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Conserved domains on  [gi|30265443|ref|NP_847820.1|]
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methyl-accepting chemotaxis protein [Bacillus anthracis str. Ames]

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List of domain hits

Name Accession Description Interval E-value
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
35-181 8.00e-45

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


:

Pssm-ID: 271268  Cd Length: 148  Bit Score: 154.25  E-value: 8.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  35 LKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDFI 114
Cdd:cd01068   1 LEERLEFLGLDEEDLALLRELRPLIEAHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELFSGDFDEAYV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265443 115 EQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKI-TTIDDFSYSINVINKLFTLEQELVIAAY 181
Cdd:cd01068  81 ERRLRIGKVHVRIGLEPRWYIGAYALLLEELIEAIAEELrPDPEELAEALLALVKALNLDMQLALEAY 148
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
222-410 2.71e-44

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.


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 154.70  E-value: 2.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 222 QQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIITDTHELLDISNKINEIIDIVKSIAEQT 301
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 302 NLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSMSATDQY 381
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180
                ....*....|....*....|....*....
gi 30265443 382 FQEIVKDMSNSKEQNKKIENELETISQVM 410
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSAST 189
 
Name Accession Description Interval E-value
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
35-181 8.00e-45

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 271268  Cd Length: 148  Bit Score: 154.25  E-value: 8.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  35 LKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDFI 114
Cdd:cd01068   1 LEERLEFLGLDEEDLALLRELRPLIEAHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELFSGDFDEAYV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265443 115 EQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKI-TTIDDFSYSINVINKLFTLEQELVIAAY 181
Cdd:cd01068  81 ERRLRIGKVHVRIGLEPRWYIGAYALLLEELIEAIAEELrPDPEELAEALLALVKALNLDMQLALEAY 148
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
222-410 2.71e-44

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  Cd Length: 200  Bit Score: 154.70  E-value: 2.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 222 QQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIITDTHELLDISNKINEIIDIVKSIAEQT 301
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 302 NLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSMSATDQY 381
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180
                ....*....|....*....|....*....
gi 30265443 382 FQEIVKDMSNSKEQNKKIENELETISQVM 410
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSAST 189
Protoglobin pfam11563
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ...
33-187 4.16e-43

Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain.


Pssm-ID: 256506  Cd Length: 156  Bit Score: 150.04  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    33 SELKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHED 112
Cdd:pfam11563   1 ARLEYRLRFLGLTEEDLAALRALRPLIEPHIPAILDRFYEKLLSHPETARIFTDESQIERLKKTLRAYLLELFSGPYDEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30265443   113 FIEQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKIT-TIDDFSYSINVINKLFTLEQELVIAAYESKYER 187
Cdd:pfam11563  81 YVEYRLRIGLVHVRIGLEPRWYIAAYAVVLESLLEALLEKIRlSAAELTALVRALSKLINLDQDLVLSAYEEELEE 156
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
199-428 7.23e-39

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: 141.65  E-value: 7.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    199 TSMTITHIATELASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIITDTH 278
Cdd:smart00283   5 AVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    279 ELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVS 358
Cdd:smart00283  85 ELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30265443    359 SSVKQISSLVSEGTDSMSATDQYFQEIVKDMSNSKEQNKKIENELE----TISQVMKGIQDDSSKMALTADSLQ 428
Cdd:smart00283 165 AAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDeqaaGSEEVNAAIDEIAQVTQETAAMSE 238
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
199-427 2.33e-34

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 132.04  E-value: 2.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 199 TSMTITHIATELASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIItdtH 278
Cdd:COG0840 153 SATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVV---K 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 279 ELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVS 358
Cdd:COG0840 230 KLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAV 309
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30265443 359 SSVKQISSLVSEGTDSMSATDQYFQEIVKDMSNSKEQNKKIENELETISQVMKGIQDDSSKMALTADSL 427
Cdd:COG0840 310 EHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQEN 378
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
239-421 1.07e-26

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 105.99  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443   239 TSLATTSEEKANKGKEQLNQQNKRMEYIqanmetiitdTHELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEF 318
Cdd:pfam00015   4 SDLAQLASEEALDEMSQIGQVVDDAVET----------MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443   319 GKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSMSATDQYFQEIV----------KD 388
Cdd:pfam00015  74 GRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVdavaeiadivQE 153
                         170       180       190
                  ....*....|....*....|....*....|...
gi 30265443   389 MSNSKEQNKKIENELETISQVMKGIQDDSSKMA 421
Cdd:pfam00015 154 IAAASDEQSAGIDQVNQAVARIDQVTQQNAALV 186
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
216-418 1.95e-25

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 107.08  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  216 KTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANmetiitdthelldiSNKINEIIDIVK 295
Cdd:PRK09793 300 QTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATS--------------SQKIGDIISVID 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  296 SIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSM 375
Cdd:PRK09793 366 GIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSV 445
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30265443  376 SATDQYFQEIVkdmSNSKEQNKKIENELETISQVMKGIQDDSS 418
Cdd:PRK09793 446 TRVNDIMGEIA---SASEEQRRGIEQVAQAVSQMDQVTQQNAS 485
46 PHA02562
endonuclease subunit; Provisional
147-364 6.44e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  147 KILKTKI----TTIDDFSYSINVIN------KLFTLEQELVIAAYESKYERMQKELEKEKEITSMTITHIATELASVS-- 214
Cdd:PHA02562 170 KLNKDKIrelnQQIQTLDMKIDHIQqqiktyNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmd 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  215 -EKTSASIQQLTAKsetiveIAKTGTSLATTSEEKA--NKG------KEQLNQQNKRMEYIQANMETIitdTHELLDISN 285
Cdd:PHA02562 250 iEDPSAALNKLNTA------AAKIKSKIEQFQKVIKmyEKGgvcptcTQQISEGPDRITKIKDKLKEL---QHSLEKLDT 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  286 KINEIIDIVKSIAEQT-NLLALNAAIESARAGEFGKGFSV--VAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVK 362
Cdd:PHA02562 321 AIDELEEIMDEFNEQSkKLLELKNKISTNKQSLITLVDKAkkVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400

                 ..
gi 30265443  363 QI 364
Cdd:PHA02562 401 EK 402
 
Name Accession Description Interval E-value
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
35-181 8.00e-45

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 271268  Cd Length: 148  Bit Score: 154.25  E-value: 8.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  35 LKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDFI 114
Cdd:cd01068   1 LEERLEFLGLDEEDLALLRELRPLIEAHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELFSGDFDEAYV 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265443 115 EQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKI-TTIDDFSYSINVINKLFTLEQELVIAAY 181
Cdd:cd01068  81 ERRLRIGKVHVRIGLEPRWYIGAYALLLEELIEAIAEELrPDPEELAEALLALVKALNLDMQLALEAY 148
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
222-410 2.71e-44

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  Cd Length: 200  Bit Score: 154.70  E-value: 2.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 222 QQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIITDTHELLDISNKINEIIDIVKSIAEQT 301
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 302 NLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSMSATDQY 381
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180
                ....*....|....*....|....*....
gi 30265443 382 FQEIVKDMSNSKEQNKKIENELETISQVM 410
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSAST 189
Protoglobin pfam11563
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ...
33-187 4.16e-43

Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain.


Pssm-ID: 256506  Cd Length: 156  Bit Score: 150.04  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    33 SELKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHED 112
Cdd:pfam11563   1 ARLEYRLRFLGLTEEDLAALRALRPLIEPHIPAILDRFYEKLLSHPETARIFTDESQIERLKKTLRAYLLELFSGPYDEA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30265443   113 FIEQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKIT-TIDDFSYSINVINKLFTLEQELVIAAYESKYER 187
Cdd:pfam11563  81 YVEYRLRIGLVHVRIGLEPRWYIAAYAVVLESLLEALLEKIRlSAAELTALVRALSKLINLDQDLVLSAYEEELEE 156
GS_GGDEF_1 cd14758
Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup; ...
34-181 2.42e-12

Globin sensor domain, coupled to DGC/GGDEF domains; uncharacterized subgroup; Globin-coupled-sensors belonging to this subfamily have a sensor domain coupled to a C-terminal diguanylate cyclase (DGC/GGDEF) domain. DGC/GGDEF likely functions as a c-di-GMP cyclase in the synthesis of the second messenger cyclic-di-GMP (c-di-GMP).


Pssm-ID: 271291  Cd Length: 148  Bit Score: 63.81  E-value: 2.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  34 ELKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDF 113
Cdd:cd14758   1 EIERRKELLGLTEEDVAALRSLKPLIEPNLDDIVEEFYDHQTSVPEIALLIGDADTLQRLKNAQRRYILDLFSGLYDLEY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30265443 114 IEQRVKIAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKITTIDDFSYSINVINKLFTLEQELVIAAY 181
Cdd:cd14758  81 VNNRLRIGLVHKRIGVEPKLYLSAINTLKELLREIITEQIEDCQECDRILEALEKLMLFDLTLVFDTY 148
GS_STAS cd14762
Globin sensor domain; coupled to a STAS domain; Globin-coupled-sensors in this subfamily have ...
44-152 9.80e-10

Globin sensor domain; coupled to a STAS domain; Globin-coupled-sensors in this subfamily have a C-terminal sulphate transporter and anti-sigma factor antagonist (STAT) domain coupled to the globin sensor domain.


Pssm-ID: 271295  Cd Length: 143  Bit Score: 56.14  E-value: 9.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  44 ISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLitiiERYSSIPKLKQTLKTHI---KELFSGDMHEDFIEQRVKI 120
Cdd:cd14762  10 ISEEDLELIRSAGEQILPRLDEIFDEFYDWLRSQPEY----EEYFSEEVIQRLKRLQDaywEDFLSGRVDDAYIERRRRI 85
                        90       100       110
                ....*....|....*....|....*....|....*
gi 30265443 121 AKRHVQIGLHRKWYTAA---YQELFRSIMKILKTK 152
Cdd:cd14762  86 GEVHARIGLPLEAYFAGmnaFHELFEEAFMRLGLA 120
GS_PAS-GGDEF-EAL cd14760
Globin sensor domain; coupled to PAS, DGC/GGDEF and EAL domains; In addition to the N-terminal ...
40-181 2.92e-09

Globin sensor domain; coupled to PAS, DGC/GGDEF and EAL domains; In addition to the N-terminal sensing domain, globin-coupled-sensors in this bacterial subfamily have a signal-sensing PAS domain, and diguanylate cyclase (DGC/GGDEF) and EAL domains. The latter two domains are involved in the synthesis and degradation of c-di-GMP, respectively, and may be involved in regulating cell surface adhesiveness, and in the transition between planktonic and biofilm growth modes.


Pssm-ID: 271293  Cd Length: 148  Bit Score: 54.71  E-value: 2.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  40 DMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDFIEQRVK 119
Cdd:cd14760   6 AFLGFTEADASRLRALHAALSSFSPTFADSFYAHLLSFEETRRFLPDEDTLERLQRAQTAYFDSLTAGRYDSDYIRERLR 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30265443 120 IAKRHVQIGLHRKWYTAAYQELFRSIMKILKTKIT-TIDDFSYSINVINKLFTLEQELVIAAY 181
Cdd:cd14760  86 VGLTHQRIGLSPQWYLGAYVKYLSDLLPEIRQLLGaDPDEFIAALQSLLKVVMLDMGLALDTY 148
SSDgbs_1 cd14763
Sensor single-domain globins; uncharacterized bacterial subgroup; This subfamily of sensor ...
35-129 2.56e-08

Sensor single-domain globins; uncharacterized bacterial subgroup; This subfamily of sensor single-domain globins, belongs to a family that includes GCSs (globin-coupled-sensors) and single-domain protoglobins (Pgbs). For GCSs, an N-terminal heme-bound oxygen-sensing/binding globin domain is coupled to a C-terminal functional/signaling domain. The first signal O2 binds to/dissociates from the heme in its sensor domain inducing a conformational change in that domain and ultimately in the signaling domain. It has been demonstrated that the Pgbs and other single domain globins can function as sensors, when coupled to an appropriate regulatory domain.


Pssm-ID: 271296  Cd Length: 142  Bit Score: 51.92  E-value: 2.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  35 LKVQMDMLHISKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSsIPKLKQTLKTHIKELFSGDMHEDFI 114
Cdd:cd14763   1 LEELVRRTGLTPEDAALLGSLAPWAKAIAPEMADAFYDRLGRDPETAEILADVP-VERLYETFAGWFRELFSGVYDEAYA 79
                        90
                ....*....|....*
gi 30265443 115 EQRVKIAKRHVQIGL 129
Cdd:cd14763  80 ERRLRIGLVHVRIGL 94
GS_GsGCS_like cd14761
Globin sensor domain of Geobacter sulfurreducens globin-coupled-sensor and related proteins; ...
45-149 1.72e-07

Globin sensor domain of Geobacter sulfurreducens globin-coupled-sensor and related proteins; GsGCS is a GCS of unknown function, comprised of an N-terminal globin sensor domain and a C- terminal transmembrane signal-transduction domain. For GCSs in general, the first signal O2 binds to/dissociates from the heme iron complex inducing a structural change in the globin domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Ferric GsGCS is bis-histidyl hexa-coordinated (provided by a His residue located at the E11 topological site, as distinct from the E7 site). Ferrous GsGCS is a penta- and hexa-coordinated mixture. The C-terminal domains of other members of this subfamily include histidine kinase, and PsiE domains.


Pssm-ID: 271294  Cd Length: 149  Bit Score: 49.18  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  45 SKEDLQIVKVLQPFIYEEIDWITEKFYANITKQPNLITIIERYSSIPKLKQTLKTHIKELFSGDMHEDFIEQRVKIAKRH 124
Cdd:cd14761  13 TEEDAENLKSLKPLAEKYKDDFVDDFYEYLFKFPDTAKFLKDEKVIKRHKEKLKVWFLSLFSGKYDNEYLSKLQRIGQAH 92
                        90       100
                ....*....|....*....|....*
gi 30265443 125 VQIGLHRKWYTAAYQELFRSIMKIL 149
Cdd:cd14761  93 VRIGLPTHYVNAAMNFVRRFIHEKI 117
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
199-428 7.23e-39

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: 141.65  E-value: 7.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    199 TSMTITHIATELASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIITDTH 278
Cdd:smart00283   5 AVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443    279 ELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVS 358
Cdd:smart00283  85 ELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAV 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30265443    359 SSVKQISSLVSEGTDSMSATDQYFQEIVKDMSNSKEQNKKIENELE----TISQVMKGIQDDSSKMALTADSLQ 428
Cdd:smart00283 165 AAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDeqaaGSEEVNAAIDEIAQVTQETAAMSE 238
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
199-427 2.33e-34

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 132.04  E-value: 2.33e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 199 TSMTITHIATELASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANMETIItdtH 278
Cdd:COG0840 153 SATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVV---K 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 279 ELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVS 358
Cdd:COG0840 230 KLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAV 309
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30265443 359 SSVKQISSLVSEGTDSMSATDQYFQEIVKDMSNSKEQNKKIENELETISQVMKGIQDDSSKMALTADSL 427
Cdd:COG0840 310 EHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQEN 378
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
239-421 1.07e-26

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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 105.99  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443   239 TSLATTSEEKANKGKEQLNQQNKRMEYIqanmetiitdTHELLDISNKINEIIDIVKSIAEQTNLLALNAAIESARAGEF 318
Cdd:pfam00015   4 SDLAQLASEEALDEMSQIGQVVDDAVET----------MEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443   319 GKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSMSATDQYFQEIV----------KD 388
Cdd:pfam00015  74 GRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVdavaeiadivQE 153
                         170       180       190
                  ....*....|....*....|....*....|...
gi 30265443   389 MSNSKEQNKKIENELETISQVMKGIQDDSSKMA 421
Cdd:pfam00015 154 IAAASDEQSAGIDQVNQAVARIDQVTQQNAALV 186
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
216-418 1.95e-25

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 107.08  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  216 KTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMEYIQANmetiitdthelldiSNKINEIIDIVK 295
Cdd:PRK09793 300 QTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATS--------------SQKIGDIISVID 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  296 SIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVKQISSLVSEGTDSM 375
Cdd:PRK09793 366 GIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSV 445
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30265443  376 SATDQYFQEIVkdmSNSKEQNKKIENELETISQVMKGIQDDSS 418
Cdd:PRK09793 446 TRVNDIMGEIA---SASEEQRRGIEQVAQAVSQMDQVTQQNAS 485
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
211-418 6.61e-24

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 102.78  E-value: 6.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  211 ASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGKEQLNQQNKRMeyiqanmetiitdtHELLDISNKINEI 290
Cdd:PRK15048 297 ASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTM--------------HEIADSSKKIADI 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  291 IDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEktnEQIIRVSSSVKQISSLVSE 370
Cdd:PRK15048 363 ISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE---DSVSRVDTGSVLVESAGET 439
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30265443  371 GTDSMSATDQYFQEIVKDMSNSKEQNKKIENELETISQVMKGIQDDSS 418
Cdd:PRK15048 440 MNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNAS 487
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
209-402 3.42e-22

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 97.72  E-value: 3.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  209 ELASVSEKTSASIQQLTAKSETIVEIAKTGTSLATTSEEKANKGkeqlnqqNKRMEYIQANMETIITDthelldiSNKIN 288
Cdd:PRK15041 297 QQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRG-------GKVVDNVVQTMRDISTS-------SQKIA 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  289 EIIDIVKSIAEQTNLLALNAAIESARAGEFGKGFSVVAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVK------ 362
Cdd:PRK15041 363 DIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVEsagetm 442
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30265443  363 -QISSLVSEGTDSM----SATDQYFQEI------VKDMSNSKEQNKKIENE 402
Cdd:PRK15041 443 aEIVSAVTRVTDIMgeiaSASDEQSRGIdqvglaVAEMDRVTQQNAALVEE 493
46 PHA02562
endonuclease subunit; Provisional
147-364 6.44e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  147 KILKTKI----TTIDDFSYSINVIN------KLFTLEQELVIAAYESKYERMQKELEKEKEITSMTITHIATELASVS-- 214
Cdd:PHA02562 170 KLNKDKIrelnQQIQTLDMKIDHIQqqiktyNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVmd 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  215 -EKTSASIQQLTAKsetiveIAKTGTSLATTSEEKA--NKG------KEQLNQQNKRMEYIQANMETIitdTHELLDISN 285
Cdd:PHA02562 250 iEDPSAALNKLNTA------AAKIKSKIEQFQKVIKmyEKGgvcptcTQQISEGPDRITKIKDKLKEL---QHSLEKLDT 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443  286 KINEIIDIVKSIAEQT-NLLALNAAIESARAGEFGKGFSV--VAGEIRKLSEQTKESIFNVTKLVEKTNEQIIRVSSSVK 362
Cdd:PHA02562 321 AIDELEEIMDEFNEQSkKLLELKNKISTNKQSLITLVDKAkkVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400

                 ..
gi 30265443  363 QI 364
Cdd:PHA02562 401 EK 402
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
202-433 6.96e-03

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 37.48  E-value: 6.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 202 TITHIATELASVSEKtsasIQQLTAKSETIVEIAK---TGTSLATTSEEKANKGKEQLNQQNKRMeyiQANMETIITDTH 278
Cdd:COG1511 235 GLNQLDSGLGTLAAG----IGELKQGAEQLNEGIGefsSGLSELNSGVQDLAAGVPQLNQGISAL---AAGLSLPDSLGD 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 279 ELLDISNKINEIIDIVKSIAEQTNLLALNA--AIESARAGEFGKGFSVVAGEIRKLSEQTKESIF-----NVTKLVEKTN 351
Cdd:COG1511 308 QFSSLQEALTQIAQGLKQKTSSSLEAAQGSlsSLQSMLALSKSLDLTAEGATVDALGAPDGVQWLdesqkTLATLSELLS 387
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30265443 352 EQIIRVSSsvkqISSLVSEGTDSMSATDQYFQEIVKDMSNSKEQNKKIENELETISQVMKGIQ-DDSSKMALTADSLQLE 430
Cdd:COG1511 388 TGIDGVSE----GLDALEQASAQLAKSLAKLKTAVAQIAASIAQLLPGASEVLKTLKSKGLDKlLNQLNGALAKGSNALV 463

                ...
gi 30265443 431 LNR 433
Cdd:COG1511 464 QGL 466
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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