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Conserved domains on  [gi|2254483703|ref|WP_251652426|]
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MULTISPECIES: globin domain-containing protein [Sphingomonas]

Protein Classification

globin family protein( domain architecture ID 229384)

globin family protein is an all-helical protein that may bind porphyrins, phycobilins, and other non-heme cofactors, and may play various roles including as a sensor or transporter of oxygen

CATH:  1.10.490.10
Gene Ontology:  GO:0019825|GO:0020037
PubMed:  32863222|16061809|19281958
SCOP:  3000554

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Globin-like super family cl21461
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 5-143 1.86e-74

Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B).


The actual alignment was detected with superfamily member cd14781:

Pssm-ID: 473869  Cd Length: 139  Bit Score: 218.50  E-value: 1.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVDPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERIA 84
Cdd:cd14781     1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLFEDPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERIA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2254483703  85 ARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14781    81 QKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY 139
 
Name Accession Description Interval E-value
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 5-143 1.86e-74

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 218.50  E-value: 1.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVDPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERIA 84
Cdd:cd14781     1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLFEDPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERIA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2254483703  85 ARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14781    81 QKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY 139
PRK13289 PRK13289
NO-inducible flavohemoprotein;
4-148 5.46e-73

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 223.52  E-value: 5.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   4 PLSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIER 82
Cdd:PRK13289    1 MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHnPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVER 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254483703  83 IAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELYAAEAA 148
Cdd:PRK13289   81 IAQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEAAS 146
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
5-139 3.31e-57

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 174.58  E-value: 3.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAaheSGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:COG1017     1 LSPETIALVKASFPLVAPHGEEITARFYERLFeLHPELRPLFNGD---MGEQRKALAAALAAYARNLDNLEALLPALERL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINRE 139
Cdd:COG1017    78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAE 133
Globin pfam00042
Globin;
29-135 6.13e-12

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 58.45  E-value: 6.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  29 TRMYQRLF-VDPEIKALF-----DMAAHESGAQPKRLAAAILAF----AQNVDKLDALKPAIERIAARHVET-HIKPEHY 97
Cdd:pfam00042   1 AEILARLFtAYPDTKAYFprfekSADDLKGSPKFKAHGKKVLAAlgeaVKHLDDLAALNAALKKLGARHKEKrGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2254483703  98 PAVANALLPAIRDVLGEaATDDILNAWGEAYWFLADIL 135
Cdd:pfam00042  81 KLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 5-143 1.86e-74

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 218.50  E-value: 1.86e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVDPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERIA 84
Cdd:cd14781     1 LSPHTIAIVKATVPALEEHGVAITAAMYKRLFEDPEIKALFNQAAQKSGEQPRALAGAILAYAKNIDNLGALGSAVERIA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2254483703  85 ARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14781    81 QKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINREKQLY 139
PRK13289 PRK13289
NO-inducible flavohemoprotein;
4-148 5.46e-73

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 223.52  E-value: 5.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   4 PLSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIER 82
Cdd:PRK13289    1 MLSAQTIAIVKATVPLLEEHGEALTAHFYDRMFSHnPELKNIFNQSNQRNGDQPEALANAVLAYARNIDNLEALLPAVER 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254483703  83 IAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELYAAEAA 148
Cdd:PRK13289   81 IAQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLADVFIGREAEIYEEAAS 146
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 5-143 1.94e-69

Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs).


Pssm-ID: 381260  Cd Length: 140  Bit Score: 205.89  E-value: 1.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd08922     1 LSEETIAIVKATAPVLAEHGEEITTRFYKRMFaEHPELKNLFNMANQASGRQPKALAAAVLAYAANIDNLEVLLPAVERI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd08922    81 AHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLADILIEREKQLY 140
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
5-139 3.31e-57

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 174.58  E-value: 3.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAaheSGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:COG1017     1 LSPETIALVKASFPLVAPHGEEITARFYERLFeLHPELRPLFNGD---MGEQRKALAAALAAYARNLDNLEALLPALERL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINRE 139
Cdd:COG1017    78 GRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAAE 133
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 5-143 2.72e-56

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 172.64  E-value: 2.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFV-DPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14783     1 LSQKTIDIVKSTAPILEENGETLTRHFYKRMFEhNPEVKPFFNPAHQHSGSQQRALAAAICAYAANIDNLEVLGNAVELI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14783    81 AQKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLADILIGREKQIY 140
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 5-143 2.37e-55

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 170.30  E-value: 2.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14778     1 LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEyPEVRPMFDMEKQKSGEQPKALAMTVLAAAQNIENLEKIRPAVEKI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14778    81 GKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIAKIFIDVEKKLY 140
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 5-143 5.52e-54

Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.


Pssm-ID: 381287  Cd Length: 140  Bit Score: 166.85  E-value: 5.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFV-DPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14779     1 LTEQQKDLVKATVPVLKEHGVALTKHFYQRMFEhNPELKNVFNMGHQESGKQQQALAMAVLAYAENIDDPEVLLPVLKLI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14779    81 AHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADILIGMESKLY 140
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 5-143 2.15e-52

Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development.


Pssm-ID: 381285  Cd Length: 140  Bit Score: 162.51  E-value: 2.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14777     1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEhPELLNIFNQTNQKKGLQQTALANTVYAAAKHIDNLEVILPVVKQI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14777    81 AHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADVFIEVEKEMY 140
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 5-143 1.58e-49

Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions.


Pssm-ID: 381288  Cd Length: 140  Bit Score: 155.31  E-value: 1.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14780     1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEyPEVRALFNQAHQASGAQPRALANAVLAYARHIDRLEVLGGAVSLI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14780    81 VNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLADLLIAAEEAVY 140
HmpEc-globin-like cd14776
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ...
 5-143 9.92e-39

Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress.


Pssm-ID: 271309  Cd Length: 138  Bit Score: 127.97  E-value: 9.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFV-DPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd14776     1 LSAETIRIVKATIPLLAAAGPALTQHFYQRMLThNPELKNIFNLAHQRTGRQPKALFDAVAAYAQNIRNLQALLPAVERI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLgeAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14776    81 AQKHTSFNIQPEQYQIVGEHLLATIEELA--PPDKDVLAAWAKAYQFLADIFIDREGEIY 138
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 5-143 1.17e-36

Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development.


Pssm-ID: 381294  Cd Length: 141  Bit Score: 122.83  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PEIKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPAIERI 83
Cdd:cd19754     1 LTPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRyPEVKPYFNETNQKLLRQPKILAFALLQYAKNIDDLTPLSGFVEQI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254483703  84 AARHVETHIKPEHYPAVANALLPAIRDVLGEA-ATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd19754    81 VSKHVGLQVKPEHYPIVGECLIETMKELLPEAvATDEFIEAWTTAYGNLANILIDAEKKEY 141
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 5-143 1.93e-32

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 381290  Cd Length: 143  Bit Score: 112.11  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVD-PE-IKALFDMAAHESGAQPKRLAAAILAFAQNVDKLDALKPA--I 80
Cdd:cd14782     1 LSAESAEVIRATLPVVGEHIEEITPLFYRRMFGEhPElLRNLFNRGNQASGEQQKALAASVAAFATHLVDPDAPPPDsvL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254483703  81 ERIAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILINREVELY 143
Cdd:cd14782    81 SRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVYWLMADQLIATEARLY 143
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 11-137 1.34e-28

Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH.


Pssm-ID: 381269 [Multi-domain]  Cd Length: 128  Bit Score: 101.86  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  11 ALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALF---DMAAhesgaQPKRLAAAILAFAQNVDKLDALKPAIERIAAR 86
Cdd:cd12131     3 ELVQQSFAKVEPIADEAAALFYERLFeLDPELKPLFkgtDMEE-----QGRKLMAMLVLVVKGLDDLEALLPALQDLGRR 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2254483703  87 HVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADILIN 137
Cdd:cd12131    78 HVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMIE 128
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 13-135 1.56e-17

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


Pssm-ID: 381254  Cd Length: 133  Bit Score: 73.64  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  13 VKATAPALQQHGVDITTRMYQRLFV-DPEIKALFDMAAHESG---------AQPKRLAAAILAFAQNVDKLDALKPAIER 82
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEaNPELKKLFPKFAGVDLdlkgspefkAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2254483703  83 IAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADIL 135
Cdd:cd01040    81 LGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 13-128 1.57e-16

Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses.


Pssm-ID: 381293 [Multi-domain]  Cd Length: 121  Bit Score: 70.73  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  13 VKATAPALQQHGVDITTRMYQRLFV-DPEIKALF--DMaahesGAQPKRLAAAILAFAQNVDKLDALKPAIERIAARHVE 89
Cdd:cd19753     1 LRASLAAVEDGPDELARRFYARLFAeAPELRDLFpaDM-----DAQRDRLARALTHVVENLDDPDGLVPFLAQLGRDHRK 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2254483703  90 THIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAY 128
Cdd:cd19753    76 YGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAY 114
Globin pfam00042
Globin;
29-135 6.13e-12

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 58.45  E-value: 6.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  29 TRMYQRLF-VDPEIKALF-----DMAAHESGAQPKRLAAAILAF----AQNVDKLDALKPAIERIAARHVET-HIKPEHY 97
Cdd:pfam00042   1 AEILARLFtAYPDTKAYFprfekSADDLKGSPKFKAHGKKVLAAlgeaVKHLDDLAALNAALKKLGARHKEKrGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2254483703  98 PAVANALLPAIRDVLGEaATDDILNAWGEAYWFLADIL 135
Cdd:pfam00042  81 KLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 5-132 1.74e-07

Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb).


Pssm-ID: 381261  Cd Length: 147  Bit Score: 47.49  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAAHESGA---QPKRLAAAILAFAQNVD--------- 71
Cdd:cd08923     1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILeIAPAAKDMFSFLKDSDEIpenNPKLKAHAMKVFKMTCEsaiqlrkkg 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254483703  72 KLDALKPAIERIAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLA 132
Cdd:cd08923    81 KVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLA 141
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 6-135 1.16e-06

Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. This subfamily also includes ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit.


Pssm-ID: 381291  Cd Length: 149  Bit Score: 45.20  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   6 SSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAAHES---GAQPKRLAAAILAFAQNVD---------K 72
Cdd:cd14784     2 SEEQEALVKKSWAVMKKDAAELGLKFFLKIFeIAPSAKQLFSFLRDSTvplEKNPKLKPHAMSVFVMTCEaavqlrkagK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254483703  73 LDALKPAIERIAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFLADIL 135
Cdd:cd14784    82 VTVRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQLVAAI 144
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 5-128 6.14e-06

Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly expressed in neurons of the brain and retina. In the human brain, it is highly expressed in the hypothalamus, amygdala, and in the pontine tegmental nuclei. It affords protection of brain neurons from ischemia and hypoxia. In rats, it plays a role in the neuroprotection of limb ischemic preconditioning (LIP). It plays roles as: a sensor of oxygen levels; a store or reservoir for oxygen; a facilitator for oxygen transport; a regulator of ROS; and a scavenger of nitric oxide. It also functions in the protection against apoptosis and in sleep regulation. This subgroup contains Ngb from mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles; the functionally pentacoordinated acoelomorph Symsagittifera roscoffensis Ngb does not belong to this subgroup.


Pssm-ID: 271272  Cd Length: 148  Bit Score: 43.29  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALFDMAAHESGAQPKRLAAA------------ILAFAQNVD 71
Cdd:cd08920     1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFeLEPDLLPLFQYNGRQFSSPQDCLSSPefldhirkvmlvIDAAVSHLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2254483703  72 KLDALKPAIERIAARHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAY 128
Cdd:cd08920    81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLY 137
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 5-131 4.77e-04

Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central nervous system, and appears to be associated with the sensory system. GbX is likely to be attached to the cell membrane via S-palmitoylation and N-myristoylation. It's unlikely to have a true respiratory function as it is membrane-associated. It has been suggested that it may protect the lipids in the cell membrane from oxidation or act as a redox-sensing or signaling protein. Zebrafish GbX is hexacoordinate, and displays cooperative O2 binding.


Pssm-ID: 271287  Cd Length: 145  Bit Score: 38.05  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLF-VDPEIKALF------DMAAHESGAQPKRLAAAILAFaqnVDKLDALK 77
Cdd:cd12137     1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFeTHPDCKDAFfpfrdvDLEDLRHSKELRAHGLRVLSF---VEKSLARL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254483703  78 PAIERIAA-------RHVETHIKPEHYPAVANALLPAIRDVLGEAATDDILNAWGEAYWFL 131
Cdd:cd12137    78 HQPDKLEEllhelgrKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYL 138
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 32-137 1.17e-03

Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B).


Pssm-ID: 381255 [Multi-domain]  Cd Length: 119  Bit Score: 36.66  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703  32 YQRLFVDPEIKALF----DMAAHEsgaqpKRLAAAILAFAQNVDKLDALKPAIERIAARHVETHIKPEHYPAVANALLPA 107
Cdd:cd01067    17 YDRLFALPSLSELFsppgRLAKCI-----RKQMHFLRYALYGLVDGDSIEEGLAGLGEAHKSLGVPISYFIAALNVMKDV 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 2254483703 108 IRDVLGEAATDDILNAWGEAYwflaDILIN 137
Cdd:cd01067    92 LTELLGDKFTPAAGEAWTKIF----DYIIS 117
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
 5-97 5.71e-03

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: 381256 [Multi-domain]  Cd Length: 146  Bit Score: 34.86  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254483703   5 LSSETMALVKATAPALQQHGVDITTRMYQRLFVDPEIKALFDMAAHESGAQPKRLAAAILAFAQNVDklDALKPAIERIA 84
Cdd:cd01068     8 LTEEDLALLRELRPLIEPHLDEILDAFYDHLLSFPELAAIFDDHSTIERLKQTQRAHWLELFSGDFD--EAYVERRRRIG 85

                          90
                  ....*....|...
gi 2254483703  85 ARHVETHIKPEHY 97
Cdd:cd01068    86 RVHVRIGLEPRWY 98
 
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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