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Conserved domains on  [gi|1387264693|ref|XP_024846452|]
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limb region 1 protein homolog isoform X5 [Bos taurus]

Protein Classification

LMBR1 domain-containing protein( domain architecture ID 6330)

LMBR1 domain-containing protein similar to fungal lysosomal cobalamin transporter that is required to export cobalamin from lysosomes allowing its conversion to cofactors

Gene Ontology:  GO:0007165

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LMBR1 super family cl04754
LMBR1-like membrane protein; Members of this family are integral membrane proteins that are ...
 146-310 4.97e-25

LMBR1-like membrane protein; Members of this family are integral membrane proteins that are around 500 residues in length. LMBR1 is not involved in preaxial polydactyly, as originally thought. Vertebrate members of this family may play a role in limb development. Lysosomal cobalamin transport escort protein LMBD1 is a lysosomal membrane chaperone required to export cobalamin from lysosome to the cytosol, allowing its conversion to cofactors. A member of this family has been shown to be a lipocalin membrane receptor.


The actual alignment was detected with superfamily member pfam04791:

Pssm-ID: 461429  Cd Length: 471  Bit Score: 105.05  E-value: 4.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 146 SAWERNLVYPAVMVLL----LIETSISVLLVACNILCLLVDETAMPK-GTRGPGIGNASLSAFGFVGAAL-EIILIFYLM 219
Cdd:pfam04791 297 SKLTPTLEYYWYCLLLpyvlLILSVILALLSVIVVWSELTFFLIKPVlSLFALFIGLHASSSFGYFGIELiEIIFILYLC 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 220 VSSVVGFYSLRVFGNF-IPKKDDTTMTKIIGNCVSILVLSSalPVMSRTLGITRFD------LLGDFGRFNWLGnFYIVL 292
Cdd:pfam04791 377 LCAYSGLFKIKVFGFYrLVPHHQTDMNSLIFNAGLLLRLTS--PLCYNFLGLIHFDshiftqLLGHMDVLPFLG-FGFNI 453

                         170
                  ....*....|....*...
gi 1387264693 293 SYNLLFAIVTTLCLVRKF 310
Cdd:pfam04791 454 YFPIFILILCLATLFNLY 471
 
Name Accession Description Interval E-value
LMBR1 pfam04791
LMBR1-like membrane protein; Members of this family are integral membrane proteins that are ...
 146-310 4.97e-25

LMBR1-like membrane protein; Members of this family are integral membrane proteins that are around 500 residues in length. LMBR1 is not involved in preaxial polydactyly, as originally thought. Vertebrate members of this family may play a role in limb development. Lysosomal cobalamin transport escort protein LMBD1 is a lysosomal membrane chaperone required to export cobalamin from lysosome to the cytosol, allowing its conversion to cofactors. A member of this family has been shown to be a lipocalin membrane receptor.


Pssm-ID: 461429  Cd Length: 471  Bit Score: 105.05  E-value: 4.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 146 SAWERNLVYPAVMVLL----LIETSISVLLVACNILCLLVDETAMPK-GTRGPGIGNASLSAFGFVGAAL-EIILIFYLM 219
Cdd:pfam04791 297 SKLTPTLEYYWYCLLLpyvlLILSVILALLSVIVVWSELTFFLIKPVlSLFALFIGLHASSSFGYFGIELiEIIFILYLC 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 220 VSSVVGFYSLRVFGNF-IPKKDDTTMTKIIGNCVSILVLSSalPVMSRTLGITRFD------LLGDFGRFNWLGnFYIVL 292
Cdd:pfam04791 377 LCAYSGLFKIKVFGFYrLVPHHQTDMNSLIFNAGLLLRLTS--PLCYNFLGLIHFDshiftqLLGHMDVLPFLG-FGFNI 453

                         170
                  ....*....|....*...
gi 1387264693 293 SYNLLFAIVTTLCLVRKF 310
Cdd:pfam04791 454 YFPIFILILCLATLFNLY 471
 
Name Accession Description Interval E-value
LMBR1 pfam04791
LMBR1-like membrane protein; Members of this family are integral membrane proteins that are ...
 146-310 4.97e-25

LMBR1-like membrane protein; Members of this family are integral membrane proteins that are around 500 residues in length. LMBR1 is not involved in preaxial polydactyly, as originally thought. Vertebrate members of this family may play a role in limb development. Lysosomal cobalamin transport escort protein LMBD1 is a lysosomal membrane chaperone required to export cobalamin from lysosome to the cytosol, allowing its conversion to cofactors. A member of this family has been shown to be a lipocalin membrane receptor.


Pssm-ID: 461429  Cd Length: 471  Bit Score: 105.05  E-value: 4.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 146 SAWERNLVYPAVMVLL----LIETSISVLLVACNILCLLVDETAMPK-GTRGPGIGNASLSAFGFVGAAL-EIILIFYLM 219
Cdd:pfam04791 297 SKLTPTLEYYWYCLLLpyvlLILSVILALLSVIVVWSELTFFLIKPVlSLFALFIGLHASSSFGYFGIELiEIIFILYLC 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387264693 220 VSSVVGFYSLRVFGNF-IPKKDDTTMTKIIGNCVSILVLSSalPVMSRTLGITRFD------LLGDFGRFNWLGnFYIVL 292
Cdd:pfam04791 377 LCAYSGLFKIKVFGFYrLVPHHQTDMNSLIFNAGLLLRLTS--PLCYNFLGLIHFDshiftqLLGHMDVLPFLG-FGFNI 453

                         170
                  ....*....|....*...
gi 1387264693 293 SYNLLFAIVTTLCLVRKF 310
Cdd:pfam04791 454 YFPIFILILCLATLFNLY 471
 
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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