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Conserved domains on  [gi|482845558|ref|NP_001264820|]
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inactive peptidyl-prolyl cis-trans isomerase FKBP6 isoform 1 [Mus musculus]

Protein Classification

FKBP_C and TPR domain-containing protein( domain architecture ID 11991378)

FKBP_C and TPR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-140 6.84e-26

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 98.81  E-value: 6.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558   50 TVTPDASVLVKYSGYLEhMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRKGELARFLFKPAYAYGTLGC-PPLIP 128
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIP 82

                          90
                  ....*....|..
gi 482845558  129 PNATVLFEIELI 140
Cdd:pfam00254  83 PNATLVFEVELL 94
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-293 2.27e-07

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.16  E-value: 2.27e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-140 6.84e-26

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 98.81  E-value: 6.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558   50 TVTPDASVLVKYSGYLEhMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRKGELARFLFKPAYAYGTLGC-PPLIP 128
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIP 82

                          90
                  ....*....|..
gi 482845558  129 PNATVLFEIELI 140
Cdd:pfam00254  83 PNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 42-142 8.60e-23

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 91.01  E-value: 8.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558  42 IIREGTGDTVTPDASVLVKYSGYLehMD-KPFDSNCFRKTPRLMKLGED--ITlwGMELGLLSMRKGELARFLFKPAYAY 118
Cdd:COG0545    5 VLKEGTGAKPKAGDTVTVHYTGTL--LDgTVFDSSYDRGEPATFPLGVGqvIP--GWDEGLQGMKVGGKRRLVIPPELAY 80

                         90       100
                 ....*....|....*....|....
gi 482845558 119 GTLGCPPLIPPNATVLFEIELIDF 142
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 37-149 3.14e-11

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 62.86  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558  37 GVLKDIIREGTGDTVTPDASVLVKYSGYLehMD-KPFDSNCFRKTPRLMKLGEDITLWgmELGLLSMRKGELARFLFKPA 115
Cdd:PRK10902 147 GLLYKVEKEGTGEAPKDSDTVVVNYKGTL--IDgKEFDNSYTRGEPLSFRLDGVIPGW--TEGLKNIKKGGKIKLVIPPE 222

                         90       100       110
                 ....*....|....*....|....*....|....
gi 482845558 116 YAYGTLGCPPlIPPNATVLFEIELIDFLDSAESD 149
Cdd:PRK10902 223 LAYGKAGVPG-IPANSTLVFDVELLDVKPAPKAD 255
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-293 2.27e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.16  E-value: 2.27e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 229-284 4.50e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 38.38  E-value: 4.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 229 YLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:cd24142   10 LLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-140 6.84e-26

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 98.81  E-value: 6.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558   50 TVTPDASVLVKYSGYLEhMDKPFDSNCFRKTPRLMKLGEDITLWGMELGLLSMRKGELARFLFKPAYAYGTLGC-PPLIP 128
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIP 82

                          90
                  ....*....|..
gi 482845558  129 PNATVLFEIELI 140
Cdd:pfam00254  83 PNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 42-142 8.60e-23

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 91.01  E-value: 8.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558  42 IIREGTGDTVTPDASVLVKYSGYLehMD-KPFDSNCFRKTPRLMKLGED--ITlwGMELGLLSMRKGELARFLFKPAYAY 118
Cdd:COG0545    5 VLKEGTGAKPKAGDTVTVHYTGTL--LDgTVFDSSYDRGEPATFPLGVGqvIP--GWDEGLQGMKVGGKRRLVIPPELAY 80

                         90       100
                 ....*....|....*....|....
gi 482845558 119 GTLGCPPLIPPNATVLFEIELIDF 142
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 37-149 3.14e-11

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 62.86  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558  37 GVLKDIIREGTGDTVTPDASVLVKYSGYLehMD-KPFDSNCFRKTPRLMKLGEDITLWgmELGLLSMRKGELARFLFKPA 115
Cdd:PRK10902 147 GLLYKVEKEGTGEAPKDSDTVVVNYKGTL--IDgKEFDNSYTRGEPLSFRLDGVIPGW--TEGLKNIKKGGKIKLVIPPE 222

                         90       100       110
                 ....*....|....*....|....*....|....
gi 482845558 116 YAYGTLGCPPlIPPNATVLFEIELIDFLDSAESD 149
Cdd:PRK10902 223 LAYGKAGVPG-IPANSTLVFDVELLDVKPAPKAD 255
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-293 2.27e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.16  E-value: 2.27e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-303 2.61e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNELK 294
Cdd:COG0457   72 DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG 151


                 ....*....
gi 482845558 295 KLSSHYRDY 303
Cdd:COG0457  152 IALEKLGRY 160
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
216-284 2.16e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.55  E-value: 2.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 216 PAVLLVLLNLSFVYLKLDRPAMALRYgEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG3063   23 PDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 214-289 2.36e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 2.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 214 VEPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDI 289
Cdd:COG3914  141 LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADA 216
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-293 3.33e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.69  E-value: 3.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG0457   38 DPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 221-284 2.99e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.80  E-value: 2.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 482845558 221 VLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG5010   90 LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 228-293 3.83e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.41  E-value: 3.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 228 VYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG5010   63 LYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNL 128
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
215-283 6.72e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.46  E-value: 6.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQ 283
Cdd:COG0457  106 DPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAA 174
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
228-303 7.21e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 40.92  E-value: 7.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 228 VYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLvRAQKEQPCNHDINNELKKLSSHYRDY 303
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDY 75
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 221-284 1.03e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 482845558 221 VLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG4235   53 ALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLP 116
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 222-284 1.15e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 1.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482845558 222 LLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG4235   20 WLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDP 82
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 153-293 2.15e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558 153 ALSAEQQEQFPLQKVLKVAATEREFGNYLFRQNRFCDAKVRYkrallllhrrlatceeQHLVE--PAVLLVLLNLSFVYL 230
Cdd:COG3914   60 LALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALY----------------RRALAlnPDNAEALFNLGNLLL 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482845558 231 KLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG3914  124 ALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 215-284 2.16e-04

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: 40.56  E-value: 2.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558 215 EPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG4783   34 DPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDP 103
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 221-296 4.26e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.25  E-value: 4.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 221 VLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNELKKL 296
Cdd:COG2956  146 AYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL 221
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 214-291 9.58e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 9.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 482845558 214 VEPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINN 291
Cdd:COG2956  173 LDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLA 250
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 214-284 1.04e-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: 38.63  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 482845558 214 VEPAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:COG4783   67 LDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 211-293 1.63e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 39.71  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482845558 211 QHLVE--PAVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHD 288
Cdd:COG2956   66 QKLLErdPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAH 145


                 ....*
gi 482845558 289 INNEL 293
Cdd:COG2956  146 AYCEL 150
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 229-284 4.50e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 38.38  E-value: 4.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 482845558 229 YLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQP 284
Cdd:cd24142   10 LLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 217-293 8.47e-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: 35.94  E-value: 8.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 482845558 217 AVLLVLLNLSFVYLKLDRPAMALRYGEQALLIDKRNAKALFRCGQACLLLTEYERARDFLVRAQKEQPCNHDINNEL 293
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
 
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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