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Conserved domains on  [gi|1958775437|ref|XP_038965485|]
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tetratricopeptide repeat protein 39A isoform X4 [Rattus norvegicus]

Protein Classification

tetratricopeptide repeat protein 39( domain architecture ID 12104540)

tetratricopeptide repeat (TPR) protein 39 such as human TTC39B, which promotes the ubiquitination and degradation of liver X receptor

Graphical summary

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List of domain hits

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 ...
1-455 0e+00

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: 636.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437   1 MTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQSLCQRHRRKSSVTDSFSSL 80
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKAQVNESIQNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437  81 VHRptidQFTEEEIHAEVCYAECLLQRAALTFlQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYSKG---------- 150
Cdd:pfam10300  81 DTS----QLYEPGTHAEVCYAECLLLKAALTF-QDESLVSFIKGGYKLRKAYQIYKECLKLINDPQQTKRsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 151 ------ESHRHFEGGVKLGVGAFNLTLSMLPTRILRLLEFVGFSGNKDYGLLQLEEGATGHSFRAVLCVMLLLCYHTFLT 224
Cdd:pfam10300 156 ndnnqaEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 225 FVLGT--GNVNIEEAEKLLKPYLNRYPKGAIFLFFAGRIEAIKGNIDAAVRRFEECCEAQQHWKQFHHMCYWELMWCFTY 302
Cdd:pfam10300 236 QVLGIpgGEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 303 KGQWKMAYFYADLLSKENSWSKATYIYMKAAYLSMFGKEDYKPFG-DDEVELFRAVPGLKLKIAGKSLPTEKFAIRKSRR 381
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775437 382 YLSPNP--ISLPIPALEMMYIWNGYAVIGKQQKLTDGMLAVITKAeemLAMGPENE-YSADDDCLVKLLKGLCLKYL 455
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA---LKANPTSEaQEPDDKCLKQLLKGLCLRHL 469
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
421-515 6.15e-07

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: 48.06  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 421 ITKAEEMLAMGPENEYSADddclVKLLKGLCLKYLGRIQEAEENFRSISANEKkikyDHYLIPNALLELALLFMEQGRNE 500
Cdd:COG1729    13 IAAFKAFLKRYPNSPLAPD----ALYWLGEAYYALGDYDEAAEAFEKLLKRYP----DSPKAPDALLKLGLSYLELGDYD 84
                          90
                  ....*....|....*
gi 1958775437 501 EAIKLLDSAKQNYKN 515
Cdd:COG1729    85 KARATLEELIKKYPD 99
 
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 ...
1-455 0e+00

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: 636.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437   1 MTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQSLCQRHRRKSSVTDSFSSL 80
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKAQVNESIQNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437  81 VHRptidQFTEEEIHAEVCYAECLLQRAALTFlQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYSKG---------- 150
Cdd:pfam10300  81 DTS----QLYEPGTHAEVCYAECLLLKAALTF-QDESLVSFIKGGYKLRKAYQIYKECLKLINDPQQTKRsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 151 ------ESHRHFEGGVKLGVGAFNLTLSMLPTRILRLLEFVGFSGNKDYGLLQLEEGATGHSFRAVLCVMLLLCYHTFLT 224
Cdd:pfam10300 156 ndnnqaEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 225 FVLGT--GNVNIEEAEKLLKPYLNRYPKGAIFLFFAGRIEAIKGNIDAAVRRFEECCEAQQHWKQFHHMCYWELMWCFTY 302
Cdd:pfam10300 236 QVLGIpgGEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 303 KGQWKMAYFYADLLSKENSWSKATYIYMKAAYLSMFGKEDYKPFG-DDEVELFRAVPGLKLKIAGKSLPTEKFAIRKSRR 381
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775437 382 YLSPNP--ISLPIPALEMMYIWNGYAVIGKQQKLTDGMLAVITKAeemLAMGPENE-YSADDDCLVKLLKGLCLKYL 455
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA---LKANPTSEaQEPDDKCLKQLLKGLCLRHL 469
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
421-515 6.15e-07

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: 48.06  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 421 ITKAEEMLAMGPENEYSADddclVKLLKGLCLKYLGRIQEAEENFRSISANEKkikyDHYLIPNALLELALLFMEQGRNE 500
Cdd:COG1729    13 IAAFKAFLKRYPNSPLAPD----ALYWLGEAYYALGDYDEAAEAFEKLLKRYP----DSPKAPDALLKLGLSYLELGDYD 84
                          90
                  ....*....|....*
gi 1958775437 501 EAIKLLDSAKQNYKN 515
Cdd:COG1729    85 KARATLEELIKKYPD 99
TPR_12 pfam13424
Tetratricopeptide repeat;
440-515 6.74e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.22  E-value: 6.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775437 440 DDCLVKLLKGLCLKYLGRIQEAEENF-RSISANEKKIKYDHYLIPNALLELALLFMEQGRNEEAIKLLDSAKQNYKN 515
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLeKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
375-516 3.20e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 375 AIRKSRRYLSPNPislpipalEMMYIWNGYAVIGKQQKLTDGMLAVITKAeemLAMGPENEYsadddclVKLLKGLCLKY 454
Cdd:COG4783    23 AEALLEKALELDP--------DNPEAFALLGEILLQLGDLDEAIVLLHEA---LELDPDEPE-------ARLNLGLALLK 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775437 455 LGRIQEAEENFRSISanekKIKYDHyliPNALLELALLFMEQGRNEEAIKLLDSAKQNYKNY 516
Cdd:COG4783    85 AGDYDEALALLEKAL----KLDPEH---PEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
 
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 ...
1-455 0e+00

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: 636.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437   1 MTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQSLCQRHRRKSSVTDSFSSL 80
Cdd:pfam10300   1 LQALDLFLNNKFEEALELLKPWSKNSMYHALGYSVVAFIQAMLTFEPEDIQQASEALKEAEQVCQRFRKKAQVNESIQNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437  81 VHRptidQFTEEEIHAEVCYAECLLQRAALTFlQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYSKG---------- 150
Cdd:pfam10300  81 DTS----QLYEPGTHAEVCYAECLLLKAALTF-QDESLVSFIKGGYKLRKAYQIYKECLKLINDPQQTKRsspgdsslsh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 151 ------ESHRHFEGGVKLGVGAFNLTLSMLPTRILRLLEFVGFSGNKDYGLLQLEEGATGHSFRAVLCVMLLLCYHTFLT 224
Cdd:pfam10300 156 ndnnqaEIDEFFESGVNLGFGIFNLMLSLLPPRILKLLEFIGFSGDREDGLRLLWEASKSPNIRAALALLTLLFYYTGVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 225 FVLGT--GNVNIEEAEKLLKPYLNRYPKGAIFLFFAGRIEAIKGNIDAAVRRFEECCEAQQHWKQFHHMCYWELMWCFTY 302
Cdd:pfam10300 236 QVLGIpgGEGPLEEAEALLLPYRKRYPNGALWLFFEARIESLKGNLDEALELFEECIESQSEWKQVHHLCYWELMWCLVF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 303 KGQWKMAYFYADLLSKENSWSKATYIYMKAAYLSMFGKEDYKPFG-DDEVELFRAVPGLKLKIAGKSLPTEKFAIRKSRR 381
Cdd:pfam10300 316 LHNWKQAANYFLLLVKESSWSHALYTYFAAACLLMLYREEEAPAAkERAVELFREVPTLKQKIAGKSLPLEKFAARKVQR 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775437 382 YLSPNP--ISLPIPALEMMYIWNGYAVIGKQQKLTDGMLAVITKAeemLAMGPENE-YSADDDCLVKLLKGLCLKYL 455
Cdd:pfam10300 396 FKARTPadAVLVSPLLELIYFWNGFSRMGKKPLLTESVLKLIEKA---LKANPTSEaQEPDDKCLKQLLKGLCLRHL 469
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
421-515 6.15e-07

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: 48.06  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 421 ITKAEEMLAMGPENEYSADddclVKLLKGLCLKYLGRIQEAEENFRSISANEKkikyDHYLIPNALLELALLFMEQGRNE 500
Cdd:COG1729    13 IAAFKAFLKRYPNSPLAPD----ALYWLGEAYYALGDYDEAAEAFEKLLKRYP----DSPKAPDALLKLGLSYLELGDYD 84
                          90
                  ....*....|....*
gi 1958775437 501 EAIKLLDSAKQNYKN 515
Cdd:COG1729    85 KARATLEELIKKYPD 99
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
419-507 3.28e-05

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 45.64  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 419 AVITKAEEMLAMGPENEYSAdddclVKLLKGLCLKYLGRIQEAEENFRSISAnekkikydHYLIPNALLELALLFMEQGR 498
Cdd:COG4700   142 EALETLEKLIAKNPDFKSSD-----AHLLYARALEALGDLEAAEAELEALAR--------RYSGPEARYRYAKFLARQGR 208

                  ....*....
gi 1958775437 499 NEEAIKLLD 507
Cdd:COG4700   209 TAEAKELLE 217
TPR_12 pfam13424
Tetratricopeptide repeat;
440-515 6.74e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.22  E-value: 6.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775437 440 DDCLVKLLKGLCLKYLGRIQEAEENF-RSISANEKKIKYDHYLIPNALLELALLFMEQGRNEEAIKLLDSAKQNYKN 515
Cdd:pfam13424   1 DVATALNNLAAVLRRLGRYDEALELLeKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
446-517 3.34e-04

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 39.24  E-value: 3.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775437 446 LLKGLCLKYLGRIQEAEENFRSISANEKkikyDHYLIPNALLELALLFMEQGRNEEAIKLLDSAKQNYKNYS 517
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFP----ESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
449-509 2.42e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.75  E-value: 2.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775437 449 GLCLKYLGRIQEAEENFRSISAnekkIKYDHyliPNALLELALLFMEQGRNEEAIKLLDSA 509
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALA----LNPDF---AEAYLNLGEALRRLGRLEEAIAALRRA 172
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
449-512 2.45e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958775437 449 GLCLKYLGRIQEAEENFRSISANEKKikydhyliPNALLELALLFMEQGRNEEAIKLLDSAKQN 512
Cdd:COG3063    33 GLLLLEQGRYDEAIALEKALKLDPNN--------AEALLNLAELLLELGDYDEALAYLERALEL 88
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
456-526 3.03e-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: 37.66  E-value: 3.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775437 456 GRIQEAEENFRSISANEKkikyDHYLIPNALLELALLFMEQGRNEEAIKLLDSAKQNYKNYSMESRTHFRI 526
Cdd:COG1729     7 GDYDEAIAAFKAFLKRYP----NSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKL 73
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
375-516 3.20e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 38.25  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775437 375 AIRKSRRYLSPNPislpipalEMMYIWNGYAVIGKQQKLTDGMLAVITKAeemLAMGPENEYsadddclVKLLKGLCLKY 454
Cdd:COG4783    23 AEALLEKALELDP--------DNPEAFALLGEILLQLGDLDEAIVLLHEA---LELDPDEPE-------ARLNLGLALLK 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775437 455 LGRIQEAEENFRSISanekKIKYDHyliPNALLELALLFMEQGRNEEAIKLLDSAKQNYKNY 516
Cdd:COG4783    85 AGDYDEALALLEKAL----KLDPEH---PEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
448-509 9.85e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775437 448 KGLCLKYLGRIQEAEENFrsisanEKKIKYDHYLiPNALLELALLFMEQGRNEEAIKLLDSA 509
Cdd:COG0457    82 LGLALQALGRYEEALEDY------DKALELDPDD-AEALYNLGLALLELGRYDEAIEAYERA 136
 
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.
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