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Conserved domains on  [gi|62288290|sp|Q28221|]
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RecName: Full=Hemoglobin subunit gamma-1; AltName: Full=Gamma-1-globin; AltName: Full=Hemoglobin gamma-1 chain

Protein Classification

hemoglobin beta-like protein( domain architecture ID 10172378)

hemoglobin beta-like protein is either one of gamma, delta, epsilon, or 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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 1.21e-85

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: 246.78  E-value: 1.21e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   8 DKAAITSLWAKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFG 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62288290  88 QLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
 
Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 1.21e-85

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: 246.78  E-value: 1.21e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   8 DKAAITSLWAKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFG 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62288290  88 QLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
27-142 6.24e-38

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 125.09  E-value: 6.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290    27 ETLGRLLVVYPWTQRFFDSFGSlsSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLK---GTFGQLSELHCDKLHVDPEN 103
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 62288290   104 FRLLGNVLVTVLAvHHGKEFTPEVQASWQKMVAGVASAL 142
Cdd:pfam00042  80 FKLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 1.21e-85

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: 246.78  E-value: 1.21e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   8 DKAAITSLWAKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFG 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62288290  88 QLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 8-143 7.50e-71

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: 209.13  E-value: 7.50e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   8 DKAAITSLWAKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSpsaimGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFG 87
Cdd:cd14765   1 EKSTIKALWGKVNVEEYGAEALARLFVVYPWTKRYFPKFDDSSS-----GNPKVKAHGKKVLGALGDAVKHLDDLKNTFS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62288290  88 QLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALG 143
Cdd:cd14765  76 DLSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 4-146 5.50e-50

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: 156.58  E-value: 5.50e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   4 FTAEDKAAITSLWAKV--NVEDAGGETLGRLLVVYPWTQRFFDSFgSLSSpsaimGNPKVKAHGAKVLTSLGEAIKNLDD 81
Cdd:cd08927   1 LSAADKALIKALWGKIagHAEAIGAEALARMFLSFPQTKTYFPHF-DLSA-----GSAQVKAHGKKVMDALGDAVKHLDD 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62288290  82 LKGTFGQLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08927  75 LPGALSKLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKY 139
Globin pfam00042
Globin;
27-142 6.24e-38

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 125.09  E-value: 6.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290    27 ETLGRLLVVYPWTQRFFDSFGSlsSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLK---GTFGQLSELHCDKLHVDPEN 103
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 62288290   104 FRLLGNVLVTVLAvHHGKEFTPEVQASWQKMVAGVASAL 142
Cdd:pfam00042  80 FKLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 5-146 2.35e-24

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: 91.83  E-value: 2.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   5 TAEDKAAITSLWAKV--NVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDD- 81
Cdd:cd08924   2 TEAERKVIQDTWARVyaNCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHDp 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62288290  82 --LKGTFGQLSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08924  82 dkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAY 148
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 12-142 2.79e-22

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: 85.58  E-value: 2.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  12 ITSLWAKV--NVEDAGGETLGRLLVVYPWTQRFFDSFGSLssPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFGQL 89
Cdd:cd01040   1 VKSSWARVkkDKEEFGVAIFLRLFEANPELKKLFPKFAGV--DLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62288290  90 SEL---HCdKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASAL 142
Cdd:cd01040  79 RKLgkrHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 11-146 6.55e-18

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: 74.80  E-value: 6.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  11 AITSLWAKVNVEDA--GGETLGRLLVVYPWTQRFFDSFGSLSSpSAIMGNPKVKAHGAKVLTSLGEAIKNlddlKGTFGQ 88
Cdd:cd08926   5 LVLKVWAKVEADLTgiGQEVLLRLFKEHPETQEHFPKFKGISQ-DDLKSNEDLKKHGVTVLTALGEILKQ----KGSHEA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62288290  89 ----LSELHCDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVASALGSRY 146
Cdd:cd08926  80 elkpLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANY 141
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 8-131 5.63e-09

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: 51.01  E-value: 5.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290   8 DKAAITSLWAKV--NVEDAGGETLGRLLVVYPWTQRFFdsfgslsspsaimGNPKVKAHGAKVLTSLGEAIKNLDD---L 82
Cdd:cd12131   1 QIELVQQSFAKVepIADEAAALFYERLFELDPELKPLF-------------KGTDMEEQGRKLMAMLVLVVKGLDDleaL 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 62288290  83 KGTFGQLSELHCdKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASW 131
Cdd:cd12131  68 LPALQDLGRRHV-KYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAW 115
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 20-104 3.24e-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: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  20 NVEDAGGETLGRLLVVYPWTQRFFDSFGSL-SSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFGQLSEL---HCD 95
Cdd:cd14766  11 KIDETGKTMFLRMLTENPELKELFPKLKNLeDEEDELRSSEILENHAARVMDTLDEAISNIENVDYVIDLLHKVgkmHAK 90


                ....*....
gi 62288290  96 KLHVDPENF 104
Cdd:cd14766  91 KPGFRPEMF 99
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 63-141 9.73e-07

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: 44.92  E-value: 9.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  63 AHGAKVLTSLGEAIKNLDD---LKGTFGQLSELHcDKLHVDPENFRLLGNVLVTVLAVHHGKEFTPEVQASWQKMVAGVA 139
Cdd:cd19753  40 AQRDRLARALTHVVENLDDpdgLVPFLAQLGRDH-RKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIA 118


                ..
gi 62288290 140 SA 141
Cdd:cd19753 119 GV 120
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 50-142 4.98e-05

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: 40.98  E-value: 4.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  50 SSPSAIMGNPKVKAHGAKVLTSLGEAIKNLDDLKGTFGQLSELhcDKLH----VDPENFRLLGNVLVTVLAVHHGKEFTP 125
Cdd:cd08920  50 SSPQDCLSSPEFLDHIRKVMLVIDAAVSHLEDLSSLEEYLTSL--GRKHravgVKLESFSTVGESLLYMLESSLGPAFTP 127

                        90
                ....*....|....*..
gi 62288290 126 EVQASWQKMVAGVASAL 142
Cdd:cd08920 128 DTREAWSTLYGAVVQAM 144
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 17-142 7.81e-03

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: 34.62  E-value: 7.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62288290  17 AKVNVEDAGGETLG-----RLLVVYPWTQRFFDSfgslsSPSAIMGNPKVKAHgakVLTSLGEAIKNLDDLKGTFGQLSE 91
Cdd:cd19754  11 DSVPILESLGVKLTekfykYMLKRYPEVKPYFNE-----TNQKLLRQPKILAF---ALLQYAKNIDDLTPLSGFVEQIVS 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 62288290  92 LHCDkLHVDPENFRLLGNVLVTVLAVHHGKEF-TPEVQASWQKMVAGVASAL 142
Cdd:cd19754  83 KHVG-LQVKPEHYPIVGECLIETMKELLPEAVaTDEFIEAWTTAYGNLANIL 133
 
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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