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Conserved domains on  [gi|17552758|ref|NP_499097|]
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Clustered mitochondria protein homolog [Caenorhabditis elegans]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11700348)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLU pfam13236
Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found ...
 355-578 1.18e-99

Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found in proteins from fungi, protozoa, plants to humans. It is required for correct functioning of the mitochondria and mitochondrial transport although the exact function of the domain is unknown. In Dictyostelium the full-length protein is required for a very late step in fission of the outer mitochondrial membrane suggesting that mitochondria are transported along microtubules, as in mammalian cells, rather than along actin filaments, as in budding yeast. Disruption of the protein-impaired cytokinesis and caused mitochondria to cluster at the cell centre. It is likely that CLU functions in a novel pathway that positions mitochondria within the cell based on their physiological state. Disruption of the CLU pathway may enhance oxidative damage, alter gene expression, cause mitochondria to cluster at microtubule plus ends, and lead eventually to mitochondrial failure.


:

Pssm-ID: 463814  Cd Length: 225  Bit Score: 316.03  E-value: 1.18e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    355 DWNEELQTTFEMTRKSISERVIRDRSYYKIHADYVNAAARGVQSILDGNILAINPGEDKKTHMYIWNNIFFSLGFDVRDH 434
Cdd:pfam13236    1 DWNEEFQSLRELPRETLQERLLRERLLSKLASDFVEAATKGAKAIIDGNVLPLNPKEPPGGHKYLYNNIFFSFAVDVRGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    435 YKELGGDAAAFAATSTDLQGVRAFATLDDPKLNTLGMAIFDYRGYRVTAQSIIPGILEREQEQ----SVVYGSIDFGKTV 510
Cdd:pfam13236   81 YPSLGGDEAARKAAGKDLKGVKALNRLDIPGLHTLLTAIVDYRGYRLIAQSILPGILSRDEETiekdTIVYGSSDGGKTV 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552758    511 VSDEKYHELLEDAAHKLKMLPHTVISEKDGVKEelkLYTSYEAKGIIGNDGRKYVLDLLRSMPPDVHY 578
Cdd:pfam13236  161 HSDEEFHELLKKIAKALNLKPHKVGDADGKPVE---LYGSADIKGIKGTDGRYYVLDLARLFPPDVNF 225
eIF3_p135 pfam12807
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a ...
 744-914 2.87e-53

Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a multi-subunit protein complex required for initiation of protein biosynthesis in eukaryotic cells. The complex promotes ribosome dissociation, the binding of the initiator methionyl-tRNA to the 40 S ribosomal subunit, and mRNA recruitment to the ribosome. The protein product from TIF31 genes in yeast is p135 which associates with the eIF3 but does not seem to be necessary for protein translation initiation.


:

Pssm-ID: 463717  Cd Length: 168  Bit Score: 183.93  E-value: 2.87e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    744 VVQPIDGDNLADIMHINGINIRYLGEIGKRLENSVSFAR-----PLVLSDIVARSAKHVIRKINVQITADQLSASTSHIL 818
Cdd:pfam12807    1 SSFPMDGQSLTEALHKRGINMRYLGKIAKKLSKSPNKARlehlkRLCVQEMIARAAKHILRKYLRGVPPPLLSAAVSHFL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    819 NCLFSVVLDPSPiaaNVAKKANKKNGKKRVTSAWSSLTTSALWNSIREDSASYYGYPIEADSLEkftelHDIQKTALFRR 898
Cdd:pfam12807   81 NCLLGSSLNPKP---TAEIDELLKGLYKKKNRAWAKLTPESLWEEIEQEVKSRFRYELPEDWVD-----SGLQKISLLRE 152

                          170
                   ....*....|....*.
gi 17552758    899 ICKVMGVQLVARDYQL 914
Cdd:pfam12807  153 ICLKTGIQLLAREYNF 168
CLU_N super family cl20917
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
 72-141 3.96e-11

Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.


The actual alignment was detected with superfamily member pfam15044:

Pssm-ID: 464466  Cd Length: 79  Bit Score: 59.97  E-value: 3.96e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552758     72 VQELYQTLLDREATCHRTCFSLY---LNGTAVDNYSEVRAI--PGFVDGCTLNVVDEPYTIRDARLHLRQVRELL 141
Cdd:pfam15044    5 VQDLRQVLSELPATKYLTNYHLEyqnGNGERLNEFVTLSEIieELDVDELKLQLKEKPYTEREALEHVLRFREFI 79
TPR_12 pfam13424
Tetratricopeptide repeat;
1072-1147 2.45e-07

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 49.31  E-value: 2.45e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552758   1072 MAQIDANIGLILFTVQEFDTALKYLQSADAITKTIGEPRKLKTGLISNLIARTHAARGDFRAALVAEKETFAIYSE 1147
Cdd:pfam13424    2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
GSKIP_dom super family cl05054
GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to ...
 229-290 3.65e-04

GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to GSK3beta. It is also found as a short domain towards the N terminus in clustered mitochondria protein, also known as clueless in Drosophila, which is involved in proper cytoplasmic distribution of mitochondria.


The actual alignment was detected with superfamily member pfam05303:

Pssm-ID: 398795  Cd Length: 103  Bit Score: 41.03  E-value: 3.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552758    229 DVLYIDITTVENRIYHVTCCTRGFYVNNSQDGRFDPTVSNSNKtVYQSVIELLQNVSPGFKK 290
Cdd:pfam05303   30 GVAYINVTTLEGNRYCIELSAAGFRIVGYRYDCVDGESEDHTK-YYETLYALLDYISPLYRE 90
FxSxx_TPR super family cl48889
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 959-1154 2.06e-03

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


The actual alignment was detected with superfamily member NF040586:

Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 42.60  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758   959 SIGASREAYECIGESLNLM--TLVYGVMHPDMPQCLRALA---RLshvLGETGDALNNQHKAAVMSERLIGLDAGNTIIE 1033
Cdd:NF040586  446 SLGRYEEARELDEDTLERQrrVLGLGEDHPHTLMTAGGLGadlRA---LGRFREALELDEETLERHRRVFGEDHPRTLRA 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  1034 YINLA--HFAFG----ALLIpgsLRPLYRARylmNLVFGEKHPVMAQIDANIGLILFTVQEFDTALKYLQSA-DAITKTI 1106
Cdd:NF040586  523 ANNLAvsLRLLGdyreALEL---DREVLRRR---RRVLGPDHPRTLLSANNLARDLRELGRYAEALDLLEEAlERYREVL 596

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17552758  1107 GEPRKLKTglisnLIARTHAAR-----GDFRAALVAEKETFAIYSELYGPNHP 1154
Cdd:NF040586  597 GGPDHPDT-----LRAAKSLAValrraGRLEEALELAEDTYERYRRRFGPDHP 644
 
Name Accession Description Interval E-value
CLU pfam13236
Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found ...
 355-578 1.18e-99

Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found in proteins from fungi, protozoa, plants to humans. It is required for correct functioning of the mitochondria and mitochondrial transport although the exact function of the domain is unknown. In Dictyostelium the full-length protein is required for a very late step in fission of the outer mitochondrial membrane suggesting that mitochondria are transported along microtubules, as in mammalian cells, rather than along actin filaments, as in budding yeast. Disruption of the protein-impaired cytokinesis and caused mitochondria to cluster at the cell centre. It is likely that CLU functions in a novel pathway that positions mitochondria within the cell based on their physiological state. Disruption of the CLU pathway may enhance oxidative damage, alter gene expression, cause mitochondria to cluster at microtubule plus ends, and lead eventually to mitochondrial failure.


Pssm-ID: 463814  Cd Length: 225  Bit Score: 316.03  E-value: 1.18e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    355 DWNEELQTTFEMTRKSISERVIRDRSYYKIHADYVNAAARGVQSILDGNILAINPGEDKKTHMYIWNNIFFSLGFDVRDH 434
Cdd:pfam13236    1 DWNEEFQSLRELPRETLQERLLRERLLSKLASDFVEAATKGAKAIIDGNVLPLNPKEPPGGHKYLYNNIFFSFAVDVRGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    435 YKELGGDAAAFAATSTDLQGVRAFATLDDPKLNTLGMAIFDYRGYRVTAQSIIPGILEREQEQ----SVVYGSIDFGKTV 510
Cdd:pfam13236   81 YPSLGGDEAARKAAGKDLKGVKALNRLDIPGLHTLLTAIVDYRGYRLIAQSILPGILSRDEETiekdTIVYGSSDGGKTV 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552758    511 VSDEKYHELLEDAAHKLKMLPHTVISEKDGVKEelkLYTSYEAKGIIGNDGRKYVLDLLRSMPPDVHY 578
Cdd:pfam13236  161 HSDEEFHELLKKIAKALNLKPHKVGDADGKPVE---LYGSADIKGIKGTDGRYYVLDLARLFPPDVNF 225
eIF3_p135 pfam12807
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a ...
 744-914 2.87e-53

Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a multi-subunit protein complex required for initiation of protein biosynthesis in eukaryotic cells. The complex promotes ribosome dissociation, the binding of the initiator methionyl-tRNA to the 40 S ribosomal subunit, and mRNA recruitment to the ribosome. The protein product from TIF31 genes in yeast is p135 which associates with the eIF3 but does not seem to be necessary for protein translation initiation.


Pssm-ID: 463717  Cd Length: 168  Bit Score: 183.93  E-value: 2.87e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    744 VVQPIDGDNLADIMHINGINIRYLGEIGKRLENSVSFAR-----PLVLSDIVARSAKHVIRKINVQITADQLSASTSHIL 818
Cdd:pfam12807    1 SSFPMDGQSLTEALHKRGINMRYLGKIAKKLSKSPNKARlehlkRLCVQEMIARAAKHILRKYLRGVPPPLLSAAVSHFL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    819 NCLFSVVLDPSPiaaNVAKKANKKNGKKRVTSAWSSLTTSALWNSIREDSASYYGYPIEADSLEkftelHDIQKTALFRR 898
Cdd:pfam12807   81 NCLLGSSLNPKP---TAEIDELLKGLYKKKNRAWAKLTPESLWEEIEQEVKSRFRYELPEDWVD-----SGLQKISLLRE 152

                          170
                   ....*....|....*.
gi 17552758    899 ICKVMGVQLVARDYQL 914
Cdd:pfam12807  153 ICLKTGIQLLAREYNF 168
CLU-central cd15466
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the ...
 747-914 1.00e-45

An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation.


Pssm-ID: 271318  Cd Length: 159  Bit Score: 161.75  E-value: 1.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  747 PIDGDNLADIMHINGINIRYLGEIGKRLEN--SVSFARPLVLSDIVARSAKHVIRKINVQITADQLSASTSHILNCLFSV 824
Cdd:cd15466    1 PIDGASLTELLHRRGINMRYLGKVAELISKlpKLPHLKRLLLTEMVARAAKHILRAYLRSVPLAELSAAVAHFLNCLLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  825 VLDPSPIAANVAKKANKKngkkrvTSAWSSLTTSALWNSIREDSASYYGYPIEADSLEKftelhDIQKTALFRRICKVMG 904
Cdd:cd15466   81 SSNPAPSAEIDEELKPAA------DTSWASLTPSFLWKEIKKEVKKRFRYDLPEESLDE-----GLRKLSLLRELCLKVG 149

                        170
                 ....*....|
gi 17552758  905 VQLVARDYQL 914
Cdd:cd15466  150 IQLLARDYDF 159
CLU_N pfam15044
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
 72-141 3.96e-11

Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.


Pssm-ID: 464466  Cd Length: 79  Bit Score: 59.97  E-value: 3.96e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552758     72 VQELYQTLLDREATCHRTCFSLY---LNGTAVDNYSEVRAI--PGFVDGCTLNVVDEPYTIRDARLHLRQVRELL 141
Cdd:pfam15044    5 VQDLRQVLSELPATKYLTNYHLEyqnGNGERLNEFVTLSEIieELDVDELKLQLKEKPYTEREALEHVLRFREFI 79
TPR_12 pfam13424
Tetratricopeptide repeat;
1072-1147 2.45e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 49.31  E-value: 2.45e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552758   1072 MAQIDANIGLILFTVQEFDTALKYLQSADAITKTIGEPRKLKTGLISNLIARTHAARGDFRAALVAEKETFAIYSE 1147
Cdd:pfam13424    2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
GSKIP_dom pfam05303
GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to ...
 229-290 3.65e-04

GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to GSK3beta. It is also found as a short domain towards the N terminus in clustered mitochondria protein, also known as clueless in Drosophila, which is involved in proper cytoplasmic distribution of mitochondria.


Pssm-ID: 398795  Cd Length: 103  Bit Score: 41.03  E-value: 3.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552758    229 DVLYIDITTVENRIYHVTCCTRGFYVNNSQDGRFDPTVSNSNKtVYQSVIELLQNVSPGFKK 290
Cdd:pfam05303   30 GVAYINVTTLEGNRYCIELSAAGFRIVGYRYDCVDGESEDHTK-YYETLYALLDYISPLYRE 90
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 959-1154 2.06e-03

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 42.60  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758   959 SIGASREAYECIGESLNLM--TLVYGVMHPDMPQCLRALA---RLshvLGETGDALNNQHKAAVMSERLIGLDAGNTIIE 1033
Cdd:NF040586  446 SLGRYEEARELDEDTLERQrrVLGLGEDHPHTLMTAGGLGadlRA---LGRFREALELDEETLERHRRVFGEDHPRTLRA 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  1034 YINLA--HFAFG----ALLIpgsLRPLYRARylmNLVFGEKHPVMAQIDANIGLILFTVQEFDTALKYLQSA-DAITKTI 1106
Cdd:NF040586  523 ANNLAvsLRLLGdyreALEL---DREVLRRR---RRVLGPDHPRTLLSANNLARDLRELGRYAEALDLLEEAlERYREVL 596

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17552758  1107 GEPRKLKTglisnLIARTHAAR-----GDFRAALVAEKETFAIYSELYGPNHP 1154
Cdd:NF040586  597 GGPDHPDT-----LRAAKSLAValrraGRLEEALELAEDTYERYRRRFGPDHP 644
 
Name Accession Description Interval E-value
CLU pfam13236
Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found ...
 355-578 1.18e-99

Clustered mitochondria; The CLU domain (CLUstered mitochondria) is a eukaryotic domain found in proteins from fungi, protozoa, plants to humans. It is required for correct functioning of the mitochondria and mitochondrial transport although the exact function of the domain is unknown. In Dictyostelium the full-length protein is required for a very late step in fission of the outer mitochondrial membrane suggesting that mitochondria are transported along microtubules, as in mammalian cells, rather than along actin filaments, as in budding yeast. Disruption of the protein-impaired cytokinesis and caused mitochondria to cluster at the cell centre. It is likely that CLU functions in a novel pathway that positions mitochondria within the cell based on their physiological state. Disruption of the CLU pathway may enhance oxidative damage, alter gene expression, cause mitochondria to cluster at microtubule plus ends, and lead eventually to mitochondrial failure.


Pssm-ID: 463814  Cd Length: 225  Bit Score: 316.03  E-value: 1.18e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    355 DWNEELQTTFEMTRKSISERVIRDRSYYKIHADYVNAAARGVQSILDGNILAINPGEDKKTHMYIWNNIFFSLGFDVRDH 434
Cdd:pfam13236    1 DWNEEFQSLRELPRETLQERLLRERLLSKLASDFVEAATKGAKAIIDGNVLPLNPKEPPGGHKYLYNNIFFSFAVDVRGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    435 YKELGGDAAAFAATSTDLQGVRAFATLDDPKLNTLGMAIFDYRGYRVTAQSIIPGILEREQEQ----SVVYGSIDFGKTV 510
Cdd:pfam13236   81 YPSLGGDEAARKAAGKDLKGVKALNRLDIPGLHTLLTAIVDYRGYRLIAQSILPGILSRDEETiekdTIVYGSSDGGKTV 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552758    511 VSDEKYHELLEDAAHKLKMLPHTVISEKDGVKEelkLYTSYEAKGIIGNDGRKYVLDLLRSMPPDVHY 578
Cdd:pfam13236  161 HSDEEFHELLKKIAKALNLKPHKVGDADGKPVE---LYGSADIKGIKGTDGRYYVLDLARLFPPDVNF 225
eIF3_p135 pfam12807
Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a ...
 744-914 2.87e-53

Translation initiation factor eIF3 subunit 135; Translation initiation factor eIF3 is a multi-subunit protein complex required for initiation of protein biosynthesis in eukaryotic cells. The complex promotes ribosome dissociation, the binding of the initiator methionyl-tRNA to the 40 S ribosomal subunit, and mRNA recruitment to the ribosome. The protein product from TIF31 genes in yeast is p135 which associates with the eIF3 but does not seem to be necessary for protein translation initiation.


Pssm-ID: 463717  Cd Length: 168  Bit Score: 183.93  E-value: 2.87e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    744 VVQPIDGDNLADIMHINGINIRYLGEIGKRLENSVSFAR-----PLVLSDIVARSAKHVIRKINVQITADQLSASTSHIL 818
Cdd:pfam12807    1 SSFPMDGQSLTEALHKRGINMRYLGKIAKKLSKSPNKARlehlkRLCVQEMIARAAKHILRKYLRGVPPPLLSAAVSHFL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758    819 NCLFSVVLDPSPiaaNVAKKANKKNGKKRVTSAWSSLTTSALWNSIREDSASYYGYPIEADSLEkftelHDIQKTALFRR 898
Cdd:pfam12807   81 NCLLGSSLNPKP---TAEIDELLKGLYKKKNRAWAKLTPESLWEEIEQEVKSRFRYELPEDWVD-----SGLQKISLLRE 152

                          170
                   ....*....|....*.
gi 17552758    899 ICKVMGVQLVARDYQL 914
Cdd:pfam12807  153 ICLKTGIQLLAREYNF 168
CLU-central cd15466
An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the ...
 747-914 1.00e-45

An uncharacterized central domain of CLU mitochondrial proteins; Mutations in the mitochondrial CLU proteins have been shown to result in clustered mitochondria. CLU proteins include Saccharomyces cerevisiae clustered mitochondria protein (Clu1p, alias translation initiation factor 31/TIF31p), Dictyostelium discoideum clustered mitochondria protein homolog (CluA), Caenorhabditis elegans clustered mitochondria protein homolog (CLUH/ Protein KIAA0664), Drosophila clueless (alias clustered mitochondria protein homolog), Arabidopsis clustered mitochondria protein (CLU, alias friendly mitochondria protein/FMT), and human clustered mitochondria protein homolog (CLUH). Dictyostelium CluA is involved in mitochondrial dynamics and is necessary for both, mitochondrial fission and fusion. Drosophila clueless is essential for cytoplasmic localization and function of cellular mitochondria. The Drosophila clu gene interacts genetically with parkin (park, the Drosophila ortholog of a human gene responsible for many familial cases of Parkinson's disease). Arabidopsis CLU/FMT is required for correct mitochondrial distribution and morphology. The specific role CLU proteins play in mitochondrial processes in not yet known. In an early study, S. cerevisiae Clu1/TIF31p was reported as sometimes being associated with the elF3 translation initiation factor. The authors noted, however, that its tentative assignment as a subunit of elf3 was uncertain, and to date there has been no direct evidence for a role of this protein in translation.


Pssm-ID: 271318  Cd Length: 159  Bit Score: 161.75  E-value: 1.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  747 PIDGDNLADIMHINGINIRYLGEIGKRLEN--SVSFARPLVLSDIVARSAKHVIRKINVQITADQLSASTSHILNCLFSV 824
Cdd:cd15466    1 PIDGASLTELLHRRGINMRYLGKVAELISKlpKLPHLKRLLLTEMVARAAKHILRAYLRSVPLAELSAAVAHFLNCLLGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  825 VLDPSPIAANVAKKANKKngkkrvTSAWSSLTTSALWNSIREDSASYYGYPIEADSLEKftelhDIQKTALFRRICKVMG 904
Cdd:cd15466   81 SSNPAPSAEIDEELKPAA------DTSWASLTPSFLWKEIKKEVKKRFRYDLPEESLDE-----GLRKLSLLRELCLKVG 149

                        170
                 ....*....|
gi 17552758  905 VQLVARDYQL 914
Cdd:cd15466  150 IQLLARDYDF 159
CLU_N pfam15044
Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, ...
 72-141 3.96e-11

Mitochondrial function, CLU-N-term; CLU_N is the N-terminal domain of the Clueless protein, also known as TIF31-like in other organizms. The function of this domain is not known. It family is found in association with pfam13236.


Pssm-ID: 464466  Cd Length: 79  Bit Score: 59.97  E-value: 3.96e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552758     72 VQELYQTLLDREATCHRTCFSLY---LNGTAVDNYSEVRAI--PGFVDGCTLNVVDEPYTIRDARLHLRQVRELL 141
Cdd:pfam15044    5 VQDLRQVLSELPATKYLTNYHLEyqnGNGERLNEFVTLSEIieELDVDELKLQLKEKPYTEREALEHVLRFREFI 79
TPR_12 pfam13424
Tetratricopeptide repeat;
1072-1147 2.45e-07

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 49.31  E-value: 2.45e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552758   1072 MAQIDANIGLILFTVQEFDTALKYLQSADAITKTIGEPRKLKTGLISNLIARTHAARGDFRAALVAEKETFAIYSE 1147
Cdd:pfam13424    2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR_10 pfam13374
Tetratricopeptide repeat;
1119-1154 2.18e-04

Tetratricopeptide repeat;


Pssm-ID: 463861 [Multi-domain]  Cd Length: 42  Bit Score: 39.79  E-value: 2.18e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 17552758   1119 NLIARTHAARGDFRAALVAEKETFAIYSELYGPNHP 1154
Cdd:pfam13374    6 NNLANALRAQGRYDEAEELLEEALAIRERVLGPDHP 41
GSKIP_dom pfam05303
GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to ...
 229-290 3.65e-04

GSKIP domain; This domain is found in GSK3-beta interaction protein (GSKIP), which binds to GSK3beta. It is also found as a short domain towards the N terminus in clustered mitochondria protein, also known as clueless in Drosophila, which is involved in proper cytoplasmic distribution of mitochondria.


Pssm-ID: 398795  Cd Length: 103  Bit Score: 41.03  E-value: 3.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552758    229 DVLYIDITTVENRIYHVTCCTRGFYVNNSQDGRFDPTVSNSNKtVYQSVIELLQNVSPGFKK 290
Cdd:pfam05303   30 GVAYINVTTLEGNRYCIELSAAGFRIVGYRYDCVDGESEDHTK-YYETLYALLDYISPLYRE 90
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 959-1154 2.06e-03

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 42.60  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758   959 SIGASREAYECIGESLNLM--TLVYGVMHPDMPQCLRALA---RLshvLGETGDALNNQHKAAVMSERLIGLDAGNTIIE 1033
Cdd:NF040586  446 SLGRYEEARELDEDTLERQrrVLGLGEDHPHTLMTAGGLGadlRA---LGRFREALELDEETLERHRRVFGEDHPRTLRA 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552758  1034 YINLA--HFAFG----ALLIpgsLRPLYRARylmNLVFGEKHPVMAQIDANIGLILFTVQEFDTALKYLQSA-DAITKTI 1106
Cdd:NF040586  523 ANNLAvsLRLLGdyreALEL---DREVLRRR---RRVLGPDHPRTLLSANNLARDLRELGRYAEALDLLEEAlERYREVL 596

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17552758  1107 GEPRKLKTglisnLIARTHAAR-----GDFRAALVAEKETFAIYSELYGPNHP 1154
Cdd:NF040586  597 GGPDHPDT-----LRAAKSLAValrraGRLEEALELAEDTYERYRRRFGPDHP 644
 
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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