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Conserved domains on  [gi|767966165|ref|XP_011518520|]
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tetratricopeptide repeat protein 17 isoform X2 [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 4.56e-12

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457    36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457   111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 9.19e-07

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457    43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457   120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199

                         170       180
                  ....*....|....*....|..
gi 767966165  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 4.56e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457    36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457   111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 9.19e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457    43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457   120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199

                         170       180
                  ....*....|....*....|..
gi 767966165  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 2.28e-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: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165   573 RMDLKAKMPDD--------------HARKIL-LSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGlYWRAVGNSTF 637
Cdd:TIGR02917  507 RIDIQEGNPDDaiqrfekvltidpkNLRAILaLAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQ-YYLGKGQLKK 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165   638 AIACLQRALNLAPLQYQDVPLvnLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:TIGR02917  586 ALAILNEAADAAPDSPEAWLM--LGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663

                          170       180
                   ....*....|....*....|.
gi 767966165   718 LttkcpECENSLKLIRCMQFY 738
Cdd:TIGR02917  664 L-----KPDNTEAQIGLAQLL 679
TPR_12 pfam13424
Tetratricopeptide repeat;
658-721 7.60e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 7.60e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966165   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 5.87e-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: 42.95  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  329 EQAIKRKHAVL--CQQKLEQKLEAQHRSLQRTLNELKE-YQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQ 405
Cdd:cd16269   207 AEAAEQERKLLeeQQRELEQKLEDQERSYEEHLRQLKEkMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286


                  ....*
gi 767966165  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 1.55e-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: 1.55e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767966165    689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
297-328 6.49e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 6.49e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767966165   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 4.56e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 4.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457    36 ELDPDDAEALYNL---GLAYLRLGRYEEALADYEQALELDPDDAE--ALNNLGLALQALGRYEEALEDYDKALELDPDDA 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG0457   111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
610-729 6.10e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG0457     2 ELDPDDAEAYNNL---GLAYRRLGRYEEAIEDYEKALELDPDDAE--ALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSL 729
Cdd:COG0457    77 EALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 621-724 1.07e-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: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  621 ILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYL 700
Cdd:COG3914    80 LLELAALLLQALGRYEEALALYRRALALNPDNAE--ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALR 157

                          90       100
                  ....*....|....*....|....
gi 767966165  701 ALKNISGALEAFRQALKLTTKCPE 724
Cdd:COG3914   158 RLGRLEEAIAALRRALELDPDNAE 181
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 610-718 2.95e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 67.71  E-value: 2.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILNEAglyWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG3914   106 ALNPDNAEALFNLGNL---LLALGRLEEALAALRRALALNPDFAE--AYLNLGEALRRLGRLEEAIAALRRALELDPDNA 180

                          90       100
                  ....*....|....*....|....*....
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:COG3914   181 EALNNLGNALQDLGRLEEAIAAYRRALEL 209
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 615-718 4.35e-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: 61.56  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  615 NAPIWLILneaGLYWRAVGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLS 694
Cdd:COG4235    16 DAEGWLLL---GRAYLRLGRYDEALAAYEKALRLDP-DNADA-LLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL 90

                          90       100
                  ....*....|....*....|....
gi 767966165  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 1.40e-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: 57.51  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  622 LNEAGLYWRAVGNSTFAIACLQRALNLAPlqYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDP--DNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLK 84

                          90       100
                  ....*....|....*....|...
gi 767966165  702 LKNISGALEAFRQALKLTTKCPE 724
Cdd:COG4783    85 AGDYDEALALLEKALKLDPEHPE 107
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 633-718 1.49e-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: 58.05  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  633 GNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAF 712
Cdd:COG5010    68 GDFEESLALLEQALQLDPNNPE--LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAAL 145


                  ....*.
gi 767966165  713 RQALKL 718
Cdd:COG5010   146 QRALGT 151
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
615-724 1.60e-08

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 56.46  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  615 NAPIWLILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLS 694
Cdd:COG4785    69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAE--AYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLN 146

                          90       100       110
                  ....*....|....*....|....*....|
gi 767966165  695 LGNAYLALKNISGALEAFRQALKLTTKCPE 724
Cdd:COG4785   147 RGIALYYLGRYELAIADLEKALELDPNDPE 176
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
621-717 4.12e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.40  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  621 ILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYL 700
Cdd:COG0457    78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAE--ALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALE 155

                          90
                  ....*....|....*..
gi 767966165  701 ALKNISGALEAFRQALK 717
Cdd:COG0457   156 KLGRYEEALELLEKLEA 172
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
628-719 5.23e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 51.71  E-value: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  628 YWRAVGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLlQALAINSSEPLTFLSLGNAYLALKNISG 707
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNAD--ALNNLGLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDYDE 77

                          90
                  ....*....|..
gi 767966165  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 2.27e-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: 50.96  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  638 AIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG4783    57 AIVLLHEALELDPDEPE--ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134


                  .
gi 767966165  718 L 718
Cdd:COG4783   135 L 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-406 9.19e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  226 WVLYNMASFYWRIKNEPyQVVECAMRALHFSSRHnkDIALVNLANVLHRAHFSADAAVVVHAALD-DSDFFTSYYTLGNI 304
Cdd:COG0457    43 EALYNLGLAYLRLGRYE-EALADYEQALELDPDD--AEALNNLGLALQALGRYEEALEDYDKALElDPDDAEALYNLGLA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  305 YAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKL 384
Cdd:COG0457   120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199

                         170       180
                  ....*....|....*....|..
gi 767966165  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 1.32e-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: 51.27  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  609 HAINKPNAPIWLILneAGLYWRAvGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSE 688
Cdd:COG2956    35 LELDPETVEAHLAL--GNLYRRR-GEYDRAIRIHQKLLERDPDRAE--ALLELAQDYLKAGLLDRAEELLEKLLELDPDD 109

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767966165  689 PLTFLSLGNAYLALKNISGALEAFRQALKLTTKCPEC 725
Cdd:COG2956   110 AEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHA 146
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 622-718 2.85e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  622 LNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDvplvnlANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG3914    51 LAEAAAAALLALAAGEAAAAAAALLLLAALLELA------ALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLA 124

                          90
                  ....*....|....*..
gi 767966165  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 5.06e-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: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  638 AIACLQRALNLAPlqYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG2956   129 AIEVLERLLKLGP--ENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALE 206


                  .
gi 767966165  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 9.23e-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: 48.57  E-value: 9.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneAGLYWRAvGNSTFAIACLQRALNLAPlqyQDVP-LVNLANLLIHYGLHLDATKLLLQALAINSSE 688
Cdd:COG2956   138 KLGPENAHAYCEL--AELYLEQ-GDYDEAIEALEKALKLDP---DCARaLLLLAELYLEQGDYEEAIAALERALEQDPDY 211

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767966165  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 1.60e-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: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  625 AGLYWRAvGNSTFAIACLQRALNLAPLQYQdvPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKN 704
Cdd:COG2956    83 AQDYLKA-GLLDRAEELLEKLLELDPDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGD 159

                          90       100
                  ....*....|....*....|
gi 767966165  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 2.28e-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: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165   573 RMDLKAKMPDD--------------HARKIL-LSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGlYWRAVGNSTF 637
Cdd:TIGR02917  507 RIDIQEGNPDDaiqrfekvltidpkNLRAILaLAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQ-YYLGKGQLKK 585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165   638 AIACLQRALNLAPLQYQDVPLvnLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:TIGR02917  586 ALAILNEAADAAPDSPEAWLM--LGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663

                          170       180
                   ....*....|....*....|.
gi 767966165   718 LttkcpECENSLKLIRCMQFY 738
Cdd:TIGR02917  664 L-----KPDNTEAQIGLAQLL 679
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 622-736 2.46e-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: 45.72  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  622 LNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLA 701
Cdd:COG5010    21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSR 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767966165  702 LKNISGALEAFRQALKLTTKCPECENSLKLIRCMQ 736
Cdd:COG5010   101 SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSL 135
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
643-718 4.61e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.06  E-value: 4.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966165  643 QRALNLAPLQYqdvplvNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:COG4785    67 LALPDLAQLYY------ERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL 136
TPR_12 pfam13424
Tetratricopeptide repeat;
658-721 7.60e-05

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 41.99  E-value: 7.60e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966165   658 LVNLANLLIHYGLHLDATKLLLQALAINSSEP--------LTFLSLGNAYLALKNISGALEAFRQALKLTTK 721
Cdd:pfam13424    6 LNNLAAVLRRLGRYDEALELLEKALEIARRLLgpdhpltaTTLLNLGRLYLELGRYEEALELLERALALAEK 77
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 610-727 3.01e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.98  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILNEAglyWRAVGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG3914   140 ALNPDFAEAYLNLGEA---LRRLGRLEEAIAALRRALELDP-DNAEA-LNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767966165  690 LTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECEN 727
Cdd:COG3914   215 DAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSP 252
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 673-718 4.87e-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: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 767966165  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 5.87e-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: 42.95  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  329 EQAIKRKHAVL--CQQKLEQKLEAQHRSLQRTLNELKE-YQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQ 405
Cdd:cd16269   207 AEAAEQERKLLeeQQRELEQKLEDQERSYEEHLRQLKEkMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286


                  ....*
gi 767966165  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 1.55e-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: 1.55e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767966165    689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
 338-424 1.89e-03

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: 38.65  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  338 VLCQQKLEQKLEA--QHRSLQRTLnELKEYQKQHDHYLRQQEI-LEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRL 414
Cdd:cd10164     3 SLREQQLQQELLLlkQQQQLQKQL-LFAEFQKQHEHLTRQHEVqLQKHLKVRAELFSEQQQQEILAAKRQQELEQQRKRE 81

                          90
                  ....*....|
gi 767966165  415 VNQQHSLHCQ 424
Cdd:cd10164    82 QQRQEELEKQ 91
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 610-717 3.43e-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: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  610 AINKPNAPIWLILneAGLYWRAvGNSTFAIACLQRALNLAPlQYQDVpLVNLANLLIHYGLHLDATKLLLQALAINSSEP 689
Cdd:COG2956   172 KLDPDCARALLLL--AELYLEQ-GDYEEAIAALERALEQDP-DYLPA-LPRLAELYEKLGDPEEALELLRKALELDPSDD 246

                          90       100
                  ....*....|....*....|....*...
gi 767966165  690 LtFLSLGNAYLALKNISGALEAFRQALK 717
Cdd:COG2956   247 L-LLALADLLERKEGLEAALALLERQLR 273
TPR_1 pfam00515
Tetratricopeptide repeat;
689-718 3.46e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.86  E-value: 3.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 767966165   689 PLTFLSLGNAYLALKNISGALEAFRQALKL 718
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
291-356 4.08e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.38  E-value: 4.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966165  291 DSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQ-KLEQKLEAQHRSLQ 356
Cdd:COG0457     4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLgRYEEALADYEQALE 70
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 695-718 6.23e-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: 6.23e-03
                           10        20
                   ....*....|....*....|....
gi 767966165   695 LGNAYLALKNISGALEAFRQALKL 718
Cdd:pfam07719    7 LGLAYYKLGDYEEALEAYEKALEL 30
TPR_1 pfam00515
Tetratricopeptide repeat;
297-328 6.49e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 6.49e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767966165   297 SYYTLGNIYAMLGEYNHSVLCYDHALQARPGF 328
Cdd:pfam00515    3 ALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
291-378 7.78e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  291 DSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQK--------LEQKLEAQ------HRSLQ 356
Cdd:COG0457    38 DPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGryeealedYDKALELDpddaeaLYNLG 117

                          90       100
                  ....*....|....*....|..
gi 767966165  357 RTLNELKEYQKQHDHYLRQQEI 378
Cdd:COG0457   118 LALLELGRYDEAIEAYERALEL 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 172-385 8.50e-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: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  172 AFQHLRGVQERVNLSAPLLPKEDPIFTYLSKRLGRSIDDIGHLIHeGLQKN-TSSWVLYNMASFYwRIKNEPYQVVECAM 250
Cdd:COG3914    59 LLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRR-ALALNpDNAEALFNLGNLL-LALGRLEEALAALR 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966165  251 RALHFSSRHNKdiALVNLANVLHRAH-FSADAAVVVHAALDDSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFE 329
Cdd:COG3914   137 RALALNPDFAE--AYLNLGEALRRLGrLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767966165  330 QAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQ---QEILEKHKLI 385
Cdd:COG3914   215 DAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDddpAELLALARAW 273
 
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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