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Conserved domains on  [gi|966980758|ref|XP_014967637|]
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tetratricopeptide repeat protein 39B-like [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Iml2-TPR_39 super family cl28743
Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to ...
40-477 2.22e-157

Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to humans, including fungal Inclusion body clearance protein Iml2 protein, animal tetratricopeptide repeat protein 39A/B/C (TT39A/B/C) and some uncharacterized proteins. Members of this family carry a tetratricopeptide repeat pfam07719 at their C terminus. This entry includes Iml2 and its paralogue-YKR018C from S. cerevisiae; Iml2 localizes to the cytoplasm and nucleus, and its expression is increased in response to DNA replication stress. It is found to be involved in lipid droplet-mediated inclusion body clearing after protein folding stress. In humans, TTC39A (also known as DEME6) is expressed in primary breast carcinomas but not in normal breast tissue, and has a putative eukaryotic RNP-1 RNA binding region and a candidate anchoring transmembrane domain. It is coordinately regulated with oestrogen receptor, but is not necessarily oestradiol-responsive. TTC39B has been linked to lipid metabolism.


The actual alignment was detected with superfamily member pfam10300:

Pssm-ID: 463047 [Multi-domain]  Cd Length: 469  Bit Score: 459.90  E-value: 2.22e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758   40 TTGLYLFLNNRFSDAINLIHPWSKNSMYHSLMYGILMVVKAILTFEPHDLQIGMMAAKDALKTCDNFRKKTkmtlSHLVS 119
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKA----QVNES 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  120 RQGI--TAITEEELHAEVCYAECLMLKSFMSlIQEESMLAFLKSGISVGSSYHIYKDCEQVLTQI--------------- 182
Cdd:pfam10300  77 IQNTdtSQLYEPGTHAEVCYAECLLLKAALT-FQDESLVSFIKGGYKLRKAYQIYKECLKLINDPqqtkrsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  183 -PDNHSKAHKHLVGGIKFGLGAFNLMLSLMPPKTLKLLNIIGYSGDREVGLALLHESASETHINNILSLLTLLFYYNYVY 261
Cdd:pfam10300 156 nDNNQAEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  262 VAFGVE--KVYNSATEDLFLVYLQKFPNCVIFKFFHARSSMLKGDFENAQLKLQECIFTQNEWKQVHHLCYWEFMWCHIL 339
Cdd:pfam10300 236 QVLGIPggEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  340 LQDWRQAYHYANLLSQHSRWSKAIYVYSKAITLALLPSDFVKSVS-EDMNSLFLKVESLKIKFLGSAVPIEKFVAEKGQR 418
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966980758  419 YGTTTG--WFTAQPLLEFIYAWSGFLVMSKKNELISSWLSIIDKGedLLQENPHKVYGTDD 477
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA--LKANPTSEAQEPDD 454
Ribosomal_L41 pfam05162
Ribosomal protein L41;
555-578 4.62e-09

Ribosomal protein L41;


:

Pssm-ID: 428342  Cd Length: 24  Bit Score: 51.90  E-value: 4.62e-09
                          10        20
                  ....*....|....*....|....
gi 966980758  555 VRAKWRKTRMHRLKCKRRKMRQKA 578
Cdd:pfam05162   1 MRAKWRKKRMRRLKRKRRKMRQRS 24
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
493-545 9.87e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.12  E-value: 9.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966980758 493 GKYSKAEYYFNCVIQKKKllkyDHYLVPYTYYELGILHYLKGDYDSATKNLDN 545
Cdd:COG1729    7 GDYDEAIAAFKAFLKRYP----NSPLAPDALYWLGEAYYALGDYDEAAEAFEK 55
 
Name Accession Description Interval E-value
Iml2-TPR_39 pfam10300
Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to ...
40-477 2.22e-157

Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to humans, including fungal Inclusion body clearance protein Iml2 protein, animal tetratricopeptide repeat protein 39A/B/C (TT39A/B/C) and some uncharacterized proteins. Members of this family carry a tetratricopeptide repeat pfam07719 at their C terminus. This entry includes Iml2 and its paralogue-YKR018C from S. cerevisiae; Iml2 localizes to the cytoplasm and nucleus, and its expression is increased in response to DNA replication stress. It is found to be involved in lipid droplet-mediated inclusion body clearing after protein folding stress. In humans, TTC39A (also known as DEME6) is expressed in primary breast carcinomas but not in normal breast tissue, and has a putative eukaryotic RNP-1 RNA binding region and a candidate anchoring transmembrane domain. It is coordinately regulated with oestrogen receptor, but is not necessarily oestradiol-responsive. TTC39B has been linked to lipid metabolism.


Pssm-ID: 463047 [Multi-domain]  Cd Length: 469  Bit Score: 459.90  E-value: 2.22e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758   40 TTGLYLFLNNRFSDAINLIHPWSKNSMYHSLMYGILMVVKAILTFEPHDLQIGMMAAKDALKTCDNFRKKTkmtlSHLVS 119
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKA----QVNES 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  120 RQGI--TAITEEELHAEVCYAECLMLKSFMSlIQEESMLAFLKSGISVGSSYHIYKDCEQVLTQI--------------- 182
Cdd:pfam10300  77 IQNTdtSQLYEPGTHAEVCYAECLLLKAALT-FQDESLVSFIKGGYKLRKAYQIYKECLKLINDPqqtkrsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  183 -PDNHSKAHKHLVGGIKFGLGAFNLMLSLMPPKTLKLLNIIGYSGDREVGLALLHESASETHINNILSLLTLLFYYNYVY 261
Cdd:pfam10300 156 nDNNQAEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  262 VAFGVE--KVYNSATEDLFLVYLQKFPNCVIFKFFHARSSMLKGDFENAQLKLQECIFTQNEWKQVHHLCYWEFMWCHIL 339
Cdd:pfam10300 236 QVLGIPggEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  340 LQDWRQAYHYANLLSQHSRWSKAIYVYSKAITLALLPSDFVKSVS-EDMNSLFLKVESLKIKFLGSAVPIEKFVAEKGQR 418
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966980758  419 YGTTTG--WFTAQPLLEFIYAWSGFLVMSKKNELISSWLSIIDKGedLLQENPHKVYGTDD 477
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA--LKANPTSEAQEPDD 454
Ribosomal_L41 pfam05162
Ribosomal protein L41;
555-578 4.62e-09

Ribosomal protein L41;


Pssm-ID: 428342  Cd Length: 24  Bit Score: 51.90  E-value: 4.62e-09
                          10        20
                  ....*....|....*....|....
gi 966980758  555 VRAKWRKTRMHRLKCKRRKMRQKA 578
Cdd:pfam05162   1 MRAKWRKKRMRRLKRKRRKMRQRS 24
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
493-545 9.87e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.12  E-value: 9.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966980758 493 GKYSKAEYYFNCVIQKKKllkyDHYLVPYTYYELGILHYLKGDYDSATKNLDN 545
Cdd:COG1729    7 GDYDEAIAAFKAFLKRYP----NSPLAPDALYWLGEAYYALGDYDEAAEAFEK 55
 
Name Accession Description Interval E-value
Iml2-TPR_39 pfam10300
Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to ...
40-477 2.22e-157

Iml2/Tetratricopeptide repeat protein 39; This is a family of proteins conserved from fungi to humans, including fungal Inclusion body clearance protein Iml2 protein, animal tetratricopeptide repeat protein 39A/B/C (TT39A/B/C) and some uncharacterized proteins. Members of this family carry a tetratricopeptide repeat pfam07719 at their C terminus. This entry includes Iml2 and its paralogue-YKR018C from S. cerevisiae; Iml2 localizes to the cytoplasm and nucleus, and its expression is increased in response to DNA replication stress. It is found to be involved in lipid droplet-mediated inclusion body clearing after protein folding stress. In humans, TTC39A (also known as DEME6) is expressed in primary breast carcinomas but not in normal breast tissue, and has a putative eukaryotic RNP-1 RNA binding region and a candidate anchoring transmembrane domain. It is coordinately regulated with oestrogen receptor, but is not necessarily oestradiol-responsive. TTC39B has been linked to lipid metabolism.


Pssm-ID: 463047 [Multi-domain]  Cd Length: 469  Bit Score: 459.90  E-value: 2.22e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758   40 TTGLYLFLNNRFSDAINLIHPWSKNSMYHSLMYGILMVVKAILTFEPHDLQIGMMAAKDALKTCDNFRKKTkmtlSHLVS 119
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKA----QVNES 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  120 RQGI--TAITEEELHAEVCYAECLMLKSFMSlIQEESMLAFLKSGISVGSSYHIYKDCEQVLTQI--------------- 182
Cdd:pfam10300  77 IQNTdtSQLYEPGTHAEVCYAECLLLKAALT-FQDESLVSFIKGGYKLRKAYQIYKECLKLINDPqqtkrsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  183 -PDNHSKAHKHLVGGIKFGLGAFNLMLSLMPPKTLKLLNIIGYSGDREVGLALLHESASETHINNILSLLTLLFYYNYVY 261
Cdd:pfam10300 156 nDNNQAEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  262 VAFGVE--KVYNSATEDLFLVYLQKFPNCVIFKFFHARSSMLKGDFENAQLKLQECIFTQNEWKQVHHLCYWEFMWCHIL 339
Cdd:pfam10300 236 QVLGIPggEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966980758  340 LQDWRQAYHYANLLSQHSRWSKAIYVYSKAITLALLPSDFVKSVS-EDMNSLFLKVESLKIKFLGSAVPIEKFVAEKGQR 418
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966980758  419 YGTTTG--WFTAQPLLEFIYAWSGFLVMSKKNELISSWLSIIDKGedLLQENPHKVYGTDD 477
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA--LKANPTSEAQEPDD 454
Ribosomal_L41 pfam05162
Ribosomal protein L41;
555-578 4.62e-09

Ribosomal protein L41;


Pssm-ID: 428342  Cd Length: 24  Bit Score: 51.90  E-value: 4.62e-09
                          10        20
                  ....*....|....*....|....
gi 966980758  555 VRAKWRKTRMHRLKCKRRKMRQKA 578
Cdd:pfam05162   1 MRAKWRKKRMRRLKRKRRKMRQRS 24
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
493-545 9.87e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.12  E-value: 9.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966980758 493 GKYSKAEYYFNCVIQKKKllkyDHYLVPYTYYELGILHYLKGDYDSATKNLDN 545
Cdd:COG1729    7 GDYDEAIAAFKAFLKRYP----NSPLAPDALYWLGEAYYALGDYDEAAEAFEK 55
 
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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