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Conserved domains on  [gi|24987572|pdb|1LFLA| ]
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Chain A, Deoxy Hemoglobin (90% Relative Humidity)

Protein Classification

Hb-alpha_like domain-containing protein (domain architecture ID 10172381)

Hb-alpha_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hb-alpha_like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
2-141 2.40e-82

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: 271278  Cd Length: 140  Bit Score: 242.09  E-value: 2.40e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIASHAEAIGAEALARMFLSYPQTKTYFPHFDLSAGSAQVKAHGKKVMNALGDAVKHLDDLPGALS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA        82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHCALDKFLSAVSLVLSSKYR 140
 
Name Accession Description Interval E-value
Hb-alpha_like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
2-141 2.40e-82

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: 271278  Cd Length: 140  Bit Score: 242.09  E-value: 2.40e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIASHAEAIGAEALARMFLSYPQTKTYFPHFDLSAGSAQVKAHGKKVMNALGDAVKHLDDLPGALS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA        82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHCALDKFLSAVSLVLSSKYR 140
Globin pfam00042
Globin;
6-106 7.25e-29

Globin;


Pssm-ID: 306539  Cd Length: 109  Bit Score: 104.31  E-value: 7.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA           6 DKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDL-----SHGSAQVKGHGKKVADALTNAVAHVDDMPN-- 78
Cdd:pfam00042   1 DKALVKASWGKVKGNAPELGAEILARLFTAYPDTKTYFPRFGGdsldaLKGSPKFKAHGKKVLAALGEAIKHLDDDGAlk 80
                          90       100
                  ....*....|....*....|....*....
1LFLA          79 -ALSALSDLHAHKLRVDPVNFKLLSHCLL 106
Cdd:pfam00042  81 aALKKLAARHAERGHVDPANFKLFGEALL 109
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
2-132 1.75e-05

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 223948  Cd Length: 150  Bit Score: 41.53  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFphfdlsHGSAQVKG-HGKKVADALTNAVAHVDDMPNAL 80
Cdd:COG1017   2 LSEETIAIIKATVPLLEEHGETITAHFYKRMFAHHPELKNIF------NMANQKNGdQPKALANAILAYAKNIDNLEALL 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1LFLA        81 SALSDLhAHK---LRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDK---FLASV 132
Cdd:COG1017  76 PVVERI-AHKhvsLQIKPEHYPIVGEHLLAAIKEVLGDAATPEVLEAWGEaygVLADV 132
 
Name Accession Description Interval E-value
Hb-alpha_like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
2-141 2.40e-82

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: 271278  Cd Length: 140  Bit Score: 242.09  E-value: 2.40e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIASHAEAIGAEALARMFLSYPQTKTYFPHFDLSAGSAQVKAHGKKVMNALGDAVKHLDDLPGALS 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA        82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHCALDKFLSAVSLVLSSKYR 140
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
5-140 1.80e-65

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: 271298  Cd Length: 134  Bit Score: 198.73  E-value: 1.80e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         5 ADKTNVKAAWGKVgaHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALS 84
Cdd:cd14765   1 EEKSTIKALWGKV--NVEEIGAEALARLFVVYPWTKRYFPKFDLSSGNPKVKAHGKKVLGALGDAVKHLDDLKATFSNLS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
1LFLA        85 DLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKY 140
Cdd:cd14765  79 ELHADKLHVDPENFKLLSDCLIVTLAAHLGKEFTPEVHAAWDKFLAVVADALSSKY 134
Hb-beta_like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
5-140 4.53e-39

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: 271276  Cd Length: 140  Bit Score: 131.61  E-value: 4.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         5 ADKTNVKAAWGKVGAHagEYGAEALERMFLSFPTTKTYFPHF-DLSH-----GSAQVKGHGKKVADALTNAVAHVDDMPN 78
Cdd:cd08925   1 EEKAEITAVWGKVDVD--EIGAKALERLLIVYPWTQRYFSSFgDLSSaaaimGNPKVAAHGKKVVGALGEAVKHLDDIKA 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1LFLA        79 ALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKY 140
Cdd:cd08925  79 TFADLSKKHSDKLHVDPENFKLLGDCLVVELAAHLGKEFTPEVQAAWEKFFAVVADALSRQY 140
Globin pfam00042
Globin;
6-106 7.25e-29

Globin;


Pssm-ID: 306539  Cd Length: 109  Bit Score: 104.31  E-value: 7.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA           6 DKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDL-----SHGSAQVKGHGKKVADALTNAVAHVDDMPN-- 78
Cdd:pfam00042   1 DKALVKASWGKVKGNAPELGAEILARLFTAYPDTKTYFPRFGGdsldaLKGSPKFKAHGKKVLAALGEAIKHLDDDGAlk 80
                          90       100
                  ....*....|....*....|....*....
1LFLA          79 -ALSALSDLHAHKLRVDPVNFKLLSHCLL 106
Cdd:pfam00042  81 aALKKLAARHAERGHVDPANFKLFGEALL 109
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
2-141 6.18e-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: 87.20  E-value: 6.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHF-DLS-----HGSAQVKGHGKKVADALTNAVAHVDD 75
Cdd:cd08924   1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFkHMEdplemERSSQLRKHARRVMGALNTVVENLHD 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1LFLA        76 ---MPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR 141
Cdd:cd08924  81 pdkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYK 149
Mb_like cd01040
myoglobin_like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
10-136 2.62e-21

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: 271266  Cd Length: 132  Bit Score: 85.22  E-value: 2.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA        10 VKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHF---DLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDL 86
Cdd:cd01040   1 VRSSWARVAKDKDEFGVAFFARLFEANPELRKLFPKFagvDLDKGSPEFRAHAKRVVGALDSVVDNLDDPEALVALLRKL 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
1LFLA        87 ---HAhKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVL 136
Cdd:cd01040  81 grrHR-KRGVTPEHFDAFGEALLETLREVLGEAWTPEVEAAWRKLLDFIAAVM 132
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
5-141 5.42e-13

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: 62.86  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         5 ADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFD-LSHG----SAQVKGHGKKVADALTNAVAHVDDMPNA 79
Cdd:cd08926   1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKgISQDdlksNEDLKKHGVTVLTALGEILKQKGSHEAE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1LFLA        80 LSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR 141
Cdd:cd08926  81 LKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYK 142
HGbI_like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
6-135 4.02e-11

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 thermophlic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealands 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: 271286  Cd Length: 128  Bit Score: 57.17  E-value: 4.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         6 DKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLshgsaqvKGHGKKVADALTNAVAHVDDMPNALSALSD 85
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELRPLFKSTDM-------EEQGKKLMATLVLVVKGLDDLETLVPALQD 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1LFLA        86 LHA-H-KLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTV 135
Cdd:cd12131  74 LGRrHvKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGVLAGT 125
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
2-132 1.75e-05

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 223948  Cd Length: 150  Bit Score: 41.53  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFphfdlsHGSAQVKG-HGKKVADALTNAVAHVDDMPNAL 80
Cdd:COG1017   2 LSEETIAIIKATVPLLEEHGETITAHFYKRMFAHHPELKNIF------NMANQKNGdQPKALANAILAYAKNIDNLEALL 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1LFLA        81 SALSDLhAHK---LRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDK---FLASV 132
Cdd:COG1017  76 PVVERI-AHKhvsLQIKPEHYPIVGEHLLAAIKEVLGDAATPEVLEAWGEaygVLADV 132
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
30-121 4.53e-04

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: 271273  Cd Length: 140  Bit Score: 37.50  E-value: 4.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA        30 ERMFLSFPTTKTYFPHfdlshgSAQVKGH-GKKVADALTNAVAHVDDmPNALSALSDLHAHK---LRVDPVNFKLLSHCL 105
Cdd:cd08922  29 KRMFKEYPELKNLFNM------TNQKLGRqPKALAFAVLAYAKNIDD-LEPLLPAVERIAHKhvsLQVKPEHYPIVGECL 101
                        90
                ....*....|....*.
1LFLA       106 LVTLAAHLPAEFTPAV 121
Cdd:cd08922 102 LEAIKEVLGDAATPEV 117
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinate heme globin chiefly ...
2-137 4.88e-03

Neuroglobins; The Ngb described in this subfamily is a hexacoordinate 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: 35.20  E-value: 4.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LFLA         2 LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQ-------VKGHGKKVADALTNAVAHVD 74
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQdclsspeFLDHIRKVMLVIDAAVSHLE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1LFLA        75 DMPNALSALSDLhAHKLRVDPVN---FKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLT 137
Cdd:cd08920  81 DLSSLEEYLTSL-GRKHRAVGVKlesFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMS 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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