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Conserved domains on  [gi|1039791024|ref|XP_017168516|]
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tumor suppressor candidate 3 isoform X3 [Mus musculus]

Protein Classification

OST3/OST6 family protein( domain architecture ID 10520659)

OST3/OST6 family protein similar to Homo sapiens magnesium transporter protein 1 and tumor suppressor candidate 3, which are required for cellular magnesium uptake and vertebrate embryonic development

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
54-295 1.70e-85

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


:

Pssm-ID: 461420  Cd Length: 294  Bit Score: 258.33  E-value: 1.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024  54 EQLMEWSSRRS-IFRMNGDKFRKFVKaPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYS-SAFCNKLFFGMV 131
Cdd:pfam04756   1 EELLSLAKKSNgVIKLNDSNYKRLLS-GPRDYSVVVLLTALDPRFGCQLCREFQPEFELVAKSWFKDhKAGSSKLFFATL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 132 DYDEGTDVFQQLNMNSAPTFMHFPSKGRPKRA----DTFDLQRIGFAAEQLAKWIADRTDVH------------------ 189
Cdd:pfam04756  80 DFDDGKDVFQSLGLQTAPHLLLFPPTGGPKISdsepDQYDFTRGGFSAEQLAAFLSRHTGVPipikrpinyskiiitfii 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 190 ------------------------------CIVFAMTSGQMWNHIRGPPYAHKNPhNGQVSYIHGSSQAQFVAESHIILV 239
Cdd:pfam04756 160 vlgvvtllkkarpyllpilqnrnlwaalslIFILLFTSGYMFNHIRGVPYVARDG-KGGISYFAGGSQNQFGIETQIVAA 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791024 240 LNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPY 295
Cdd:pfam04756 239 LYGLLALLVILLTIKVPRIKDPKVQRVAVIVWAGVLFLFFSFLLSVFRIKNPGYPF 294
 
Name Accession Description Interval E-value
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
54-295 1.70e-85

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 258.33  E-value: 1.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024  54 EQLMEWSSRRS-IFRMNGDKFRKFVKaPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYS-SAFCNKLFFGMV 131
Cdd:pfam04756   1 EELLSLAKKSNgVIKLNDSNYKRLLS-GPRDYSVVVLLTALDPRFGCQLCREFQPEFELVAKSWFKDhKAGSSKLFFATL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 132 DYDEGTDVFQQLNMNSAPTFMHFPSKGRPKRA----DTFDLQRIGFAAEQLAKWIADRTDVH------------------ 189
Cdd:pfam04756  80 DFDDGKDVFQSLGLQTAPHLLLFPPTGGPKISdsepDQYDFTRGGFSAEQLAAFLSRHTGVPipikrpinyskiiitfii 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 190 ------------------------------CIVFAMTSGQMWNHIRGPPYAHKNPhNGQVSYIHGSSQAQFVAESHIILV 239
Cdd:pfam04756 160 vlgvvtllkkarpyllpilqnrnlwaalslIFILLFTSGYMFNHIRGVPYVARDG-KGGISYFAGGSQNQFGIETQIVAA 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791024 240 LNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPY 295
Cdd:pfam04756 239 LYGLLALLVILLTIKVPRIKDPKVQRVAVIVWAGVLFLFFSFLLSVFRIKNPGYPF 294
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
73-183 8.22e-04

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 37.92  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024  73 FRKFVKAPPRnysMIVMFTAlqpqRQCSVCRQANEEYQILANSwryssafCNKLFFGMVDYDEGTDVFQQLNMNSAPTFM 152
Cdd:cd02947     3 FEELIKSAKP---VVVDFWA----PWCGPCKAIAPVLEELAEE-------YPKVKFVKVDVDENPELAEEYGVRSIPTFL 68
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039791024 153 HFpSKGrpKRADTFdlqrIGF-AAEQLAKWIA 183
Cdd:cd02947    69 FF-KNG--KEVDRV----VGAdPKEELEEFLE 93
 
Name Accession Description Interval E-value
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
54-295 1.70e-85

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 258.33  E-value: 1.70e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024  54 EQLMEWSSRRS-IFRMNGDKFRKFVKaPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYS-SAFCNKLFFGMV 131
Cdd:pfam04756   1 EELLSLAKKSNgVIKLNDSNYKRLLS-GPRDYSVVVLLTALDPRFGCQLCREFQPEFELVAKSWFKDhKAGSSKLFFATL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 132 DYDEGTDVFQQLNMNSAPTFMHFPSKGRPKRA----DTFDLQRIGFAAEQLAKWIADRTDVH------------------ 189
Cdd:pfam04756  80 DFDDGKDVFQSLGLQTAPHLLLFPPTGGPKISdsepDQYDFTRGGFSAEQLAAFLSRHTGVPipikrpinyskiiitfii 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024 190 ------------------------------CIVFAMTSGQMWNHIRGPPYAHKNPhNGQVSYIHGSSQAQFVAESHIILV 239
Cdd:pfam04756 160 vlgvvtllkkarpyllpilqnrnlwaalslIFILLFTSGYMFNHIRGVPYVARDG-KGGISYFAGGSQNQFGIETQIVAA 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791024 240 LNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPY 295
Cdd:pfam04756 239 LYGLLALLVILLTIKVPRIKDPKVQRVAVIVWAGVLFLFFSFLLSVFRIKNPGYPF 294
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
73-183 8.22e-04

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 37.92  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791024  73 FRKFVKAPPRnysMIVMFTAlqpqRQCSVCRQANEEYQILANSwryssafCNKLFFGMVDYDEGTDVFQQLNMNSAPTFM 152
Cdd:cd02947     3 FEELIKSAKP---VVVDFWA----PWCGPCKAIAPVLEELAEE-------YPKVKFVKVDVDENPELAEEYGVRSIPTFL 68
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039791024 153 HFpSKGrpKRADTFdlqrIGF-AAEQLAKWIA 183
Cdd:cd02947    69 FF-KNG--KEVDRV----VGAdPKEELEEFLE 93
 
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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