|
Name |
Accession |
Description |
Interval |
E-value |
| ADP_ribosyl_GH |
pfam03747 |
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ... |
6-328 |
1.49e-30 |
|
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.
Pssm-ID: 461037 [Multi-domain] Cd Length: 200 Bit Score: 120.37 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 6 AAMLLGSVGDALGYRNvckENSTVGmKIQEELQRSG----GLDHLVLSPGEWpvSDNTIMHIATAEALTT-DYWCLDDLY 80
Cdd:pfam03747 1 GALLGLAVGDALGAPV---EFWSYD-EIRREYGGIGtpmpGGGHLGLPPGEW--TDDTQMALALLESLLEaGGFDPEDLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 81 REMvrcyveiveklperrpdpatiegcaqlkpnnyllawhtpfnekgsgfgaATKAMCIGLRYwkPERLETLIEVSVECG 160
Cdd:pfam03747 75 RRL-------------------------------------------------AMRIAPLGLLY--PGDPEEAAELARESA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 161 RMTHNHPTGFLGSLCTALFVSFAAQGKPLVQWGRdmlravplaeeycrktirhtaeyqehwfyfeakwqfyleerkiskd 240
Cdd:pfam03747 104 RLTHGHPRAVAGAVAYAAAIAAALRGADLEEALE---------------------------------------------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 241 senkaifpdnydaeerektyrkwssEGRGGRRGHDAPMIAYDALLAAGNSWTELCHRAMFHGGESAATGTIAGCLFGLLY 320
Cdd:pfam03747 138 -------------------------AIGGGGYVVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYY 192
|
....*...
gi 2033470018 321 GLDLVPKG 328
Cdd:pfam03747 193 GLEAIPEE 200
|
|
| DraG |
COG1397 |
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones]; |
1-350 |
8.25e-24 |
|
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441007 Cd Length: 256 Bit Score: 102.63 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1 MEKFKAAMLLGSVGDALGyrnvckenSTV-GMKIQEELQRSGGLDHLV----LSPGEWpvSDNTIMHIATAEAL-TTDYW 74
Cdd:COG1397 2 LDRARGALLGLAIGDALG--------APVeFYSREEIRARYGPITDYVgggnLPPGEW--TDDTQMALALAESLlEAGGF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 75 CLDDLYREMVRCYVEivekLPERRPDPATIEGCAqlkpnNYLLAWHTPFNEKGSGFGAATKAMCIGLRYwkPERLETLIE 154
Cdd:COG1397 72 DPEDLARRFLRWLRT----GPGRDIGPTTRRALR-----NLRRGGAGESGEGSAGNGAAMRIAPLGLAY--AGDPEEAAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 155 VSVECGRMTHNHPTGFLGSLCTALFVSFAAQGKPLVQWgrDMLRAVPLAeeycrktirhtaeyqehwfyfeakwqFYLee 234
Cdd:COG1397 141 LARASAALTHGHPRAIAGAVAYAAAVAAALRGADLEEG--YVVETLPAA--------------------------LWA-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 235 rkiskdsenkAIFPDNYDaeerektyrkwssegrggrrghdapmiayDALLAAGNswtelchramfHGGESAATGTIAGC 314
Cdd:COG1397 191 ----------LLRADDFE-----------------------------EALLLAVN-----------LGGDTDTTAAIAGA 220
|
330 340 350
....*....|....*....|....*....|....*.
gi 2033470018 315 LFGLLYGLDLVPKGLYQDLEDKEKLEDLGAALYRLS 350
Cdd:COG1397 221 LAGALYGLEAIPERWLEPLERRDRLEELAERLAALA 256
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1532-1757 |
6.31e-16 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 82.91 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1532 SQGQAQKQFQNWAQGQAQGHAQEQAQWQ--TQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQ 1609
Cdd:NF040676 147 TEKKADEKTKQVAKVQKSVKAKEEAKTQkvAKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPKEEVKVQEEVK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1689
Cdd:NF040676 227 PKEEEKVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1690 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTH 1757
Cdd:NF040676 307 EIAKAKEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQ 374
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1603-1750 |
1.61e-14 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 78.67 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:NF040676 232 KVQEIVKPKEEAKVQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQEIAKA 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1683 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQE 1750
Cdd:NF040676 312 KEEAKAREIAKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
1600-1738 |
2.60e-13 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 74.82 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1600 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEqtqiEAQGQAQKGAQERAREQ 1679
Cdd:NF040676 245 VQEEVKVKEEAKVQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEAKAQEIAKAKEEE----KAQEIAKAKEEAKAREI 320
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1680 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE 1738
Cdd:NF040676 321 AKAKEEEKAREIAKAKEEAKAREIAKAKEEAKAREIAKAKEEERAKEASKNNIQSAKRE 379
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1605-1770 |
3.22e-13 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 73.69 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQAQWQTQIKAQKWA--QEQTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKgAQERAREQAQK 1682
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAaeQERLKQLEKERLAAQEQKKQAEEAAKQAA-----LKQKQAEE-AAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKGAQerAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1762
Cdd:PRK09510 148 KAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
....*...
gi 2033470018 1763 QAQKGAQE 1770
Cdd:PRK09510 226 AAAKAAAE 233
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1808 |
1.16e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQG--QAQKGAQE-RAREQ 1679
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEaKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1680 AQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQ 1755
Cdd:PTZ00121 1475 AKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1756 THI----EAQGQAQKGAQEWARDRARDQGWEQTQIETQR-----------QTQKGAQERAWEQGREQA 1808
Cdd:PTZ00121 1555 EELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARieevmklyeeeKKMKAEEAKKAEEAKIKA 1622
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1531-1795 |
2.41e-12 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 71.05 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1531 HSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE 1610
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1611 EAQGQAQWQTQIKAQKWAQ----EQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:pfam08017 105 RSQGNVLERRQRDAENKSQgnvlERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQTHI 1758
Cdd:pfam08017 185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRDAEN 264
|
250 260 270
....*....|....*....|....*....|....*..
gi 2033470018 1759 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKG 1795
Cdd:pfam08017 265 RSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVG 301
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1609-1844 |
2.69e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1609 QEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1688
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1689 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGA 1768
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1769 QewARDRARDQGW--EQTQIETQRQTQKGAQERAWEQGREQALTSGMAprAWEQPISGIAEGVDAAGRSGGSRSPAPR 1844
Cdd:COG1196 500 E--ADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA--AALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1541-1752 |
1.11e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.06 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1541 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAqgqvqgqaqKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqt 1620
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQA---------AEQERLKQLEKERLAAQEQKKQAEEAAKQAAL--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1621 qikAQKWAQEQTQKGAQervQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1700
Cdd:PRK09510 130 ---KQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1701 REQAQKGAQERAREQAQKGAQERAREQA--QKGAQERAREQAQKGAQERAQEQG 1752
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAaeAKAAAEKAAAAKAAEKAAAAKAAA 257
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1499-1767 |
5.31e-11 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 66.81 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1499 QVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQG 1578
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1579 QVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQE 1658
Cdd:pfam08017 105 RSQGNVLE----RRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1659 QTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKGAQERAR----EQAQK 1730
Cdd:pfam08017 181 DAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQgnvlERRQRDAENKSQgnvlERRQR 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2033470018 1731 GAQERAR----EQAQKGAQERAQEQGREQTHIEAQGQAQKG 1767
Cdd:pfam08017 261 DAENRSQgnvlERRQRDAENRSQGNVLERRQRDAENKSQVG 301
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1601-1805 |
7.08e-11 |
|
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: 66.02 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1601 QGEVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1680
Cdd:TIGR02794 70 QKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1681 QKGAQERAREQAQKGAQERAREQAQKGAQERareQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1760
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2033470018 1761 QGQAQKGAqewardrARDQGWEQTQIETQRQTQKGAQERAWEQGR 1805
Cdd:TIGR02794 226 ERKADEAE-------LGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1608-1808 |
7.49e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 67.24 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQaqkgaqeR 1687
Cdd:PRK12678 54 AIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAA-------Q 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1767
Cdd:PRK12678 127 ARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRR 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2033470018 1768 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:PRK12678 207 DRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDR 247
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1608-1805 |
7.75e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 67.24 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1687
Cdd:PRK12678 71 AAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGAqerareQAQKGAQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1767
Cdd:PRK12678 151 QPATEARAD------AAERTEEEERDERRRRGDREDRQAEAERGERGR-REERGRDGDDRDRRDRREQGDRREERGRRDG 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 2033470018 1768 AQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1805
Cdd:PRK12678 224 GDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGR 261
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1609-1809 |
8.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1609 QEEAQgQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtQIEAQGQAQKGAQERAR---EQAQKGAQ 1685
Cdd:COG1196 219 KEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA------ELEAELEELRLELEELElelEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1686 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1765
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2033470018 1766 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQAL 1809
Cdd:COG1196 372 AELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1809 |
1.38e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgaQERAREQAQK 1682
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---EAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR-EQAQKGAQERAQEQGREQT 1756
Cdd:PTZ00121 1452 KAEEaKKAEEAKKKAEEaKKADEAKKKAEEaKKADEAKKKAEEAKKkaDEAKKAAEAKKKaDEAKKAEEAKKADEAKKAE 1531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1757 HIEAQGQAQKGAQEWARDRARdqgwEQTQIETQRQTQKGAQERAWEQGREQAL 1809
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELK----KAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1628-1834 |
1.79e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 65.83 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1707
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1708 AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIE 1787
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2033470018 1788 TQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGR 1834
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAA 207
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1618-1837 |
2.29e-10 |
|
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: 64.48 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1618 WQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1697
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1698 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQAQKGAQ--EWA 1772
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEakkKAEAEAKAKAEAEAKAKAEEAKAkaEAA 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2033470018 1773 RDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGG 1837
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAA 266
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1806 |
2.57e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAqEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQE-RAREQAQ 1681
Cdd:PTZ00121 1319 EAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQE--RAQEQGR 1753
Cdd:PTZ00121 1398 KKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEaKKAEEAKKKAEEakKADEAKK 1477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1754 EQTHIEAQGQAQKGAQEWAR--DRARDQGWEQTQIETQRQTQ---KGAQERAWEQGRE 1806
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKKAEeakKADEAKKAEEAKK 1535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1806 |
4.83e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQE-RAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQE-RAREQAQKGAQERAQ------- 1749
Cdd:PTZ00121 1386 KAEEkKKADEAKKKAEEdkkKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEaKKADEAKKKAEEAKKaeeakkk 1465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1750 -EQGREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQE-RAWEQGRE 1806
Cdd:PTZ00121 1466 aEEAKKADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1606-1808 |
5.33e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1606 KWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERaqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQ 1685
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-----------LELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1686 ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQ 1765
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2033470018 1766 KGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:COG1196 383 ELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1608-1894 |
5.95e-10 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 63.91 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQaqeqtqiEAQGQAQKGAQERAREQAQKGAQER 1687
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQ--AEAEKRAAAEAEQKAKEEAEEERLAEL-------EAKRQAEEEAREAKAEAEQRAAELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKG 1767
Cdd:COG3064 73 AEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1768 AQEWAR--DRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPAPRD 1845
Cdd:COG3064 153 EAEAARaaAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREA 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2033470018 1846 GGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGG 1894
Cdd:COG3064 233 ALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVV 281
|
|
| Glutenin_hmw |
pfam03157 |
High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
1479-1911 |
7.97e-10 |
|
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.
Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 64.20 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1479 PGSPAAQGQAQKQVQewdrGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQW 1558
Cdd:pfam03157 167 PTSPQQSGQRQQPGQ----GQQLRQGQQGQQSGQGQPGYYPTSSQQPGQLQQTGQGQQGQQPERGQQGQQPGQGQQPGQG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1559 QtqieaQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQW---QTQIKAQKWAQEQTQKG 1635
Cdd:pfam03157 243 Q-----QGQQPGQPQQLGQGQQGYYPISPQQPRQWQQSGQGQQGYYPTSLQQPGQGQSGYyptSQQQAGQLQQEQQLGQE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1636 AQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQ 1715
Cdd:pfam03157 318 QQDQQPGQGRQGQQPGQGQQGQQPAQGQQPGQGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1716 AQKGAQERAREQAQKGAQERAREQAQKGaqeraqEQGREQTHIEAQGQAQKGAQ-EWARDRARDQGWEQTQIETQRQTQK 1794
Cdd:pfam03157 398 GQQPGQGQQPGQGQPGYYPTSPQQSGQG------QPGYYPTSPQQSGQGQQPGQgQQPGQEQPGQGQQPGQGQQGQQPGQ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1795 GAQERAWEQGREqaltsGMAPRAWEQPISGIAEGV-DAAGRSGGSRSPAPRDGGQSGGSGLGEPSAGYPPPGSRPLRGKS 1873
Cdd:pfam03157 472 PEQGQQPGQGQP-----GYYPTSPQQSGQGQQLGQwQQQGQGQPGYYPTSPLQPGQGQPGYYPTSPQQPGQGQQLGQLQQ 546
|
410 420 430
....*....|....*....|....*....|....*...
gi 2033470018 1874 IATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPG 1911
Cdd:pfam03157 547 PTQGQQGQQSGQGQQGQQPGQGQQGQQPGQGQQGQQPG 584
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1484-1758 |
8.75e-10 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 62.96 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1484 AQGQAQKQVQEWDRGQVQGHAQEQAQWQTQIEAQGQAQEQAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIE 1563
Cdd:pfam08017 26 SQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1564 AQGQAQEPAQGGAQGQVQGQAQKwaqgQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQ 1643
Cdd:pfam08017 106 SQGNVLERRQRDAENKSQGNVLE----RRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1644 AQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR----EQAQKG 1719
Cdd:pfam08017 182 AENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERRQRD 261
|
250 260 270
....*....|....*....|....*....|....*....
gi 2033470018 1720 AQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1758
Cdd:pfam08017 262 AENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQV 300
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1601-1799 |
1.77e-09 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 62.19 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1601 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1680
Cdd:pfam08017 59 QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER----RQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1681 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQGREQT 1756
Cdd:pfam08017 135 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQgnvlERRQRDA 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2033470018 1757 HIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1799
Cdd:pfam08017 215 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLER 257
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1636-1753 |
7.26e-09 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 56.59 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1636 AQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQER 1711
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2033470018 1712 AREQAQKGAQE-RAREQAQKGAQERAReQAQKGAQERAQEQGR 1753
Cdd:pfam05672 97 ERLQKQKEEAEaKAREEAERQRQEREK-IMQQEEQERLERKKR 138
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1672-1799 |
7.40e-09 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 56.59 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1672 AQERAREQAQKGAQerAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQ 1749
Cdd:pfam05672 9 AEEAARILAEKRRQ--AREQRER--EEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEERRREEEERQRKAEEE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1750 EQGREQTHIEAQGQAQKGAQEwARDRARDQGwEQTQIETQRQTQKGAQER 1799
Cdd:pfam05672 85 AEEREQREQEEQERLQKQKEE-AEAKAREEA-ERQRQEREKIMQQEEQER 132
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1611-1765 |
9.57e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.89 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1611 EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKgAQERAREQAQkgaQERARE 1690
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETARA 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1691 QAQKG---AQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAQEQGrEQTHIEAQGQAQ 1765
Cdd:COG2268 263 EAEAAyeiAEANAEREVQRQLEIAEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEA-EAEAIRAKGLAE 339
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1662-1807 |
1.21e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 60.30 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1662 IEAQGQAQKGAQERAREQ-----AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1736
Cdd:PRK12678 52 IAAIKEARGGGAAAAAATpaapaAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1737 R--EQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1807
Cdd:PRK12678 132 ErgEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRD 204
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1645-1838 |
1.56e-08 |
|
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: 58.70 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1645 QKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAReqaQKGAQERAREQAQKGAQERAREQA--QKGAQE 1722
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR---QKELEQRAAAEKAAKQAEQAAKQAeeKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1723 RAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW-----ARDRARDQGWEQTQIETQRQTQKGAQ 1797
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAkkkaeAEAKAKAEAEAKAKAEEAKAKAEAAK 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2033470018 1798 ERAWEQGREQA-LTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1838
Cdd:TIGR02794 203 AKAAAEAAAKAeAEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1541-1779 |
1.82e-08 |
|
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: 58.70 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1541 QNWAQGQAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKwaqgqiqgqaqkqvqgEVQKWAQEEAQGQAQWQT 1620
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE----------------QRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1621 QIKAQKWAQEQTQKGAQERvqgqAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQER 1699
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEA----KAKAEAEAERKAKE-----EAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1700 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG---REQTHIEAQGQAQKGAQEWARDRA 1776
Cdd:TIGR02794 185 AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglASGSNAEKQGGARGAAAGSEVDKY 264
|
...
gi 2033470018 1777 RDQ 1779
Cdd:TIGR02794 265 AAI 267
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1605-1799 |
2.17e-08 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 58.72 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQA----QWQTQIKAQKWAQEQTQKGAQERVQGQA----QKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1676
Cdd:pfam08017 35 QRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVlerrQRDAENRSQGNVLERRQRDAENRSQGNVLERR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1677 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQ----EQG 1752
Cdd:pfam08017 115 QRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQgnvlERR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2033470018 1753 REQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQER 1799
Cdd:pfam08017 195 QRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1608-1807 |
2.43e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQwqtqiKAQKwaqEQTQKGAQERVQGQAQKGAQE-RAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQE 1686
Cdd:PTZ00121 1092 ATEEAFGKAE-----EAKK---TETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1687 RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQThieaqgQAQK 1766
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE------EAKK 1237
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2033470018 1767 GAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQ 1807
Cdd:PTZ00121 1238 DAEE-AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1808 |
4.45e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQaqeqtqieaqgQAQKGAQE-RAREQAQ 1681
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-----------EAKKKAEEaKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR-EQAQKGAQE---------RAQ 1749
Cdd:PTZ00121 1322 KKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEkkkadeakkKAE 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2033470018 1750 EQGREQTHIEAQGQAQKGAQEWAR--------DRARDQGWEQTQIETQRqtQKGAQERAWEQGREQA 1808
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKkaeekkkaDEAKKKAEEAKKADEAK--KKAEEAKKAEEAKKKA 1466
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1809 |
4.53e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEqTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--------------EQAQKGAQERAR-EQAQKGAQER 1747
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmklyeeekkmkaEEAKKAEEAKIKaEELKKAEEEK 1632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2033470018 1748 AQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1809
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1663-1755 |
4.54e-08 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 54.28 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQE-R 1735
Cdd:pfam05672 30 EEQERLEKEEEERLRkeELRRRAEEERARreEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQKEEAEaK 109
|
90 100
....*....|....*....|
gi 2033470018 1736 AREQAQKGAQERAQEQGREQ 1755
Cdd:pfam05672 110 AREEAERQRQEREKIMQQEE 129
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1600-1845 |
5.09e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 57.74 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1600 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQ 1679
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAR---------EAKAEAEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1680 AQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1758
Cdd:COG3064 76 AKKLAEaEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1759 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGS 1838
Cdd:COG3064 156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
|
....*..
gi 2033470018 1839 RSPAPRD 1845
Cdd:COG3064 236 AVEATEE 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1798 |
8.58e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKgaqERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQE--RAQEQGREQ 1755
Cdd:PTZ00121 1676 KAEEAKKAEEDE---KKAAEALKKEAEEaKKAEELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEdkKKAEEAKKD 1752
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2033470018 1756 THIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1798
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1803 |
9.18e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKwAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQ 1679
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1680 AQKGAQERAREQAQKGAQERAREQAQKG-----AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1754
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAeelkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2033470018 1755 QTHIEAQG--QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQ 1803
Cdd:PTZ00121 1607 MKAEEAKKaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1492-1740 |
1.02e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1492 VQEWDRGQVQGHAQEQAQWQTQieaqgqaqeqAQGGTQGHSQGQAQKQFQNWAQGQAQGHAQEQAQWQTQIEAQGQAQEp 1571
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRK----------KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAL- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1572 aqggaqgqvqgqaqkwaqGQIQGQAQKQVQGEVQKWAQEEAQGQAQwqtqiKAQKWAQEQTQKGAQErvqgQAQKGAQEr 1651
Cdd:PRK09510 130 ------------------KQKQAEEAAAKAAAAAKAKAEAEAKRAA-----AAAKKAAAEAKKKAEA----EAAKKAAA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1652 aqeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaQKGAQERAREQAQKG 1731
Cdd:PRK09510 182 -----------EAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE--AKAAAEKAAAAKAAE 248
|
....*....
gi 2033470018 1732 AQERAREQA 1740
Cdd:PRK09510 249 KAAAAKAAA 257
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1605-1808 |
1.94e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.31 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQER------------------VQGQAQKGAQERAQEQAQEQTQIEAQG 1666
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkelekeeereederiLEYLKEKAEREEEREAEREEIEEEKER 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1667 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG---AQERAREQAQKG 1743
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKErrlAEEAEREEEEFE 264
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2033470018 1744 AQERAQEQGREQTHIEAQGQAQKgAQEWARDRARdqgweqtQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMK-RLEHRRELEK-------QIEEREEQRAAEREEELEEGERLR 321
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1665-1839 |
3.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1665 QGQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKG 1743
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1744 AQERAQEQGREQTHIEAQGQAQKGAQEWARDRARdQGWEQTQIETQRQTQKgAQERAWEQGREQALTSGMAPRAWEQPIS 1823
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEE-AKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
170
....*....|....*.
gi 2033470018 1824 GIAEGVDAAGRSGGSR 1839
Cdd:PTZ00121 1263 AHFARRQAAIKAEEAR 1278
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1601-1808 |
4.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1601 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQ----KGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERA 1676
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1677 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1754
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1755 QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1610-1798 |
6.79e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQgQAQWQTQIKAQKWAQEqTQKGAQErvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERArEQAQKG-----A 1684
Cdd:PTZ00121 1215 EEAR-KAEDAKKAEAVKKAEE-AKKDAEE-----AKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKAdelkkA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1685 QE-RAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGREQThiEA 1760
Cdd:PTZ00121 1287 EEkKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--EE 1364
|
170 180 190
....*....|....*....|....*....|....*...
gi 2033470018 1761 QGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQE 1798
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1603-1808 |
9.04e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKwAQE----EAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1678
Cdd:PTZ00121 1192 ELRK-AEDarkaEAARKAEEERKAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1679 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE-RAREQAQKGAQErareqAQKGAQE---RAQEQGRE 1754
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEaKKADEAKKKAEE-----AKKKADAakkKAEEAKKA 1344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2033470018 1755 QTHIEAQGQAQKGAQEWARDRAR--DQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1603-1928 |
1.24e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 53.50 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQK 1682
Cdd:COG3064 56 EAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1762
Cdd:COG3064 136 KAEEERKAAEAEAAAKAEAEAAR--AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1763 QAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSGGSRSPA 1842
Cdd:COG3064 214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1843 PRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLGKSPTEPKPEAGGCGTPQAPAQEGSPDHPGAERALQDRMEA 1922
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
....*.
gi 2033470018 1923 SEPERR 1928
Cdd:COG3064 374 ALLLGK 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1610-1806 |
1.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQiEAQGQAQKGAQE--RAREQAQKGAQER 1687
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRK--AEELRKAEDARKAEAARKAEEERKAEEARKAED-AKKAEAVKKAEEakKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGAQER----AREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE---------RAQEQGR 1753
Cdd:PTZ00121 1250 NNEEIRKFEEARmahfARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadeakkKAEEAKK 1329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1754 EQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1806
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1662-1800 |
2.73e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.18 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1662 IEAQGQAQ----KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQkgaQERAR 1737
Cdd:COG2268 186 LDALGRRKiaeiIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAEL-AKKKAEERRE---AETAR 261
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1738 EQAQKGAQERAQEQGReqthiEAQGQAQKGAQEwardrardqgwEQTQIETQRQTQKGAQERA 1800
Cdd:COG2268 262 AEAEAAYEIAEANAER-----EVQRQLEIAERE-----------REIELQEKEAEREEAELEA 308
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1609-1745 |
2.90e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.18 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1609 QEEAQGQAQWQTQIKAQKWAQEQTQKgaqERVQGQAQKGAQEraqeqaqeqTQIEAQgQAQKGAQERAREQAQKGAQERA 1688
Cdd:COG2268 221 REAEEAELEQEREIETARIAEAEAEL---AKKKAEERREAET---------ARAEAE-AAYEIAEANAEREVQRQLEIAE 287
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1689 REQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQErAREQAQKgaqERAREQAQKGAQ 1745
Cdd:COG2268 288 REREIELQEkEAEREEAELEADVRKPAEAEKQAAE-AEAEAEA---EAIRAKGLAEAE 341
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1603-1809 |
3.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQwqtQIKAQKWAQEQTQKGAQERVQGQAQKG----AQERAQEQAQEQTQIEAQGQAQ--------- 1669
Cdd:pfam17380 349 ELERIRQEERKRELE---RIRQEEIAMEISRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQqqkvemeqi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1670 KGAQERARE-QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA 1748
Cdd:pfam17380 426 RAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033470018 1749 Q---EQGREQTHIEAQGQAQKGA--QEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQAL 1809
Cdd:pfam17380 506 QamiEEERKRKLLEKEMEERQKAiyEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1608-1808 |
3.27e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIK-AQKWAQ-----EQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1681
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEeAKKKAEdarkaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERA------REQAQKGAqerarEQAQKGAQERAQEQGREQ 1755
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKaeavkkAEEAKKDA-----EEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1756 THIEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1662-1770 |
3.99e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1662 IEAQGQAQKGAQERAREQAQKgAQER-------AREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1734
Cdd:COG2268 208 AERETEIAIAQANREAEEAEL-EQEReietariAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEI 285
|
90 100 110
....*....|....*....|....*....|....*..
gi 2033470018 1735 RAREQAQKGAQ-ERAQEQGREQTHIEAQGQAQKGAQE 1770
Cdd:COG2268 286 AEREREIELQEkEAEREEAELEADVRKPAEAEKQAAE 322
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1610-1807 |
4.78e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQeqaqeqtqiEAQGQAQKGAQERAREQAQKGAQErar 1689
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK---------KVEQLKKKEAEEKKKAEELKKAEE--- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1690 EQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAR--EQAQKGAQE--RAQEQGR---EQTHIEAQg 1762
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEEAKkaEELKKKEAEekKKAEELKkaeEENKIKAE- 1733
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2033470018 1763 QAQKGAQEWAR--DRARDQGWEQTQIEtqrQTQKGAQERAWEQGREQ 1807
Cdd:PTZ00121 1734 EAKKEAEEDKKkaEEAKKDEEEKKKIA---HLKKEEEKKAEEIRKEK 1777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1604-1820 |
6.16e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1604 VQKWAQEEAQGQAQWQTQIKAQKWAQEQTQK--GAQERVQGQAQKGAQERAQEQaqeqtqieAQGQAQKGAQERAREQAQ 1681
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELE--------ELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1761
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1762 GQAQKGAQEwARDRARDQ----GWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQ 1820
Cdd:TIGR02168 467 REELEEAEQ-ALDAAERElaqlQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1603-1805 |
6.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGA-QERAQEQAQEQTQIEAQGQAQKGAQERAREQAQ 1681
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQKGAQERAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKgaqERAQEQGREQTHIEAQ 1761
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELEELIEELESELEALLN---ERASLEEALALLRSEL 896
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1762 GQAQKGAQEW--ARDRARDQGWEQTQIETQRQTQKGA--------QERAWEQGR 1805
Cdd:TIGR02168 897 EELSEELRELesKRSELRRELEELREKLAQLELRLEGlevridnlQERLSEEYS 950
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1628-1735 |
6.90e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 48.11 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQ 1705
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRReeEERQRKAEEEAEEREQREQEEQERLQKQ 102
|
90 100 110
....*....|....*....|....*....|.
gi 2033470018 1706 KGAQE-RAREQAQKGAQERAReQAQKGAQER 1735
Cdd:pfam05672 103 KEEAEaKAREEAERQRQEREK-IMQQEEQER 132
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1631-1802 |
7.32e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.72 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1631 QTQKGAQERVQGQAQKGAQERAQEQAQeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqaqkgaQE 1710
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE------EE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1711 RAREQAQKGAQERAREQAQ---KGAQERAREQAQKGAqERAQEQGREQTHIEAQ-GQAQKGAQEWArdrardqgwEQTQI 1786
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEefrRKLQELQRKKQQEEA-ERAEAEKQRQKELEMQlAEEQKRLMEMA---------EEERL 477
|
170
....*....|....*.
gi 2033470018 1787 ETQRQTQKGAQERAWE 1802
Cdd:pfam15709 478 EYQRQKQEAEEKARLE 493
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1563-1780 |
7.49e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 51.06 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1563 EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQg 1642
Cdd:PRK12678 57 EARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1643 QAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGaqeRAREQAQ----KGAQERAREQAQKGAQERAREQAQK 1718
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG---DREDRQAeaerGERGRREERGRDGDDRDRRDRREQG 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1719 GAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI--EAQGQAQKGAQEWARDRARDQG 1780
Cdd:PRK12678 213 DRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGddGEGRGGRRGRRFRDRDRRGRRG 276
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1610-1808 |
8.05e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQGQAQWQTQIKAQKwaQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAR 1689
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARK--AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1690 EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQ 1769
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
170 180 190
....*....|....*....|....*....|....*....
gi 2033470018 1770 EWARDRARDQGWEQTQIETQRQTQKGAQERAwEQGREQA 1808
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKA-DAAKKKA 1338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1658-1781 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1658 EQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAR 1737
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2033470018 1738 EQAQkgaQERAQEQGREQTHIEAQ-GQAQKGAQEWARDRARDQGW 1781
Cdd:COG4913 326 DELE---AQIRGNGGDRLEQLEREiERLERELEERERRRARLEAL 367
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1603-1773 |
1.34e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQ-KGAQERAREQAQ 1681
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFE--EIRLRKQRLEEERQRQEEEERKQRLQlQAAQERARQQQE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 ---KGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQK--GAQERAREQAQKGAQErAREQAQKGAQERAQEQgrEQ 1755
Cdd:pfam15709 427 efrRKLQELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQE-AEEKARLEAEERRQKE--EE 503
|
170
....*....|....*...
gi 2033470018 1756 THIEAQGQAQKGAQEWAR 1773
Cdd:pfam15709 504 AARLALEEAMKQAQEQAR 521
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1535-1812 |
1.51e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1535 QAQKQFQNWAQGQAQghAQEQA-QWQTQI-EAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQE-- 1610
Cdd:TIGR00618 236 QQTQQSHAYLTQKRE--AQEEQlKKQQLLkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRih 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1611 -EAQGQAQWQTQIKAQKWA-QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERA 1688
Cdd:TIGR00618 314 tELQSKMRSRAKLLMKRAAhVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1689 REQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAQEQGREQTHieaqgqAQKGA 1768
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELCAAAITCTAQCEKLEKIH------LQESA 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2033470018 1769 QewaRDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQALTSG 1812
Cdd:TIGR00618 466 Q---SLKEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCG 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1647-1790 |
1.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1647 GAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERARE 1726
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1727 QAQkgaQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQR 1790
Cdd:COG1196 711 EAE---EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1112-1506 |
2.22e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 49.60 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1112 GAMAAAGSVASRATPAPAPGSTQSPGDRtAGEPETLGQWGSRALSESHPRGEALPRDPHSHGLLAPGGSLEPKSGAAGRS 1191
Cdd:PRK07764 417 PAAAAAPAPAAAPQPAPAPAPAPAPPSP-AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1192 LLRGVALVQHPEDIATLARH-PEDAAALARHPEAarlyisnTSAASRHTAAVGG-RKDVAVegnlLGFSTES---GIPAS 1266
Cdd:PRK07764 496 APAAPAAPAGADDAATLRERwPEILAAVPKRSRK-------TWAILLPEATVLGvRGDTLV----LGFSTGGlarRFASP 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1267 DHPRPQARSVAE------SPSYGPGlpPSPPENPQAKGREGVRFPRGAEPDHLLPAVPPAEVDMGWVGGTHQRGPPHLQA 1340
Cdd:PRK07764 565 GNAEVLVTALAEelggdwQVEAVVG--PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1341 HLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVAPSGskvvlnPAKEPQTWWAQ 1420
Cdd:PRK07764 643 PAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAGQADD 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1421 DLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEGtrAARNPAVPPGEPEGPGSPAAQGQAQKQVQEWDRGQV 1500
Cdd:PRK07764 717 PAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP--PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMD 794
|
....*.
gi 2033470018 1501 QGHAQE 1506
Cdd:PRK07764 795 DEDRRD 800
|
|
| DUF5384 |
pfam17358 |
Family of unknown function (DUF5384); This is a family of unknown function found in ... |
1663-1761 |
2.53e-05 |
|
Family of unknown function (DUF5384); This is a family of unknown function found in Proteobacteria.
Pssm-ID: 407453 [Multi-domain] Cd Length: 145 Bit Score: 46.13 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE-QAQ 1741
Cdd:pfam17358 1 EQQGKEDRVAAERQAAYEREWEEEQARAEAAAAAARRARAAAAAAAAAAAKERAKAEALADKKRDQSYEDELRALEiEER 80
|
90 100
....*....|....*....|.
gi 2033470018 1742 KGAQERAQEQG-REQTHIEAQ 1761
Cdd:pfam17358 81 KLALAAQKARAkRENDFIDQE 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1600-1755 |
2.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1600 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERARE 1678
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1679 QAQKGAQERAREQAQKgaqeRAREQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAQEQGRE 1754
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEK----KKAEELKKAEEENKIkaEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
.
gi 2033470018 1755 Q 1755
Cdd:PTZ00121 1776 E 1776
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1634-1753 |
3.41e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 46.22 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1634 KGAQERVQGQAQKgaQERAQEQAQEQTQIEAQGQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAR 1713
Cdd:pfam11600 1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2033470018 1714 EQAQKGAQERAREQAQKGAQE----RAREQAQKGAQERAQEQGR 1753
Cdd:pfam11600 78 DEKEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEK 121
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1623-1805 |
3.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1623 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQkgAQERARE 1702
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLE--------LLEAELEELRAELARLEAELERLEARLDALR--EELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1703 QAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQK-----GAQERAQEQGREQTHIEAQGQAQKGAQEWARDRAR 1777
Cdd:COG4913 330 AQIRGNGGDRLEQLE---REIERLERELEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*...
gi 2033470018 1778 DQGWEQTQIETQRQTQKGAQERAWEQGR 1805
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1623-1770 |
4.03e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.46 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1623 KAQKWAQEQTQKgaQERVQgQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQaqKGAQERARE 1702
Cdd:pfam05262 214 RAQQLKEELDKK--QIDAD-KAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ--KREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1703 QAQKGAQE--RAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQEQGREQTHIEAqgQAQKGAQE 1770
Cdd:pfam05262 289 EIKKNDEEalKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEDLQKTKPQVEA--QPTSLNED 354
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1667-1807 |
4.99e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1667 QAQKGAQERAREQAQKGAQERAREQAQKGAQE---RAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKG 1743
Cdd:PRK04863 469 QAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSELEQRLRQQQR---AERLLAEFCKR 545
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1744 A----------QERAQEQGREQTHIEAQgQAQKGAQewaRDRARDQGwEQTQIETQRQTQKG-----AQERAwEQGREQ 1807
Cdd:PRK04863 546 LgknlddedelEQLQEELEARLESLSES-VSEARER---RMALRQQL-EQLQARIQRLAARApawlaAQDAL-ARLREQ 618
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1609-1807 |
6.62e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.34 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1609 QEEAQGQAQWQTQIKAQKWAQEQTQkgaQERVQGQAQKGAQEraqeqaqeqtqiEAQGQAQKGAQERAR----EQAQKGA 1684
Cdd:pfam15558 54 LLLQQSQEQWQAEKEQRKARLGREE---RRRADRREKQVIEK------------ESRWREQAEDQENQRqeklERARQEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1685 QERAREQAQkgaqeraREQAQKGAQERAREQAQKGAQERAREQAQK---------------GAQERAREQAQKGA---QE 1746
Cdd:pfam15558 119 EQRKQCQEQ-------RLKEKEEELQALREQNSLQLQERLEEACHKrqlkereeqkkvqenNLSELLNHQARKVLvdcQA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1747 RAQEQGR----EQTHIEAQ----GQAQKGAQEwARDRARDqgwEQTQIETqrqtqkgAQERAWEQGREQ 1807
Cdd:pfam15558 192 KAEELLRrlslEQSLQRSQenyeQLVEERHRE-LREKAQK---EEEQFQR-------AKWRAEEKEEER 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1623-1808 |
6.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1623 KAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR- 1701
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKi 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1702 --EQAQKGAQERAR-EQAQKGAQERAR--EQAQKGAQE---RAREQAQKGAQE--RAQEQGREQTHIEAQGQAQKGAQEW 1771
Cdd:PTZ00121 1621 kaEELKKAEEEKKKvEQLKKKEAEEKKkaEELKKAEEEnkiKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190
....*....|....*....|....*....|....*....
gi 2033470018 1772 ARDRARDQGWEQTQIETQRQTQKGAQERAW--EQGREQA 1808
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaEEAKKEA 1739
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1665-1794 |
7.71e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 45.06 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1665 QGQAQKgaQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGA 1744
Cdd:pfam11600 8 QSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2033470018 1745 QERAQEQGRE--QTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQK 1794
Cdd:pfam11600 85 KLRLKEEKRKekQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITRFLQK 136
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1674-1755 |
8.86e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 44.77 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1674 ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKGAQ---ERAREQAQkgaQERAR--EQAQKGAQ--- 1745
Cdd:PRK05759 48 ERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKKRAAqiiEEAKAEAE---AEAARikAQAQAEIEqer 113
|
90
....*....|
gi 2033470018 1746 ERAQEQGREQ 1755
Cdd:PRK05759 114 KRAREELRKQ 123
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1605-1806 |
9.63e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQAQWQTQikaQKWAQEQTQKGAQERVQgQAQKGAQEraqeqaqeqtqIEAQGQAQKGAQERAREQAQKGA 1684
Cdd:pfam13868 36 AEEKEEERRLDEMMEEE---RERALEEEEEKEEERKE-ERKRYRQE-----------LEEQIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1685 QERaREQAQKGAQERAREQAQKGAQERA---------REQAQKGAQERARE----------QAQKGAQERAREQAQKgAQ 1745
Cdd:pfam13868 101 EQM-DEIVERIQEEDQAEAEEKLEKQRQlreeidefnEEQAEWKELEKEEEreederileyLKEKAEREEEREAERE-EI 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2033470018 1746 ERAQEqgREQTHIEAQGQAQKGAQEwARDRARDQGWEQTQIETQRQTQKGAQERAWEQGRE 1806
Cdd:pfam13868 179 EEEKE--REIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQRQE 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1608-1816 |
1.05e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQgqaQWQTQIKAQK------WAQEQTQKGAQERVQGQAQKGA----QERAQEQAQEQTQIEAQGQAQKGAQERAR 1677
Cdd:TIGR00618 251 AQEEQL---KKQQLLKQLRarieelRAQEAVLEETQERINRARKAAPlaahIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1678 EQAQKGAQERAREQAQKG-------AQERAREQAQKGAQERAREQAQKGAQERAREQAQKgaQERAREQAQKGAQERAQE 1750
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRllqtlhsQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDIL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033470018 1751 QgREQTHIEAQGQAQKGAQEwarDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPR 1816
Cdd:TIGR00618 406 Q-REQATIDTRTSAFRDLQG---QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1686-1755 |
1.14e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 43.97 E-value: 1.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1686 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAQ---ERAREQAQKgAQERAQEQGREQ 1755
Cdd:cd06503 43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEAErilEQAKAEIEQ-EKEKALAELRKE 118
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1658-1831 |
1.19e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.92 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1658 EQtqieaqgqaqkgaqERAREQAQKgAQERAREQAQKGaqERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAR 1737
Cdd:pfam05262 214 RA--------------QQLKEELDK-KQIDADKAQQKA--DFAQDNADK--QRDEVRQKQQEAKNLPKPADTSSPKEDKQ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1738 -EQAQKGAQERAQEQGREQTHiEAQGQAQKGAQEWARD-RARDQGWEQTQIETQRQTQKGAQ--ERAWEQGREQALTSGM 1813
Cdd:pfam05262 275 vAENQKREIEKAQIEIKKNDE-EALKAKDHKAFDLKQEsKASEKEAEDKELEAQKKREPVAEdlQKTKPQVEAQPTSLNE 353
|
170
....*....|....*...
gi 2033470018 1814 APRAWEQPISGIaEGVDA 1831
Cdd:pfam05262 354 DAIDSSNPVYGL-KVVDP 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1620-1822 |
1.27e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1620 TQIKAQKWAQEQTQKGAQERVQGQAQ---KGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER-AREQAQKG 1695
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKReAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1696 AQERAREQAQKG---AQERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQE---RAQEQGREQTHIEAQGQA-QKGA 1768
Cdd:TIGR00618 259 QQLLKQLRARIEelrAQEAVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRihtELQSKMRSRAKLLMKRAAhVKQQ 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1769 QEWARDRARDQGWEQTQIETQRQTQkgaQERAWEQGREQALTSGMAPRAWEQPI 1822
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHE---VATSIREISCQQHTLTQHIHTLQQQK 388
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1664-1786 |
1.35e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1664 AQGQAQKGAQERAREQAQKGA---QERAREQAQKGAQERAREQAQKgAQERAREQAQKGA-QERAREQAQKGAQE-RARE 1738
Cdd:COG1566 86 AQAEAQLAAAEAQLARLEAELgaeAEIAAAEAQLAAAQAQLDLAQR-ELERYQALYKKGAvSQQELDEARAALDAaQAQL 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2033470018 1739 QAQKGAQERAQEQGREQTHIEAQGQAQKGAQEwARDRARDQgWEQTQI 1786
Cdd:COG1566 165 EAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAELN-LARTTI 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1608-1762 |
1.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQ------ERAREQAQ 1681
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlerEIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQK-----GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaqERAQEQGREQT 1756
Cdd:COG4913 354 LEERERRRARLEAllaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR----RELRELEAEIA 429
|
....*.
gi 2033470018 1757 HIEAQG 1762
Cdd:COG4913 430 SLERRK 435
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1601-1738 |
1.44e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1601 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQEraqeqaqeqtqIEAQGQAQKGAQERAREQA 1680
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAER-----------AEAEKQRQKELEMQLAEEQ 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1681 QK--GAQERAREQAQKGAQErAREQAQKGAQERarEQAQKGAQERAREQAQKGAQERARE 1738
Cdd:pfam15709 466 KRlmEMAEEERLEYQRQKQE-AEEKARLEAEER--RQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1619-1800 |
1.45e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1619 QTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERA-------QEQAQEQTQIEAQGQAQkgaQERAREQAQKGAQERAREQ 1691
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAremervrLEEQERQQQVERLRQQE---EERKRKKLELEKEKRDRKR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1692 aqkgAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEW 1771
Cdd:pfam17380 489 ----AEEQRRKILEKELEERKQAMIE---EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA 561
|
170 180
....*....|....*....|....*....
gi 2033470018 1772 ARDRARDQGWEQTQiETQRQTQKGAQERA 1800
Cdd:pfam17380 562 TEERSRLEAMERER-EMMRQIVESEKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1686-1808 |
1.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1686 ERAREQAQK----GAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIE- 1759
Cdd:COG1196 206 ERQAEKAERyrelKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEe 285
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1760 AQGQAQKGAQEWARDRARDQGWEQTQIE-TQRQTQKGAQERAWEQGREQA 1808
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRElEERLEELEEELAELEEELEEL 335
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1673-1778 |
2.05e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 43.61 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1673 QERAREQAQKGAQ-ERAREQAQKgAQERAREQAQKgaqerAREQAQkgaqeRAREQAQKgaqeRAREQAQKgAQERAQEq 1751
Cdd:PRK05759 34 EERQKKIADGLAAaERAKKELEL-AQAKYEAQLAE-----ARAEAA-----EIIEQAKK----RAAQIIEE-AKAEAEA- 96
|
90 100
....*....|....*....|....*..
gi 2033470018 1752 grEQTHIEAQGQAQKGAQewaRDRARD 1778
Cdd:PRK05759 97 --EAARIKAQAQAEIEQE---RKRARE 118
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1688-1826 |
2.13e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQerareQAQKGAQERAQEQGREQTHIEAQGQAQKG 1767
Cdd:pfam13904 62 AAKQRQRQ-KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKAR-----QQTKKREESHKQKAAESASKSLAKPERKV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1768 AQEWARDRArdQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIA 1826
Cdd:pfam13904 136 SQEEAKEVL--QEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQKWMKNVK 192
|
|
| 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 ... |
1680-1765 |
2.32e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.07 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1680 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1758
Cdd:pfam00430 38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115
|
....*..
gi 2033470018 1759 EAQGQAQ 1765
Cdd:pfam00430 116 RQQVVAL 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1616-1833 |
2.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1616 AQWQTQIKAQKWAQEQTQKGAQERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqERAREQAQKG 1695
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVASAEREIAEL---EAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1696 AQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKgAQERAQEQGREQTHIEAQGQAQKGAQEWAR-- 1773
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEE-ELDELQDRLEAAEDLARLELRALLEERFAAal 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1774 -DRARDQgwEQTQIETQRQTQKGAQERAweqgrEQALTSGMAP--RAWEQPISGIAEGVDAAG 1833
Cdd:COG4913 760 gDAVERE--LRENLEERIDALRARLNRA-----EEELERAMRAfnREWPAETADLDADLESLP 815
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1665-1779 |
2.78e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.79 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1665 QGQAQkGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAReqaQKGA 1744
Cdd:PRK06991 149 QAQAD-AARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAAAAPAADDAEAKKRAIIAA-ALERAR---KKKE 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 2033470018 1745 QERAQEQG-REQTHIEAQGQAQKGAQEWARDRARDQ 1779
Cdd:PRK06991 224 ELAAQGAGpKNTEGVSAAVQAQIDAAEARRKRLAEQ 259
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1673-1808 |
2.98e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.31 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1673 QERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQErAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQG 1752
Cdd:pfam13904 70 KELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQ-QTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEWE 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2033470018 1753 REQThieAQGQAQKgaQEWARDRARDQgweqtQIETQRQTQKgaqERAWEQGREQA 1808
Cdd:pfam13904 149 RKKL---EQQQRKR--EEEQREQLKKE-----EEEQERKQLA---EKAWQKWMKNV 191
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1617-1836 |
3.03e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 46.14 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1617 QWQTQIkaQKWAQEQTQKGAQERVQ--GQAQKGA---QERAQEQAQEQTQIEAQGQAQKGaQERAREQAQKGAQERAREQ 1691
Cdd:TIGR00927 603 KWNKQI--ELWVKEQLSRRPVAKVMalGDLSKGDvaeAEHTGERTGEEGERPTEAEGENG-EESGGEAEQEGETETKGEN 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1692 AQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQKG-AQERAQEQGRE-QTHIEAQGQAQKGA 1768
Cdd:TIGR00927 680 ESEGEIPAERKGEQEGEGEiEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIeTGEEGEEVEDEgEGEAEGKHEVETEG 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1769 QEWARDRARDQGWEQTQIETQRQTQKGAQ-ERAWEQGREQALTSGMAPRAWEQPISGIAEGVDAAGRSG 1836
Cdd:TIGR00927 760 DRKETEHEGETEAEGKEDEDEGEIQAGEDgEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEV 828
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1674-1807 |
3.13e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1674 ERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERaREQAQKGAQERARE-QAQKGAQERAREQAQKGAQERAQEQG 1752
Cdd:pfam13868 50 EEERERALE--EEEEKEEERKEERKRYRQELEEQIEER-EQKRQEEYEEKLQErEQMDEIVERIQEEDQAEAEEKLEKQR 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2033470018 1753 REQTHIEAQGQAQKGAQEWARDRARDqgwEQTQIEtQRQTQKGAQERAWEQGREQ 1807
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEERE---EDERIL-EYLKEKAEREEEREAEREE 177
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1672-1808 |
3.19e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1672 AQERAREQAQKGAQERAR----EQAQKGAQERAREQAQKGAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQ 1745
Cdd:pfam02029 4 EEEAARERRRRAREERRRqkeeEEPSGQVTESVEPNEHNSYEEDSElkPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1746 ERAQEQGREQTHI------EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:pfam02029 84 ERQKEFDPTIADEkesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQA 152
|
|
| V_ATP_synt_G |
TIGR01147 |
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ... |
1667-1749 |
3.38e-04 |
|
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130217 [Multi-domain] Cd Length: 113 Bit Score: 42.12 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1667 QAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1746
Cdd:TIGR01147 13 QAEKRAAEKVSE-ARKRKTKRLKQAKEEAQKEVEKYKQQREKEFKEFEAKHLGGNGAAEEKAEAETQAKIREIKKAVQKN 91
|
...
gi 2033470018 1747 RAQ 1749
Cdd:TIGR01147 92 KDA 94
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
1600-1754 |
3.57e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.93 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1600 VQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQ--EQTQIEAQGQAQKGAQERAR 1677
Cdd:PTZ00341 979 VEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEydEENVEEIEENAEENVEENIE 1058
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2033470018 1678 EQAQKGAQERArEQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1754
Cdd:PTZ00341 1059 ENIEEYDEENV-EEIEENIEENIEENVEENVEENV-EEIEENVEENVEENAEENAEENAEENAEEYDDENPEEHNEE 1133
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1605-1791 |
3.70e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgQAQKGA--QERAQEqaqeqtqieaqgqaqkgaqERAREQAQK 1682
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-KAERDElrAKLYQE-------------------EQERKERQK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1683 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQG 1762
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAE---REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI 299
|
170 180
....*....|....*....|....*....
gi 2033470018 1763 QAQKGAQEWARDRARDQGWEQTQIETQRQ 1791
Cdd:pfam13868 300 EEREEQRAAEREEELEEGERLREEEAERR 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1547-1753 |
4.22e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1547 QAQGHAQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQK 1626
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1627 WAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEaqgQAQKGAQERAR--EQAQKGAQERAR--EQAQKGAQERAR 1701
Cdd:PTZ00121 1668 KKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAE---ELKKKEAEEKKkaEELKKAEEENKIkaEEAKKEAEEDKK 1744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1702 --EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGR 1753
Cdd:PTZ00121 1745 kaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| 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 ... |
1668-1749 |
4.64e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 42.30 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1668 AQKGAQERARE-QAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQE 1746
Cdd:pfam00430 38 EIAEAEERRKDaAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAEL 115
|
...
gi 2033470018 1747 RAQ 1749
Cdd:pfam00430 116 RQQ 118
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1668-1754 |
4.68e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.49 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1668 AQKGAQERAREQAQKGAQERAREQAQKgaqeraREQAQKGAQERAREQAQKGAQER--AREQAQKGAQERAREQA---QK 1742
Cdd:cd16269 201 EAERAKAEAAEQERKLLEEQQRELEQK------LEDQERSYEEHLRQLKEKMEEERenLLKEQERALESKLKEQEallEE 274
|
90
....*....|..
gi 2033470018 1743 GAQERAQEQGRE 1754
Cdd:cd16269 275 GFKEQAELLQEE 286
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1677-1807 |
5.73e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1677 REQaQKGAQERAREQAQKGAQ---ERAR-EQA-QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQ 1751
Cdd:pfam15709 328 REQ-EKASRDRLRAERAEMRRlevERKRrEQEeQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE 406
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1752 GREQthiEAQGQAqkgaqewARDRARDQGWE--QTQIETQRQTQKGAQERAWEQGREQ 1807
Cdd:pfam15709 407 ERKQ---RLQLQA-------AQERARQQQEEfrRKLQELQRKKQQEEAERAEAEKQRQ 454
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1686-1808 |
6.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1686 ERAREQAQKgAQERAR--EQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQ 1763
Cdd:COG4913 238 ERAHEALED-AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2033470018 1764 AQKGAQEwardrardqgwEQTQIETQRQTQKGAQERAWEQGREQA 1808
Cdd:COG4913 317 RLDALRE-----------ELDELEAQIRGNGGDRLEQLEREIERL 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1600-1777 |
6.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1600 VQGEVQKWAQEEAQGQAQwQTQIKAQKWAQEQTQKGAQERVQgQAQKGAQERAQEQAQEQTQIE-AQGQAQKGAQERARE 1678
Cdd:COG4372 43 LQEELEQLREELEQAREE-LEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELEsLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1679 QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERArEQAQKGAQERAREQAQKGAQERAQEQGREQTHI 1758
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170
....*....|....*....
gi 2033470018 1759 EAQGQAQKGAQEWARDRAR 1777
Cdd:COG4372 200 EELAEAEKLIESLPRELAE 218
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1532-1741 |
8.02e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1532 SQGQAQKQFQNWAQGQAQGHAQEQAQwQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEE 1611
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQAR-QKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1612 AQGQAQWQTQIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERARE 1690
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEaKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2033470018 1691 QAQKGAQERAREQAQKGAQE-RAREQAQKGAQERAREQAQKGAQERAREQAQ 1741
Cdd:TIGR02794 224 EAERKADEAELGDIFGLASGsNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1552-1777 |
8.70e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.87 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1552 AQEQAQWQTQIEAQ----GQAQEPAQGGAQGQVQGQAQKWAQgqiqgqaqkqvQGEVQKWAQEEAQGQAQWQTQIKaqKW 1627
Cdd:pfam15558 57 QQSQEQWQAEKEQRkarlGREERRRADRREKQVIEKESRWRE-----------QAEDQENQRQEKLERARQEAEQR--KQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKgAQERV----QGQAQKGAQERAQEQAQEQTQIEAQGQAQKGA---QERAREQAQKGAQERareqaqkgaQERA 1700
Cdd:pfam15558 124 CQEQRLK-EKEEElqalREQNSLQLQERLEEACHKRQLKEREEQKKVQEnnlSELLNHQARKVLVDC---------QAKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1701 REQAQKGAQE----RAREQAQKGAQERAREQAQKGAQEraREQAQKgAQERAQEQGRE-QTHIEA--------QGQAQKG 1767
Cdd:pfam15558 194 EELLRRLSLEqslqRSQENYEQLVEERHRELREKAQKE--EEQFQR-AKWRAEEKEEErQEHKEAlaeladrkIQQARQV 270
|
250
....*....|
gi 2033470018 1768 AQEWARDRAR 1777
Cdd:pfam15558 271 AHKTVQDKAQ 280
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1610-1809 |
9.48e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1610 EEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQA---QKGAQERAREQAQKGAQE 1686
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1687 RAREQAQKgAQERAREQAQKGAQERAREQAQKGAQER-AREQAQKGAQERAREQAQKGAQERAQEQgrEQTHIEAQGQAQ 1765
Cdd:TIGR00618 277 AVLEETQE-RINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRAAHVKQQSSIE--EQRRLLQTLHSQ 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2033470018 1766 KgaqewarDRARDQGWEQTQIETQRQTQKGAQE--RAWEQGREQAL 1809
Cdd:TIGR00618 354 E-------IHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLT 392
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1663-1745 |
1.06e-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: 40.88 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAREQAQKGAqERAREQAQKGAQERA 1736
Cdd:cd06503 44 KAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAEI-EQEKEKALAELRKEV 119
|
....*....
gi 2033470018 1737 REQAQKGAQ 1745
Cdd:cd06503 120 ADLAVEAAE 128
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1673-1827 |
1.08e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 44.26 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1673 QERaREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQK-GAQERAREQAQKGAQERAREQAQKgaQERAQEQ 1751
Cdd:PRK10811 604 QDR-RKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQqTAETRESQQAEVTEKARTQDEQQQ--APRRERQ 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1752 GREQthiEAQGQAQKGAQEWARDRARDQGWEQTQIETQ-------RQ-TQK-----GAQERAWEQGREQALTSGMAPRAW 1818
Cdd:PRK10811 681 RRRN---DEKRQAQQEAKALNVEEQSVQETEQEERVQQvqprrkqRQlNQKvrieqSVAEEAVAPVVEETVAAEPVVQEV 757
|
....*....
gi 2033470018 1819 EQPISGIAE 1827
Cdd:PRK10811 758 PAPRTELVK 766
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1663-1746 |
1.11e-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: 41.31 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQgQAQKGAQER---AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQERAREQ 1739
Cdd:COG0711 49 EAE-AALAEYEEKlaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAEVADL 123
|
....*..
gi 2033470018 1740 AQKGAQE 1746
Cdd:COG0711 124 AVAIAEK 130
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1608-1788 |
1.15e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1608 AQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQER 1687
Cdd:PRK05035 463 EREKAAREARHKKAAEARAAKDKDAVAAALARVK--AKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1688 AREQAQKGAQE--RAREQAQKGAQerarEQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAq 1765
Cdd:PRK05035 541 AAADPKKAAVAaaIARAKAKKAAQ----QAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA- 615
|
170 180
....*....|....*....|...
gi 2033470018 1766 KGAQEWARDRARDQGWEQTQIET 1788
Cdd:PRK05035 616 AVAAAIARAKAKKAEQQANAEPE 638
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1674-1750 |
1.26e-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: 41.31 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1674 ERAREQAQKGAQER------AREQAQKgAQERAREQAQKgAQERAREQAQKGAqERAREQAQKgAQERAREQAQKGAQER 1747
Cdd:COG0711 44 ERAKEEAEAALAEYeeklaeARAEAAE-IIAEARKEAEA-IAEEAKAEAEAEA-ERIIAQAEA-EIEQERAKALAELRAE 119
|
...
gi 2033470018 1748 AQE 1750
Cdd:COG0711 120 VAD 122
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1624-1749 |
1.30e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.60 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1624 AQKWAQEQTQKgaqERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQ 1703
Cdd:pfam11600 3 SQKSVQSQEEK---EKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1704 AQKGAQERAREQAQKGAQE----RAREQAQKGAQERAREQAQKGAQERAQ 1749
Cdd:pfam11600 80 KEKAEKLRLKEEKRKEKQEaleaKLEEKRKKEEEKRLKEEEKRIKAEKAE 129
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1601-1810 |
1.35e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1601 QGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQA 1680
Cdd:TIGR00927 682 EGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDR 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1681 QKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEA 1760
Cdd:TIGR00927 762 KETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2033470018 1761 QGQA---QKGAQ-EWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALT 1810
Cdd:TIGR00927 842 QGEAkqdEKGVDgGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1605-1816 |
1.45e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1605 QKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAqgqAQKGAQERA---REQAQ 1681
Cdd:PRK10246 226 QVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSL---AQPARQLRPhweRIQEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQkgaQERAREQAQKGAQERAREQAQKGAQERAREQAQKGA----QERAREQAQKGAQERAQ--EQGREQ 1755
Cdd:PRK10246 303 SAALAHTRQQIE---EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwlaeHDRFRQWNNELAGWRAQfsQQTSDR 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2033470018 1756 THIEAQgQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQgREQALTSGMAPR 1816
Cdd:PRK10246 380 EQLRQW-QQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQ 438
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
1682-1805 |
1.51e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 41.21 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERAREQAQKgaQERAREQAQKGAQERAREQAQKGAQERAREQAqKGAQERAREQAQKGAQERAQEQGREQTHIEAQ 1761
Cdd:pfam11600 1 RRSQKSVQSQEEK--EKQRLEKDKERLRRQLKLEAEKEEKERLKEEA-KAEKERAKEEARRKKEEEKELKEKERREKKEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2033470018 1762 GQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1805
Cdd:pfam11600 78 DEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEK 121
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1668-1773 |
1.66e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1668 AQKGAQERAREQAQKGAQERAREQAQKGAQERAREQaqkgaqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1747
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQ------ERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEER 250
|
90 100 110
....*....|....*....|....*....|..
gi 2033470018 1748 AQ---EQGREQTHiEAQGQA---QKGAQEWAR 1773
Cdd:cd16269 251 ENllkEQERALES-KLKEQEallEEGFKEQAE 281
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1621-1831 |
1.81e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1621 QIKAQKWAQEQTQKGAQE-RVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQER 1699
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEaKARFEARQARLEREKA--------AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1700 AREQAQKG--------AQERAREQAQKGAQERAREQA------QKGAQERAREQAQKGAQERAQEQGREqthiEAQGQAQ 1765
Cdd:PRK05035 505 PIVIKAGArpdnsaviAAREARKAQARARQAEKQAAAaadpkkAAVAAAIARAKAKKAAQQAANAEAEE----EVDPKKA 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033470018 1766 KGAQEWARDRARDQgweQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISGIAEGVDA 1831
Cdd:PRK05035 581 AVAAAIARAKAKKA---AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
935-1493 |
1.94e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 935 ADHSVPETLLTQRLQTDPAGGKENK-GSFENSHGPRNPDDISGertselrdvkhPLPESNEISMQKKGSATNDPAASQNL 1013
Cdd:PHA03247 2564 PDRSVPPPRPAPRPSEPAVTSRARRpDAPPQSARPRAPVDDRG-----------DPRGPAPPSPLPPDTHAPDPPPPSPS 2632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1014 LRGNTshASSSQQVPSPTGRNPTGAPTSLAASSKGRTGPEGVTPMGMTVPgalEECRRPLLIESSQPLKAAEEITSHDVR 1093
Cdd:PHA03247 2633 PAANE--PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP---QRPRRRAARPTVGSLTSLADPPPPPPT 2707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1094 ENPLSSLNEP--PKPGMKACGAMAAAGSVASRATPAPAPGSTQSPGDRTAGEPETLgqwgSRALSESHPRGEALPrdPHS 1171
Cdd:PHA03247 2708 PEPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT----AGPPAPAPPAAPAAG--PPR 2781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1172 HGLLAPGGSLEPKSGAAGRSLLRGVALVQHPEDIATLARHPEDAAALARHPEAARLYISNTSAASRHTAAVGGrkDVAVE 1251
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGG--SVAPG 2859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1252 GNLLGFSTESGIPA--SDHPRPQARSVAE-------SPSYGPGLPPSPPENPQAKGREgvrFPRGAEPDHLLPAVPPaev 1322
Cdd:PHA03247 2860 GDVRRRPPSRSPAAkpAAPARPPVRRLARpavsrstESFALPPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPP--- 2933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1323 dmgwvggthqRGPPHLQAHLPPTAGDT-QAKLRASVPEPRTQAGESQERPLTQAdlgRQQSHQAQEETPQP------GDA 1395
Cdd:PHA03247 2934 ----------PPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVPRF---RVPQPAPSREAPASstppltGHS 3000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1396 GKRVAPSGSKVVLN------PAKEPQTWWAQDLAGDKGMAIGVGGACQRSDQGQQHLQGPweergrstawgegtraarNP 1469
Cdd:PHA03247 3001 LSRVSSWASSLALHeetdppPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPP------------------EP 3062
|
570 580
....*....|....*....|....
gi 2033470018 1470 AVPPGEPEGPGSPAAQGQAQKQVQ 1493
Cdd:PHA03247 3063 HDPFAHEPDPATPEAGARESPSSQ 3086
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1619-1812 |
1.95e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1619 QTQIKAQKWAQEQTQKGAQ-ERVQGQAQKgAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQ---- 1693
Cdd:COG4372 42 KLQEELEQLREELEQAREElEQLEEELEQ-ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEleel 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1694 KGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWAR 1773
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190
....*....|....*....|....*....|....*....
gi 2033470018 1774 DRARDQgWEQTQIETQRQTQKGAQERAWEQGREQALTSG 1812
Cdd:COG4372 201 ELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
1673-1760 |
1.97e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 39.73 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1673 QERAREQAQKGAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQE-RAQEQ 1751
Cdd:pfam16999 13 REAALDQQIEAARKEAEREVEAAEAEAARILRE--AEAKAKALQAEYRQELAAETAR--IREEARARAEAEAQAvRTRAE 88
|
....*....
gi 2033470018 1752 GREQTHIEA 1760
Cdd:pfam16999 89 GRLQQAVEL 97
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1686-1755 |
2.04e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.54 E-value: 2.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2033470018 1686 ERAREQAQKgAQERAREQAQKGAQERA--REQAQKGAQ---ERAREQAQKGAqERAREQAQK---GAQERAQEQGREQ 1755
Cdd:COG0711 44 ERAKEEAEA-ALAEYEEKLAEARAEAAeiIAEARKEAEaiaEEAKAEAEAEA-ERIIAQAEAeieQERAKALAELRAE 119
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1674-1817 |
2.15e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.66 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1674 ERAREQAQKGAQERAREQAQKG-AQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERaqEQG 1752
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARKRlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQK--REG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2033470018 1753 REQTHIEAQGQAQKGAQEWARDRARdqgweqtqiETQRQTQKGAQERAWEQGREQALTSGMAPRA 1817
Cdd:PRK07735 82 TEEVTEEEKAKAKAKAAAAAKAKAA---------ALAKQKREGTEEVTEEEKAAAKAKAAAAAKA 137
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1628-1785 |
2.19e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 43.05 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKGAQERVQGQAQKGAQE--RAQEQAQEqtqiEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQ 1705
Cdd:pfam13779 592 GQPQQQQQQGQSEMQQAMDELGDllREQQQLLD----ETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQ 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1706 KGAQERAREQAQKGA--------QERAREQAQKGAQE---RArEQAQKGAqERAQEQGREQTHIEAQGQA----QKGAQE 1770
Cdd:pfam13779 668 GGAEALGDLAERQQAlrrrleelQDELKELGGKEPGQalgDA-GRAMRDA-EEALGQGDLAGAVDAQGRAlealRKGAQQ 745
|
170
....*....|....*
gi 2033470018 1771 WARDRARDQGWEQTQ 1785
Cdd:pfam13779 746 LAEAMQQQQGQGQQP 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1662-1771 |
2.52e-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: 42.44 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1662 IEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQ 1741
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
90 100 110
....*....|....*....|....*....|
gi 2033470018 1742 KGAQERAQEQGREQTHIEAQGQAQKGAQEW 1771
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| AhaH |
TIGR02926 |
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ... |
1687-1767 |
2.53e-03 |
|
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.
Pssm-ID: 131972 [Multi-domain] Cd Length: 85 Bit Score: 38.67 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1687 RAREQAQKGAQErAREQAQKGAQErAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQAQK 1766
Cdd:TIGR02926 6 KAEEDAEELIEE-AEEERKQRIAE-AREEARE-LLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEIEAMKSKAK 82
|
.
gi 2033470018 1767 G 1767
Cdd:TIGR02926 83 E 83
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1552-1754 |
2.55e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.97 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1552 AQEQAQWQTQIEAQGQAQEPAQGGAQGQVQGQAQKWAQGQIQGQAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQ 1631
Cdd:PRK12678 73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1632 TQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREqAQKGAQERAREQAQKGAQERAREQAQKGAQER 1711
Cdd:PRK12678 153 ATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRD-GDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2033470018 1712 AREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGRE 1754
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGR 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1480-1724 |
2.86e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1480 GSPAAQGQAQKQVQEwdrgQVQGHAQEQAQWQTQIEAQGQAQEQAQggtqghsqgQAQKQFQNWAQGQAqghaqeqaqwq 1559
Cdd:PRK09510 73 SAKRAEEQRKKKEQQ----QAEELQQKQAAEQERLKQLEKERLAAQ---------EQKKQAEEAAKQAA----------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1560 tqiEAQGQAQEpaqggaqgqvqgqaqkwaqgqiqgqaQKQVQGEVQKWAQEEAQGQAQwqtqiKAQKWAQEQTQKGAQER 1639
Cdd:PRK09510 129 ---LKQKQAEE--------------------------AAAKAAAAAKAKAEAEAKRAA-----AAAKKAAAEAKKKAEAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1640 VQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQErAREQAQKGAQERAREQAQKG 1719
Cdd:PRK09510 175 AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAE-AKAAAEKAAAAKAAEKAAAA 253
|
....*
gi 2033470018 1720 AQERA 1724
Cdd:PRK09510 254 KAAAE 258
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1698-1779 |
3.44e-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: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1698 ERAREQAQKgAQERAREQ---AQKGAQE---RAREQAQKgAQERAREQAQKGAqERAQEQGREQthIEAQGQAqkgaqew 1771
Cdd:cd06503 43 EKAKEEAEE-LLAEYEEKlaeARAEAQEiieEARKEAEK-IKEEILAEAKEEA-ERILEQAKAE--IEQEKEK------- 110
|
....*...
gi 2033470018 1772 ARDRARDQ 1779
Cdd:cd06503 111 ALAELRKE 118
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1672-1817 |
3.51e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1672 AQERA---REQAQKgAQERAREQAqkgaqERAREQAQKGAqERAREQAQKGAQERaREQAQKGAQERAREQAQKGAQERA 1748
Cdd:NF041483 511 AIERAttlRRQAEE-TLERTRAEA-----ERLRAEAEEQA-EEVRAAAERAAREL-REETERAIAARQAEAAEELTRLHT 582
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2033470018 1749 QEQGR----EQTHIEAQGQAQKGAQEWAR--DRARDQGWEQTqietqRQTQKGAQERAwEQGREQALTSGMAPRA 1817
Cdd:NF041483 583 EAEERltaaEEALADARAEAERIRREAAEetERLRTEAAERI-----RTLQAQAEQEA-ERLRTEAAADASAARA 651
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
656-841 |
4.17e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 656 PPSARETGPSGNKAVGKGPLEEEPQRQPRPSKPVTPQVMAQRDGHAVPSLAFSCAPCTGGVLPGLVPASSPLGPASPWGT 735
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 736 GSAGGDGTADPTAESTAGGVQEVRGARLTWPPGPPGECAGEGPEITMTVCSSEDEREGAGFPDPGRD-PLFATQKYFPeq 814
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPvPLPPEPDDPP-- 749
|
170 180
....*....|....*....|....*..
gi 2033470018 815 kVPEHIPPLNAPSVQAARRTQPATEPP 841
Cdd:PRK07764 750 -DPAGAPAQPPPPPAPAPAAAPAAAPP 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1628-1799 |
4.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQ-AQKGAQERAREQAQK 1706
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAElERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1707 GAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGREQTHIEAQGQA-QKGAQEWARDRARDQGWEQTQ 1785
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAlRAEAAALLEALEEELEALEEA 406
|
170
....*....|....
gi 2033470018 1786 IETQRQTQKGAQER 1799
Cdd:COG4913 407 LAEAEAALRDLRRE 420
|
|
| 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 ... |
1664-1745 |
4.38e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 39.22 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1664 AQGQAQKGAQERAREQAQKGAQErAREQAQKGAqERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAR--EQAQ 1741
Cdd:pfam00430 47 KDAAAALAEAEQQLKEARAEAQE-IIENAKKRA-EKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQvvALAV 124
|
....
gi 2033470018 1742 KGAQ 1745
Cdd:pfam00430 125 QIAE 128
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1663-1805 |
4.48e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.25 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKgAQERAREQAQK 1742
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQI-DLARRRVLAPI 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033470018 1743 GA--QERAQEQGREQT--------HIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGR 1805
Cdd:pfam00529 136 GGisRESLVTAGALVAqaqanllaTVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1672-1813 |
4.54e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.90 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1672 AQERAREQAQKGA--QERAR-----------------EQAQKGAQERAREQAQKGAQ----------ERAREQAQKGAQE 1722
Cdd:pfam13779 494 AQERLSEALERGAsdEEIAKlmqelrealddymqalaEQAQQNPQDLQQPDDPNAQEmtqqdlqrmlDRIEELARSGRRA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1723 RARE-----------------QAQKGAQERAREQAQKGAQE--RAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQ 1783
Cdd:pfam13779 574 EAQQmlsqlqqmlenlqagqpQQQQQQGQSEMQQAMDELGDllREQQQLLDETFRQLQQQGGQQQGQPGQQGQQGQGQQP 653
|
170 180 190
....*....|....*....|....*....|....
gi 2033470018 1784 TQIETQRQTQKGAQERAWEQG----REQALTSGM 1813
Cdd:pfam13779 654 GQGGQQPGAQMPPQGGAEALGdlaeRQQALRRRL 687
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1663-1745 |
4.62e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQ-ERAREQAQKGAQERAREQAQ 1741
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQlEQLQEKAAETSQERKQKRKE 220
|
....
gi 2033470018 1742 KGAQ 1745
Cdd:PRK11448 221 ITDQ 224
|
|
| Glutenin_hmw |
pfam03157 |
High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
1332-1764 |
5.64e-03 |
|
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.
Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 41.86 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1332 QRGPPHLQAHLPPTAGDTQAKLRASVPEPRTQAGESQERPLTQADLGRQQSHQAQEETPQPGDAGKRVA----PSGSKVV 1407
Cdd:pfam03157 349 QGQPGYYPTSPQQPGQGQPGYYPTSQQQPQQGQQPEQGQQGQQQGQGQQGQQPGQGQQPGQGQPGYYPTspqqSGQGQPG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1408 LNPAKEPQTWWAQDLAGDKGMAIGVGGACQRSDQGQQHLQGPWEERGRSTAWGEgtraarnPAVPPGEPEGPGspaaQGQ 1487
Cdd:pfam03157 429 YYPTSPQQSGQGQQPGQGQQPGQEQPGQGQQPGQGQQGQQPGQPEQGQQPGQGQ-------PGYYPTSPQQSG----QGQ 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1488 AQKQVQEWDRGQvQGHAQEQAQWQTQieaqgQAQEQAQGGTQGHSQGQAQKQFQNWAQGQaQGHAQEQAQwQTQIEAQGQ 1567
Cdd:pfam03157 498 QLGQWQQQGQGQ-PGYYPTSPLQPGQ-----GQPGYYPTSPQQPGQGQQLGQLQQPTQGQ-QGQQSGQGQ-QGQQPGQGQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1568 AQEPAQGGAQGQVQGQAQKwaqgqiqgqAQKQVQGEVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKGAQervQGQAQKG 1647
Cdd:pfam03157 570 QGQQPGQGQQGQQPGQGQQ---------PGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQ---LGQGQQG 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1648 AQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQ 1727
Cdd:pfam03157 638 YYPTSPQQPGQGQQPGQWQQSGQGQQGYYPTSPQQSGQAQQPGQGQQPGQWLQPGQGQQGYYPTSPQQPGQGQQLGQGQQ 717
|
410 420 430
....*....|....*....|....*....|....*...
gi 2033470018 1728 AQKGAQERAREQAQKGAQERAQEQGREQT-HIEAQGQA 1764
Cdd:pfam03157 718 SGQGQQGYYPTSPGQGQQSGQGQQGYDSPyHVSAEHQA 755
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
1616-1734 |
5.69e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 39.56 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1616 AQWQTQIKAQKWAQEQTQKGAQErvqgqAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERArEQAQKGAQERAREQAQKG 1695
Cdd:pfam16535 28 AAWKAMQEAQQQKGLELSDEFQT-----ALSEAEEATDAYEKAINKLKNAKSKAKAAEKKI-DQAQTRLQSLAPDSPGKA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2033470018 1696 AQERAREQAQKGAQE-RAREQAQKG--AQERAREQAQKGAQE 1734
Cdd:pfam16535 102 KLEAAEQQAGIKKDAlQADRTLDKAldAASKLTTKAMAKEKE 143
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1686-1807 |
5.99e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.18 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1686 ERAREQAQKGA----QERAREQAQKGAQERAREQAQkgAQERAREQAQKGAQERAREQAQkgaQERAQEQGREQTHIEAQ 1761
Cdd:pfam15558 21 QRMRELQQQAAlaweELRRRDQKRQETLERERRLLL--QQSQEQWQAEKEQRKARLGREE---RRRADRREKQVIEKESR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2033470018 1762 GQAQKGAQEWARDRARDQGWEQTQIETQRQTQK-GAQERAWEQGREQ 1807
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEQRKQCQEQRlKEKEEELQALREQ 142
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1609-1755 |
6.11e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1609 QEEAQGQAQWQTQIKAQKWAQEQTQKgAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQkgAQERAREQAQKGAQERA 1688
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERK-ERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRK 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033470018 1689 REQAQKGAQERAREQAQKGAQERA--REQAQKGAQERAREQAQKgAQERAREQAQKGAQERAQEQGREQ 1755
Cdd:pfam13868 270 QAEDEEIEQEEAEKRRMKRLEHRRelEKQIEEREEQRAAEREEE-LEEGERLREEEAERRERIEEERQK 337
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1663-1748 |
6.17e-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: 39.39 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQ---KGAQERAREQAQKgAQERAREQAqkgaqERAREQAQKgAQERAREQAQKGAQERAREQAQKGAQERAREQ 1739
Cdd:COG0711 63 EARAEAAeiiAEARKEAEAIAEE-AKAEAEAEA-----ERIIAQAEA-EIEQERAKALAELRAEVADLAVAIAEKILGKE 135
|
....*....
gi 2033470018 1740 AQKGAQERA 1748
Cdd:COG0711 136 LDAAAQAAL 144
|
|
| PHA00671 |
PHA00671 |
hypothetical protein |
1685-1769 |
6.40e-03 |
|
hypothetical protein
Pssm-ID: 106979 [Multi-domain] Cd Length: 135 Bit Score: 38.87 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1685 QERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREqAQKGAQERAQEQGREQTHIEAQGQA 1764
Cdd:PHA00671 26 QEKAQRSAQQQAQQQAQQQADQAKAESDRLTQEYQKQTEAYQQQAKIMQQQLLD-SQQSFNRANQKQPNSQRALSAVGSA 104
|
....*
gi 2033470018 1765 QKGAQ 1769
Cdd:PHA00671 105 AKSGQ 109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1603-1843 |
6.74e-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: 40.90 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQWQTQIKAQKWAQEQTQKgaQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGA-QERAREQAQ 1681
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALAR--RIRALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1682 KGAQERARE--QAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAQEQGR-EQTHI 1758
Cdd:COG4942 116 LGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAlEALKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1759 EAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPISG-------------- 1824
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSGrvvrrfgerdgggg 275
|
250 260
....*....|....*....|
gi 2033470018 1825 IAEGVDAAGRSGGS-RSPAP 1843
Cdd:COG4942 276 RNKGIDIAAPPGAPvRAVAD 295
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1628-1787 |
7.67e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1628 AQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtqiEAQGQAQKgAQERAREQAQKGAQERARE---QAQKGAQERAREQA 1704
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLE--------QQTEQAKK-LEEKAQAALTKGNEELAREalaEKKSLEKQAEALET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1705 QKGAQERAREQAQKGAQERAREQAQKGAQER---AREQAQKGAQERAQEQG------------REQTHIEAQGQAQKGAQ 1769
Cdd:pfam04012 105 QLAQQRSAVEQLRKQLAALETKIQQLKAKKNllkARLKAAKAQEAVQTSLGslstssatdsfeRIEEKIEEREARADAAA 184
|
170
....*....|....*...
gi 2033470018 1770 EWARDRARDQGWEQTQIE 1787
Cdd:pfam04012 185 ELASAVDLDAKLEQAGIQ 202
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1663-1882 |
7.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1663 EAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQK 1742
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1743 GAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAWEQPI 1822
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGA 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1823 SGIAEGVDAAGRSGGSRSPAPRDGGQSGGSGLGEPSAGYPPPGSRPLRGKSIATSPLGLG 1882
Cdd:COG3883 311 GGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLS 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1659-1862 |
7.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1659 QTQIEAQGQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERAREQAQKGAQERARE 1738
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1739 QAQKGAQERAQEQGREQTHIEAQGQAQKGAQEWARDRARDQGWEQTQIETQRQTQKGAQERAWEQGREQALTSGMAPRAW 1818
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASG 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2033470018 1819 EQPISGIAEGVDAAGRSGGSRSPAPRDGGQSGGSGLGEPSAGYP 1862
Cdd:COG3883 302 GSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGS 345
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1603-1756 |
9.34e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1603 EVQKWAQEEAQGQAQwqTQIKAQKWAQEQTQKGAQERVQGQAQKGAQERAQEqaqeqtqIEAQGQAQKGA---QERAREQ 1679
Cdd:pfam17380 447 EMERVRLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-------LEKELEERKQAmieEERKRKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1680 AQKGAQER----AREQAQKGAQERAREQAQkgAQERAR--EQAQKGAQERAREQaqkgAQERAREQAQKGAQERAQEQGR 1753
Cdd:pfam17380 518 LEKEMEERqkaiYEEERRREAEEERRKQQE--MEERRRiqEQMRKATEERSRLE----AMEREREMMRQIVESEKARAEY 591
|
...
gi 2033470018 1754 EQT 1756
Cdd:pfam17380 592 EAT 594
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1629-1758 |
9.50e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.00 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033470018 1629 QEQTQKGAQERVQGQAQKGAQERAQEQAQEQTQIEAQGQAQKGAQERAREQAQKgaqerAREQAqKGAQERAREQAqkga 1708
Cdd:PRK06669 32 IKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLK-----KTDEA-SSIIEKLQMQI---- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2033470018 1709 qERAREQAQKgAQERAREQA-QKGAQErAREQAQKGAQERAQEQGREQTHI 1758
Cdd:PRK06669 102 -EREQEEWEE-ELERLIEEAkAEGYEE-GYEKGREEGLEEVRELIEQLNKI 149
|
|
| |
