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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632649   5 ELFYESFERCR-IDQEFLETFLADFCEHNPRFSERFENIGLEQQTKMLKASIILIYNSAG-LPSVRNSVKKLGKRHKDLG 82
Cdd:cd12131    3 ELVQQSFAKVEpIADEAAALFYERLFELDPELKPLFKGTDMEEQGRKLMAMLVLVVKGLDdLEALLPALQDLGRRHVKYG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515632649  83 MdisEQELNEWF-NSLLNTVKKY-DPHYDESVEQAWTETLEAGLTIMK 128
Cdd:cd12131   83 V---KPEHYPLVgEALLWTLEEGlGDEWTPEVKQAWTDAYGILAGTMI 127

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632649   5 ELFYESFERCR-IDQEFLETFLADFCEHNPRFSERFENIGLEQQTKMLKASIILIYNSAG-LPSVRNSVKKLGKRHKDLG 82
Cdd:cd12131    3 ELVQQSFAKVEpIADEAAALFYERLFELDPELKPLFKGTDMEEQGRKLMAMLVLVVKGLDdLEALLPALQDLGRRHVKYG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515632649  83 MdisEQELNEWF-NSLLNTVKKY-DPHYDESVEQAWTETLEAGLTIMK 128
Cdd:cd12131   83 V---KPEHYPLVgEALLWTLEEGlGDEWTPEVKQAWTDAYGILAGTMI 127

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515632649   5 ELFYESFERCR-IDQEFLETFLADFCEHNPRFSERFENIGLEQQTKMLKASIILIYNSAG-LPSVRNSVKKLGKRHKDLG 82
Cdd:cd12131    3 ELVQQSFAKVEpIADEAAALFYERLFELDPELKPLFKGTDMEEQGRKLMAMLVLVVKGLDdLEALLPALQDLGRRHVKYG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515632649  83 MdisEQELNEWF-NSLLNTVKKY-DPHYDESVEQAWTETLEAGLTIMK 128
Cdd:cd12131   83 V---KPEHYPLVgEALLWTLEEGlGDEWTPEVKQAWTDAYGILAGTMI 127