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Conserved domains on  [gi|11967939|ref|NP_071859|]
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neuroglobin isoform 2 [Mus musculus]

Protein Classification

globin family protein; hemoglobin alpha subunit family protein( domain architecture ID 10172370)

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
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 1-148 2.85e-100

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: 284.04  E-value: 2.85e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   1 MERPESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVE 80
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11967939  81 DLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRGW 148
Cdd:cd08920  81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
 
Name Accession Description Interval E-value
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 1-148 2.85e-100

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: 284.04  E-value: 2.85e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   1 MERPESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVE 80
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11967939  81 DLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRGW 148
Cdd:cd08920  81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
7-147 1.68e-27

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 99.08  E-value: 1.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   7 ELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLF-QYNGRQfsspedclsspefldhIRKVMLVIDAAVTNVEDLSSL 85
Cdd:COG1017   7 ALVKASFPLVAPHGEEITARFYERLFELHPELRPLFnGDMGEQ----------------RKALAAALAAYARNLDNLEAL 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11967939  86 EEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRG 147
Cdd:COG1017  71 LPALERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAA 132
Globin pfam00042
Globin;
27-144 1.43e-14

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 65.39  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939    27 LFARLFALEPSLLPLFqynGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLTSLGRKH-RAVGVRLSS 105
Cdd:pfam00042   3 ILARLFTAYPDTKAYF---PRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 11967939   106 FSTVGESLLYMLEKcLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:pfam00042  80 FKLFGEALLVVLAE-HLGEFTPETKAAWDKALDVIAAAL 117
PRK13289 PRK13289
NO-inducible flavohemoprotein;
20-138 3.14e-06

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 45.17  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   20 PL--EHGTVL----FARLFALEPSLLPLF----QYNGRQfsspedclssPEFLDHirkvmlVIDAAVTNVEDLSSLEEYL 89
Cdd:PRK13289  15 PLleEHGEALtahfYDRMFSHNPELKNIFnqsnQRNGDQ----------PEALAN------AVLAYARNIDNLEALLPAV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 11967939   90 TSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYG 138
Cdd:PRK13289  79 ERIAQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYG 127
 
Name Accession Description Interval E-value
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 1-148 2.85e-100

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: 284.04  E-value: 2.85e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   1 MERPESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVE 80
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11967939  81 DLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRGW 148
Cdd:cd08920  81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 9-144 7.08e-35

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: 117.94  E-value: 7.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   9 IRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFqynGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEY 88
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLF---PKFAGVDLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDAL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 11967939  89 LTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd01040  78 LRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 12-144 5.84e-30

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).


Pssm-ID: 381255 [Multi-domain]  Cd Length: 119  Bit Score: 105.23  E-value: 5.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  12 SWRVVSRSPLEHGTVLFARLFAlEPSLLPLFQYNGRqfsspedclsspeFLDHIRKVMLVIDAAVTNVEDLSSLEEYLTS 91
Cdd:cd01067   1 AWGYLEENQEEIVDDFYDRLFA-LPSLSELFSPPGR-------------LAKCIRKQMHFLRYALYGLVDGDSIEEGLAG 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 11967939  92 LGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd01067  67 LGEAHKSLGVPISYFIAALNVMKDVLTELLGDKFTPAAGEAWTKIFDYIISSM 119
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 7-144 4.60e-29

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: 103.01  E-value: 4.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   7 ELIRQSW-RVVSRSPlEHGTVLFARLFALEPSLLPLFqyngrqfsspedclSSPEFLDHIRKVMLVIDAAVTNVEDLSSL 85
Cdd:cd12131   3 ELVQQSFaKVEPIAD-EAAALFYERLFELDPELKPLF--------------KGTDMEEQGRKLMAMLVLVVKGLDDLEAL 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 11967939  86 EEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd12131  68 LPALQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTM 126
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
7-147 1.68e-27

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 99.08  E-value: 1.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   7 ELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLF-QYNGRQfsspedclsspefldhIRKVMLVIDAAVTNVEDLSSL 85
Cdd:COG1017   7 ALVKASFPLVAPHGEEITARFYERLFELHPELRPLFnGDMGEQ----------------RKALAAALAAYARNLDNLEAL 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11967939  86 EEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRG 147
Cdd:COG1017  71 LPALERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIAA 132
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 9-144 6.28e-21

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: 81.90  E-value: 6.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   9 IRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFqyngrqfsspedclssPEFLDHIRKVML-VIDAAVTNVEDLSSLEE 87
Cdd:cd19753   1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLF----------------PADMDAQRDRLArALTHVVENLDDPDGLVP 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11967939  88 YLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd19753  65 FLAQLGRDHRKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIAGVM 121
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 9-144 2.25e-18

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: 75.82  E-value: 2.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   9 IRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEY 88
Cdd:cd14766   1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEEDELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11967939  89 LTSLGRKHRAV-GVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd14766  81 LHKVGKMHAKKpGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
Globin pfam00042
Globin;
27-144 1.43e-14

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 65.39  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939    27 LFARLFALEPSLLPLFqynGRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLTSLGRKH-RAVGVRLSS 105
Cdd:pfam00042   3 ILARLFTAYPDTKAYF---PRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 11967939   106 FSTVGESLLYMLEKcLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:pfam00042  80 FKLFGEALLVVLAE-HLGEFTPETKAAWDKALDVIAAAL 117
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 5-147 1.91e-13

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: 63.47  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   5 ESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLF-QYNGRQFsspEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLS 83
Cdd:cd12137   5 QKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFfPFRDVDL---EDLRHSKELRAHGLRVLSFVEKSLARLHQPD 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11967939  84 SLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSRG 147
Cdd:cd12137  82 KLEELLHELGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMKEG 145
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 7-146 1.52e-12

Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. This subfamily also includes ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit.


Pssm-ID: 381291  Cd Length: 149  Bit Score: 60.99  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   7 ELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYngrQFSSPEDCLSSPEFLDHIRKV-MLVIDAAVTNVED--LS 83
Cdd:cd14784   7 ALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSF---LRDSTVPLEKNPKLKPHAMSVfVMTCEAAVQLRKAgkVT 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11967939  84 SLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSR 146
Cdd:cd14784  84 VRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQLVAAIKA 146
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 22-143 2.99e-12

Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; 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. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development.


Pssm-ID: 381285  Cd Length: 140  Bit Score: 60.05  E-value: 2.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHGT----VLFARLFALEPSLLPLF----QYNGRQfsspedclssPEFLDHIrkvmlVIDAAVtNVEDLSSLEEYLTSLG 93
Cdd:cd14777  18 EKGTeitkRFYKRMFEEHPELLNIFnqtnQKKGLQ----------QTALANT-----VYAAAK-HIDNLEVILPVVKQIA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQA 143
Cdd:cd14777  82 HKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADV 131
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 49-148 4.93e-11

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: 56.88  E-value: 4.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  49 FSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLsslEEYLTSLGRKH-RAVGVRLSSFSTVGESLLYMLEKCLGPDFTP 127
Cdd:cd08925  42 LSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDI---KATFADLSEKHsEKLHVDPENFKLLGDCLVVVLAAHFGKEFTP 118

                        90       100
                ....*....|....*....|.
gi 11967939 128 ATRTAWSRLYGAVVQAMSRGW 148
Cdd:cd08925 119 EVQAAWEKFFAVVVDALSKGY 139
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 22-139 8.88e-11

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: 381260  Cd Length: 140  Bit Score: 56.05  E-value: 8.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHG----TVLFARLFALEPSLLPLF----QYNGRQFsspedclsspefldhiRKVMLVIDAAVTNVEDLSSLEEYLTSLG 93
Cdd:cd08922  18 EHGeeitTRFYKRMFAEHPELKNLFnmanQASGRQP----------------KALAAAVLAYAANIDNLEVLLPAVERIA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGA 139
Cdd:cd08922  82 HKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGF 127
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 5-145 3.47e-10

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: 54.28  E-value: 3.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   5 ESELIRQSWRVVSrsPLEHGTVLFARLFALEPSLLPLFQYNGRQFSSpedclsSPEFLDHIRKVMLVIDAAVTNVEDLSS 84
Cdd:cd14765   1 EKSTIKALWGKVN--VEEYGAEALARLFVVYPWTKRYFPKFDDSSSG------NPKVKAHGKKVLGALGDAVKHLDDLKN 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11967939  85 LeeyLTSLGRKH-RAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMS 145
Cdd:cd14765  73 T---FSDLSELHaDKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 5-148 6.46e-09

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: 51.38  E-value: 6.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   5 ESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQyngrQFSSPEDCLS---SPEFLDHIRKVMLVIDAAVTNVED 81
Cdd:cd08924   5 ERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFS----QFKHMEDPLEmerSSQLRKHARRVMGALNTVVENLHD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11967939  82 LSSLEEYLTSLGR----KHRAVGVRLSSFSTVgesLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMSR-----GW 148
Cdd:cd08924  81 PDKVSSVLALVGKahalKHKVEPVYFKILSGV---ILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAaykevGW 153
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 22-142 1.37e-07

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 47.81  E-value: 1.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHG----TVLFARLFALEPSLLPLF----QYNGRQfsspedclssPEFLdhirkVMLVIDAAvTNVEDLSSLEEYLTSLG 93
Cdd:cd14778  18 EHGveitTEFYKNMFTEYPEVRPMFdmekQKSGEQ----------PKAL-----AMTVLAAA-QNIENLEKIRPAVEKIG 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQ 142
Cdd:cd14778  82 KTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIAK 130
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 22-144 6.64e-07

Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; Flavohemoglobins (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 maintains Medicago truncatula-Sinorhizobium meliloti symbiosis. Alcaligenes eutrophus FHP contains a phospholipid-binding site.


Pssm-ID: 381287  Cd Length: 140  Bit Score: 45.89  E-value: 6.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHGTVL----FARLFALEPSLLPLF----QYNGRQfsspEDCLSspefldhirkvMLVIdAAVTNVEDLSSLEEYLTSLG 93
Cdd:cd14779  18 EHGVALtkhfYQRMFEHNPELKNVFnmghQESGKQ----QQALA-----------MAVL-AYAENIDDPEVLLPVLKLIA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAM 144
Cdd:cd14779  82 HKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLADIL 132
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 5-145 9.52e-07

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: 45.25  E-value: 9.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   5 ESELIRQSWRVVSRSPLEHGTVLFARLFALEPSLLPLFQYngrqFS-SPedclSSPEFLDHIRKVMLVIDAAVTNVEDLS 83
Cdd:cd08927   5 DKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPH----FDlSA----GSAQVKAHGKKVMDALGDAVKHLDDLP 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11967939  84 SleeYLTSLGRKHrAVGVRL--SSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYGAVVQAMS 145
Cdd:cd08927  77 G---ALSKLSDLH-AYKLRVdpVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLS 136
PRK13289 PRK13289
NO-inducible flavohemoprotein;
20-138 3.14e-06

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 45.17  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939   20 PL--EHGTVL----FARLFALEPSLLPLF----QYNGRQfsspedclssPEFLDHirkvmlVIDAAVTNVEDLSSLEEYL 89
Cdd:PRK13289  15 PLleEHGEALtahfYDRMFSHNPELKNIFnqsnQRNGDQ----------PEALAN------AVLAYARNIDNLEALLPAV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 11967939   90 TSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYG 138
Cdd:PRK13289  79 ERIAQKHVSLQIKPEHYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYG 127
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 22-138 1.26e-05

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; 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.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 42.45  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHGTVL----FARLFALEPSLLPLF----QYNGRQfsspedclsspefldhIRKVMLVIDAAVTNVEDLSSLEEYLTSLG 93
Cdd:cd14783  18 ENGETLtrhfYKRMFEHNPEVKPFFnpahQHSGSQ----------------QRALAAAICAYAANIDNLEVLGNAVELIA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLYG 138
Cdd:cd14783  82 QKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYG 126
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 78-138 5.63e-05

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: 40.78  E-value: 5.63e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11967939  78 NVEDLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDF-TPATRTAWSRLYG 138
Cdd:cd19754  66 NIDDLTPLSGFVEQIVSKHVGLQVKPEHYPIVGECLIETMKELLPEAVaTDEFIEAWTTAYG 127
HmpEc-globin-like cd14776
Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins ...
 28-138 9.24e-05

Globin domain of Escherichia coli flavohemoglobin (Hmp) and related proteins; Flavohemoglobins (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. This subfamily includes Vibrio fischeri Hmp and E.coli Hmp. NO scavenging by flavoHb affects the swarming behavior of Escherichia coli, and protects against NO during initiation of the squid-Vibrio symbiosis. E.coli Hmp can catalyze the reduction of several alkylhydroperoxide substrates into their corresponding alcohols using NADH as an electron donor, and it has been suggested that it participates in the repair of the lipid membrane oxidative damage generated during oxidative/nitrosative stress.


Pssm-ID: 271309  Cd Length: 138  Bit Score: 40.14  E-value: 9.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  28 FARLFALEPSLLPLF----QYNGRQfssPEDCLSSpefldhirkvmlvIDAAVTNVEDLSSLEEYLTSLGRKHRAVGVRL 103
Cdd:cd14776  28 YQRMLTHNPELKNIFnlahQRTGRQ---PKALFDA-------------VAAYAQNIRNLQALLPAVERIAQKHTSFNIQP 91

                        90       100       110
                ....*....|....*....|....*....|....*
gi 11967939 104 SSFSTVGESLLYMLEKCLGPDftPATRTAWSRLYG 138
Cdd:cd14776  92 EQYQIVGEHLLATIEELAPPD--KDVLAAWAKAYQ 124
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 80-137 4.96e-04

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; 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.


Pssm-ID: 381290  Cd Length: 143  Bit Score: 38.15  E-value: 4.96e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 11967939  80 EDLSSLEEYLTSLGRKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLY 137
Cdd:cd14782  71 PDAPPPDSVLSRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVY 128
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 22-137 3.56e-03

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; 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. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 35.53  E-value: 3.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11967939  22 EHGTV----LFARLFAlEPSLLPLF----QYNGRQfsspedclsspefldhIRKVMLVIDAAVTNVEDLSSLEEYLTSLG 93
Cdd:cd14781  18 EHGVAitaaMYKRLFE-DPEIKALFnqaaQKSGEQ----------------PRALAGAILAYAKNIDNLGALGSAVERIA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 11967939  94 RKHRAVGVRLSSFSTVGESLLYMLEKCLGPDFTPATRTAWSRLY 137
Cdd:cd14781  81 QKHVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAY 124
 
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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