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Conserved domains on  [gi|808154180|ref|NP_001294872|]
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tetratricopeptide repeat protein 17 isoform 2 precursor [Homo sapiens]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11419012)

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

CATH:  1.25.40.10
Gene Ontology:  GO:0005515
PubMed:  10517866|30708253
SCOP:  3001345

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
610-736 5.60e-12

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 5.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457   36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457  111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 1.10e-06

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457   43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457  120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199
                        170       180
                 ....*....|....*....|..
gi 808154180 385 IQEEQILRNIIHETQMAKEAQL 406
Cdd:COG0457  200 LLALEQALRKKLAILTLAALAE 221
 
Name Accession Description Interval E-value
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
610-736 5.60e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 5.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457   36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457  111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 1.10e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457   43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457  120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199
                        170       180
                 ....*....|....*....|..
gi 808154180 385 IQEEQILRNIIHETQMAKEAQL 406
Cdd:COG0457  200 LLALEQALRKKLAILTLAALAE 221
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
573-738 1.97e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.54  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180  573 RMDLKAKMPDD--------------HARKIL-LSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGlYWRAVGNSTF 637
Cdd:TIGR02917 507 RIDIQEGNPDDaiqrfekvltidpkNLRAILaLAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQ-YYLGKGQLKK 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180  638 AIACLQRALNLAPLQYQDVPLvnLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:TIGR02917 586 ALAILNEAADAAPDSPEAWLM--LGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
                         170       180
                  ....*....|....*....|.
gi 808154180  718 LttkcpECENSLKLIRCMQFY 738
Cdd:TIGR02917 664 L-----KPDNTEAQIGLAQLL 679
TPR_12 pfam13424
Tetratricopeptide repeat;
658-721 7.71e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 7.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808154180  658 LVNLANLLIHYGLHLDATKLLLQALAINSSEP--------LTFLSLGNAYLALKNISGALEAFRQALKLTTK 721
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLLgpdhpltaTTLLNLGRLYLELGRYEEALELLERALALAEK 77
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
329-410 4.64e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 329 EQAIKRKHAVL--CQQKLEQKLEAQHRSLQRTLNELKE-YQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQ 405
Cdd:cd16269  207 AEAAEQERKLLeeQQRELEQKLEDQERSYEEHLRQLKEkMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286

                 ....*
gi 808154180 406 LGNHQ 410
Cdd:cd16269  287 IRSLK 291
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
689-718 1.53e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 37.04  E-value: 1.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 808154180   689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
297-328 6.82e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 6.82e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 808154180  297 SYYTLGNIYAMLGEYNHSVLCYDHALQARPGF 328
Cdd:pfam00515   3 ALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
Name Accession Description Interval E-value
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
610-736 5.60e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 5.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457   36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457  111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
610-729 7.48e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.57  E-value: 7.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457    2 ELDPDDAEAYNNL---GLAYRRLGRYEEAIEDYEKALELDPDDAE--ALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSL 729
Cdd:COG0457   77 EALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
621-724 1.02e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.87  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 621 ILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYL 700
Cdd:COG3914   80 LLELAALLLQALGRYEEALALYRRALALNPDNAE--ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALR 157
                         90       100
                 ....*....|....*....|....
gi 808154180 701 ALKNISGALEAFRQALKLTTKCPE 724
Cdd:COG3914  158 RLGRLEEAIAALRRALELDPDNAE 181
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
610-718 2.71e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 67.33  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILNEAglyWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG3914  106 ALNPDNAEALFNLGNL---LLALGRLEEALAALRRALALNPDFAE--AYLNLGEALRRLGRLEEAIAALRRALELDPDNA 180
                         90       100
                 ....*....|....*....|....*....
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:COG3914  181 EALNNLGNALQDLGRLEEAIAAYRRALEL 209
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
615-718 4.38e-11

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: 61.18  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 615 NAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLS 694
Cdd:COG4235   16 DAEGWLLL---GRAYLRLGRYDEALAAYEKALRLDP-DNADA-LLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90
                         90       100
                 ....*....|....*....|....
gi 808154180 695 LGNAYLALKNISGALEAFRQALKL 718
Cdd:COG4235   91 LGLAAFQQGDYAEAIAAWQKLLAL 114
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
622-724 1.57e-09

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: 57.12  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 622 LNEAGLYWRAVGNSTFAIACLQRALNLAPlqYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG4783    7 LYALAQALLLAGDYDEAEALLEKALELDP--DNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLK 84
                         90       100
                 ....*....|....*....|...
gi 808154180 702 LKNISGALEAFRQALKLTTKCPE 724
Cdd:COG4783   85 AGDYDEALALLEKALKLDPEHPE 107
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
633-718 1.95e-09

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: 57.28  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 633 GNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAF 712
Cdd:COG5010   68 GDFEESLALLEQALQLDPNNPE--LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAAL 145

                 ....*.
gi 808154180 713 RQALKL 718
Cdd:COG5010  146 QRALGT 151
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
615-724 1.97e-08

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 55.69  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 615 NAPIWLILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLS 694
Cdd:COG4785   69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAE--AYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN 146
                         90       100       110
                 ....*....|....*....|....*....|
gi 808154180 695 LGNAYLALKNISGALEAFRQALKLTTKCPE 724
Cdd:COG4785  147 RGIALYYLGRYELAIADLEKALELDPNDPE 176
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
621-717 4.64e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.01  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 621 ILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYL 700
Cdd:COG0457   78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAE--ALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALE 155
                         90
                 ....*....|....*..
gi 808154180 701 ALKNISGALEAFRQALK 717
Cdd:COG0457  156 KLGRYEEALELLEKLEA 172
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
628-719 5.89e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 51.32  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 628 YWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLlQALAINSSEPLTFLSLGNAYLALKNISG 707
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNAD--ALNNLGLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDYDE 77
                         90
                 ....*....|..
gi 808154180 708 ALEAFRQALKLT 719
Cdd:COG3063   78 ALAYLERALELD 89
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
638-718 2.59e-07

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: 50.58  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 638 AIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG4783   57 AIVLLHEALELDPDEPE--ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134

                 .
gi 808154180 718 L 718
Cdd:COG4783  135 L 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 1.10e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457   43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457  120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199
                        170       180
                 ....*....|....*....|..
gi 808154180 385 IQEEQILRNIIHETQMAKEAQL 406
Cdd:COG0457  200 LLALEQALRKKLAILTLAALAE 221
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
609-725 1.34e-06

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: 50.88  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 609 HAINKPNAPIWLILneAGLYwRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSE 688
Cdd:COG2956   35 LELDPETVEAHLAL--GNLY-RRRGEYDRAIRIHQKLLERDPDRAE--ALLELAQDYLKAGLLDRAEELLEKLLELDPDD 109
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 808154180 689 PLTFLSLGNAYLALKNISGALEAFRQALKLTTKCPEC 725
Cdd:COG2956  110 AEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHA 146
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
622-718 2.68e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.15  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 622 LNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDvplvnlANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG3914   51 LAEAAAAALLALAAGEAAAAAAALLLLAALLELA------ALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLA 124
                         90
                 ....*....|....*..
gi 808154180 702 LKNISGALEAFRQALKL 718
Cdd:COG3914  125 LGRLEEALAALRRALAL 141
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
638-718 5.17e-06

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: 49.34  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 638 AIACLQRALNLAPlqYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG2956  129 AIEVLERLLKLGP--ENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALE 206

                 .
gi 808154180 718 L 718
Cdd:COG2956  207 Q 207
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
610-719 1.01e-05

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: 48.19  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneAGLYWRAvGNSTFAIACLQRALNLAPlqyQDVP-LVNLANLLIHYGLHLDATKLLLQALAINSSE 688
Cdd:COG2956  138 KLGPENAHAYCEL--AELYLEQ-GDYDEAIEALEKALKLDP---DCARaLLLLAELYLEQGDYEEAIAALERALEQDPDY 211
                         90       100       110
                 ....*....|....*....|....*....|.
gi 808154180 689 PLTFLSLGNAYLALKNISGALEAFRQALKLT 719
Cdd:COG2956  212 LPALPRLAELYEKLGDPEEALELLRKALELD 242
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
625-724 1.58e-05

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: 47.80  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 625 AGLYWRAvGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKN 704
Cdd:COG2956   83 AQDYLKA-GLLDRAEELLEKLLELDPDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGD 159
                         90       100
                 ....*....|....*....|
gi 808154180 705 ISGALEAFRQALKLTTKCPE 724
Cdd:COG2956  160 YDEAIEALEKALKLDPDCAR 179
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
573-738 1.97e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.54  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180  573 RMDLKAKMPDD--------------HARKIL-LSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGlYWRAVGNSTF 637
Cdd:TIGR02917 507 RIDIQEGNPDDaiqrfekvltidpkNLRAILaLAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQ-YYLGKGQLKK 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180  638 AIACLQRALNLAPLQYQDVPLvnLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:TIGR02917 586 ALAILNEAADAAPDSPEAWLM--LGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
                         170       180
                  ....*....|....*....|.
gi 808154180  718 LttkcpECENSLKLIRCMQFY 738
Cdd:TIGR02917 664 L-----KPDNTEAQIGLAQLL 679
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
622-736 2.87e-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: 45.34  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 622 LNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG5010   21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSR 100
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 808154180 702 LKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG5010  101 SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSL 135
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
643-718 5.35e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 5.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808154180 643 QRALNLAPLQYqdvplvNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:COG4785   67 LALPDLAQLYY------ERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL 136
TPR_12 pfam13424
Tetratricopeptide repeat;
658-721 7.71e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 7.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808154180  658 LVNLANLLIHYGLHLDATKLLLQALAINSSEP--------LTFLSLGNAYLALKNISGALEAFRQALKLTTK 721
Cdd:pfam13424   6 LNNLAAVLRRLGRYDEALELLEKALEIARRLLgpdhpltaTTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
610-727 2.81e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.60  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILNEAglyWRAVGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG3914  140 ALNPDFAEAYLNLGEA---LRRLGRLEEAIAALRRALELDP-DNAEA-LNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 808154180 690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECEN 727
Cdd:COG3914  215 DAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSP 252
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
673-718 4.54e-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: 41.14  E-value: 4.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 808154180 673 DATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRL 46
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
329-410 4.64e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 329 EQAIKRKHAVL--CQQKLEQKLEAQHRSLQRTLNELKE-YQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQ 405
Cdd:cd16269  207 AEAAEQERKLLeeQQRELEQKLEDQERSYEEHLRQLKEkMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286

                 ....*
gi 808154180 406 LGNHQ 410
Cdd:cd16269  287 IRSLK 291
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
338-424 7.90e-04

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 39.81  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 338 VLCQQKLEQKLEA--QHRSLQRTLnELKEYQKQHDHYLRQQEI-LEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRL 414
Cdd:cd10164    3 SLREQQLQQELLLlkQQQQLQKQL-LFAEFQKQHEHLTRQHEVqLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKRE 81
                         90
                 ....*....|
gi 808154180 415 VNQQHSLHCQ 424
Cdd:cd10164   82 QQRQEELEKQ 91
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
689-718 1.53e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 37.04  E-value: 1.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 808154180   689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
689-718 3.67e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.86  E-value: 3.67e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 808154180  689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
610-717 3.80e-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: 40.48  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG2956  172 KLDPDCARALLLL---AELYLEQGDYEEAIAALERALEQDP-DYLPA-LPRLAELYEKLGDPEEALELLRKALELDPSDD 246
                         90       100
                 ....*....|....*....|....*...
gi 808154180 690 LtFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG2956  247 L-LLALADLLERKEGLEAALALLERQLR 273
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
291-356 4.54e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.99  E-value: 4.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808154180 291 DSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQ-KLEQKLEAQHRSLQ 356
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLgRYEEALADYEQALE 70
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
695-718 6.67e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 35.19  E-value: 6.67e-03
                          10        20
                  ....*....|....*....|....
gi 808154180  695 LGNAYLALKNISGALEAFRQALKL 718
Cdd:pfam07719   7 LGLAYYKLGDYEEALEAYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
297-328 6.82e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 6.82e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 808154180  297 SYYTLGNIYAMLGEYNHSVLCYDHALQARPGF 328
Cdd:pfam00515   3 ALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
172-385 8.05e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 172 AFQHLRGVQERVNLSAPLLPKEDPIFTYLSKRLGRSIDDIGHLIHeGLQKN-TSSWVLYNMASFYwRIKNEPYQVVECAM 250
Cdd:COG3914   59 LLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRR-ALALNpDNAEALFNLGNLL-LALGRLEEALAALR 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 251 RALHFSSRHNKdiALVNLANVLHRAH-FSADAAVVVHAALDDSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFE 329
Cdd:COG3914  137 RALALNPDFAE--AYLNLGEALRRLGrLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808154180 330 QAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQ---QEILEKHKLI 385
Cdd:COG3914  215 DAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDddpAELLALARAW 273
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
291-378 8.66e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 291 DSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQK--------LEQKLEAQ------HRSLQ 356
Cdd:COG0457   38 DPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGryeealedYDKALELDpddaeaLYNLG 117
                         90       100
                 ....*....|....*....|..
gi 808154180 357 RTLNELKEYQKQHDHYLRQQEI 378
Cdd:COG0457  118 LALLELGRYDEAIEAYERALEL 139
ClassIIa_HDAC_Gln-rich-N cd10149
Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, ...
338-419 9.26e-03

Glutamine-rich N-terminal helical domain of various Class IIa histone deacetylases (HDAC4, HDAC5 and HDCA9); This superfamily consists of a glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDAC9; it is missing in HDAC7. It is referred to as the glutamine-rich domain, and confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors. This domain is able to repress transcription independently of the HDAC's C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197397 [Multi-domain]  Cd Length: 90  Bit Score: 36.59  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154180 338 VLCQQKLEQKLEA--QHRSLQRTLnELKEYQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRLV 415
Cdd:cd10149    3 VLREQQLQQELLAlkQQQQIQKQL-LIAEFQKQHENLTRQHEAQLQEHIKQQQEMLAIKQQQELLEKQRKLEQQRQEQEL 81

                 ....
gi 808154180 416 NQQH 419
Cdd:cd10149   82 EKQR 85
 
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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