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Conserved domains on  [gi|499386170|ref|WP_011073637|]
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bacteriohemerythrin [Shewanella oneidensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
35-383 6.38e-75

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 246.47  E-value: 6.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILIFNINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDTSEW 114
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQ 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 115 MKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTT 194
Cdd:COG0840  265 VASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRE 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 195 QIHQTKSVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQIT 274
Cdd:COG0840  345 SVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIE 424

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 275 ALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELALKNA 354
Cdd:COG0840  425 EIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENA 504

                        330       340
                 ....*....|....*....|....*....
gi 499386170 355 HHTNLTNLSSLKVYNMSQEIGSLLHRFHV 383
Cdd:COG0840  505 ASVEEVAAAAEELAELAEELQELVSRFKL 533
bact_hemeryth super family cl41411
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 398-523 2.27e-51

bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.


The actual alignment was detected with superfamily member NF033749:

Pssm-ID: 468167  Cd Length: 129  Bit Score: 171.53  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 398 FVKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAY-GLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKH 476
Cdd:NF033749   1 LITWSDELSVGIKEIDEQHKKLVDLINELHDAMKTGGkGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEH 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499386170 477 AQLVGQVLDFQKRVARGE-DVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:NF033749  81 DKLVAKVLDLQKKFEAGEaTLSIELLNFLKDWLVNHILGTDKKYGPFL 128
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
35-383 6.38e-75

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 246.47  E-value: 6.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILIFNINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDTSEW 114
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQ 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 115 MKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTT 194
Cdd:COG0840  265 VASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRE 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 195 QIHQTKSVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQIT 274
Cdd:COG0840  345 SVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIE 424

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 275 ALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELALKNA 354
Cdd:COG0840  425 EIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENA 504

                        330       340
                 ....*....|....*....|....*....
gi 499386170 355 HHTNLTNLSSLKVYNMSQEIGSLLHRFHV 383
Cdd:COG0840  505 ASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 121-382 2.42e-54

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: 184.03  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   121 DIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTTQIHQTK 200
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   201 SVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGA 280
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   281 QQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELALKNAHHTNLT 360
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 499386170   361 NLSSLKVYNMSQEIGSLLHRFH 382
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 398-523 2.27e-51

bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.


Pssm-ID: 468167  Cd Length: 129  Bit Score: 171.53  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 398 FVKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAY-GLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKH 476
Cdd:NF033749   1 LITWSDELSVGIKEIDEQHKKLVDLINELHDAMKTGGkGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEH 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499386170 477 AQLVGQVLDFQKRVARGE-DVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:NF033749  81 DKLVAKVLDLQKKFEAGEaTLSIELLNFLKDWLVNHILGTDKKYGPFL 128
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 148-347 5.14e-49

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: 167.80  E-value: 5.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 148 TQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTTQIHQTKSVIEHLAADTNSISSIIETISQVAEQT 227
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 228 NLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGAQQGVEVMLKNVTIADETALMVEQAHKS 307
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499386170 308 LGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMA 347
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 400-523 2.67e-43

hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.


Pssm-ID: 274154  Cd Length: 126  Bit Score: 149.79  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  400 KWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQL 479
Cdd:TIGR02481   1 KWDDSLSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 499386170  480 VGQVLDFQKRVARG--EDVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:TIGR02481  81 VKKIEELQEAVAEGadESLAEELLDFLKDWLVNHILKEDKKYAPYL 126
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
399-529 1.49e-42

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 148.24  E-value: 1.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 399 VKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQ 478
Cdd:COG2703    1 LEWSDELSVGIPEIDEQHKELFELINELYDALESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499386170 479 LVGQVLDFQKRVARG-EDVADELMAFLKSWLVNHIQKSDKEYAQFLLAHGAE 529
Cdd:COG2703   81 FLEELEELRERLEAGdLELARELLEFLKDWLVNHILKEDKKYARYLKKKGAG 132
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 165-349 4.74e-39

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: 140.26  E-value: 4.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  165 AQAADIAQNSAKHGDKIMGHIV---NKINDMTTQIHQTKSVIEhlaadtnsissiietisQVAEQTNLLALNAAIESARA 241
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVgqmEQIAQSSKKISDIISVID-----------------EIAFQTNLLALNAAIEAARA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  242 GEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDM 321
Cdd:pfam00015  64 GEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADI 143

                         170       180
                  ....*....|....*....|....*...
gi 499386170  322 SHQIATASEEQHAVAEEINKNISAMAEL 349
Cdd:pfam00015 144 VQEIAAASDEQSAGIDQVNQAVARMDQV 171
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 411-520 1.24e-34

Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four marine invertebrate phyla including priapulida, brachiopoda, sipunculida, and annelida, as well as in protozoa. Myohemerythrin (Mhr), a hemerythrin homolog, is found in the muscle tissue of sipunculids as well as in polycheate and oligocheate annelids. In addition to oxygen transport, Mhr proteins are involved in cadmium fixation and host anti-bacterial defense. Hr and Mhr proteins have the same "four alpha helix bundle" motif and active site structure. Hr forms oligomers, the octameric form being most prevalent, while Mhr is monomeric.


Pssm-ID: 213982  Cd Length: 113  Bit Score: 125.93  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 411 EINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQLVGQVLDFQKRV 490
Cdd:cd12107    2 EIDEQHKELFELINRLYEAIAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKARL 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499386170 491 ARG-EDVADELMAFLKSWLVNHIQKSDKEYA 520
Cdd:cd12107   82 EAGdLELAEELLDFLKDWLVNHILGEDKKLA 112
PRK00808 PRK00808
bacteriohemerythrin;
399-526 8.57e-34

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 125.18  E-value: 8.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 399 VKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAyGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQ 478
Cdd:PRK00808   4 LVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSP-DRLAVAEVIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499386170 479 LVGQVLDFQKRVARGEDVADELMAFLKSWLVNHIQKSDKEYAQFLLAH 526
Cdd:PRK00808  83 FIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKAN 130
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
35-354 1.09e-33

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 134.31  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILI--FNI-NKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDT 111
Cdd:PRK15041 194 WILVGVMIVVLAVIFAvwFGIkASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNG 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 112 SEWMKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKIND 191
Cdd:PRK15041 274 ANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRD 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 192 MTTQIHQTKSVIEHLAAdtnsissiietisqVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQ 271
Cdd:PRK15041 354 ISTSSQKIADIISVIDG--------------IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKS 419

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 272 QITalqkgaqqgvevmlKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELAL 351
Cdd:PRK15041 420 LIE--------------DSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQ 485


                 ...
gi 499386170 352 KNA 354
Cdd:PRK15041 486 QNA 488
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 411-523 1.02e-08

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 53.77  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  411 EINRQHQRLVSLVNELHRTLS--EAYGLEAIKRIVQGLVDYTANHFSYEEELF-------ARFGYPQTNGHKEKHAQLVG 481
Cdd:pfam01814   5 LLDAEHRRLRELLALLRALADalGDSHLRKLAELLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHDEIRE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499386170  482 QVLDFQKRVARGE--DVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:pfam01814  85 LLEELEALLKGAEpgAAFAELLEALAEWLREHIAKEEEVLFPLL 128
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
35-383 6.38e-75

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 246.47  E-value: 6.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILIFNINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDTSEW 114
Cdd:COG0840  185 AAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQ 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 115 MKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTT 194
Cdd:COG0840  265 VASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRE 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 195 QIHQTKSVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQIT 274
Cdd:COG0840  345 SVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAEATKEIEELIE 424

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 275 ALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELALKNA 354
Cdd:COG0840  425 EIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQAIEQIAAAAQENA 504

                        330       340
                 ....*....|....*....|....*....
gi 499386170 355 HHTNLTNLSSLKVYNMSQEIGSLLHRFHV 383
Cdd:COG0840  505 ASVEEVAAAAEELAELAEELQELVSRFKL 533
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 121-382 2.42e-54

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: 184.03  E-value: 2.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   121 DIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTTQIHQTK 200
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   201 SVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGA 280
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170   281 QQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELALKNAHHTNLT 360
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240

                          250       260
                   ....*....|....*....|..
gi 499386170   361 NLSSLKVYNMSQEIGSLLHRFH 382
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 398-523 2.27e-51

bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.


Pssm-ID: 468167  Cd Length: 129  Bit Score: 171.53  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 398 FVKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAY-GLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKH 476
Cdd:NF033749   1 LITWSDELSVGIKEIDEQHKKLVDLINELHDAMKTGGkGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEH 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499386170 477 AQLVGQVLDFQKRVARGE-DVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:NF033749  81 DKLVAKVLDLQKKFEAGEaTLSIELLNFLKDWLVNHILGTDKKYGPFL 128
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
 148-347 5.14e-49

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: 167.80  E-value: 5.14e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 148 TQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTTQIHQTKSVIEHLAADTNSISSIIETISQVAEQT 227
Cdd:cd11386    1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 228 NLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGAQQGVEVMLKNVTIADETALMVEQAHKS 307
Cdd:cd11386   81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 499386170 308 LGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMA 347
Cdd:cd11386  161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 400-523 2.67e-43

hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.


Pssm-ID: 274154  Cd Length: 126  Bit Score: 149.79  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  400 KWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQL 479
Cdd:TIGR02481   1 KWDDSLSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 499386170  480 VGQVLDFQKRVARG--EDVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:TIGR02481  81 VKKIEELQEAVAEGadESLAEELLDFLKDWLVNHILKEDKKYAPYL 126
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
399-529 1.49e-42

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 148.24  E-value: 1.49e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 399 VKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQ 478
Cdd:COG2703    1 LEWSDELSVGIPEIDEQHKELFELINELYDALESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499386170 479 LVGQVLDFQKRVARG-EDVADELMAFLKSWLVNHIQKSDKEYAQFLLAHGAE 529
Cdd:COG2703   81 FLEELEELRERLEAGdLELARELLEFLKDWLVNHILKEDKKYARYLKKKGAG 132
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
 165-349 4.74e-39

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: 140.26  E-value: 4.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  165 AQAADIAQNSAKHGDKIMGHIV---NKINDMTTQIHQTKSVIEhlaadtnsissiietisQVAEQTNLLALNAAIESARA 241
Cdd:pfam00015   1 SDLAQLASEEAQDGGKEVANVVgqmEQIAQSSKKISDIISVID-----------------EIAFQTNLLALNAAIEAARA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  242 GEHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDM 321
Cdd:pfam00015  64 GEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADI 143

                         170       180
                  ....*....|....*....|....*...
gi 499386170  322 SHQIATASEEQHAVAEEINKNISAMAEL 349
Cdd:pfam00015 144 VQEIAAASDEQSAGIDQVNQAVARMDQV 171
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 411-520 1.24e-34

Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four marine invertebrate phyla including priapulida, brachiopoda, sipunculida, and annelida, as well as in protozoa. Myohemerythrin (Mhr), a hemerythrin homolog, is found in the muscle tissue of sipunculids as well as in polycheate and oligocheate annelids. In addition to oxygen transport, Mhr proteins are involved in cadmium fixation and host anti-bacterial defense. Hr and Mhr proteins have the same "four alpha helix bundle" motif and active site structure. Hr forms oligomers, the octameric form being most prevalent, while Mhr is monomeric.


Pssm-ID: 213982  Cd Length: 113  Bit Score: 125.93  E-value: 1.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 411 EINRQHQRLVSLVNELHRTLSEAYGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQLVGQVLDFQKRV 490
Cdd:cd12107    2 EIDEQHKELFELINRLYEAIAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKARL 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499386170 491 ARG-EDVADELMAFLKSWLVNHIQKSDKEYA 520
Cdd:cd12107   82 EAGdLELAEELLDFLKDWLVNHILGEDKKLA 112
PRK00808 PRK00808
bacteriohemerythrin;
399-526 8.57e-34

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 125.18  E-value: 8.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 399 VKWGPELDIGMSEINRQHQRLVSLVNELHRTLSEAyGLEAIKRIVQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQ 478
Cdd:PRK00808   4 LVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSP-DRLAVAEVIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499386170 479 LVGQVLDFQKRVARGEDVADELMAFLKSWLVNHIQKSDKEYAQFLLAH 526
Cdd:PRK00808  83 FIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKAN 130
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
35-354 1.09e-33

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 134.31  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILI--FNI-NKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDT 111
Cdd:PRK15041 194 WILVGVMIVVLAVIFAvwFGIkASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNG 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 112 SEWMKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKIND 191
Cdd:PRK15041 274 ANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRD 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 192 MTTQIHQTKSVIEHLAAdtnsissiietisqVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQ 271
Cdd:PRK15041 354 ISTSSQKIADIISVIDG--------------IAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKS 419

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 272 QITalqkgaqqgvevmlKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELAL 351
Cdd:PRK15041 420 LIE--------------DSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQ 485


                 ...
gi 499386170 352 KNA 354
Cdd:PRK15041 486 QNA 488
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
 40-354 4.02e-32

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 129.74  E-value: 4.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  40 LCLIALAVILIFNINKL-IRH--LRQLERAAHHLGE---GDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDTSE 113
Cdd:PRK15048 194 LAVIALVVVLILLVAWYgIRRmlLTPLAKIIAHIREiagGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSD 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 114 WMKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVN---KIN 190
Cdd:PRK15048 274 AIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKtmhEIA 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 191 DMTTQIHQTKSVIEhlaadtnsissiietisQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQ 270
Cdd:PRK15048 354 DSSKKIADIISVID-----------------GIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIK 416

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 271 QQITalqkgaqqgvevmlKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEINKNISAMAELA 350
Cdd:PRK15048 417 ALIE--------------DSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482


                 ....
gi 499386170 351 LKNA 354
Cdd:PRK15048 483 QQNA 486
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
100-393 1.91e-29

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 121.72  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 100 DVSRTILSLIDTSEWMKKVATDIKTISEQAKQGVLE-------QERQTELAATAMTQMVSTVQE----VSQNAASTAQAA 168
Cdd:PRK09793 244 EITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEivagnndLSSRTEQQAASLAQTAASMEQltatVGQNADNARQAS 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 169 DIAQNSA----KHGDKI--MGHIVNKINDMTTQIHQTKSVIEhlaadtnsissiietisQVAEQTNLLALNAAIESARAG 242
Cdd:PRK09793 324 ELAKNAAttaqAGGVQVstMTHTMQEIATSSQKIGDIISVID-----------------GIAFQTNILALNAAVEAARAG 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 243 EHGRGFAVVADEVRNLAKRTSEATAEIQQQITALQKGAQQGvevmlknvtiadetALMVEQAHKSLGEIVTHVESITDMS 322
Cdd:PRK09793 387 EQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQG--------------SKLVNNAAATMTDIVSSVTRVNDIM 452

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499386170 323 HQIATASEEQHAVAEEINKNISAMAELALKNAHHTNLTNLSSLKVYNMSQEIGSLLHRFHVDKQLFTSSQA 393
Cdd:PRK09793 453 GEIASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHES 523
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 400-519 2.53e-12

hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of various oligomeric states from the vascular fluid (hemerythrin) and muscle (myohemerythrin) of some marine invertebrates. Each unit binds 2 non-heme Fe using 5 H, one E and one D. One member of this family,from the sandworm Nereis diversicolor, is an unusual (non-metallothionein) cadmium-binding protein. Homologous proteins, excluded from this narrowly defined family, are found in archaea and bacteria (see pfam01814).


Pssm-ID: 129168  Cd Length: 115  Bit Score: 63.62  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  400 KWGPELDIGMSEINRQHQRLVSLVNelhrTLSEAYGLEAIKRivqgLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQL 479
Cdd:TIGR00058   6 VWDESFKVFYDNLDEEHKTLFNGIF----ALAADNSATALKE----LIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDDF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499386170  480 VGQVLDFQKRVARGEdvadelMAFLKSWLVNHIQKSDKEY 519
Cdd:TIGR00058  78 LAVLRGLKAPVPQDD------LLYAKDWLVNHIKTTDFKY 111
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 411-523 1.02e-08

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 53.77  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  411 EINRQHQRLVSLVNELHRTLS--EAYGLEAIKRIVQGLVDYTANHFSYEEELF-------ARFGYPQTNGHKEKHAQLVG 481
Cdd:pfam01814   5 LLDAEHRRLRELLALLRALADalGDSHLRKLAELLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHDEIRE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499386170  482 QVLDFQKRVARGE--DVADELMAFLKSWLVNHIQKSDKEYAQFL 523
Cdd:pfam01814  85 LLEELEALLKGAEpgAAFAELLEALAEWLREHIAKEEEVLFPLL 128
PRK01917 PRK01917
cation-binding hemerythrin HHE family protein; Provisional
 401-527 6.07e-06

cation-binding hemerythrin HHE family protein; Provisional


Pssm-ID: 179353  Cd Length: 139  Bit Score: 45.94  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 401 WGPELDIGMSEINRQHQRLVSLVNELHRTlSEAYGLEAIkrivQGLVDYTANHFSYEEELFARFGYPQTNGHKEKHAQLV 480
Cdd:PRK01917   6 WSEELHLGDPFTDATHAEFVQLLNAVARA-DDADFLQAL----DAWIDHTRHHFAQEERWMEATKFGPRHCHRAEHDEVL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499386170 481 GQVLDFQKRVARGEDVA--DELMAFLKSWLVNHIQKSDKEYAQFLLAHG 527
Cdd:PRK01917  81 AVAADVREKVARDGDFElgRRLVAELPEWFDQHVRTMDAMMVSHLKMLG 129
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 35-108 1.76e-05

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 47.26  E-value: 1.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499386170  35 YLLATLCLIALAVILIFNI-NKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSL 108
Cdd:COG5000   11 LLLIALLLLLLALWLALLLaRRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREEL 85
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
56-105 2.50e-03

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 36.07  E-value: 2.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 499386170    56 LIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTI 105
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETI 52
PRK10604 PRK10604
sensor protein RstB; Provisional
 36-110 4.35e-03

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 39.59  E-value: 4.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499386170  36 LLATLCL-IALAVILIfnINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILS---LID 110
Cdd:PRK10604 141 LLALIGLsLAFPVFLW--MRPHWQDMLKLEAAAQRLGDGHLAERIHFDEGSSLERLGVAFNQMADNINALIASkkqLID 217
HAMP pfam00672
HAMP domain;
51-99 4.37e-03

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 35.29  E-value: 4.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 499386170   51 FNINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGE 99
Cdd:pfam00672   1 LLARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAE 49
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 35-339 9.10e-03

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 38.71  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170  35 YLLATLCLIALAVILIFNINKLIRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGEDVSRTILSLIDTSEW 114
Cdd:COG3850  121 LLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEEL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 115 MKKVATDIKTISEQAKQGVLEQERQTELAATAMTQMVSTVQEVSQNAASTAQAADIAQNSAKHGDKIMGHIVNKINDMTT 194
Cdd:COG3850  201 EAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLL 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499386170 195 QIHQTKSVIEHLAADTNSISSIIETISQVAEQTNLLALNAAIESARAGEHGRGFAVVADEVRNLAKRTSEATAEIQQQIT 274
Cdd:COG3850  281 LELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGA 360

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499386170 275 ALQKGAQQGVEVMLKNVTIADETALMVEQAHKSLGEIVTHVESITDMSHQIATASEEQHAVAEEI 339
Cdd:COG3850  361 ALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIA 425
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 57-99 9.45e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 34.34  E-value: 9.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499386170  57 IRHLRQLERAAHHLGEGDLSYQLDEKDAGVFNSVVHSINRMGE 99
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAE 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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