NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1254044751|ref|NP_001343626|]
View 

Globin domain-containing protein [Caenorhabditis elegans]

Protein Classification

globin( domain architecture ID 10099307)

M-family globin similar to a variety of single-domain globins such as myoglobin and hemoglobin

CATH:  1.10.490.10
Gene Ontology:  GO:0019825|GO:0020037|GO:0005344|GO:0005506|GO:0015671
PubMed:  32863222|16061809|19281958|23209182
SCOP:  4000551

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 84-227 1.33e-16

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: 75.95  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254044751  84 RTHWIQLQKSNKQ-GLAIrgcFLTMLEKYPQVRPIWGFGKRIEgrgdetwkPEIVEDFYFRHHCASLQAALNMIIQNKDD 162
Cdd:cd01040     2 KSSWARVKKDKEEfGVAI---FLRLFEANPELKKLFPKFAGVD--------LDLKGSPEFKAHAKRVVGALDSLIDNLDD 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254044751 163 KSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSWICLLQTIRLHM 227
Cdd:cd01040    71 PEALDALLRKLGKRHKRRGVTPEHFEVFGEALLETLEEVL--GEAFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 84-227 1.33e-16

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: 75.95  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254044751  84 RTHWIQLQKSNKQ-GLAIrgcFLTMLEKYPQVRPIWGFGKRIEgrgdetwkPEIVEDFYFRHHCASLQAALNMIIQNKDD 162
Cdd:cd01040     2 KSSWARVKKDKEEfGVAI---FLRLFEANPELKKLFPKFAGVD--------LDLKGSPEFKAHAKRVVGALDSLIDNLDD 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254044751 163 KSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSWICLLQTIRLHM 227
Cdd:cd01040    71 PEALDALLRKLGKRHKRRGVTPEHFEVFGEALLETLEEVL--GEAFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 84-227 1.33e-16

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: 75.95  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254044751  84 RTHWIQLQKSNKQ-GLAIrgcFLTMLEKYPQVRPIWGFGKRIEgrgdetwkPEIVEDFYFRHHCASLQAALNMIIQNKDD 162
Cdd:cd01040     2 KSSWARVKKDKEEfGVAI---FLRLFEANPELKKLFPKFAGVD--------LDLKGSPEFKAHAKRVVGALDSLIDNLDD 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254044751 163 KSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSWICLLQTIRLHM 227
Cdd:cd01040    71 PEALDALLRKLGKRHKRRGVTPEHFEVFGEALLETLEEVL--GEAFTPEVEAAWRKLLDYIANAI 133
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 88-216 2.85e-03

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: 37.80  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254044751  88 IQLQKSNKQGLAIRGCFLT------MLEKYPQVRPIWGFGKRIEGRgdetwKPEivedfyfrhhcaSLQAALNMIIQNKD 161
Cdd:cd14778     6 IEIIKSTVPVLKEHGVEITtefyknMFTEYPEVRPMFDMEKQKSGE-----QPK------------ALAMTVLAAAQNIE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1254044751 162 DKSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSW 216
Cdd:cd14778    69 NLEKIRPAVEKIGKTHVNLNVKPEHYPIVGACLLGAIKEVL--GDTATDEILEAW 121
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 149-217 4.34e-03

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: 37.14  E-value: 4.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254044751 149 LQAALNMIIQNKDDKSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSWI 217
Cdd:cd12131    50 LMAMLVLVVKGLDDLEALLPALQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGL--GDEWTPEVKQAWT 116
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 147-217 5.93e-03

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: 36.45  E-value: 5.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254044751 147 ASLQAALNMIIQNKDDKSGMRRMLNEMGAHHFFYDACEPHFEVFQDSLLESMKLVLngGDSLDDDIEQSWI 217
Cdd:cd19753    43 DRLARALTHVVENLDDPDGLVPFLAQLGRDHRKYGVAPEHYPAVGAALLAALRHFA--GEAWTPELEAAWA 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH