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Conserved domains on  [gi|17509143|ref|NP_492188|]
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Globin-like protein 26 [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

Graphical summary

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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) ...
35-161 1.06e-17

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: 75.18  E-value: 1.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509143  35 VRNAWRHMSqKGPSNCGSTITRRMMARKSTI-----------GDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQ 103
Cdd:cd01040   1 VKSSWARVK-KDKEEFGVAIFLRLFEANPELkklfpkfagvdLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17509143 104 EIGQKHAKYrrskGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQL 161
Cdd:cd01040  80 KLGKRHKRR----GVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
35-161 1.06e-17

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: 75.18  E-value: 1.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509143  35 VRNAWRHMSqKGPSNCGSTITRRMMARKSTI-----------GDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQ 103
Cdd:cd01040   1 VKSSWARVK-KDKEEFGVAIFLRLFEANPELkklfpkfagvdLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17509143 104 EIGQKHAKYrrskGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQL 161
Cdd:cd01040  80 KLGKRHKRR----GVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
77-161 2.61e-05

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 41.51  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509143    77 HNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAkyrRSKGMKIDYWDKLGEAITETIREYQGWKihRESLRAA-TVLVS 155
Cdd:pfam00042  37 HGKKVLAALGEAVKHLDDLAALNAALKKLGARHK---EKRGVDPANFKLFGEALLVVLAEHLGEF--TPETKAAwDKALD 111

                  ....*.
gi 17509143   156 YVVDQL 161
Cdd:pfam00042 112 VIAAAL 117
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
35-161 1.06e-17

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: 75.18  E-value: 1.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509143  35 VRNAWRHMSqKGPSNCGSTITRRMMARKSTI-----------GDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQ 103
Cdd:cd01040   1 VKSSWARVK-KDKEEFGVAIFLRLFEANPELkklfpkfagvdLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17509143 104 EIGQKHAKYrrskGMKIDYWDKLGEAITETIREYQGWKIHRESLRAATVLVSYVVDQL 161
Cdd:cd01040  80 KLGKRHKRR----GVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
77-161 2.61e-05

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 41.51  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509143    77 HNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAkyrRSKGMKIDYWDKLGEAITETIREYQGWKihRESLRAA-TVLVS 155
Cdd:pfam00042  37 HGKKVLAALGEAVKHLDDLAALNAALKKLGARHK---EKRGVDPANFKLFGEALLVVLAEHLGEF--TPETKAAwDKALD 111

                  ....*.
gi 17509143   156 YVVDQL 161
Cdd:pfam00042 112 VIAAAL 117
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
85-139 1.57e-04

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: 39.84  E-value: 1.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17509143  85 LQKVMQSLDEPDKISKLCQEIGQKHAKYrrskGMKIDYWDKLGEAITETIREYQG 139
Cdd:cd12131  54 LVLVVKGLDDLEALLPALQDLGRRHVKY----GVKPEHYPLVGEALLWTLEEGLG 104
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
58-135 2.91e-04

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: 39.20  E-value: 2.91e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17509143  58 MMARKSTIGDILDRSTLDYHNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYrrskGMKIDYWDKLGEAITETIR 135
Cdd:cd12137  43 FPFRDVDLEDLRHSKELRAHGLRVLSFVEKSLARLHQPDKLEELLHELGRKHYRY----NAKVKYVDLVGQQFIFAIE 116
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
74-133 9.86e-03

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: 34.99  E-value: 9.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509143  74 LDYHNLQIVEFLQKVMQSLDEPDKISKLCQEIGQKHAKYrrsKGMKIDYWDK----LGEAITET 133
Cdd:cd14766  53 LENHAARVMDTLDEAISNIENVDYVIDLLHKVGKMHAKK---PGFRPEMFWKieepFLEAVSET 113
 
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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