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Conserved domains on  [gi|18859087|ref|NP_571928|]
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neuroglobin [Danio rerio]

Protein Classification

globin family protein( domain architecture ID 229384)

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

CATH:  1.10.490.10
Gene Ontology:  GO:0019825|GO:0020037
PubMed:  32863222|16061809|19281958
SCOP:  3000554

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Globin-like super family cl21461
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 4-150 3.53e-95

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).


The actual alignment was detected with superfamily member cd08920:

Pssm-ID: 473869  Cd Length: 148  Bit Score: 271.71  E-value: 3.53e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTN-CGDAPECLSSPEFLEHVTKVMLVIDAAVSHLD 82
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRqFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859087  83 DLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGW 150
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 ...
 4-150 3.53e-95

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: 271.71  E-value: 3.53e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTN-CGDAPECLSSPEFLEHVTKVMLVIDAAVSHLD 82
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRqFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859087  83 DLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGW 150
Cdd:cd08920  81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
4-146 1.02e-21

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 84.82  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGknkvPHGIVLFT----RLFELDPALLTLFSYSTncGDAPECLsspeflehvtkvMLVIDAAVS 79
Cdd:COG1017   1 LSPETIALVKASFPLVA----PHGEEITArfyeRLFELHPELRPLFNGDM--GEQRKAL------------AAALAAYAR 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18859087  80 HLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:COG1017  63 NLDNLEALLPALERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVM 129
Globin pfam00042
Globin;
30-146 1.15e-12

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 60.77  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087    30 LFTRLFELDPALLTLFSYSTNCGDAPEclSSPEFLEHVTKVMLVIDAAVSHLDDLHTLEDFLLNLGRKH-QAVGVNTQSF 108
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEKSADDLK--GSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18859087   109 ALVGESLLYMLQsSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:pfam00042  81 KLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 4-150 3.53e-95

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: 271.71  E-value: 3.53e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTN-CGDAPECLSSPEFLEHVTKVMLVIDAAVSHLD 82
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRqFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859087  83 DLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGW 150
Cdd:cd08920  81 DLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 12-146 1.64e-32

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: 112.16  E-value: 1.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  12 IRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTncGDAPECLSSPEFLEHVTKVMLVIDAAVSHLDDLHTLEDFL 91
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFA--GVDLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18859087  92 LNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:cd01040  79 RKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 8-147 3.02e-25

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: 93.38  E-value: 3.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   8 DKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSystncgdapeclsSPEFLEHVTKVMLVIDAAVSHLDDLHTL 87
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFK-------------GTDMEEQGRKLMAMLVLVVKGLDDLEAL 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  88 EDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMT 147
Cdd:cd12131  68 LPALQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMI 127
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
4-146 1.02e-21

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 84.82  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGknkvPHGIVLFT----RLFELDPALLTLFSYSTncGDAPECLsspeflehvtkvMLVIDAAVS 79
Cdd:COG1017   1 LSPETIALVKASFPLVA----PHGEEITArfyeRLFELHPELRPLFNGDM--GEQRKAL------------AAALAAYAR 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18859087  80 HLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:COG1017  63 NLDNLEALLPALERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVM 129
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 4-149 4.03e-20

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: 80.81  E-value: 4.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPAL---LTLFSystncGDAPECL-SSPEFLEHVTKVMLVIDAAVS 79
Cdd:cd12137   1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCkdaFFPFR-----DVDLEDLrHSKELRAHGLRVLSFVEKSLA 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  80 HLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRG 149
Cdd:cd12137  76 RLHQPDKLEELLHELGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMKEG 145
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 12-146 2.19e-15

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: 68.50  E-value: 2.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  12 IRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTNCGDA-PECLSSPEFLEHVTKVMLVIDAAVSHLDDLHTLEDF 90
Cdd:cd14766   1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEeDELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18859087  91 LLNLGRKHQAV-GVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:cd14766  81 LHKVGKMHAKKpGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 30-146 1.36e-14

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: 66.11  E-value: 1.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  30 LFTRLFELDPALLTLFsystncgdapeclssPEFLEHVTKVML-VIDAAVSHLDDLHTLEDFLLNLGRKHQAVGVNTQSF 108
Cdd:cd19753  19 FYARLFAEAPELRDLF---------------PADMDAQRDRLArALTHVVENLDDPDGLVPFLAQLGRDHRKYGVAPEHY 83

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18859087 109 ALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:cd19753  84 PAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIAGVM 121
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 4-148 1.51e-14

Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is 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; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb).


Pssm-ID: 381261  Cd Length: 147  Bit Score: 66.36  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTNCGDAPEclSSPEFLEHVTKVM-LVIDAAVS--H 80
Cdd:cd08923   1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSDEIPE--NNPKLKAHAMKVFkMTCESAIQlrK 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859087  81 LDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTR 148
Cdd:cd08923  79 KGKVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLAAAIKK 146
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 5-146 4.45e-13

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: 62.53  E-value: 4.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   5 SEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTNCGDAPEclSSPEFLEHVTKV-MLVIDAAVSHLDD 83
Cdd:cd14784   2 SEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLRDSTVPLE--KNPKLKPHAMSVfVMTCEAAVQLRKA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859087  84 --LHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:cd14784  80 gkVTVRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQLVAAI 144
Globin pfam00042
Globin;
30-146 1.15e-12

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 60.77  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087    30 LFTRLFELDPALLTLFSYSTNCGDAPEclSSPEFLEHVTKVMLVIDAAVSHLDDLHTLEDFLLNLGRKH-QAVGVNTQSF 108
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEKSADDLK--GSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18859087   109 ALVGESLLYMLQsSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:pfam00042  81 KLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 15-146 1.25e-11

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: 58.23  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  15 SWESLGKNKVPHGIVLFTRLFElDPALLTLFSYSTncgdapeclsspEFLEHVTKVMLVIDAAVSHLDDLHTLEDFLLNL 94
Cdd:cd01067   1 AWGYLEENQEEIVDDFYDRLFA-LPSLSELFSPPG------------RLAKCIRKQMHFLRYALYGLVDGDSIEEGLAGL 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859087  95 GRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAM 146
Cdd:cd01067  68 GEAHKSLGVPISYFIAALNVMKDVLTELLGDKFTPAAGEAWTKIFDYIISSM 119
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 4-145 3.73e-11

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: 57.35  E-value: 3.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSySTN--CGDAPECLSSpeflehvtkvmlVIDAAVSHL 81
Cdd:cd14777   1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFN-QTNqkKGLQQTALAN------------TVYAAAKHI 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859087  82 DDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSA 145
Cdd:cd14777  68 DNLEVILPVVKQIAHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIADV 131
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-150 1.04e-10

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: 56.11  E-value: 1.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   8 DKGLIRDSWESLGKNKVphGIVLFTRLFELDPALLTLFSYSTNCGDAPECLSSPEFLEHVTKVMLVIDAAVSHLDDLHTL 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEV--GAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859087  88 edfLLNLGRKHQ-AVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGW 150
Cdd:cd08925  79 ---FADLSEKHSeKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 4-154 1.39e-10

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: 56.39  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTNCGDAPECLSSPEFLEHVTKVMLVIDAAVSHLDD 83
Cdd:cd08924   1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859087  84 LHTLEDFLLNLGRKHQ-AVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMTRGWAKNG 154
Cdd:cd08924  81 PDKVSSVLALVGKAHAlKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVG 152
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 4-135 1.92e-10

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: 55.65  E-value: 1.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFS---YSTNcgdapeclsSPEFLEHVTKVMLVIDAAVSH 80
Cdd:cd08927   1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPhfdLSAG---------SAQVKAHGKKVMDALGDAVKH 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18859087  81 LDDLHTledFLLNLGRKH-QAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAW 135
Cdd:cd08927  72 LDDLPG---ALSKLSDLHaYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAAL 124
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 32-147 9.15e-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: 53.51  E-value: 9.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  32 TRLFELDPALLTLFSYSTNCGDApeclsSPEFLEHVTKVMLVIDAAVSHLDDLHTLedfLLNLGRKHQ-AVGVNTQSFAL 110
Cdd:cd14765  23 ARLFVVYPWTKRYFPKFDDSSSG-----NPKVKAHGKKVLGALGDAVKHLDDLKNT---FSDLSELHAdKLHVDPENFKL 94

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18859087 111 VGESLLYMLQSSLGPAYTTSLRQAWLTMYSIVVSAMT 147
Cdd:cd14765  95 LSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 4-139 1.35e-06

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: 45.12  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSweslgknkVP----HGIVL----FTRLFELDPALLTLFSYS-TNCGDAPECLSspeflehvtkvMLVI 74
Cdd:cd14779   1 LTEQQKDLVKAT--------VPvlkeHGVALtkhfYQRMFEHNPELKNVFNMGhQESGKQQQALA-----------MAVL 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18859087  75 dAAVSHLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMY 139
Cdd:cd14779  62 -AYAENIDDPEVLLPVLKLIAHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAY 125
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 4-135 1.57e-06

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: 44.88  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSweslgknkVP----HGIVLFT----RLFELDPALLTLFSySTNC--GDAPECLSSpeflehvtkvmlV 73
Cdd:cd08922   1 LSEETIAIVKAT--------APvlaeHGEEITTrfykRMFAEHPELKNLFN-MANQasGRQPKALAA------------A 59

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859087  74 IDAAVSHLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAW 135
Cdd:cd08922  60 VLAYAANIDNLEVLLPAVERIAHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAW 121
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 4-142 3.95e-05

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: 41.26  E-value: 3.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087   4 LSEKDKGLIRDSWESLGKNKVPHGIVLFTRLFELDPALLTLFSYSTN-CGDAPECLSspeflehvtkvMLVIDAAvSHLD 82
Cdd:cd14778   1 LDQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQkSGEQPKALA-----------MTVLAAA-QNIE 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  83 DLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMYSIV 142
Cdd:cd14778  69 NLEKIRPAVEKIGKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEI 128
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 79-139 2.44e-04

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: 38.86  E-value: 2.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859087  79 SHLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTT-SLRQAWLTMY 139
Cdd:cd19754  65 KNIDDLTPLSGFVEQIVSKHVGLQVKPEHYPIVGECLIETMKELLPEAVATdEFIEAWTTAY 126
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 76-139 1.52e-03

Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) 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. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions.


Pssm-ID: 381288  Cd Length: 140  Bit Score: 36.66  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859087  76 AAVSHLDDLHTLEDFLLNLGRKHQAVGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMY 139
Cdd:cd14780  62 AYARHIDRLEVLGGAVSLIVNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAY 125
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 26-139 8.93e-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.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 34.74  E-value: 8.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859087  26 HGIVL----FTRLFELDPALLTLFSYS-TNCGDAPECLSSpeflehvtkvmlVIDAAVSHLDDLHTLEDFLLNLGRKHQA 100
Cdd:cd14783  19 NGETLtrhfYKRMFEHNPEVKPFFNPAhQHSGSQQRALAA------------AICAYAANIDNLEVLGNAVELIAQKHAS 86

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18859087 101 VGVNTQSFALVGESLLYMLQSSLGPAYTTSLRQAWLTMY 139
Cdd:cd14783  87 LGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAY 125
 
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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