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Conserved domains on  [gi|145360169|ref|NP_179693|]
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lipid-binding protein [Arabidopsis thaliana]

Protein Classification

Tim44 domain-containing protein( domain architecture ID 709172)

Tim44 domain-containing protein similar to mitochondrial 39S ribosomal protein L45 and to mitochondrial import inner membrane translocase subunit Tim44, an essential component of the eukaryotic PAM complex which is required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner

Gene Ontology:  GO:0030150|GO:0001405|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
3a0801s03tim44 super family cl27183
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 143-344 1.62e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


The actual alignment was detected with superfamily member TIGR00984:

Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 39.86  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  143 VREQVEKMKELVEDGKKRVTVMQNIIHS-VLETQRKEWgefldelsKDGKKTMTELDGMICSQLGTLRDNMRHNVDEIWQ 221
Cdd:TIGR00984   3 FRDELQKSQELQESIKQLQDRSGKLNESdALKKARKAY--------EKAESGTLKSSEVVGKTLGKLGDTMKKMAHKAWE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  222 ElrdELRSKVDEDIKASRQDLNKDVKSVADQLRET--YLAVQETIKEAKTHETYLINQNNRRVIRGEDVEGFTELREQVQ 299
Cdd:TIGR00984  75 S---ELGKKMKKAGAETAKTAAEHVDKSAEPVRDTavYKHVSQSMKDGKDSSRYGFIADKEQRRRPRELTKRTDGRDFAK 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 145360169  300 QLAFEAEitaEELSSATVELVEAGIEQWEedNFDYITTLRHMYLD 344
Cdd:TIGR00984 152 SRVVEAN---ESVTDVVLHSDSSWYSKVE--DFKESNVVYRKIQE 191
 
Name Accession Description Interval E-value
3a0801s03tim44 TIGR00984
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 143-344 1.62e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 39.86  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  143 VREQVEKMKELVEDGKKRVTVMQNIIHS-VLETQRKEWgefldelsKDGKKTMTELDGMICSQLGTLRDNMRHNVDEIWQ 221
Cdd:TIGR00984   3 FRDELQKSQELQESIKQLQDRSGKLNESdALKKARKAY--------EKAESGTLKSSEVVGKTLGKLGDTMKKMAHKAWE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  222 ElrdELRSKVDEDIKASRQDLNKDVKSVADQLRET--YLAVQETIKEAKTHETYLINQNNRRVIRGEDVEGFTELREQVQ 299
Cdd:TIGR00984  75 S---ELGKKMKKAGAETAKTAAEHVDKSAEPVRDTavYKHVSQSMKDGKDSSRYGFIADKEQRRRPRELTKRTDGRDFAK 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 145360169  300 QLAFEAEitaEELSSATVELVEAGIEQWEedNFDYITTLRHMYLD 344
Cdd:TIGR00984 152 SRVVEAN---ESVTDVVLHSDSSWYSKVE--DFKESNVVYRKIQE 191
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 144-267 4.27e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 37.63  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  144 REQV-EKMKELVEDGKKRVTVMQNIIHSVLETQRKEWGEFLDELSKDGKKTMTELDGMICSQLGTLRDNMRHNVDEI--- 219
Cdd:pfam01442  39 RERLqKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALrar 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 145360169  220 WQELRDELRSKVDEDIKASRQDLNKDVKSVADQLRETYLAVQETIKEA 267
Cdd:pfam01442 119 LAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQ 166
 
Name Accession Description Interval E-value
3a0801s03tim44 TIGR00984
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 143-344 1.62e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 39.86  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  143 VREQVEKMKELVEDGKKRVTVMQNIIHS-VLETQRKEWgefldelsKDGKKTMTELDGMICSQLGTLRDNMRHNVDEIWQ 221
Cdd:TIGR00984   3 FRDELQKSQELQESIKQLQDRSGKLNESdALKKARKAY--------EKAESGTLKSSEVVGKTLGKLGDTMKKMAHKAWE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  222 ElrdELRSKVDEDIKASRQDLNKDVKSVADQLRET--YLAVQETIKEAKTHETYLINQNNRRVIRGEDVEGFTELREQVQ 299
Cdd:TIGR00984  75 S---ELGKKMKKAGAETAKTAAEHVDKSAEPVRDTavYKHVSQSMKDGKDSSRYGFIADKEQRRRPRELTKRTDGRDFAK 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 145360169  300 QLAFEAEitaEELSSATVELVEAGIEQWEedNFDYITTLRHMYLD 344
Cdd:TIGR00984 152 SRVVEAN---ESVTDVVLHSDSSWYSKVE--DFKESNVVYRKIQE 191
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 144-267 4.27e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 37.63  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360169  144 REQV-EKMKELVEDGKKRVTVMQNIIHSVLETQRKEWGEFLDELSKDGKKTMTELDGMICSQLGTLRDNMRHNVDEI--- 219
Cdd:pfam01442  39 RERLqKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALrar 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 145360169  220 WQELRDELRSKVDEDIKASRQDLNKDVKSVADQLRETYLAVQETIKEA 267
Cdd:pfam01442 119 LAPYAEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQELREKLEPQ 166
 
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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