|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
165-502 |
8.37e-78 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 253.40 E-value: 8.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 165 ARGVMTLMFILLAAMLWFVAAPVVTYILCALVVLLASACFEWQIVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLR 244
Cdd:COG0840 163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 245 AVGQLGLMCRWLINDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITAS 324
Cdd:COG0840 243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 325 NAAVQGGEAMTTVI--------------KTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVA 390
Cdd:COG0840 323 ELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 391 GEVRHLASRSANAANDIRKLIDAS--------------ADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQ 456
Cdd:COG0840 403 DEVRKLAERSAEATKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16130967 457 ADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAV 502
Cdd:COG0840 483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELV 528
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
259-506 |
1.78e-77 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 243.73 E-value: 1.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 259 DVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVI 338
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 339 KTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLI------- 411
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 412 -------DASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEES 484
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 16130967 485 AQVSAMVKHRASRLEDAVTVLH 506
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
208-503 |
8.79e-74 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 243.38 E-value: 8.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 208 IVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQlglMCRWLINdvssQVSSVRNGSETLAKGTDE------- 280
Cdd:PRK15048 216 LLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSH---MQRSLTD----TVTHVREGSDAIYAGTREiaagntd 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 281 LNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLIND 360
Cdd:PRK15048 289 LSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 361 IAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVK 440
Cdd:PRK15048 369 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVT 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130967 441 NVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVT 503
Cdd:PRK15048 449 RVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVS 511
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
286-485 |
4.77e-65 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 209.40 E-value: 4.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 286 QQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQT 365
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 366 NILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQL 445
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130967 446 IAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESA 485
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
318-474 |
1.61e-44 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 154.51 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 318 KLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLA 397
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 398 SRSANAANDIRKLIDA--------------SADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSL 463
Cdd:pfam00015 82 ERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161
|
170
....*....|.
gi 16130967 464 TRAVDELNLIT 474
Cdd:pfam00015 162 NQAVARMDQVT 172
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
30-115 |
3.95e-18 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 79.30 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 30 ITHANDTFVQVSGYTLQELQG--QPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPM-VREG 106
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIrDENG 80
|
....*....
gi 16130967 107 KISGYMSIR 115
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
21-116 |
1.57e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 82.38 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAV 100
Cdd:COG2202 24 IIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103
|
90
....*....|....*..
gi 16130967 101 PMVRE-GKISGYMSIRT 116
Cdd:COG2202 104 PVRDEdGEITGFVGIAR 120
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
21-121 |
1.59e-11 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 66.47 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAV 100
Cdd:TIGR02938 17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96
|
90 100
....*....|....*....|..
gi 16130967 101 PMVRE-GKISGYMSIRTRATDE 121
Cdd:TIGR02938 97 PVLNEaGETTHFLGMHRDITEL 118
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
24-117 |
2.54e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 54.56 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 24 TDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMV 103
Cdd:cd00130 8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87
|
90
....*....|....*
gi 16130967 104 RE-GKISGYMSIRTR 117
Cdd:cd00130 88 DEgGEVIGLLGVVRD 102
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
30-119 |
4.08e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 42.90 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 30 ITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMVRE-GKI 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEdGTV 252
|
90
....*....|.
gi 16130967 109 SGYMSIRTRAT 119
Cdd:PRK13558 253 THYVGFQTDVT 263
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
80-121 |
1.11e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.78 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16130967 80 SGIVKNRRKNGDHYWVRANAVPMVRE-GKISGYMSIRTRATDE 121
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEdGEVEGILGVVRDITER 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
165-502 |
8.37e-78 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 253.40 E-value: 8.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 165 ARGVMTLMFILLAAMLWFVAAPVVTYILCALVVLLASACFEWQIVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLR 244
Cdd:COG0840 163 LAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLAD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 245 AVGQLGLMCRWLINDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITAS 324
Cdd:COG0840 243 AFNRMIENLRELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 325 NAAVQGGEAMTTVI--------------KTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVA 390
Cdd:COG0840 323 ELAEEGGEVVEEAVegieeiresveetaETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 391 GEVRHLASRSANAANDIRKLIDAS--------------ADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQ 456
Cdd:COG0840 403 DEVRKLAERSAEATKEIEELIEEIqseteeaveameegSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQ 482
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16130967 457 ADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAV 502
Cdd:COG0840 483 SAGTEEVNQAIEQIAAAAQENAASVEEVAAAAEELAELAEELQELV 528
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
259-506 |
1.78e-77 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 243.73 E-value: 1.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 259 DVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVI 338
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 339 KTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLI------- 411
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIkeiqeet 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 412 -------DASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEES 484
Cdd:smart00283 161 neavaamEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
|
250 260
....*....|....*....|..
gi 16130967 485 AQVSAMVKHRASRLEDAVTVLH 506
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
208-503 |
8.79e-74 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 243.38 E-value: 8.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 208 IVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQlglMCRWLINdvssQVSSVRNGSETLAKGTDE------- 280
Cdd:PRK15048 216 LLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSH---MQRSLTD----TVTHVREGSDAIYAGTREiaagntd 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 281 LNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLIND 360
Cdd:PRK15048 289 LSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 361 IAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVK 440
Cdd:PRK15048 369 IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVT 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130967 441 NVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVT 503
Cdd:PRK15048 449 RVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVS 511
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
210-506 |
1.25e-73 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 242.94 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 210 RPIENVAHqalkVATGE---RNSVEHLNRSDELGLTLRAVGqlGLMCRwLINDVSSQVSSVRNGSETLAKGTDELNEHTQ 286
Cdd:PRK15041 224 RLIDSIRH----IAGGDlvkPIEVDGSNEMGQLAESLRHMQ--GELMR-TVGDVRNGANAIYSGASEIATGNNDLSSRTE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 287 QTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQTN 366
Cdd:PRK15041 297 QQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTN 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 367 ILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLI 446
Cdd:PRK15041 377 ILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIM 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 447 AQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVTVLH 506
Cdd:PRK15041 457 GEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
187-505 |
2.02e-67 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 226.11 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 187 VVTYILCALVVLLASACFEWQ---IVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQLGLMCRWLINDVSSQ 263
Cdd:PRK09793 190 LVFISMIIVAAIYISSALWWTrkmIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKG 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 264 VSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDD 343
Cdd:PRK09793 270 SQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 344 IADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQ 423
Cdd:PRK09793 350 IATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 424 QVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVT 503
Cdd:PRK09793 430 LVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVA 509
|
..
gi 16130967 504 VL 505
Cdd:PRK09793 510 VF 511
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
286-485 |
4.77e-65 |
|
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 209.40 E-value: 4.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 286 QQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQT 365
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 366 NILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQL 445
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16130967 446 IAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESA 485
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
318-474 |
1.61e-44 |
|
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 154.51 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 318 KLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLA 397
Cdd:pfam00015 2 DLAQLASEEAQDGGKEVANVVGQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 398 SRSANAANDIRKLIDA--------------SADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSL 463
Cdd:pfam00015 82 ERSAQAAKEIEALIIEiqkqtndstasiesTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 161
|
170
....*....|.
gi 16130967 464 TRAVDELNLIT 474
Cdd:pfam00015 162 NQAVARMDQVT 172
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
30-115 |
3.95e-18 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 79.30 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 30 ITHANDTFVQVSGYTLQELQG--QPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPM-VREG 106
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIrDENG 80
|
....*....
gi 16130967 107 KISGYMSIR 115
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
21-116 |
1.57e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 82.38 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAV 100
Cdd:COG2202 24 IIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSIS 103
|
90
....*....|....*..
gi 16130967 101 PMVRE-GKISGYMSIRT 116
Cdd:COG2202 104 PVRDEdGEITGFVGIAR 120
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
21-121 |
1.59e-11 |
|
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]
Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 66.47 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAV 100
Cdd:TIGR02938 17 ISITDLKANILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVA 96
|
90 100
....*....|....*....|..
gi 16130967 101 PMVRE-GKISGYMSIRTRATDE 121
Cdd:TIGR02938 97 PVLNEaGETTHFLGMHRDITEL 118
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
21-114 |
5.31e-11 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 60.00 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKN-RRKNGDHYWVRANA 99
Cdd:TIGR00229 16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDGSEIWVEVSV 95
|
90
....*....|....*
gi 16130967 100 VPMVREGKISGYMSI 114
Cdd:TIGR00229 96 SPIRTNGGELGVVGI 110
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
24-117 |
2.54e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 54.56 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 24 TDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMV 103
Cdd:cd00130 8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87
|
90
....*....|....*
gi 16130967 104 RE-GKISGYMSIRTR 117
Cdd:cd00130 88 DEgGEVIGLLGVVRD 102
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
27-107 |
6.08e-07 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 47.46 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 27 QSYITHANDTFVQVSGYTLQELQGQP-HNMVRHPDmPKAAFADMWFTLKKGepWSGIVKNRRKNGDHYWVRANAVPMVRE 105
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPE-DSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
..
gi 16130967 106 GK 107
Cdd:pfam13426 78 GG 79
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
8-114 |
9.69e-07 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 51.13 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 8 TQQNTPLADDTT-LMSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNR 86
Cdd:COG5809 140 EEKFRLIFNHSPdGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFW 219
|
90 100
....*....|....*....|....*...
gi 16130967 87 RKNGDHYWVRANAVPMVREGKISGYMSI 114
Cdd:COG5809 220 TKDGRWRLLEASGAPIKKNGEVDGIVII 247
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
21-112 |
7.16e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 45.10 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGI-VKNRRKNGDHYWVRANA 99
Cdd:pfam00989 14 IFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFeVSFRVPDGRPRHVEVRA 93
|
90
....*....|....
gi 16130967 100 VPMV-REGKISGYM 112
Cdd:pfam00989 94 SPVRdAGGEILGFL 107
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
20-120 |
1.06e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 46.94 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 20 LMSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKG-EPWSGIVKNRRKNGDHYWVRAN 98
Cdd:COG2202 149 GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEAS 228
|
90 100
....*....|....*....|..
gi 16130967 99 AVPMVREGKISGYMSIRTRATD 120
Cdd:COG2202 229 AVPLRDGGEVIGVLGIVRDITE 250
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
21-114 |
4.60e-05 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 45.92 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQP-HNMVRHPDMPKAafadmwftLKKGEPWSGIVKNRRKNGDHywVRANA 99
Cdd:COG3829 24 IIVVDADGRITYVNRAAERILGLPREEVIGKNvTELIPNSPLLEV--------LKTGKPVTGVIQKTGGKGKT--VIVTA 93
|
90
....*....|....*
gi 16130967 100 VPMVREGKISGYMSI 114
Cdd:COG3829 94 IPIFEDGEVIGAVET 108
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
30-119 |
4.08e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 42.90 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 30 ITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMVRE-GKI 108
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEdGTV 252
|
90
....*....|.
gi 16130967 109 SGYMSIRTRAT 119
Cdd:PRK13558 253 THYVGFQTDVT 263
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
23-114 |
8.43e-04 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 41.76 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 23 TTDLQSYITHANDTFVQVSGYTLQELQGQP-HNMVRHPDMPKAAFADmwfTLKKGEP-WSGIVKNRRKNGDHYWVRANAV 100
Cdd:COG3852 22 VLDADGRITYVNPAAERLLGLSAEELLGRPlAELFPEDSPLRELLER---ALAEGQPvTEREVTLRRKDGEERPVDVSVS 98
|
90
....*....|....
gi 16130967 101 PMVREGKISGYMSI 114
Cdd:COG3852 99 PLRDAEGEGGVLLV 112
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
80-121 |
1.11e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.78 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16130967 80 SGIVKNRRKNGDHYWVRANAVPMVRE-GKISGYMSIRTRATDE 121
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEdGEVEGILGVVRDITER 43
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
212-503 |
1.94e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 40.77 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 212 IENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQLGLMCRWLINDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDN 291
Cdd:COG0840 36 LLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 292 VQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQTNILALN 371
Cdd:COG0840 116 LELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 372 AAVEAARAGEQGKGFAVVAGEVRHLASR------SANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQL 445
Cdd:COG0840 196 IILALLLSRSITRPLRELLEVLERIAEGdltvriDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVASASEELAAS 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130967 446 IAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVT 503
Cdd:COG0840 276 AEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVE 333
|
|
| TMP_3 |
pfam20155 |
Tape measure protein; This entry represents phage tape measure proteins that are required to ... |
258-449 |
5.24e-03 |
|
Tape measure protein; This entry represents phage tape measure proteins that are required to assemble the page tail. The protein serves as a base for tail tube protein polymerization and acts as a template for tail length determination.
Pssm-ID: 466312 [Multi-domain] Cd Length: 192 Bit Score: 38.36 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 258 NDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGG---EAM 334
Cdd:pfam20155 11 TKLQARLKLATGSAEEAAEVQQQLFDIAQRTGSSLEETAELYARLAAALKELGLSQDQVLDLTEALSKALAVSGasaEEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130967 335 TTVIKTMDDIADST--------QRIGTITSLINDIAfqtnilalnaaveaarageqgKGFAVVAGEVRHLASRSANAAND 406
Cdd:pfam20155 91 SSALLQLGQALASGklrgeefnSVLEQAPGLLQALA---------------------KGLGVSTGELRKMASDGKLTADV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16130967 407 IRKLIDASADKVQsgsQQVHAAGRTMEDIVAQVKN-VTQLIAQI 449
Cdd:pfam20155 150 FFDALLKASDELA---GEFAKMPLTIGGAFTNLKNaWTKLVGEL 190
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
21-60 |
5.92e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 35.45 E-value: 5.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16130967 21 MSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPD 60
Cdd:smart00091 14 IFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPE 53
|
|
| |
