Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein whose expression has long been considered limited to cardiomyocytes and striated skeletal muscle cell, however it has recently been found localized in a wide variety of tissues including smooth muscle cells. As a physiological catalyst, it can modulate reactive oxygen species levels, facilitate oxygen diffusion within the cell, and scavenge or generate NO depending on oxygen tensions within the cell. Through its NO dioxygenase and nitrite reductase activities, Mb regulates mitochondrial function in energy-demanding tissues.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A        5 DEWNHVLGIWAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTtIDALKSSEEVKKHGTTVLTALGRILKQKNNHEQ 84
Cdd:cd08926   1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGIS-QDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LHS_A       85 ELKPLAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKYKEFGFQG 153
Cdd:cd08926  80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148

Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein whose expression has long been considered limited to cardiomyocytes and striated skeletal muscle cell, however it has recently been found localized in a wide variety of tissues including smooth muscle cells. As a physiological catalyst, it can modulate reactive oxygen species levels, facilitate oxygen diffusion within the cell, and scavenge or generate NO depending on oxygen tensions within the cell. Through its NO dioxygenase and nitrite reductase activities, Mb regulates mitochondrial function in energy-demanding tissues.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A        5 DEWNHVLGIWAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTtIDALKSSEEVKKHGTTVLTALGRILKQKNNHEQ 84
Cdd:cd08926   1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGIS-QDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LHS_A       85 ELKPLAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKYKEFGFQG 153
Cdd:cd08926  80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148

Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein whose expression has long been considered limited to cardiomyocytes and striated skeletal muscle cell, however it has recently been found localized in a wide variety of tissues including smooth muscle cells. As a physiological catalyst, it can modulate reactive oxygen species levels, facilitate oxygen diffusion within the cell, and scavenge or generate NO depending on oxygen tensions within the cell. Through its NO dioxygenase and nitrite reductase activities, Mb regulates mitochondrial function in energy-demanding tissues.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A        5 DEWNHVLGIWAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTtIDALKSSEEVKKHGTTVLTALGRILKQKNNHEQ 84
Cdd:cd08926   1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGIS-QDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LHS_A       85 ELKPLAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKYKEFGFQG 153
Cdd:cd08926  80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148

Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to bind O2, NO and carbon monoxide. It has both nitric oxide dioxygenase and lipid peroxidase activities, and potentially participates in the maintenance of normal phenotype by implementing a homeostatic effect, to counteract stress conditions imposed on a cell. Cygb is implicated in multiple human pathologies: it is up-regulated in fibrosis and neurodegenerative disorders, and down-regulated in multiple cancer types, and may have a tumor suppressor role. It is expressed ubiquitously across a broad range of vertebrate organs including liver, heart, brain, lung, retina, and gut. In the human brain, it was detected at high levels in the habenula, hypothalamus, thalamus, hippocampus and pontine tegmental nuclei, detected at a low level in the cerebral cortex, and undetected in the cerebellar cortex.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A        2 LSDDEWNHVLGIWAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTTIDALKSSEEVKKHGTTVLTALGRILKQKNN 81
Cdd:cd08924   1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1LHS_A       82 HEQE---LKPLAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKYKEFGF 151
Cdd:cd08924  81 PDKVssvLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A       14 WAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTtiDALKSSEEVKKHGTTVLTALGRILKQKNNHE---QELKPLA 90
Cdd:cd01040   5 WARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVD--LDLKGSPEFKAHAKRVVGALDSLIDNLDDPEaldALLRKLG 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1LHS_A       91 ESHAtKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELF 138
Cdd:cd01040  83 KRHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYI 129

Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport protein of erythrocytes. It is an allosterically modulated heterotetramer. Hemoglobin A (HbA) is the most common Hb in adult humans, and is formed from two alpha-chains and two beta-chains (alpha2beta2). An equilibrium exists between deoxygenated/unliganded/T(tense state) Hb having low oxygen affinity, and oxygenated /liganded/R(relaxed state) Hb having a high oxygen affinity. Various endogenous heterotropic effectors bind Hb to modulate its oxygen affinity and cooperative behavior, e.g. hydrogen ions, chloride ions, carbon dioxide and 2,3-bisphosphoglycerate. Hb is also an allosterically regulated nitrite reductase; the plasma nitrite anion may be activated by hemoglobin in areas of hypoxia to bring about vasodilation. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A        9 HVLGIWAKVEPDlsAHGQEVIIRLFQLHPETQERFAKFKNLTTIDALKSSEEVKKHGTTVLTALGRILKQKNNHEQELKP 88
Cdd:cd08925   4 AITAVWGKVDVD--EVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFAD 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1LHS_A       89 LAESHATKHKIPVKYLEFICEIIVKVIAEKHPSDFGADSQAAMKKALELFRNDMASKY 146
Cdd:cd08925  82 LSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139

Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 genes encoding globins that are all transcribed. These are very diverse in gene and protein structure and are localized in a variety of cells. The C. elegans globin GLB-25 (locus tag T06A1.3), like the majority of them, was expressed in neuronal cells in the head and tail portions of the body and in the nerve cord.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LHS_A       14 WAKVEPDLSAHGQEVIIRLFQLHPETQERFAKFKNLTTI-DALKSSEEVKKHGTTVLTALGRILKQKNNHE---QELKPL 89
Cdd:cd14766   5 WKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEeDELRSSEILENHAARVMDTLDEAISNIENVDyviDLLHKV 84

                ....*
1LHS_A       90 AESHA 94
Cdd:cd14766  85 GKMHA 89