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Conserved domains on  [gi|2462506415|ref|XP_054191238|]
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WD and tetratricopeptide repeats protein 1 isoform X1 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 12822048)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
39-215 3.38e-19

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319   196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319   273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                         170
                  ....*....|....*..
gi 2462506415 199 CLAVGASGPFVRLYDIR 215
Cdd:COG2319   344 TLASGSDDGTVRLWDLA 360
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 359-468 2.49e-13

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 359 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 438
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506415 439 LARCLFELKYVAEALECLDDFKGKFPEQAH 468
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 546-626 2.71e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 58.89  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506415 626 G 626
Cdd:cd00200   217 G 217
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
39-215 3.38e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319   196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319   273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                         170
                  ....*....|....*..
gi 2462506415 199 CLAVGASGPFVRLYDIR 215
Cdd:COG2319   344 TLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 34-163 7.52e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 87.39  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAAD 113
Cdd:cd00200   164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD-LSTGKCLGTLRGHENGVNSVAFSPD--GYLLASGSED 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462506415 114 SKVHVHDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYD 163
Cdd:cd00200   241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPD-GKRLASGSADGTIRIWD 289
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 359-468 2.49e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 359 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 438
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506415 439 LARCLFELKYVAEALECLDDFKGKFPEQAH 468
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 546-626 2.71e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.89  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506415 626 G 626
Cdd:cd00200   217 G 217
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 368-438 1.35e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506415 368 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 438
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
WD40 COG2319
WD40 repeat [General function prediction only];
546-626 2.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319   170 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------TGKLLRTLT 243


                  .
gi 2462506415 626 G 626
Cdd:COG2319   244 G 244
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 39-75 3.32e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.92  E-value: 3.32e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462506415   39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
39-75 8.23e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 8.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 361-467 7.69e-06

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 49.21  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 361 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 440
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462506415 441 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 467
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 569-608 2.77e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 2.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462506415  569 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 608
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
571-608 3.29e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462506415 571 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 608
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
396-430 5.34e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462506415 396 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 430
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 402-460 9.53e-04

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 39.98  E-value: 9.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506415  402 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 460
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 363-430 1.99e-03

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506415 363 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 430
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
39-215 3.38e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319   196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319   273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                         170
                  ....*....|....*..
gi 2462506415 199 CLAVGASGPFVRLYDIR 215
Cdd:COG2319   344 TLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 34-163 7.52e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 87.39  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAAD 113
Cdd:cd00200   164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD-LSTGKCLGTLRGHENGVNSVAFSPD--GYLLASGSED 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462506415 114 SKVHVHDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYD 163
Cdd:cd00200   241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPD-GKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
39-306 1.23e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.81  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMhTGHTANIFSVKFLPHagDRILITGAADSKVHV 118
Cdd:COG2319   154 LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPD--GKLLASGSADGTVRL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 119 HDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319   231 WDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG----ELLRTLT---GHSGGVNSVAFSP-DGK 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 199 CLAVGASGPFVRLYDIRmihnhrksmkqspsagvhtfcdrqkplpdgaaqyyvAGHLPVKLPDYNNRLRVlvatyVTFSP 278
Cdd:COG2319   302 LLASGSDDGTVRLWDLA------------------------------------TGKLLRTLTGHTGAVRS-----VAFSP 340

                         250       260
                  ....*....|....*....|....*...
gi 2462506415 279 NGTELLVNMGGEQVYLFDLTYKQRPYTF 306
Cdd:COG2319   341 DGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 39-216 4.14e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 85.08  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD-----------------------------------------PL 77
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDletgellrtlkghtgpvrdvaasadgtylasgssdktirlwDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  78 HHKKLLSMHTGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmwPNTF-WSAAED 156
Cdd:cd00200    81 ETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP--DGTFvASSSQD 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 157 GLIRQYDLReNSKHSEVLIDLTEYCgqlveaKCLTVNPqDNNCLAVGASGPFVRLYDIRM 216
Cdd:cd00200   157 GTIKLWDLR-TGKCVATLTGHTGEV------NSVAFSP-DGEKLLSSSSDGTIKLWDLST 208
WD40 COG2319
WD40 repeat [General function prediction only];
43-165 1.06e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.65  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  43 LQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAADSKVHVHDLT 122
Cdd:COG2319   284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLRTLTGHTGAVRSVAFSPD--GKTLASGSDDGTVRLWDLA 360

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462506415 123 VKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 165
Cdd:COG2319   361 TGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 42-232 6.30e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 78.92  E-value: 6.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  42 ELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMhTGHTANIFSVKFLPHagDRILITGAADSKVHVHDL 121
Cdd:cd00200    88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPD--GTFVASSSQDGTIKLWDL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 122 TVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLREnSKHSEVLIdlteycGQLVEAKCLTVNPqDNNCLA 201
Cdd:cd00200   165 RTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLST-GKCLGTLR------GHENGVNSVAFSP-DGYLLA 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462506415 202 VGASGPFVRLYDIRMI--------HNHR-KSMKQSPSAGV 232
Cdd:cd00200   236 SGSEDGTIRVWDLRTGecvqtlsgHTNSvTSLAWSPDGKR 275
WD40 COG2319
WD40 repeat [General function prediction only];
34-306 1.64e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.10  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAAD 113
Cdd:COG2319    65 AAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGAVRSVAFSP--DGKTLASGSAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 114 SKVHVHDLTVKETIHMFGDHTNRVKRIAtapMWPN--TFWSAAEDGLIRQYDLRENSKhsevlidLTEYCGQLVEAKCLT 191
Cdd:COG2319   142 GTVRLWDLATGKLLRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKL-------LRTLTGHTGAVRSVA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 192 VNPqDNNCLAVGASGPFVRLYD------IRMIHNHrksmkqspSAGVHT--FcdrqkpLPDGaaQYYVAGHLP--VKL-- 259
Cdd:COG2319   212 FSP-DGKLLASGSADGTVRLWDlatgklLRTLTGH--------SGSVRSvaF------SPDG--RLLASGSADgtVRLwd 274

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462506415 260 PDYNNRLRVL-----VATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTF 306
Cdd:COG2319   275 LATGELLRTLtghsgGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL 326
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 359-468 2.49e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 359 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 438
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506415 439 LARCLFELKYVAEALECLDDFKGKFPEQAH 468
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
377-457 3.07e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 3.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG0457    57 RYEEALADYEQALELDPDDAEALNNLGLALQAL---GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAY 133


                  .
gi 2462506415 457 D 457
Cdd:COG0457   134 E 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 363-457 4.48e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 72.33  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 363 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARC 442
Cdd:COG3914    79 ALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLAL---GRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90
                  ....*....|....*
gi 2462506415 443 LFELKYVAEALECLD 457
Cdd:COG3914   156 LRRLGRLEEAIAALR 170
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
377-457 8.21e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.88  E-value: 8.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG0457    23 RYEEAIEDYEKALELDPDDAEALYNLGLAYLRL---GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDY 99


                  .
gi 2462506415 457 D 457
Cdd:COG0457   100 D 100
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 357-457 9.64e-12

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: 63.44  E-value: 9.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 357 ELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAH 436
Cdd:COG5010    49 KLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRS---GDKDEAKEYYEKALALSPDNPNAY 125

                          90       100
                  ....*....|....*....|.
gi 2462506415 437 FRLARCLFELKYVAEALECLD 457
Cdd:COG5010   126 SNLAALLLSLGQDDEAKAALQ 146
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
377-457 1.11e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 65.41  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG0457    91 RYEEALEDYDKALELDPDDAEALYNLGLALLEL---GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELL 167


                  .
gi 2462506415 457 D 457
Cdd:COG0457   168 E 168
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 369-467 2.38e-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: 61.56  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 369 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKY 448
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAA---GDTEEAEELLERALALDPDNPEALYLLGLAAFQQGD 100

                          90
                  ....*....|....*....
gi 2462506415 449 VAEALECLDDFKGKFPEQA 467
Cdd:COG4235   101 YAEAIAAWQKLLALLPADA 119
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 367-477 2.45e-11

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: 61.75  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 367 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 446
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQL---GDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462506415 447 KYVAEALECLDDFKGKFPEqaHSSACDALGR 477
Cdd:COG4783    86 GDYDEALALLEKALKLDPE--HPEAYLRLAR 114
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
377-465 7.31e-11

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 59.03  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKwdgdHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG3063     7 DLEEAEEYYEKALELDPDNADALNNLGLLLLEQG----RYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                  ....*....
gi 2462506415 457 DDFKGKFPE 465
Cdd:COG3063    83 ERALELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 377-466 3.53e-10

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: 58.66  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG4783    53 DLDEAIVLLHEALELDPDEPEARLNLGLALLKA---GDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAAL 129

                          90
                  ....*....|
gi 2462506415 457 DDFKGKFPEQ 466
Cdd:COG4783   130 EKALELDPDD 139
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 546-626 2.71e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.89  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506415 626 G 626
Cdd:cd00200   217 G 217
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 376-467 2.82e-09

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: 58.59  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 376 QQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALEC 455
Cdd:COG2956   124 GDWEKAIEVLERLLKLGPENAHAYCELAELYLEQ---GDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAA 200

                          90
                  ....*....|..
gi 2462506415 456 LDDFKGKFPEQA 467
Cdd:COG2956   201 LERALEQDPDYL 212
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 377-468 5.30e-09

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: 57.82  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 456
Cdd:COG2956    57 EYDRAIRIHQKLLERDPDRAEALLELAQDYLKA---GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL 133

                          90
                  ....*....|..
gi 2462506415 457 DDFKGKFPEQAH 468
Cdd:COG2956   134 ERLLKLGPENAH 145
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
358-482 5.57e-09

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 56.85  E-value: 5.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 358 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 437
Cdd:COG4785    69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLL---GDYDAALEDFDRALELDPDYAYAYL 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462506415 438 RLARCLFELKYVAEALEcldDFKgKFPEQAHSSACDALGRDITAA 482
Cdd:COG4785   146 NRGIALYYLGRYELAIA---DLE-KALELDPNDPERALWLYLAER 186
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
389-457 5.77e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 5.77e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506415 389 VQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 457
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRL---GRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYE 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 367-482 5.81e-09

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: 57.82  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 367 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 446
Cdd:COG2956   149 ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQ---GDYEEAIAALERALEQDPDYLPALPRLAELYEKL 225

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462506415 447 KYVAEALECLDDFKGKFPEqahSSACDALGRDITAA 482
Cdd:COG2956   226 GDPEEALELLRKALELDPS---DDLLLALADLLERK 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 546-608 5.82e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.73  E-value: 5.82e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 608
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 525-608 6.43e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.73  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 525 DYQFRYCGHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVV 604
Cdd:cd00200    42 ELLRTLKGHTGPVRDVA----ASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTI 117


                  ....
gi 2462506415 605 RLWN 608
Cdd:cd00200   118 KVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 522-626 6.91e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.73  E-value: 6.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 522 RSYDYQFRYC-----GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLA 596
Cdd:cd00200    76 RLWDLETGECvrtltGHTSYVSSVA----FSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVA 151

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506415 597 TSGIDPVVRLWNPRpesedlTGRVVEDMEG 626
Cdd:cd00200   152 SSSQDGTIKLWDLR------TGKCVATLTG 175
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 368-438 1.35e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506415 368 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 438
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
WD40 COG2319
WD40 repeat [General function prediction only];
546-626 2.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319   170 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------TGKLLRTLT 243


                  .
gi 2462506415 626 G 626
Cdd:COG2319   244 G 244
WD40 COG2319
WD40 repeat [General function prediction only];
546-626 2.63e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.46  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319   254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 327


                  .
gi 2462506415 626 G 626
Cdd:COG2319   328 G 328
WD40 COG2319
WD40 repeat [General function prediction only];
546-626 5.64e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319   128 FSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 201


                  .
gi 2462506415 626 G 626
Cdd:COG2319   202 G 202
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 376-465 7.60e-08

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: 51.15  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 376 QQWTQAIQLYSKAVQRAPHNAML---YGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLK---AHFRLARCLFELKYV 449
Cdd:COG1729     7 GDYDEAIAAFKAFLKRYPNSPLApdaLYWLGEAYYAL---GDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDY 83

                          90
                  ....*....|....*.
gi 2462506415 450 AEALECLDDFKGKFPE 465
Cdd:COG1729    84 DKARATLEELIKKYPD 99
WD40 COG2319
WD40 repeat [General function prediction only];
546-630 1.02e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.92  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319   212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA------TGELLRTLT 285


                  ....*
gi 2462506415 626 GASQA 630
Cdd:COG2319   286 GHSGG 290
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 39-75 3.32e-07

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.92  E-value: 3.32e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2462506415   39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 367-467 5.59e-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: 51.65  E-value: 5.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 367 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 446
Cdd:COG2956    13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRR---GEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA 89

                          90       100
                  ....*....|....*....|.
gi 2462506415 447 KYVAEALECLDDFKGKFPEQA 467
Cdd:COG2956    90 GLLDRAEELLEKLLELDPDDA 110
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 367-457 6.80e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 52.69  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 367 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 446
Cdd:COG3914    49 AALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQAL---GRYEEALALYRRALALNPDNAEALFNLGNLLLAL 125

                          90
                  ....*....|.
gi 2462506415 447 KYVAEALECLD 457
Cdd:COG3914   126 GRLEEALAALR 136
WD40 pfam00400
WD domain, G-beta repeat;
39-75 8.23e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 8.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462506415  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 545-617 9.80e-07

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 50.80  E-value: 9.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506415 545 FFGSNAQyIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLT 617
Cdd:cd00200   185 FSPDGEK-LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
WD40 COG2319
WD40 repeat [General function prediction only];
546-610 1.56e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.07  E-value: 1.56e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPR 610
Cdd:COG2319   296 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 532-630 1.65e-06

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 50.41  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 532 GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRp 611
Cdd:cd00200     7 GHTGGVTCVA----FSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81

                          90
                  ....*....|....*....
gi 2462506415 612 esedlTGRVVEDMEGASQA 630
Cdd:cd00200    82 -----TGECVRTLTGHTSY 95
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 380-457 3.38e-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: 46.92  E-value: 3.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506415 380 QAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 457
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRL---GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 361-467 7.69e-06

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 49.21  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 361 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 440
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462506415 441 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 467
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
373-457 1.66e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.45  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 373 FACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYvAEA 452
Cdd:COG4785   118 LLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYL---GRYELAIADLEKALELDPNDPERALWLYLAERKLDP-EKA 193


                  ....*
gi 2462506415 453 LECLD 457
Cdd:COG4785   194 LALLL 198
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 358-456 5.05e-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: 44.18  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 358 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 437
Cdd:COG5010    16 LLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKL---GDFEESLALLEQALQLDPNNPELYY 92

                          90
                  ....*....|....*....
gi 2462506415 438 RLARCLFELKYVAEALECL 456
Cdd:COG5010    93 NLALLYSRSGDKDEAKEYY 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
353-457 5.58e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.91  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 353 SPQVELPPYLERVKQQANEAFACQQW----TQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISL 428
Cdd:COG4785    26 LAALLFAAVLALAIALADLALALAAAalaaAALAAERIDRALALPDLAQLYYERGVAYDSL---GDYDLAIADFDQALEL 102

                          90       100
                  ....*....|....*....|....*....
gi 2462506415 429 NPCHLKAHFRLARCLFELKYVAEALECLD 457
Cdd:COG4785   103 DPDLAEAYNNRGLAYLLLGDYDAALEDFD 131
WD40 COG2319
WD40 repeat [General function prediction only];
546-630 1.08e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 546 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 625
Cdd:COG2319    86 FSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA------TGKLLRTLT 159


                  ....*
gi 2462506415 626 GASQA 630
Cdd:COG2319   160 GHSGA 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 569-608 2.77e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 2.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462506415  569 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 608
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
571-608 3.29e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 3.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462506415 571 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 608
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
396-430 5.34e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462506415 396 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 430
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 402-460 9.53e-04

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 39.98  E-value: 9.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506415  402 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 460
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 377-430 1.13e-03

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: 39.94  E-value: 1.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462506415 377 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 430
Cdd:COG5010   103 DKDEAKEYYEKALALSPDNPNAYSNLAALLLSL---GQDDEAKAALQRALGTSP 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
405-454 1.43e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.23  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462506415 405 AYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALE 454
Cdd:COG3063     1 LYLKL---GDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA 47
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 367-465 1.64e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 40.63  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506415 367 QQANEAFACQQWTQAIQLYSKAVQRAP-----HNAMLYgnRAAAYMKrkwDGDHYDALRDCLKAISLNPCHLK---AHFR 438
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPgspyaEQAQLM--LAYAYYK---QGDYEEAIAAADRFIKLYPNSPNadyAYYL 111

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462506415 439 LARCLFEL--------KYVAEALECLDDFKGKFPE 465
Cdd:COG4105   112 RGLSYYEQspdsdrdqTSTRKAIEAFQELINRYPD 146
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 396-430 1.79e-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: 36.27  E-value: 1.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462506415  396 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 430
Cdd:smart00028   1 AEALYNLGNAYLKL---GDYDEALEYYEKALELDP 32
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 363-430 1.99e-03

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506415 363 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 430
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
TPR_19 pfam14559
Tetratricopeptide repeat;
412-457 2.46e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.79  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462506415 412 DGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 457
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLA 46
WD40 COG2319
WD40 repeat [General function prediction only];
34-76 4.10e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 4.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462506415  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDP 76
Cdd:COG2319   359 LATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
ANAPC3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
 394-459 6.83e-03

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


Pssm-ID: 463743 [Multi-domain]  Cd Length: 82  Bit Score: 36.08  E-value: 6.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506415 394 HNAMLYGNRAAAYMKRK-----W-------DGDHYDALrDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDF 459
Cdd:pfam12895   6 KNAIFLAERLLAAEPESpedayLlaqclflNGQYKRAY-ELLRKAKLNGSSLGCRYLFAQCLLKLKKYDEALDALGKA 82
TPR_11 pfam13414
TPR repeat;
369-408 9.28e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 34.37  E-value: 9.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462506415 369 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMK 408
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
 
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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