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Conserved domains on  [gi|15228313|ref|NP_187663|]
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hemoglobin 2 [Arabidopsis thaliana]

Protein Classification

globin family protein; hemoglobin alpha subunit family protein( domain architecture ID 10172375)

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
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 6-152 1.57e-98

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: 280.15  E-value: 1.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   6 FTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEG 85
Cdd:cd08923   1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSDEIPENNPKLKAHAMKVFKMTCESAIQLRKKG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228313  86 KVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIKTE 152
Cdd:cd08923  81 KVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLAAAIKKE 147
 
Name Accession Description Interval E-value
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 6-152 1.57e-98

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: 280.15  E-value: 1.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   6 FTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEG 85
Cdd:cd08923   1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSDEIPENNPKLKAHAMKVFKMTCESAIQLRKKG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228313  86 KVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIKTE 152
Cdd:cd08923  81 KVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLAAAIKKE 147
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
7-146 2.40e-19

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 78.66  E-value: 2.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFsflrdsdevphnNPKLKAHAVKVFKMTCETAIQLREEGK 86
Cdd:COG1017   2 SPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLF------------NGDMGEQRKALAAALAAYARNLDNLEA 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  87 VVVAdttLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:COG1017  70 LLPA---LERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLA 126
Globin pfam00042
Globin;
30-149 6.46e-19

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 76.94  E-value: 6.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313    30 LHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEGKVVvadTTLQYLGSIHLKSGVIDP 109
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALN---AALKKLGARHKEKRGVDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15228313   110 -HFEVVKEALLRTLKEGLGEkYNEEVEGAWSQAYDHLALAI 149
Cdd:pfam00042  78 aNFKLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
PRK13289 PRK13289
NO-inducible flavohemoprotein;
110-146 5.27e-05

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 42.09  E-value: 5.27e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15228313  110 HFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:PRK13289  94 HYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLA 130
 
Name Accession Description Interval E-value
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 6-152 1.57e-98

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: 280.15  E-value: 1.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   6 FTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEG 85
Cdd:cd08923   1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSDEIPENNPKLKAHAMKVFKMTCESAIQLRKKG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228313  86 KVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIKTE 152
Cdd:cd08923  81 KVVVADTTLKRLGSVHLKKGVADPHFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLAAAIKKE 147
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 6-154 2.53e-65

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: 196.20  E-value: 2.53e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   6 FTEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEG 85
Cdd:cd14784   1 FSEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLRDSTVPLEKNPKLKPHAMSVFVMTCEAAVQLRKAG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228313  86 KVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIKTEMK 154
Cdd:cd14784  81 KVTVRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQLVAAIKAEMK 149
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 14-149 3.22e-25

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: 93.67  E-value: 3.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  14 VKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMtCETAIQ-LREEGKVvvaDT 92
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRVVGA-LDSLIDnLDDPEAL---DA 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228313  93 TLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAI 149
Cdd:cd01040  77 LLRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
7-146 2.40e-19

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 78.66  E-value: 2.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFsflrdsdevphnNPKLKAHAVKVFKMTCETAIQLREEGK 86
Cdd:COG1017   2 SPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLF------------NGDMGEQRKALAAALAAYARNLDNLEA 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  87 VVVAdttLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:COG1017  70 LLPA---LERLGRKHVSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLA 126
Globin pfam00042
Globin;
30-149 6.46e-19

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 76.94  E-value: 6.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313    30 LHFFSQILEIAPAAKGLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEGKVVvadTTLQYLGSIHLKSGVIDP 109
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALN---AALKKLGARHKEKRGVDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15228313   110 -HFEVVKEALLRTLKEGLGEkYNEEVEGAWSQAYDHLALAI 149
Cdd:pfam00042  78 aNFKLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 10-146 7.08e-18

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: 74.51  E-value: 7.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  10 QEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFsflRDSDevphnnpkLKAHAVKVFKMTcETAIQ-LREEGKVV 88
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLF---KGTD--------MEEQGRKLMAML-VLVVKgLDDLEALL 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15228313  89 vadTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd12131  69 ---PALQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILA 123
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 14-146 1.57e-12

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: 60.33  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  14 VKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFsflrdsdevPhnnPKLKAHAVKVFKMTCETAIQLREEGKVVvadTT 93
Cdd:cd19753   1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLF---------P---ADMDAQRDRLARALTHVVENLDDPDGLV---PF 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228313  94 LQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd19753  66 LAQLGRDHRKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIA 118
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 7-150 5.19e-12

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: 59.62  E-value: 5.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSDEVPHN-NPKLKAHAVKVFKmTCETAI-QLREE 84
Cdd:cd12137   2 TERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLEDLRhSKELRAHGLRVLS-FVEKSLaRLHQP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228313  85 GKVvvaDTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLALAIK 150
Cdd:cd12137  81 DKL---EELLHELGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMK 143
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 7-154 4.73e-10

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: 54.51  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSflrDSDEVPHNNPKLKAHAVKVFKMTCETAIQLreegk 86
Cdd:cd08922   2 SEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFN---MANQASGRQPKALAAAVLAYAANIDNLEVL----- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228313  87 vvvaDTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA-LAIKTEMK 154
Cdd:cd08922  74 ----LPAVERIAHKHVSLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLAdILIEREKQ 138
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 7-142 1.24e-08

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: 50.99  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSF-LRDSDEVPH--NNPKLKAHAVKVFkMTCETAIQLRE 83
Cdd:cd08920   2 SRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYnGRQFSSPQDclSSPEFLDHIRKVM-LVIDAAVSHLE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228313  84 EgkVVVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAY 142
Cdd:cd08920  81 D--LSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLY 137
FHP_Ae-globin-like cd14779
Globin domain of Alcaligenes eutrophus flavohemoglobin (FHP) and related proteins; ...
 7-154 3.53e-08

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: 49.36  E-value: 3.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSflrdsdeVPHNNPKLKAHAVKVFKMTCETAIqlrEEGK 86
Cdd:cd14779   2 TEQQKDLVKATVPVLKEHGVALTKHFYQRMFEHNPELKNVFN-------MGHQESGKQQQALAMAVLAYAENI---DDPE 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228313  87 VVVAdtTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA-LAIKTEMK 154
Cdd:cd14779  72 VLLP--VLKLIAHKHVSLGIRAEQYPIVGEHLLASIKEVLGDAATDELISAWAAAYGQLAdILIGMESK 138
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 13-146 1.28e-06

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: 45.11  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  13 LVKESWEILKQDIPKYSLH-------FFSQILEIAPAAKGLFSFLRDSDevpHNNPKLKAHAVKVFKMTCETAIQLReeg 85
Cdd:cd14778   1 LDQQTIEIIKSTVPVLKEHgveitteFYKNMFTEYPEVRPMFDMEKQKS---GEQPKALAMTVLAAAQNIENLEKIR--- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228313  86 kvvvadTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd14778  75 ------PAVEKIGKTHVNLNVKPEHYPIVGACLLGAIKEVLGDTATDEILEAWEKAYGEIA 129
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 7-155 6.45e-06

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: 43.21  E-value: 6.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSflrDSDEVPHNNPKLKAHAVKVFKMTCEtaiQLREEGK 86
Cdd:cd14780   2 SPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFN---QAHQASGAQPRALANAVLAYARHID---RLEVLGG 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  87 VVVAdttlqyLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA-LAIKTEMKQ 155
Cdd:cd14780  76 AVSL------IVNKHVSLNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLAdLLIAAEEAV 139
PRK13289 PRK13289
NO-inducible flavohemoprotein;
110-146 5.27e-05

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 42.09  E-value: 5.27e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15228313  110 HFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:PRK13289  94 HYPIVGEHLLAAIREVLGDAATDEVLDAWGEAYGVLA 130
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 7-140 2.54e-04

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: 39.05  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDSD--EVPHNNPKLKAHAVKVFKMTCETAIQLREE 84
Cdd:cd08924   2 TEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEdpLEMERSSQLRKHARRVMGALNTVVENLHDP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228313  85 GKVvvaDTTLQYLGSIHLKSGVIDP-HFEVVKEALLRTLKEGLGEKYNEEVEGAWSQ 140
Cdd:cd08924  82 DKV---SSVLALVGKAHALKHKVEPvYFKILSGVILEVLAEEFAQDFTPEVQSAWSK 135
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 15-135 2.63e-04

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: 38.84  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313  15 KESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSF---LRDSDEVPHNNPKLKAHAVKVFKmTCETAIQLREEgkvvvAD 91
Cdd:cd14766   2 KKSWKGIARKIDETGKTMFLRMLTENPELKELFPKlknLEDEEDELRSSEILENHAARVMD-TLDEAISNIEN-----VD 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15228313  92 TTLQYL---GSIHLKSGVIDP-HFEVVKEALLRTLKEGLGEKYNEEVE 135
Cdd:cd14766  76 YVIDLLhkvGKMHAKKPGFRPeMFWKIEEPFLEAVSETLGDRYTDNME 123
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 8-146 9.13e-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: 271316  Cd Length: 140  Bit Score: 37.44  E-value: 9.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   8 EKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSFLRDsdevpHNNPKLKAHAVKVfkmtCETAIQLReegKV 87
Cdd:cd14783   3 QKTIDIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQ-----HSGSQQRALAAAI----CAYAANID---NL 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228313  88 VVADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd14783  71 EVLGNAVELIAQKHASLGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLA 129
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 7-146 4.62e-03

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: 35.40  E-value: 4.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAAKGLFSflrdsdevpHNNPKL----KAHAVKVFkmtcETAIQLR 82
Cdd:cd14777   2 SEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFN---------QTNQKKglqqTALANTVY----AAAKHID 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228313  83 EEGKVVVAdttLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd14777  69 NLEVILPV---VKQIAHKHRALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEKAYGVIA 129
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 101-146 4.98e-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: 35.14  E-value: 4.98e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15228313 101 HLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA 146
Cdd:cd14781  83 HVGLHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLA 128
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 7-146 6.43e-03

Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development.


Pssm-ID: 381294  Cd Length: 141  Bit Score: 35.00  E-value: 6.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228313   7 TEKQEALVKESWEILKQDIPKYSLHFFSQILEIAPAakgLFSFLRDSDEVPHNNPKLKAHAVKVFKMTCETAIQLREEGK 86
Cdd:cd19754   2 TPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRYPE---VKPYFNETNQKLLRQPKILAFALLQYAKNIDDLTPLSGFVE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15228313  87 VVVadttlqylgSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKY-NEEVEGAWSQAYDHLA 146
Cdd:cd19754  79 QIV---------SKHVGLQVKPEHYPIVGECLIETMKELLPEAVaTDEFIEAWTTAYGNLA 130
FHb-globin_2 cd14782
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 90-152 6.79e-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: 381290  Cd Length: 143  Bit Score: 35.07  E-value: 6.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228313  90 ADTTLQYLGSIHLKSGVIDPHFEVVKEALLRTLKEGLGEKYNEEVEGAWSQAYDHLA-LAIKTE 152
Cdd:cd14782  76 PDSVLSRIAHKHASLGITPEQYTIVHRHLFAAIAEVLGAAVTPEVAAAWDEVYWLMAdQLIATE 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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