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Conserved domains on  [gi|118595749|sp|P02153|]
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RecName: Full=Myoglobin; AltName: Full=Nitrite reductase MB; AltName: Full=Pseudoperoxidase MB

Protein Classification

globin family protein; hemoglobin alpha subunit family protein( domain architecture ID 10172380)

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| hemoglobin alpha subunit family protein is either one of alpha, zeta, mu, theta, or related hemoglobin (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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 6-154 5.60e-82

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.


:

Pssm-ID: 271277  Cd Length: 148  Bit Score: 238.12  E-value: 5.60e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   6 GEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLkSEDEMKASEELKKHGATVLTALGGILKKKGQHEA 85
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGI-SQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118595749  86 ELKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKYKELGFQG 154
Cdd:cd08926   80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
 
Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 6-154 5.60e-82

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.


Pssm-ID: 271277  Cd Length: 148  Bit Score: 238.12  E-value: 5.60e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   6 GEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLkSEDEMKASEELKKHGATVLTALGGILKKKGQHEA 85
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGI-SQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118595749  86 ELKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKYKELGFQG 154
Cdd:cd08926   80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
Globin pfam00042
Globin;
28-143 7.76e-18

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 74.25  E-value: 7.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   28 EVLISLFKGHPETLEKFDKFKhlKSEDEMKASEELKKHGATVLTALGGILKKKGQHE---AELKPLAQSHATKHKIPVKY 104
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFE--KSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 118595749  105 LEFISDAIVHVLqKKHPGDFGADAQGAMKKALELFRNDM 143
Cdd:pfam00042  80 FKLFGEALLVVL-AEHLGEFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 6-154 5.60e-82

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.


Pssm-ID: 271277  Cd Length: 148  Bit Score: 238.12  E-value: 5.60e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   6 GEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLkSEDEMKASEELKKHGATVLTALGGILKKKGQHEA 85
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGI-SQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118595749  86 ELKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKYKELGFQG 154
Cdd:cd08926   80 ELKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 3-152 5.48e-22

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.


Pssm-ID: 271275  Cd Length: 153  Bit Score: 85.66  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   3 LSDGEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLKSEDEMKASEELKKHGATVLTALGGILKKKGQ 82
Cdd:cd08924    1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118595749  83 HE---AELKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKYKELGF 152
Cdd:cd08924   81 PDkvsSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153
Globin pfam00042
Globin;
28-143 7.76e-18

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 74.25  E-value: 7.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   28 EVLISLFKGHPETLEKFDKFKhlKSEDEMKASEELKKHGATVLTALGGILKKKGQHE---AELKPLAQSHATKHKIPVKY 104
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFE--KSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 118595749  105 LEFISDAIVHVLqKKHPGDFGADAQGAMKKALELFRNDM 143
Cdd:pfam00042  80 FKLFGEALLVVL-AEHLGEFTPETKAAWDKALDVIAAAL 117
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 11-139 6.62e-15

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: 67.09  E-value: 6.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749  11 VLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLksEDEMKASEELKKHGATVLTALGGI---LKKKGQHEAEL 87
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGV--DLDLKGSPEFKAHAKRVVGALDSLidnLDDPEALDALL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 118595749  88 KPLAQSHAtKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELF 139
Cdd:cd01040   79 RKLGKRHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYI 129
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 3-147 1.24e-11

Hemoglobin alpha, zeta, mu, theta, 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.


Pssm-ID: 381263  Cd Length: 140  Bit Score: 58.35  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   3 LSDGEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFkhlkseDEMKASEELKKHGATVLTALGGILKKKGQ 82
Cdd:cd08927    1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHF------DLSAGSAQVKAHGKKVMDALGDAVKHLDD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118595749  83 HEAELKPLAQSHATKHKI-PVKYlEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKY 147
Cdd:cd08927   75 LPGALSKLSDLHAYKLRVdPVNF-KLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKY 139
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 3-119 1.85e-09

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: 52.69  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   3 LSDGEWQLVLNVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLKSEDeMKASEELKKHGATVLTALGGILKKKGQ 82
Cdd:cd12137    1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLED-LRHSKELRAHGLRVLSFVEKSLARLHQ 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 118595749  83 HEaELKPLAQSHATKH---KIPVKYLEFISD----AIVHVLQKK 119
Cdd:cd12137   80 PD-KLEELLHELGRKHyryNAKVKYVDLVGQqfifAIEPVLKEQ 122
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 7-144 3.86e-08

Hemoglobins; 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 Hb throughout most of gestation. These Hb types have differences in O2 affinity and in their interactions with allosteric effectors.


Pssm-ID: 381278  Cd Length: 131  Bit Score: 48.89  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   7 EWQLVLNVWGKVEADipSHGQEVLISLFKGHPETLEKFDKFKHLKSedemkASEELKKHGATVLTALGGILKKKGQHEAE 86
Cdd:cd14765    1 EKSTIKALWGKVNVE--EYGAEALARLFVVYPWTKRYFPKFDDSSS-----GNPKVKAHGKKVLGALGDAVKHLDDLKNT 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118595749  87 LKPLAQSHATKHKIPVKYLEFISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMA 144
Cdd:cd14765   74 FSDLSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 13-74 3.38e-07

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.


Pssm-ID: 381279  Cd Length: 137  Bit Score: 46.55  E-value: 3.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118595749  13 NVWGKVEADIPSHGQEVLISLFKGHPETLEKFDKFKHLK-SEDEMKASEELKKHGATVLTALG 74
Cdd:cd14766    3 KSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEdEEDELRSSEILENHAARVMDTLD 65
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 7-147 7.23e-06

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.


Pssm-ID: 381262  Cd Length: 139  Bit Score: 43.01  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118595749   7 EWQLVLNVWGKVEADipSHGQEVLISLFKGHPETLEKFDKFKHLKSEDEMKASEELKKHGATVLTALGGILKkkgqHEAE 86
Cdd:cd08925    1 EKAAITAVWGKVDVD--EVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIK----HLDD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118595749  87 LKPLAQSHATKH--KIPVKYLEF--ISDAIVHVLQKKHPGDFGADAQGAMKKALELFRNDMAAKY 147
Cdd:cd08925   75 IKATFADLSEKHseKLHVDPENFklLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
 
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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