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Conserved domains on  [gi|193787436|dbj|BAG52642|]
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unnamed protein product [Homo sapiens]

Protein Classification

lipase maturation factor family protein( domain architecture ID 10535984)

lipase maturation factor family protein similar to vertebrate lipase maturation factor, which is involved in the maturation of specific proteins in the endoplasmic reticulum, and may be required for maturation and transport of active lipoprotein lipase through the secretory pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
1-308 8.46e-126

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


:

Pssm-ID: 462004  Cd Length: 419  Bit Score: 366.66  E-value: 8.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436    1 MDFHYETQPMPNPVAYYLHHSPWWFHRFETLSNHFIELLVPFFLFLG-RRACIIHGVLQILFQAVLIVSGNLSFLNWLTM 79
Cdd:pfam06762  70 LDYHYETQPLPTPLSWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTI 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436   80 VPSLACFDDATLGFLFPSGPG-----------SLKDRVLQMQRDIRGARPEPRF-----GSVVRRAANVSLGV-LLAWLS 142
Cdd:pfam06762 150 VLSLSLLDDAFLYFWTPESRKkpprtrllsviETLLSLLVYGLLIYGTVSLFGLkisenGTFLRRVTLPSIVLgLVSLLS 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  143 VPVVLNLLSSR-------------------------------QVMNTHFNSLHIVNTYGAFGSITKERAEVILQGTASSN 191
Cdd:pfam06762 230 VPVCALLRSNKliqsiqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  192 ASapdamWEDYEFKCKPGDPSRRPCLISPYHYRLDWLMWFAAFQTYEHNDWIIHLAGKLLASDAEALSLLAHNPFAGRpP 271
Cdd:pfam06762 310 GP-----WKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-P 383
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 193787436  272 PRWVRGEHYRYKFSRPgGRHAAEGKWWVRKRIGAYFP 308
Cdd:pfam06762 384 PKYVRAELYRYRFTTP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
1-308 8.46e-126

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


Pssm-ID: 462004  Cd Length: 419  Bit Score: 366.66  E-value: 8.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436    1 MDFHYETQPMPNPVAYYLHHSPWWFHRFETLSNHFIELLVPFFLFLG-RRACIIHGVLQILFQAVLIVSGNLSFLNWLTM 79
Cdd:pfam06762  70 LDYHYETQPLPTPLSWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTI 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436   80 VPSLACFDDATLGFLFPSGPG-----------SLKDRVLQMQRDIRGARPEPRF-----GSVVRRAANVSLGV-LLAWLS 142
Cdd:pfam06762 150 VLSLSLLDDAFLYFWTPESRKkpprtrllsviETLLSLLVYGLLIYGTVSLFGLkisenGTFLRRVTLPSIVLgLVSLLS 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  143 VPVVLNLLSSR-------------------------------QVMNTHFNSLHIVNTYGAFGSITKERAEVILQGTASSN 191
Cdd:pfam06762 230 VPVCALLRSNKliqsiqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  192 ASapdamWEDYEFKCKPGDPSRRPCLISPYHYRLDWLMWFAAFQTYEHNDWIIHLAGKLLASDAEALSLLAHNPFAGRpP 271
Cdd:pfam06762 310 GP-----WKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-P 383
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 193787436  272 PRWVRGEHYRYKFSRPgGRHAAEGKWWVRKRIGAYFP 308
Cdd:pfam06762 384 PKYVRAELYRYRFTTP-GERRATGAWWKRERVGEYFP 419
 
Name Accession Description Interval E-value
LMF1 pfam06762
Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation ...
1-308 8.46e-126

Lipase maturation factor; This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. It acts as a chaperone required for maturation and transport of active lipoprotein lipase (LPL), through the secretory pathway.


Pssm-ID: 462004  Cd Length: 419  Bit Score: 366.66  E-value: 8.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436    1 MDFHYETQPMPNPVAYYLHHSPWWFHRFETLSNHFIELLVPFFLFLG-RRACIIHGVLQILFQAVLIVSGNLSFLNWLTM 79
Cdd:pfam06762  70 LDYHYETQPLPTPLSWYAHQLPSWFHKLETLGNHVVELVVPFLFFAPiRRLRIVAFFIQVLLQLLIILTGNYGFLNLLTI 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436   80 VPSLACFDDATLGFLFPSGPG-----------SLKDRVLQMQRDIRGARPEPRF-----GSVVRRAANVSLGV-LLAWLS 142
Cdd:pfam06762 150 VLSLSLLDDAFLYFWTPESRKkpprtrllsviETLLSLLVYGLLIYGTVSLFGLkisenGTFLRRVTLPSIVLgLVSLLS 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  143 VPVVLNLLSSR-------------------------------QVMNTHFNSLHIVNTYGAFGSITKERAEVILQGTASSN 191
Cdd:pfam06762 230 VPVCALLRSNKliqsiqlaivtlaavllfalslvpfsvrnllSRMNASFNPLHLVNSYGLFGSMTGGRPEVVIEGSNDGE 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193787436  192 ASapdamWEDYEFKCKPGDPSRRPCLISPYHYRLDWLMWFAAFQTYEHNDWIIHLAGKLLASDAEALSLLAHNPFAGRpP 271
Cdd:pfam06762 310 GP-----WKEYEFKYKPGDVNRRPPFVAPYHPRLDWQMWFAALGTYQQNPWFLSLLYRLLQNDPEVLGLLDHNPFPDK-P 383
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 193787436  272 PRWVRGEHYRYKFSRPgGRHAAEGKWWVRKRIGAYFP 308
Cdd:pfam06762 384 PKYVRAELYRYRFTTP-GERRATGAWWKRERVGEYFP 419
 
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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