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Conserved domains on  [gi|442627192|ref|NP_001260319|]
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Utx histone demethylase, isoform E [Drosophila melanogaster]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11420782)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 668-776 2.48e-33

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


:

Pssm-ID: 396791  Cd Length: 114  Bit Score: 124.33  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  668 QLYMKVPGSRTPGHQENNNFCSININIGPGDCEWFAVPDAYWGGVHNLCEKNN-------ISYLHGSWWPvlEDLYKENI 740
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 442627192  741 PVYRFIQKPGDLVWVNAGCVHWVQSIGWCNNIAWNV 776
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
68-203 6.66e-21

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 93.15  E-value: 6.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  68 ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWC 147
Cdd:COG0457    8 AEAYNNLGLAYR-------RLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442627192 148 SIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG0457   81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERA 136
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 668-776 2.48e-33

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 124.33  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  668 QLYMKVPGSRTPGHQENNNFCSININIGPGDCEWFAVPDAYWGGVHNLCEKNN-------ISYLHGSWWPvlEDLYKENI 740
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 442627192  741 PVYRFIQKPGDLVWVNAGCVHWVQSIGWCNNIAWNV 776
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
68-203 6.66e-21

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 93.15  E-value: 6.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  68 ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWC 147
Cdd:COG0457    8 AEAYNNLGLAYR-------RLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442627192 148 SIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG0457   81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERA 136
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 84-250 1.42e-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: 48.93  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192   84 LGEKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDAL 163
Cdd:TIGR02917 508 IDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL 587

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  164 QAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQISFQKSSLIRKKQAIRMKKDTIGLSKGLSQRIT---- 239
Cdd:TIGR02917 588 AILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALElkpd 667

                         170
                  ....*....|.
gi 442627192  240 FLEGQLSQAPL 250
Cdd:TIGR02917 668 NTEAQIGLAQL 678
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 652-698 2.61e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 42.62  E-value: 2.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 442627192   652 NMLSHVGHVILGMNT-VQLYMKVPGSRTPGHQENNNfcSININIGPGD 698
Cdd:smart00558  13 NLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 668-776 2.48e-33

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 124.33  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  668 QLYMKVPGSRTPGHQENNNFCSININIGPGDCEWFAVPDAYWGGVHNLCEKNN-------ISYLHGSWWPvlEDLYKENI 740
Cdd:pfam02373   1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 442627192  741 PVYRFIQKPGDLVWVNAGCVHWVQSIGWCNNIAWNV 776
Cdd:pfam02373  79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
68-203 6.66e-21

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 93.15  E-value: 6.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  68 ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWC 147
Cdd:COG0457    8 AEAYNNLGLAYR-------RLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442627192 148 SIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG0457   81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERA 136
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
34-200 1.40e-20

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 91.99  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  34 FQIAHLYEVQNKHKAAKDGYEfllneknISLELK---ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQ 110
Cdd:COG0457   12 NNLGLAYRRLGRYEEAIEDYE-------KALELDpddAEALYNLGLAYL-------RLGRYEEALADYEQALELDPDDAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 111 SLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESC 190
Cdd:COG0457   78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157

                        170
                 ....*....|
gi 442627192 191 GQLRDAYACY 200
Cdd:COG0457  158 GRYEEALELL 167
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 11-206 1.77e-18

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: 86.71  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  11 ALKHLQlALLYTYPSTfseLQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKnislELKADVYRQLGWMYHcveclgeKKER 90
Cdd:COG2956   27 AIDLLE-EALELDPET---VEAHLALGNLYRRRGEYDRAIRIHQKLLERD----PDRAEALLELAQDYL-------KAGL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  91 EANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAV 170
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKAL 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 442627192 171 QLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQ 206
Cdd:COG2956  172 KLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ 207
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 86-203 1.35e-17

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 87.74  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  86 EKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQA 165
Cdd:COG3914   89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAA 168

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442627192 166 YICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG3914  169 LRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRA 206
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 29-247 3.06e-16

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: 80.16  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  29 ELQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKnislELKADVYRQLGWMYhcveclgEKKEREANALNFLQKSIEADPKS 108
Cdd:COG2956   75 RAEALLELAQDYLKAGLLDRAEELLEKLLELD----PDDAEALRLLAEIY-------EQEGDWEKAIEVLERLLKLGPEN 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 109 GQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYE 188
Cdd:COG2956  144 AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE 223

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442627192 189 SCGQLRDAYAcYLNATKQISFQKSSLIRKKQAIRMKkdtiglsKGLSQRITFLEGQLSQ 247
Cdd:COG2956  224 KLGDPEEALE-LLRKALELDPSDDLLLALADLLERK-------EGLEAALALLERQLRR 274
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 94-200 4.43e-16

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: 75.43  E-value: 4.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  94 ALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLD 173
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81

                         90       100
                 ....*....|....*....|....*..
gi 442627192 174 KDHKAAWTNLGILYESCGQLRDAYACY 200
Cdd:COG4235   82 PDNPEALYLLGLAAFQQGDYAEAIAAW 108
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
102-205 9.62e-16

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 77.74  E-value: 9.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 102 IEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWT 181
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                         90       100
                 ....*....|....*....|....
gi 442627192 182 NLGILYESCGQLRDAYACYLNATK 205
Cdd:COG0457   81 NLGLALQALGRYEEALEDYDKALE 104
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 67-203 4.86e-14

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: 70.22  E-value: 4.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  67 KADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTW 146
Cdd:COG4783    3 CAEALYALAQALL-------LAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEAR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442627192 147 CSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG4783   76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKA 132
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-176 2.32e-12

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: 65.21  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  30 LQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKNISlelkADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSG 109
Cdd:COG4783    4 AEALYALAQALLLAGDYDEAEALLEKALELDPDN----PEAFALLGEILL-------QLGDLDEAIVLLHEALELDPDEP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627192 110 QSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDH 176
Cdd:COG4783   73 EARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 11-206 3.19e-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: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  11 ALKHLQLALLYTYPSTFSELQVKFQIAHLYEVQNKHKAAKDGYEFLLneknisleLKADVYRQLGWMYHcveclgEKKER 90
Cdd:COG3914    1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLL--------LAALAEAAAAALLA------LAAGE 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  91 EANALNFLQKSIEADPKSGQSLYLLGRcyaginkVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAV 170
Cdd:COG3914   67 AAAAAAALLLLAALLELAALLLQALGR-------YEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRAL 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 442627192 171 QLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQ 206
Cdd:COG3914  140 ALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALEL 175
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 66-205 3.73e-11

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: 64.75  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  66 LKADVYRQLGWMYhcvecLGEK---KEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGN 142
Cdd:COG2956    1 LLLPVAAALGWYF-----KGLNyllNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627192 143 ADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATK 205
Cdd:COG2956   76 AEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK 138
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 68-215 1.76e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 64.63  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  68 ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWC 147
Cdd:COG3914  112 AEALFNLGNLLL-------ALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALN 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 148 SIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTN-LGILYESCG-QLRDAYACYLNATKQISFQKSSLI 215
Cdd:COG3914  185 NLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNlLFALRQACDwEVYDRFEELLAALARGPSELSPFA 254
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 87-203 5.25e-10

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: 58.82  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  87 KKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAY 166
Cdd:COG5010   32 AGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYY 111

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 442627192 167 ICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNA 203
Cdd:COG5010  112 EKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRA 148
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 110-206 5.25e-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: 55.58  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 110 QSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYES 189
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLK 84

                         90
                 ....*....|....*..
gi 442627192 190 CGQLRDAYACYLNATKQ 206
Cdd:COG4783   85 AGDYDEALALLEKALKL 101
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 127-206 6.34e-09

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: 55.01  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 127 DAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQ 206
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
37-198 2.38e-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: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  37 AHLYEVQNKHKAAKDGYEFLLNEKNISLELkADVYRQLGWMYHCVECLgekkEREANALNFLQKSIEAD---PKSGQSLY 113
Cdd:COG4785    3 ALALALLLALALAAAAASKAAILLAALLFA-AVLALAIALADLALALA----AAALAAAALAAERIDRAlalPDLAQLYY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 114 LLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQL 193
Cdd:COG4785   78 ERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRY 157


                 ....*
gi 442627192 194 RDAYA 198
Cdd:COG4785  158 ELAIA 162
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 15-174 2.78e-08

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: 53.81  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  15 LQLALLYTYPSTFSELQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKNISLELKADVYRQLGWMYHcveclgeKKEREANA 94
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYN-------KLGDFEES 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  95 LNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDK 174
Cdd:COG5010   74 LALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
86-175 3.53e-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: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  86 EKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAfLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQA 165
Cdd:COG3063    3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLLELGDYDEALAY 81

                         90
                 ....*....|
gi 442627192 166 YICAVQLDKD 175
Cdd:COG3063   82 LERALELDPS 91
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
118-200 8.84e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 50.55  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 118 CYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQaYICAVQLDKDHKAAWTNLGILYESCGQLRDAY 197
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79


                 ...
gi 442627192 198 ACY 200
Cdd:COG3063   80 AYL 82
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 113-216 4.43e-07

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: 52.42  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 113 YLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQ 192
Cdd:COG2956   12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91

                         90       100
                 ....*....|....*....|....
gi 442627192 193 LRDAYACYLNATKQISFQKSSLIR 216
Cdd:COG2956   92 LDRAEELLEKLLELDPDDAEALRL 115
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 68-166 1.14e-06

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: 48.46  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  68 ADVYRQLGWMYHcveclgeKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWC 147
Cdd:COG4235   17 AEGWLLLGRAYL-------RLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALY 89

                         90
                 ....*....|....*....
gi 442627192 148 SIGVLYQQQNQPTDALQAY 166
Cdd:COG4235   90 LLGLAAFQQGDYAEAIAAW 108
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 84-250 1.42e-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: 48.93  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192   84 LGEKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDAL 163
Cdd:TIGR02917 508 IDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL 587

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  164 QAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQISFQKSSLIRKKQAIRMKKDTIGLSKGLSQRIT---- 239
Cdd:TIGR02917 588 AILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALElkpd 667

                         170
                  ....*....|.
gi 442627192  240 FLEGQLSQAPL 250
Cdd:TIGR02917 668 NTEAQIGLAQL 678
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 652-698 2.61e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 42.62  E-value: 2.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 442627192   652 NMLSHVGHVILGMNT-VQLYMKVPGSRTPGHQENNNfcSININIGPGD 698
Cdd:smart00558  13 NLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
6-133 8.87e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192   6 GEFHIALKHLQLALlytypstfsELQVK-----FQIAHLYEVQNKHKAAKDGYEfllneknISLELK---ADVYRQLGWM 77
Cdd:COG0457   56 GRYEEALADYEQAL---------ELDPDdaealNNLGLALQALGRYEEALEDYD-------KALELDpddAEALYNLGLA 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442627192  78 YHCvecLGEKKEreanALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYR 133
Cdd:COG0457  120 LLE---LGRYDE----AIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLE 168
TPR COG0790
TPR repeat [General function prediction only];
35-206 2.90e-04

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 43.38  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  35 QIAHLYEVQNKHKAAKDGYEFLLNEKNISLELKADVYRQLGWMYHcvECLGEKKEREAnALNFLQKSIEADpkSGQSLYL 114
Cdd:COG0790   30 AAAAAAAAAAALAAAAGAAAAAAAAAAAAAAGGAEAQYNLGLMYA--EGRGVPKDYEK-ALEWFEKAAEQG--DAEAQYN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192 115 LGRCYA---GINKvhDAFLA---YRNSVEKseGNADTWCSIGVLYQQ-QNQPTDALQA---YICAVqlDKDHKAAWTNLG 184
Cdd:COG0790  105 LGLMYEeglGVPQ--DYAKAlewYEKAAEQ--GDADAQYNLGLLYLNgEGVPKDPAKAaewYRKAA--EQGDADAQYNLG 178

                        170       180
                 ....*....|....*....|....*..
gi 442627192 185 ILYEScGQ-----LRDAYACYLNATKQ 206
Cdd:COG0790  179 VLYEN-GRgvpkdPAKALEWYRKAAEQ 204
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 34-144 2.93e-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: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  34 FQIAHLYEVQNKHKAAKDGYEFL--LNEKNislelkADVYRQLGWMYhcveclgEKKEREANALNFLQKSIEADPKSGQS 111
Cdd:COG4235   21 LLLGRAYLRLGRYDEALAAYEKAlrLDPDN------ADALLDLAEAL-------LAAGDTEEAEELLERALALDPDNPEA 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 442627192 112 LYLLGRCYAGINKVHDAFLAYRNSVEKSEGNAD 144
Cdd:COG4235   88 LYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 143-206 3.86e-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: 41.72  E-value: 3.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627192 143 ADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQ 206
Cdd:COG4783    4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALEL 67
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 87-166 4.78e-04

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 40.75  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  87 KKEREANALNFLQKSIEADPKS---GQSLYLLGRCYAGINKVHDAFLAYRNSVE---KSEGNADTWCSIGVLYQQQNQPT 160
Cdd:COG1729    5 KAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKrypDSPKAPDALLKLGLSYLELGDYD 84


                 ....*.
gi 442627192 161 DALQAY 166
Cdd:COG1729   85 KARATL 90
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 146-206 3.57e-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: 3.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627192 146 WCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQ 206
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLER 71
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 43-133 3.95e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.05  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627192  43 QNKHKAAKDGYEFLLnEKNISLELKADVYRQLGWMYhcveclgEKKEREANALNFLQKSIEADPKS---GQSLYLLGRCY 119
Cdd:COG1729    6 AGDYDEAIAAFKAFL-KRYPNSPLAPDALYWLGEAY-------YALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSY 77

                         90
                 ....*....|....
gi 442627192 120 AGINKVHDAFLAYR 133
Cdd:COG1729   78 LELGDYDKARATLE 91
 
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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