGTGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 945 TTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNG-TTL 1023
Cdd:COG3468 236 GGVGGGGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGnGGG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1024 AAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLI 1103
Cdd:COG3468 316 GGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGL 395
|
410 420
....*....|....*....|....*..
gi 903393592 1104 SDVGNVMTHVGDGTTIGIAKGKANLIT 1130
Cdd:COG3468 396 TTGGTGNNGGGGVGGGGGGGLTLTGGT 422
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
44-1541 |
9.14e-08 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 59.01 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 44 VTVGSIGATVYTGSGNDTVVGGSAYLKVEDSTGHLIVKGAAGYADINKSGDGNVSFAGAAGGVSIDHLGNHGDVSYGGAA 123
Cdd:COG3210 19 AVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGTLETGLTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 124 AYNGITRKGLSGNVTFAGAGGYNALWHETNQGNLSFTGAGAGNKLDRTWSNRYQGSHGDVTFDGAGAANSISSRVETGNI 203
Cdd:COG3210 99 NIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGTNIGNSIP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 204 TFRGAGADNHLVRKGKVGDITLQGAGASNRIERTHQAEDVYTQTRGNIRFEGVGGYNSLYSDVAHGDIHFSGGGAYNTII 283
Cdd:COG3210 179 TTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSLSVAAGAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 284 RKGSGNDFAKEGMTNAKADEIVLTKAVMSGSWIGQDH---HVTAVKSASEPNTYLFAFADSTYTKINKVQLRNDPQTGEL 360
Cdd:COG3210 259 TGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTttnGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTAN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 361 KYYSTAWYKEVNHLSNLANQ--DISDNGGFTAVNINGAYTLSDLKVEHQQSVTVHAVEKSLTEYEWVTYANGAVIDAKEV 438
Cdd:COG3210 339 SGAGLVSGGTGGNNGTTGTGagSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 439 SLSDAKMGGHAIYADGTKVDVKAVKSNRQPNTYIYAKVLGPYTKIVVVELANDPETGALKYQARSWYKEGDHTANIANQD 518
Cdd:COG3210 419 GSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNAT 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 519 ISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTDQTLFKPANDSGESSGDV----------RFNGAGGGNVI 588
Cdd:COG3210 499 ISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAasgsntantlGVLAATGGTSN 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 589 KSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYAGGAVNVL 668
Cdd:COG3210 579 ATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANG 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 669 VRLGDGQYLAHLLAYGNISVQKGSGDSRVVM-LGGYNTHTQIGSGNGLWLAAGGFNVMTQVGK------GDVAAVLAGGA 741
Cdd:COG3210 659 SNTTGVNTAGGTGGGTTGTVTSGATGGTTGTtLNAATGGTLNNAGNTLTISTGSITVTGQIGAlanangDTVTFGNLGTG 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 742 NVLTKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANIL--TKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVG 819
Cdd:COG3210 739 ATLTLNAGVTITSGNAGTLSIGLTANTTASGTTLTLANANGNTSAgaTLDNAGAEISIDITADGTITAAGTTAINVTGSG 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 820 GANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAwalmGGLGNV 899
Cdd:COG3210 819 GTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATST----GTANAG 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 900 FTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKV 979
Cdd:COG3210 895 TLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGS 974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 980 GNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDF 1059
Cdd:COG3210 975 SAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGIS 1054
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1060 MGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVN 1139
Cdd:COG3210 1055 GGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTST 1134
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1140 VTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYTGAWGKANVITKVGHGQNVVLAKG 1219
Cdd:COG3210 1135 ASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTT 1214
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1220 EANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANINTKVGDGVSVNVAWGKYNI 1299
Cdd:COG3210 1215 NVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSAT 1294
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1300 NTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNTSSNKLSALFDNIKQTVLGVGGSQ 1379
Cdd:COG3210 1295 SAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSL 1374
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1380 AINYLVQGDEASSSGTHKGRGAIATPEITKLDGFQMDAIKEVSSDLGDSLTGSVTKVDTPDLNKMQHALNVDDSSVQAPN 1459
Cdd:COG3210 1375 AATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNAD 1454
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1460 LIVNGDFELGEHGWQSTHGVEASYAGSVYGVEGEGHGARVTELDTYTNTSLYQDLANLAQGEVIAVSFDFAKRAGLSNNE 1539
Cdd:COG3210 1455 ASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGS 1534
|
..
gi 903393592 1540 GI 1541
Cdd:COG3210 1535 SV 1536
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1602-1861 |
9.43e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1602 QQANAIR-EHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAgSQSQLESTDQQALENNGQAqrdavkEESEAVTA 1680
Cdd:PRK09510 70 QQKSAKRaEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQE-QKKQAEEAAKQAALKQKQA------EEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1681 ELAKLAQGldvldgqathtgesgdqwrndfagglldgvqsqlDDAKQLAndkiAAAKQTLSDNNSKVKESVAKSEAGVAQ 1760
Cdd:PRK09510 143 AAAKAKAE----------------------------------AEAKRAA----AAAKKAAAEAKKKAEAEAAKKAAAEAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1761 GEQNRAgveqdiADAQADAE-KRKADALAKGKDAQQAE--SDAHHAVNNAQSRGDRDVQlAENKANQAQADAQGAKQNEG 1837
Cdd:PRK09510 185 KKAEAE------AAAKAAAEaKKKAEAEAKKKAAAEAKkkAAAEAKAAAAKAAAEAKAA-AEKAAAAKAAEKAAAAKAAA 257
|
250 260 270
....*....|....*....|....*....|...
gi 903393592 1838 DRPDRQG---------VTGSGLSGNAHSVEGAG 1861
Cdd:PRK09510 258 EVDDLFGgldsgknapKTGGGAKGNGAQGAGAG 290
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1606-1843 |
9.92e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1606 AIREHATQNPAAQNAlsdKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALenngQAQRDAVKEESEAVTAELAKL 1685
Cdd:PRK05035 437 EIRAIEQEKKKAEEA---KARFEARQARLEREKAAREARHKKAAEARAAKDKDAV----AAALARVKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1686 AQGLDVLDGQATHTGESGDQWRNDFAggllDGVQSQLDDAKQlanDKIAAAkqtlsdnnskvkesVAKSEAGVAQGEQNR 1765
Cdd:PRK05035 510 AGARPDNSAVIAAREARKAQARARQA----EKQAAAAADPKK---AAVAAA--------------IARAKAKKAAQQAAN 568
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 1766 AGVEQDIADAQADAEKRKADALAKgKDAQQAESDAhhavnNAQSRGDRDVQLAENKANQAQADAQGAKQNEGDRPDRQ 1843
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAK-KAAQQAASAE-----PEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP 640
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
615-1134 |
1.10e-07 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 58.25 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 615 GNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSGD 694
Cdd:COG4625 4 GGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 695 SRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISNDDQLSN 774
Cdd:COG4625 84 GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 775 TTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGV 854
Cdd:COG4625 164 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 855 MGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAK 934
Cdd:COG4625 244 GGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 935 GNVATKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVM 1014
Cdd:COG4625 324 GGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1015 TKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTklGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVG 1094
Cdd:COG4625 404 GAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGG--GGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGN 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 903393592 1095 EGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGD 1134
Cdd:COG4625 482 NTYTGTTTVNGGGNYTQSAGSTLAVEVDAANSDRLVVTGT 521
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
3179-3284 |
1.11e-07 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 56.07 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3179 SGKVVLFLHG-SGSSAEEQASAirnHYQKQGIDMLAVNLRGYGESDGgPSEKGLY-------QDARTMFNYLvndkGIDP 3250
Cdd:TIGR03695 1 AKPVLVFLHGfLGSGADWQALI---EALGPHFRCLAIDLPGHGSSQS-PSDIERYdfeeaaqLLLATLLDQL----GIEP 72
|
90 100 110
....*....|....*....|....*....|....
gi 903393592 3251 snIIIHGYSMGGPIAADLARYAAQNgqaVSGLLL 3284
Cdd:TIGR03695 73 --FFLVGYSMGGRIALYYALQYPER---VQGLIL 101
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
1037-1466 |
1.20e-07 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 58.03 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1037 GDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDG 1116
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1117 TTIGIAKGKANLITKVGDGLGVNVTWGqANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSVVQGEANIITHVGNGDDYT 1196
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGGG-GGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1197 GAWGKANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYG 1276
Cdd:COG3468 160 GTGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1277 DANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNT 1356
Cdd:COG3468 240 GGGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1357 SSNKLSALFDNIKQTVLGVGGSQAINYLVQGDEASSSGTHKGRGAIATPEITKLDGFQMDAIKEVSSDLGDSLTGSVTKV 1436
Cdd:COG3468 320 SNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGG 399
|
410 420 430
....*....|....*....|....*....|
gi 903393592 1437 DTPDLNKMQHALNVDDSSVQAPNLIVNGDF 1466
Cdd:COG3468 400 TGNNGGGGVGGGGGGGLTLTGGTLTVNGNY 429
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
939-1395 |
1.28e-07 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 58.03 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 939 TKVGNGTTLAAMVGNVNIFTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLFAGEVNVMTKVG 1018
Cdd:COG3468 1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1019 NGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVVTHVGDATTAAVLAGKGNILTKVGEGTT 1098
Cdd:COG3468 81 SGGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1099 VGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQVGDGDRYNFAKGEANLITKVGDGQEVSV 1178
Cdd:COG3468 161 TGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1179 VQGEAniithvGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANIVTQVGDGDSFNALWSKGNIVTKVGDGMQVTAAKGQ 1258
Cdd:COG3468 241 GGGSA------GGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1259 ANITTTVGNGLNVTAAYGDANINTKVGDGVSVNVAWGkyniNTKVGDGLNVAVMKGKANANIHVGDGLNINASYAQNNVA 1338
Cdd:COG3468 315 GGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGG----GTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 903393592 1339 IKVGNGDFYSLAVASSNTSSNklsalfdnikqtVLGVGGSQAINYLVQGDEASSSGT 1395
Cdd:COG3468 391 VGTGLTTGGTGNNGGGGVGGG------------GGGGLTLTGGTLTVNGNYTGNNGT 435
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
3181-3284 |
2.78e-07 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 54.95 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3181 KVVLFLHGSGSSAEEqASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGL---YQDARTMFNYLVNDKgidpSNIIIHG 3257
Cdd:COG1647 16 KGVLLLHGFTGSPAE-MRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWedwLEDVEEAYEILKAGY----DKVIVIG 90
|
90 100
....*....|....*....|....*..
gi 903393592 3258 YSMGGPIAAdlarYAAQNGQAVSGLLL 3284
Cdd:COG1647 91 LSMGGLLAL----LLAARYPDVAGLVL 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1547-1941 |
3.80e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 56.76 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1547 GEVVFSSSGDESAWQQKNLKLTAQAGSNRIEFKGTGHNDGLGyildnvvatSESSQQANAIREHATQNPAAQNALSDKER 1626
Cdd:NF041483 653 GENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG---------TEAAEALAAAQEEAARRRREAEETLGSAR 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1627 AEADRQR-LEQEKQKQL---------DAVAGSQSQLESTDQQA------LENNGQAQRDAVKEESEAVTAELAKLAQGLD 1690
Cdd:NF041483 724 AEADQEReRAREQSEELlasarkrveEAQAEAQRLVEEADRRAtelvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1691 -VLDGQATHTGESGDQWRNDF----------AGGLLDGVQSQLDDAKQLA----NDKIAAAKQTLSDNNSKVKESVAKSE 1755
Cdd:NF041483 804 hAAERTRTEAQEEADRVRSDAyaererasedANRLRREAQEETEAAKALAertvSEAIAEAERLRSDASEYAQRVRTEAS 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1756 AGVAQGEQNRAgveQDIADAQADAEKRKADALAKG------------KDAQQAESDAHHAVNNAQSRGDRDVQLAENKAN 1823
Cdd:NF041483 884 DTLASAEQDAA---RTRADAREDANRIRSDAAAQAdrligeatseaeRLTAEARAEAERLRDEARAEAERVRADAAAQAE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1824 QAQADAQGakqnEGDRPDRQGVTGSGlSGNAHSVEGAGETDsHVNTDSQTNADGRFSEGLTEQEQeALEGATNAVNRLQI 1903
Cdd:NF041483 961 QLIAEATG----EAERLRAEAAETVG-SAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADR-TLDEARKDANKRRS 1033
|
410 420 430
....*....|....*....|....*....|....*...
gi 903393592 1904 NAGIRAKNSVSSMTSMFSETNSKSIVVPTKVSPEPERQ 1941
Cdd:NF041483 1034 EAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQ 1071
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
3183-3285 |
4.27e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 53.63 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3183 VLFLHGSGSSAEEQASAirnhyQKQGIDMLAVNLRGYGESDGGPSEkglYQDARTMFNYLvnDKGIDPSNIIIHGYSMGG 3262
Cdd:pfam12697 1 VVLVHGAGLSAAPLAAL-----LAAGVAVLAPDLPGHGSSSPPPLD---LADLADLAALL--DELGAARPVVLVGHSLGG 70
|
90 100
....*....|....*....|...
gi 903393592 3263 PIAADLARYAaqngqAVSGLLLD 3285
Cdd:pfam12697 71 AVALAAAAAA-----LVVGVLVA 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1602-1909 |
4.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1602 QQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTdqqalenngQAQRDAVKEESEAVTAE 1681
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL---------EEELEEAEEELEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1682 LAKLAQGLDVLDGQATHTGESGDQWRNDfagglldgvQSQLDDAKQLANDKIAAAKQTLSDNNSKvKESVAKSEAGVAQG 1761
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEE---------LLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1762 EQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGdrpD 1841
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG---F 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 1842 RQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQINAGIRA 1909
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1596-1836 |
5.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1596 ATSESSQQANAIREHATQNPAAQNALSDKE------RAEADRQRLE-QEKQKQLDAVAGSQSQLEstdqqalenngqAQR 1668
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEaeleelRLELEELELElEEAQAEEYELLAELARLE------------QDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1669 DAVKEESEAVTAELAKLAQGLDVLDGQATHTGESGDQWRNDF--AGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSK 1746
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1747 VKESVA--KSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQ 1824
Cdd:COG1196 385 AEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250
....*....|..
gi 903393592 1825 AQADAQGAKQNE 1836
Cdd:COG1196 465 LAELLEEAALLE 476
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1718-2135 |
1.17e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1718 VQSQLDDAKQLANDKIAAAKQTLSDNNS-KVKESVAKSEAgVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQ- 1795
Cdd:COG3064 14 AQERLEQAEAEKRAAAEAEQKAKEEAEEeRLAELEAKRQA-EEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1796 --AESDAHHAVNNAQSRGDRDVQLAEN-KANQAQADAQGAKQNEGDRpdrqgvtgsglsgnahSVEGAGETDSHVNTDSQ 1872
Cdd:COG3064 93 aaAEKAKAAKEAEAAAAAEKAAAAAEKeKAEEAKRKAEEEAKRKAEE----------------ERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1873 TNADGRFSEGLTEQEQEALEGATNAVNRLQINAGIRAKNSVSSMTSMFSETNSKSIVVPTKVSPEPERQEVTRRDVRISG 1952
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1953 VNLESLSAVQGSQPTGQLASKSVPGFKSHFASTSIGIENELSGLVVVLPKNSAQTFGYVHDSQGNPLFMLTKDMNQGGYS 2032
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 2033 NPVGINDIQGVNNWQTHTIELVTYPSEISDTAAVESRKEAMLWLAKEFTDHINQSNHQSLPHLVSDDGRFTLVISNSKHL 2112
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
410 420
....*....|....*....|...
gi 903393592 2113 IAAGNGTSIDAQGKTIGMTPSGQ 2135
Cdd:COG3064 397 GGGLLGLRLDLGAALLEAASAVE 419
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1617-1882 |
3.95e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1617 AQNALSDKERAEADRQRLEQEKQKQLDAVagsQSQLESTDQQALENngQAQRDAVKEESEAVTAELAK----LAQGLDVL 1692
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNEL--QAELEALQAEIDKLQAEIAEaeaeIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1693 DGQATH---TGESGDQWR-----NDFaGGLLDGVQ--SQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGVAQGE 1762
Cdd:COG3883 89 GERARAlyrSGGSVSYLDvllgsESF-SDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1763 QNRAGVEQDIADAQA---------DAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAK 1833
Cdd:COG3883 168 AAKAELEAQQAEQEAllaqlsaeeAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 903393592 1834 QNEGDRPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEG 1882
Cdd:COG3883 248 GAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGG 296
|
|
| 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 ... |
1769-1843 |
4.40e-06 |
|
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: 48.85 E-value: 4.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 903393592 1769 EQDIADAQADAEKRKADALAKGKDAQ----QAESDAHHAVNNAQSRGdrdVQLAENKANQAQADAQGAKQNEGDRPDRQ 1843
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEAEqqlkEARAEAQEIIENAKKRA---EKLKEEIVAAAEAEAERIIEQAAAEIEQE 107
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1598-1865 |
4.78e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.29 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1598 SESSQQANAIREHATQ--NPAAQNALSDKE--RAEADR--QRLEQEKQKQLDAvAGSQSQlESTDQ-QALENNGQAQRDA 1670
Cdd:NF041483 174 AEAEQALAAARAEAERlaEEARQRLGSEAEsaRAEAEAilRRARKDAERLLNA-ASTQAQ-EATDHaEQLRSSTAAESDQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1671 VKEESeavtAELAKLAQgldvldgQATHtgESGDQWRNDFAGGlldgvQSQLDDAKQLANDKIAAAKQTLSDNNSKVKES 1750
Cdd:NF041483 252 ARRQA----AELSRAAE-------QRMQ--EAEEALREARAEA-----EKVVAEAKEAAAKQLASAESANEQRTRTAKEE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1751 VAK--SEAgVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAvnnaqsrgdRDVQLAENKANQAQAD 1828
Cdd:NF041483 314 IARlvGEA-TKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLA---------KAARTAEEVLTKASED 383
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 903393592 1829 AQG---AKQNEGDRPDRQGVT-GSGLSGNAH----SVEGAGETDS 1865
Cdd:NF041483 384 AKAttrAAAEEAERIRREAEAeADRLRGEAAdqaeQLKGAAKDDT 428
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1627-1833 |
6.98e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1627 AEADRQRLEQEKQKQLD--------AVAGSQSQLESTDQQALENNGqAQRDAVKEESEAVTAELAKLAQGLdvLDGQATH 1698
Cdd:NF041483 154 AEQLRARTESQARRLLDesraeaeqALAAARAEAERLAEEARQRLG-SEAESARAEAEAILRRARKDAERL--LNAASTQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1699 TGESGDQwrndfAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAgveQDIADAQAD 1778
Cdd:NF041483 231 AQEATDH-----AEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAA---KQLASAESA 302
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 903393592 1779 AEKRKADALAK--------GKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQAD---AQGAK 1833
Cdd:NF041483 303 NEQRTRTAKEEiarlvgeaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEdtaAQLAK 368
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
430-848 |
8.71e-06 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 52.26 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 430 GAVIDAKEVSLSDAKMGGHAIYADGTKVDVKAVKSNRQPNTYIYAKVLGPYTKIVVVELANDPETGALKYQARSWYKEGD 509
Cdd:COG3468 2 ASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 510 HTANIANQDISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTDQTLFKPANDSGESSGDVRF-----NGAGG 584
Cdd:COG3468 82 GGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGtgaaaAGGGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 585 GNVIKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYAGGA 664
Cdd:COG3468 162 GSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 665 VNVLVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVL 744
Cdd:COG3468 242 GGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 745 TKMGEGELTSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGT---TTGVMVGGA 821
Cdd:COG3468 322 AGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDgvgTGLTTGGTG 401
|
410 420
....*....|....*....|....*..
gi 903393592 822 NILTKVGNGDTTGILLGVGNVLTHVGD 848
Cdd:COG3468 402 NNGGGGVGGGGGGGLTLTGGTLTVNGN 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1562-1835 |
1.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1562 QKNLKLTAQAGSNRIEFKGTGHNDGLG----------YILDNVVATSESSQQANA-IREhatQNPAAQNALSDKERAead 1630
Cdd:COG3206 124 RKNLTVEPVKGSNVIEISYTSPDPELAaavanalaeaYLEQNLELRREEARKALEfLEE---QLPELRKELEEAEAA--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1631 rqrLEQEKQKQLDAVAGSQSQLESTDQQALEnngqAQRDAVKEESEAVTAELAKLAQGLDVLDGQATHTGESgdqwrndf 1710
Cdd:COG3206 198 ---LEEFRQKNGLVDLSEEAKLLLQQLSELE----SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1711 agGLLDGVQSQLDDAKQlandKIAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIaDAQADAEKRKADALAKG 1790
Cdd:COG3206 263 --PVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL-EAELEALQAREASLQAQ 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 903393592 1791 KDAQQAESDAHHAVNNAQSRGDRDVQLAE-------NKANQAQADAQGAKQN 1835
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVARelyesllQRLEEARLAEALTVGN 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1599-1836 |
1.24e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.71 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1599 ESSQQANA---IREhatqnpaAQNALSD-KERAEADRQ-RLEQEKQK-----QLDAVagsQSQLEST-DQQALENNGQAQ 1667
Cdd:pfam01576 255 ETAQKNNAlkkIRE-------LEAQISElQEDLESERAaRNKAEKQRrdlgeELEAL---KTELEDTlDTTAAQQELRSK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1668 RD--------AVKEESEAVTAELAKLAQgldvldgqaTHTGEsgdqwrndfagglLDGVQSQLDDAKQlANDKIAAAKQT 1739
Cdd:pfam01576 325 REqevtelkkALEEETRSHEAQLQEMRQ---------KHTQA-------------LEELTEQLEQAKR-NKANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1740 LSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQA---DAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQ 1816
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQArlsESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
250 260
....*....|....*....|
gi 903393592 1817 LAENKANQAQaDAQGAKQNE 1836
Cdd:pfam01576 462 DVSSLESQLQ-DTQELLQEE 480
|
|
| PHA02515 |
PHA02515 |
hypothetical protein; Provisional |
1202-1316 |
1.66e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 107197 [Multi-domain] Cd Length: 508 Bit Score: 50.93 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1202 ANVITKVGHGQNV-VLAKGEANIVTQVGDGDSFNALWSKG---NIVTKVGDGMQVTAAKgQANITTTVGNGLNVTAAYGD 1277
Cdd:PHA02515 278 ANINTVAGANANVnTVASNILDVGTVAGNIDDVQAVAGNAaniNVVADNADNINATAAN-QANINAAVGNADNINAAVAN 356
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 903393592 1278 -ANINTKVGDGVSVN-VAWGKYNINTKVGDGLNVAVMKGKA 1316
Cdd:PHA02515 357 qANINAVVGNANNINaVAANEGNVNTVVDNLADVQTVAGIA 397
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
3148-3297 |
1.75e-05 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 49.19 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3148 SQKITLQGEAG-RLTGYYHQgtaPsEGETSSPsgkVVLFLHGSGSSAEEQASAIRnHYQKQGIDMLAVNLRGYGESDGGP 3226
Cdd:COG0412 3 TETVTIPTPDGvTLPGYLAR---P-AGGGPRP---GVVVLHEIFGLNPHIRDVAR-RLAAAGYVVLAPDLYGRGGPGDDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3227 SEKGLY----------QDARTMFNYLVNDKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQAVS--GLLLDRPMPSMTKA 3294
Cdd:COG0412 75 DEARALmgaldpellaADLRAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAAAVSfyGGLPADDLLDLAAR 154
|
...
gi 903393592 3295 ITA 3297
Cdd:COG0412 155 IKA 157
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1632-1834 |
1.77e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1632 QRLEQEKQKQLDAVAGSQSQLESTDQQALENngQAQRDAVKEESEAVTAELAKLAQGLDVLDGQAThtgESGDQWRNdfa 1711
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEEL--ESKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEE--- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1712 gglLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKV---KESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALA 1788
Cdd:TIGR02168 370 ---LESRLEELEEQLETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 903393592 1789 KGKDAQQAEsdaHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQ 1834
Cdd:TIGR02168 447 EELEELQEE---LERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| Hia |
COG5295 |
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
753-1356 |
1.78e-05 |
|
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 50.92 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 753 TSGMLGGANVITHISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDT 832
Cdd:COG5295 3 SNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 833 TGILLGV-GNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEGNAWALMGGLGNVFTKVGNGDALAL 911
Cdd:COG5295 83 VASGGASaATAASTGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAGGSNTATATGS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 912 MVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTLAAMVGNVNifTHIGHGSTFAAMIGQANIMTKVGNDLTAALMVGK 991
Cdd:COG5295 163 STANAATAAAGATSTSASGSSSGASGAAAASAATGASAGGTASA--AASASSSATGTSASVGVNAGAATGSAASAGGSAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 992 ANIMTHVGDGTSLGLFAGEVNVMTKVGNGTTLAAMFGKANIMTHVGDGLTGVLALGEANIVTKLGDDFMGVVAAAKANVV 1071
Cdd:COG5295 241 AGAASGNATTASASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1072 THVGDATTAAVLAGKGNILTKVGEGTTVGLLISDVGNVMTHVGDGTTIGIAKGKANLITKVGDGLGVNVTWGQANVFTQV 1151
Cdd:COG5295 321 AALGSAGGSSGVGTASGASAAAATNDGTANGAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1152 GDGDRYNFAKGEANLITKVGDGQEVSVVQGEANiithvGNGDDYTGAWGKANVITKVGHGQNVVLAKGEANIVTQVGDGD 1231
Cdd:COG5295 401 SSTGASAGGGASAAGGAAAGSAAAGTSSNTSAV-----GASNGASGTSSSASSAGAAGGGTAGAGGAANVGAATTAASAA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1232 SFNALWSKGNIVTKVGDGMQVTAAKGQANITTTVGNGLNVTAAYGDANINTKVGDGVSVNVAWGKYNINTKVGDGLNVAV 1311
Cdd:COG5295 476 ATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNS 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 903393592 1312 MKGKANANIHVGDGLNINASYAQNNVAIKVGNGDFYSLAVASSNT 1356
Cdd:COG5295 556 VAVGNNTATGANSVALGAGSVASGANSVSVGAAGAENVAAGATDT 600
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1611-1905 |
2.61e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1611 ATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTdqqalenngQAQRDAVKEESEAVTAELAKLAQGLD 1690
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA---------RSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1691 VLDGQathtgesgdqwrndfagglLDGVQSQLDDAKQlANDKIAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQ 1770
Cdd:COG4372 98 QAQEE-------------------LESLQEEAEELQE-ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1771 DIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGDRPDRQGVTGSGL 1850
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 903393592 1851 SGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQINA 1905
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1624-1843 |
6.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1624 KERAEADR-QRLeQEKQKQLDAVAGSQSQLESTDQQALEnngQAQRDAVKEESEAVTAELAKLAQGLDVLDGQATHTGES 1702
Cdd:COG1196 207 RQAEKAERyREL-KEELKELEAELLLLKLRELEAELEEL---EAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1703 GDQWRNDFAggLLDGVQSQLDDAKQLANDKIAAAKQTLSDNnskvKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKR 1782
Cdd:COG1196 283 LEEAQAEEY--ELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 903393592 1783 KAdALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNEGDRPDRQ 1843
Cdd:COG1196 357 EA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1589-1811 |
1.27e-04 |
|
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: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1589 YILDnvvaTSESSQQANAIREHATQNPAAQNALsdkERAEADRQRLEQ--EKQKQLDAVAGSQSQLESTDQQALENNGQA 1666
Cdd:COG4913 216 YMLE----EPDTFEAADALVEHFDDLERAHEAL---EDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1667 QRDAVKEESEAVTAELAKLAQGLDVLDGQATHTGESGDQWRNDFA---GGLLDGVQSQLDDAKQLANDKIAAAKQtLSDN 1743
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgngGDRLEQLEREIERLERELEERERRRAR-LEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 1744 NSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRG 1811
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
3174-3361 |
1.79e-04 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 45.63 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3174 ETSSPSGKVVLFLHGSG------SSAEEQASAIRNHyqkQGIDMLAVNlrgYGESDGGPSEKGLyQDARTMFNYLVN--- 3244
Cdd:COG0657 7 AGAKGPLPVVVYFHGGGwvsgskDTHDPLARRLAAR---AGAAVVSVD---YRLAPEHPFPAAL-EDAYAALRWLRAnaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3245 DKGIDPSNIIIHGYSMGGPIAADLARYAAQNGQ-AVSGLLLDRPMPSMTkaitahevANPAgivgaiakavngqfsvEKN 3323
Cdd:COG0657 80 ELGIDPDRIAVAGDSAGGHLAAALALRARDRGGpRPAAQVLIYPVLDLT--------ASPL----------------RAD 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 903393592 3324 LEGLPketSILLLT-DNEGLGNEGEKLRTKLTASGYNVT 3361
Cdd:COG0657 136 LAGLP---PTLIVTgEADPLVDESEALAAALRAAGVPVE 171
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1587-1854 |
2.43e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1587 LGYILDNVvATSESSQQANA-----------IREHATQNPAAQNALSDKERAEADRQ----RLEQEKQKQLDAVAGSQSQ 1651
Cdd:COG2268 167 NGLELESV-AITDLEDENNYldalgrrkiaeIIRDARIAEAEAERETEIAIAQANREaeeaELEQEREIETARIAEAEAE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1652 LESTDQQAlenngQAQRDAVKEESEAvTAELAKLAQGLDvldgqathtgesgdqwrndfagglldgVQSQLDDAKQLAND 1731
Cdd:COG2268 246 LAKKKAEE-----RREAETARAEAEA-AYEIAEANAERE---------------------------VQRQLEIAEREREI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1732 KIAAAkqtlsdnnsKVKESVAKSEAGV-AQGEQNRAGVEQDiADAQADAEKRKADALAKGKdaqQAESDAHHAVNNAQsr 1810
Cdd:COG2268 293 ELQEK---------EAEREEAELEADVrKPAEAEKQAAEAE-AEAEAEAIRAKGLAEAEGK---RALAEAWNKLGDAA-- 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 903393592 1811 gdRDVQLAENKANQAQADAQGAKQNEGDRPDRQGVTGSGLSGNA 1854
Cdd:COG2268 358 --ILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSAV 399
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
3150-3284 |
2.96e-04 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 45.15 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3150 KITLQGEAGRLTGYYHQGTAPsegetssPSGkVVLFLH------GSgssaeeqasaIRNH--------YQKQGIDMLAVN 3215
Cdd:COG2945 1 KVLINGPAGRLEGRLDLPEGP-------PRG-VALILHphplfgGT----------MDNKvvytlaraLVAAGFAVLRFN 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 903393592 3216 LRGYGES----DGGPSEKglyQDARTMFNYLVNDkgiDPSNIIIHGYSMGGPIAADLaryaAQNGQAVSGLLL 3284
Cdd:COG2945 63 FRGVGRSegefDEGRGEL---DDAAAALDWLRAQ---NPLPLWLAGFSFGAYVALQL----AMRLPEVEGLIL 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1569-1830 |
5.31e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1569 AQAGSNRIEFKGTGHNDGLgyildnvvaTSESSQQANAIREHATqnpAAQNALSDKERAEADRQRLEQ-EKQKQLDAVAG 1647
Cdd:NF041483 900 AREDANRIRSDAAAQADRL---------IGEATSEAERLTAEAR---AEAERLRDEARAEAERVRADAaAQAEQLIAEAT 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1648 SQSqlESTDQQALENNGQAQRDA--VKEESEAVTAELAKLAQGL---------DVLDgqatHTGESGDQWRNDFAGGLLD 1716
Cdd:NF041483 968 GEA--ERLRAEAAETVGSAQQHAerIRTEAERVKAEAAAEAERLrteareeadRTLD----EARKDANKRRSEAAEQADT 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1717 GVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESV--AKSEAGVAQGEQNRAG---VEQDIADAQ---------ADAEKR 1782
Cdd:NF041483 1042 LITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaARKEAERIVAEATVEGnslVEKARTDADellvgarrdATAIRE 1121
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 903393592 1783 KADALakgKDAQQAESDAHH---------AVNNAQSRGDRDVQLAENKANQAQADAQ 1830
Cdd:NF041483 1122 RAEEL---RDRITGEIEELHerarresaeQMKSAGERCDALVKAAEEQLAEAEAKAK 1175
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
3178-3282 |
8.61e-04 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 44.75 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3178 PSGKVVLFLHG-SGSSaeeqasaiRNHY--------QKQGIDMLAVNLRGYGesdGGP--------SekGLYQDARTMFN 3240
Cdd:COG0429 59 PSKPLVVLLHGlEGSS--------DSHYarglaralYARGWDVVRLNFRGCG---GEPnllprlyhS--GDTEDLVWVLA 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 903393592 3241 YLVNDKGidPSNIIIHGYSMGGPIaadLARYAAQNGQAVSGL 3282
Cdd:COG0429 126 HLRARYP--YAPLYAVGFSLGGNL---LLKYLGEQGDDAPPL 162
|
|
| PHA02515 |
PHA02515 |
hypothetical protein; Provisional |
1241-1377 |
8.62e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 107197 [Multi-domain] Cd Length: 508 Bit Score: 45.15 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1241 NIVTKVGDGMQVTA-AKGQANITTTVGNGLNV-TAAYGDANINTKVGDGVSVN-VAWGKYNINTKVGDGLNV-AVMKGKA 1316
Cdd:PHA02515 259 SVVSVAGDLENIDAvADNAANINTVAGANANVnTVASNILDVGTVAGNIDDVQaVAGNAANINVVADNADNInATAANQA 338
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 903393592 1317 NANIHVGDGLNINASYA-QNNVAIKVGNGDFYSlAVASSNTSSNklsALFDNIK--QTVLGVGG 1377
Cdd:PHA02515 339 NINAAVGNADNINAAVAnQANINAVVGNANNIN-AVAANEGNVN---TVVDNLAdvQTVAGIAA 398
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
3176-3284 |
9.06e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3176 SSPSGKVVLFLHGSGSSAEEQASAIRnHYQKQGIDMLAVnlRG-YGESDGGPS------------EKGLYQDARTMFNYL 3242
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLLPLAP-ELALPGAAVLAP--RApVPEGPGGRAwfdlsflegredEEGLAAAAEALAAFI 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 903393592 3243 ---VNDKGIDPSNIIIHGYSMGGPIAADLaryAAQNGQAVSGLLL 3284
Cdd:COG0400 78 delEARYGIDPERIVLAGFSQGAAMALSL---ALRRPELLAGVVA 119
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1594-1811 |
1.21e-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: 44.37 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1594 VVATSESSQQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQL----DAVAGSQSQLESTDQQALENNG----- 1664
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaaleRRIAALARRIRALEQELAALEAelael 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1665 QAQRDAVKEESEAVTAELAKLAQGLDVLDGQAT-----HTGESGD-----QWRNDFAGGLLDGVQSQLDDAKQLA--NDK 1732
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAalRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1733 IAAAKQTLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADA------LAKGKDAQQAESDAHHAVNN 1806
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAeelealIARLEAEAAAAAERTPAAGF 248
|
....*
gi 903393592 1807 AQSRG 1811
Cdd:COG4942 249 AALKG 253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1598-1902 |
1.76e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1598 SESSQQANAIREHatQNpAAQNALSDKE---RAEADRQRLEQEKQKQLDAVAGSQSQLESTdqqalenngQAQRDAVKEE 1674
Cdd:PRK04863 324 SDLEQDYQAASDH--LN-LVQTALRQQEkieRYQADLEELEERLEEQNEVVEEADEQQEEN---------EARAEAAEEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1675 SEAVTAELAKLAQGLDVLDG------QATHTGESGDQW--RNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDnnsk 1746
Cdd:PRK04863 392 VDELKSQLADYQQALDVQQTraiqyqQAVQALERAKQLcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSV---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1747 vkesvakSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKgkdaqQAESDAHHAVNNAQSRG-----DRDVQLaENK 1821
Cdd:PRK04863 468 -------AQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR-----RLREQRHLAEQLQQLRMrlselEQRLRQ-QQR 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1822 ANQAQADAQG-AKQNEGDRPDRQGVTgsglsgnahsvEGAGETDSHVNtDSQTNADGRFSEglTEQEQEALEG------- 1893
Cdd:PRK04863 535 AERLLAEFCKrLGKNLDDEDELEQLQ-----------EELEARLESLS-ESVSEARERRMA--LRQQLEQLQAriqrlaa 600
|
330
....*....|....*.
gi 903393592 1894 -------ATNAVNRLQ 1902
Cdd:PRK04863 601 rapawlaAQDALARLR 616
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1596-1849 |
1.80e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1596 ATSESSQQANAIREHATQNPAAQNAlSDKERAEADRQRLEQEKQKqldAVAGSQSQLESTDQQALENNGQAQRDAVkEES 1675
Cdd:PRK07735 27 VAKHGAEISKLEEENREKEKALPKN-DDMTIEEAKRRAAAAAKAK---AAALAKQKREGTEEVTEEEKAKAKAKAA-AAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1676 EAVTAELAKlaqglDVLDGQATHTGESGDQWRNDFAgglldgvQSQLDDAKQLANDKIAAAKQTLSDNNSKVKEsVAKSE 1755
Cdd:PRK07735 102 KAKAAALAK-----QKREGTEEVTEEEKAAAKAKAA-------AAAKAKAAALAKQKREGTEEVTEEEEETDKE-KAKAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1756 AGVAQGEQNRAGVEQDIADAQADAE--KRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKAnQAQADAQgAK 1833
Cdd:PRK07735 169 AAAAAKAKAAALAKQKAAEAGEGTEevTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKA-KAIAAAK-AK 246
|
250
....*....|....*.
gi 903393592 1834 QNEGDRPDRQGVTGSG 1849
Cdd:PRK07735 247 AAAAARAKTKGAEGKK 262
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1723-1833 |
1.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 44.09 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1723 DDAKQLANDKIAAAKqTLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQ--QAESDA 1800
Cdd:PRK12472 207 DEAKTAAAAAAREAA-PLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAEERQQKAAQQAAEAATQldTAKADA 285
|
90 100 110
....*....|....*....|....*....|...
gi 903393592 1801 HHAVNNAQSRGDRDVQLAENKANQAQAdAQGAK 1833
Cdd:PRK12472 286 EAKRAAAAATKEAAKAAAAKKAETAKA-ATDAK 317
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1591-1909 |
2.05e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1591 LDNVVATSESSQQANAIREHATQNPAAQNA-----LSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQA-LENNG 1664
Cdd:COG3064 44 LAELEAKRQAEEEAREAKAEAEQRAAELAAeaakkLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAeKEKAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1665 QAQRDAvkEESEAVTAELAKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNN 1744
Cdd:COG3064 124 EAKRKA--EEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1745 SKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQ 1824
Cdd:COG3064 202 ALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1825 AQADAQGAKQNEGDRPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGRFSEGLTEQEQEALEGATNAVNRLQIN 1904
Cdd:COG3064 282 AAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATG 361
|
....*
gi 903393592 1905 AGIRA 1909
Cdd:COG3064 362 ALGDA 366
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1614-1819 |
2.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1614 NPAAQNALSDKERAEADRQR-----LEQEKQKQLDAVAGSQSQLESTDQQA--LENNGQAQR-DAVKEESEAVT---AEL 1682
Cdd:COG3096 833 DPEAELAALRQRRSELERELaqhraQEQQLRQQLDQLKEQLQLLNKLLPQAnlLADETLADRlEELREELDAAQeaqAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1683 AKLAQGLDVLDGQAT---HTGESGDQWRNDfagglLDGVQSQLDDAKQlandKIAAAKQTLSDnnskvKESVAKSEAgVA 1759
Cdd:COG3096 913 QQHGKALAQLEPLVAvlqSDPEQFEQLQAD-----YLQAKEQQRRLKQ----QIFALSEVVQR-----RPHFSYEDA-VG 977
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 903393592 1760 QGEQNRAGVEQDIAD-AQADAEKRKADALAKGKDAQQaeSDAHHAVNNAQSRGDRDVQ-LAE 1819
Cdd:COG3096 978 LLGENSDLNEKLRARlEQAEEARREAREQLRQAQAQY--SQYNQVLASLKSSRDAKQQtLQE 1037
|
|
| auto_AIDA-I |
NF033176 |
autotransporter adhesin AIDA-I; |
574-1034 |
2.24e-03 |
|
autotransporter adhesin AIDA-I;
Pssm-ID: 380183 [Multi-domain] Cd Length: 1287 Bit Score: 44.26 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 574 SGDVRFNG---AGGGNVIKSNVTRGNVHFNGGGIANVilhssqfgnteFNGGGAANVIVKSGEEGDLTFRGAGLANVLvh 650
Cdd:NF033176 53 SSGVVSGGvvsSGETQVVYSNGQTSNATVNSGGIQNV-----------NNGGKTTSTTVNSSGAQNVGNSGTAISTIV-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 651 qSEQGKMDVYAGGAVNVLVRLGDGQYLAHLLAYGNISVQKGSgdSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGK 730
Cdd:NF033176 120 -NSGGVQRVSSGGVTSATSLSGGAQNIYNLGHASNTVIFNGG--NQTIFSGGISDDTNISSGGQQRVSSGGVASNTTINS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 731 GDVAAVLAGGANVLTKMGEGELTSGMLGGANVITHISN-------------DDQLS-NTTAVALGGANILTKKGKGNTLA 796
Cdd:NF033176 197 SGTQNILSGGSTVSTHISSGGNQYISAGGNASATVVSSggfqrvssggtatGTVLSgGTQNVSSGGSAISTSVYSSGVQT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 797 VMGGGANVLTHVGDGTTTGVMVGGANILTKVGNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNifTKVGDGTSIAVM-- 874
Cdd:NF033176 277 VYAGATVTDTTVNSGGKQNISSGGIVSGTIVNSSGTQNIYSGGSALSANIKGSQIVNSDGTAIN--TLVNDGGYQHIRng 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 875 -IGAGNIFTHVGE------GNAWALMGGLGNVFTKVGNGDALALMVAEANVFTHIGDGMSVALMLAKGNVATKVGNGTTL 947
Cdd:NF033176 355 gVASGTIINQSGRvnissgGYAESTIINSGGTQSVLSGGYASGTLINNSGRENVSNGGSAYNTIINAGGNQYIYSNGEAS 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 948 AAMVgNVNIFTHIGHGSTFAA--MIGQANIMTKVGNDLTAALMVGKANIMTHVGDGTSLGLF-AGEVNVMTKVGNGTTLa 1024
Cdd:NF033176 435 GTTV-NTSGFQRVNSGGTATGtkLSGGNQNVSSGGKAIAAEVYSGGKQTVYAGGEASGTQIFdGGVVNVSGGSVSGASV- 512
|
490
....*....|
gi 903393592 1025 AMFGKANIMT 1034
Cdd:NF033176 513 NLNGRLNVFA 522
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1769-1834 |
3.10e-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: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 903393592 1769 EQDIADAQADAEKRKADALAKGKDAQQ----AESDAHHAVNNAQSRGDRDVQLAENKAN--------QAQADAQGAKQ 1834
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEklaeARAEAQEIIEEARKEAEKIKEEILAEAKeeaerileQAKAEIEQEKE 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1625-1836 |
3.41e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1625 ERAEADRQRLEQ---EKQKQLDAVAGSQSQLES---------TDQQALENNGQAQRDAVKEESEAVTAELAKLAQGLDVL 1692
Cdd:TIGR02168 680 EELEEKIEELEEkiaELEKALAELRKELEELEEeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1693 DGQATHTGESGDQWRNDFAGGL-----------------------LDGVQSQLDD-----------AKQLANDKIAAAKQ 1738
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEaeieeleaqieqlkeelkalreaLDELRAELTLlneeaanlrerLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1739 --TLSDNNSKVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKAdALAKGKDAQQAESDAHHAVNNAQSRGDRDVQ 1816
Cdd:TIGR02168 840 leDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE-ALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260
....*....|....*....|
gi 903393592 1817 LAENKANQAQADAQGAKQNE 1836
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRI 938
|
|
| Lipase_2 |
pfam01674 |
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ... |
3183-3281 |
4.34e-03 |
|
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.
Pssm-ID: 396304 [Multi-domain] Cd Length: 218 Bit Score: 41.95 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 3183 VLFLHGSGSSAEEQASAIRNHYQKQGIDMLAVNLRGYGESDGGPSEKGLY-----QDARTMFNYLVNDKGIDPSNIIihG 3257
Cdd:pfam01674 4 VIFVHGNSGLAAGGWSKLSQYFKERGYTLAELYATTWGDGNESTSLQRAEkceyvKQIRRFIEAVLGYTGAAKVDIV--A 81
|
90 100
....*....|....*....|....
gi 903393592 3258 YSMGGPIaadlARYAAQNGQAVSG 3281
Cdd:pfam01674 82 HSMGVPI----ARKAILGGNCVDT 101
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
508-887 |
4.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 43.23 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 508 GDHTANIANQDISSATGYNPMGKGGYSLSDLHYSVNAVRSTSETVADIEEYTDQTLFKPANDSGESSGDVRFNGAGGGNV 587
Cdd:COG4625 115 GGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 588 IKSNVTRGNVHFNGGGIANVILHSSQFGNTEFNGGGAANVIVKSGEEGDLTFRGAGLANVLVHQSEQGKMDVYAGGAVNV 667
Cdd:COG4625 195 GGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 668 LVRLGDGQYLAHLLAYGNISVQKGSGDSRVVMLGGYNTHTQIGSGNGLWLAAGGFNVMTQVGKGDVAAVLAGGANVLTKM 747
Cdd:COG4625 275 SGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 748 GEGELTSGMLGGANVIThISNDDQLSNTTAVALGGANILTKKGKGNTLAVMGGGANVLTHVGDGTTTGVMVGGANILTKV 827
Cdd:COG4625 355 AGGGGGGGTGGGGGGGG-GGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGG 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 828 GNGDTTGILLGVGNVLTHVGDGQTLGVMGAAGNIFTKVGDGTSIAVMIGAGNIFTHVGEG 887
Cdd:COG4625 434 GGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGG 493
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1599-1917 |
5.39e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1599 ESSQQANAIREHATQNPAAQNALSDKERAEADRQRLEQEKQKQLDAVAGSQSQLESTDQQALENNGQAQRDAVKEESEAV 1678
Cdd:COG3064 99 KAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1679 TAELAKLAQGLDVLDGQATHTGESGDQWRNDFAGGLLDGVQSQLDDAKQLANDKIAAAKQTLSDNNSKVKESVAKSEA-- 1756
Cdd:COG3064 179 AAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAvg 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1757 GVAQGEQNRAGVEQDIADAQADAEKRKADALAKGKDAQQAESDAHHAVNNAQSRGDRDVQLAENKANQAQADAQGAKQNE 1836
Cdd:COG3064 259 VLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1837 GDRPDRQGVTGSGLSGNAHSVEGAGETDSHVNTDSQTNADGR--FSEGLTEQEQEALEGATNAVNRLQINAGIRAKNSVS 1914
Cdd:COG3064 339 AALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLadVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAV 418
|
...
gi 903393592 1915 SMT 1917
Cdd:COG3064 419 ELR 421
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1716-1800 |
6.62e-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: 39.73 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1716 DGVQSQLDDAKQLAndkiAAAKQTLSDNNSKVKEsvAKSEA------GVAQGEQNRagvEQDIADAQADAEKRKADALAk 1789
Cdd:cd06503 33 EKIAESLEEAEKAK----EEAEELLAEYEEKLAE--ARAEAqeiieeARKEAEKIK---EEILAEAKEEAERILEQAKA- 102
|
90
....*....|.
gi 903393592 1790 gkDAQQAESDA 1800
Cdd:cd06503 103 --EIEQEKEKA 111
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1746-1829 |
8.17e-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: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 903393592 1746 KVKESVAKSEAGVAQGEQNRAGVEQDIADAQADAEKRKADAlakgkdAQQAESDAHHAVNNAQSRGDRDVQLAENKANQA 1825
Cdd:COG0711 35 KIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEA------RKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQE 108
|
....
gi 903393592 1826 QADA 1829
Cdd:COG0711 109 RAKA 112
|
|
| |
