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Conserved domains on  [gi|22095349|ref|NP_055838|]
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WD and tetratricopeptide repeats protein 1 isoform b [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 3.37e-19

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319 196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319 273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                       170
                ....*....|....*..
gi 22095349 199 CLAVGASGPFVRLYDIR 215
Cdd:COG2319 344 TLASGSDDGTVRLWDLA 360
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 358-467 2.48e-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: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 358 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 437
Cdd:COG3914 109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                        90       100       110
                ....*....|....*....|....*....|
gi 22095349 438 LARCLFELKYVAEALECLDDFKGKFPEQAH 467
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 ...
 545-625 2.78e-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: 2.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                .
gi 22095349 625 G 625
Cdd:cd00200 217 G 217
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
39-215 3.37e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319 196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319 273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                       170
                ....*....|....*..
gi 22095349 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 8.24e-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: 8.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAAD 113
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD-LSTGKCLGTLRGHENGVNSVAFSPD--GYLLASGSED 240

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22095349 114 SKVHVHDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYD 163
Cdd:cd00200 241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPD-GKRLASGSADGTIRIWD 289
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 358-467 2.48e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 358 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 437
Cdd:COG3914 109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                        90       100       110
                ....*....|....*....|....*....|
gi 22095349 438 LARCLFELKYVAEALECLDDFKGKFPEQAH 467
Cdd:COG3914 186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 545-625 2.78e-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: 2.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                .
gi 22095349 625 G 625
Cdd:cd00200 217 G 217
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 367-437 1.34e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22095349  367 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 437
Cdd:PLN03088   8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
WD40 COG2319
WD40 repeat [General function prediction only];
545-625 2.34e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319 170 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------TGKLLRTLT 243


                .
gi 22095349 625 G 625
Cdd:COG2319 244 G 244
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 39-75 3.42e-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: 3.42e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 22095349     39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
39-75 8.63e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 8.63e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 22095349    39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 360-466 7.68e-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: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349   360 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 439
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 22095349   440 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 466
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 568-607 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 22095349    568 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 607
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
570-607 3.45e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 3.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 22095349   570 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 607
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
395-429 5.33e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 22095349   395 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 429
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 401-459 9.34e-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: 9.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22095349    401 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 459
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 362-429 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 22095349 362 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 429
Cdd:cd24142   1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
39-215 3.37e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.36  E-value: 3.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAADSKVHV 118
Cdd:COG2319 196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGKLLRTLTGHSGSVRSVAFSP--DGRLLASGSADGTVRL 272

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 119 HDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319 273 WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATG----KLLRTLT---GHTGAVRSVAFSP-DGK 343

                       170
                ....*....|....*..
gi 22095349 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 8.24e-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: 8.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAAD 113
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD-LSTGKCLGTLRGHENGVNSVAFSPD--GYLLASGSED 240

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 22095349 114 SKVHVHDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYD 163
Cdd:cd00200 241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPD-GKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
39-317 8.37e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.20  E-value: 8.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMhTGHTANIFSVKFLPHagDRILITGAADSKVHV 118
Cdd:COG2319 154 LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPD--GKLLASGSADGTVRL 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 119 HDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLRENskhsEVLIDLTeycGQLVEAKCLTVNPqDNN 198
Cdd:COG2319 231 WDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG----ELLRTLT---GHSGGVNSVAFSP-DGK 301

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 199 CLAVGASGPFVRLYDIRmihnhrksmkqspsagvhtfcdrqkplpdgaaqyyvAGHLPVKLPDYNNRLRVlvatyVTFSP 278
Cdd:COG2319 302 LLASGSDDGTVRLWDLA------------------------------------TGKLLRTLTGHTGAVRS-----VAFSP 340

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 22095349 279 NGTELLVNMGGEQVYLFDLTYKQRPYTFLLprkcHSSGV 317
Cdd:COG2319 341 DGKTLASGSDDGTVRLWDLATGELLRTLTG----HTGAV 375
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 39-216 4.50e-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: 4.50e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD-----------------------------------------PL 77
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDletgellrtlkghtgpvrdvaasadgtylasgssdktirlwDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  78 HHKKLLSMHTGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmwPNTF-WSAAED 156
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP--DGTFvASSSQD 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 157 GLIRQYDLReNSKHSEVLIDLTEYCgqlveaKCLTVNPqDNNCLAVGASGPFVRLYDIRM 216
Cdd:cd00200 157 GTIKLWDLR-TGKCVATLTGHTGEV------NSVAFSP-DGEKLLSSSSDGTIKLWDLST 208
WD40 COG2319
WD40 repeat [General function prediction only];
43-165 1.05e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.65  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  43 LQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPHagDRILITGAADSKVHVHDLT 122
Cdd:COG2319 284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD-LATGKLLRTLTGHTGAVRSVAFSPD--GKTLASGSDDGTVRLWDLA 360

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 22095349 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 6.65e-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: 78.53  E-value: 6.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  42 ELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMhTGHTANIFSVKFLPHagDRILITGAADSKVHVHDL 121
Cdd:cd00200  88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL-RGHTDWVNSVAFSPD--GTFVASSSQDGTIKLWDL 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 122 TVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLREnSKHSEVLIdlteycGQLVEAKCLTVNPqDNNCLA 201
Cdd:cd00200 165 RTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLST-GKCLGTLR------GHENGVNSVAFSP-DGYLLA 235

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22095349 202 VGASGPFVRLYDIRMI--------HNHR-KSMKQSPSAGV 232
Cdd:cd00200 236 SGSEDGTIRVWDLRTGecvqtlsgHTNSvTSLAWSPDGKR 275
WD40 COG2319
WD40 repeat [General function prediction only];
34-353 1.37e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.10  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDpLHHKKLLSMHTGHTANIFSVKFLPhaGDRILITGAAD 113
Cdd:COG2319  65 AAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGAVRSVAFSP--DGKTLASGSAD 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 114 SKVHVHDLTVKETIHMFGDHTNRVKRIAtapMWPN--TFWSAAEDGLIRQYDLRENSKhsevlidLTEYCGQLVEAKCLT 191
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKL-------LRTLTGHTGAVRSVA 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 192 VNPqDNNCLAVGASGPFVRLYDIRmihnhrksmkqspsagvhtfcdrqkplpdgaaqyyvAGHLPVKLPDYNNRlrvlvA 271
Cdd:COG2319 212 FSP-DGKLLASGSADGTVRLWDLA------------------------------------TGKLLRTLTGHSGS-----V 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 272 TYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTFllprKCHSSGVQNGKMSTNG---VSNGVSNGLHL--HSNGFRLPE 346
Cdd:COG2319 250 RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTL----TGHSGGVNSVAFSPDGkllASGSDDGTVRLwdLATGKLLRT 325


                ....*..
gi 22095349 347 SRGHVSP 353
Cdd:COG2319 326 LTGHTGA 332
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 358-467 2.48e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 358 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 437
Cdd:COG3914 109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                        90       100       110
                ....*....|....*....|....*....|
gi 22095349 438 LARCLFELKYVAEALECLDDFKGKFPEQAH 467
Cdd:COG3914 186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-456 2.76e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 2.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG0457  57 RYEEALADYEQALELDPDDAEALNNLGLALQAL---GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAY 133


                .
gi 22095349 456 D 456
Cdd:COG0457 134 E 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 362-456 4.47e-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: 4.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 362 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARC 441
Cdd:COG3914  79 ALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLAL---GRLEEALAALRRALALNPDFAEAYLNLGEA 155

                        90
                ....*....|....*
gi 22095349 442 LFELKYVAEALECLD 456
Cdd:COG3914 156 LRRLGRLEEAIAALR 170
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-456 8.28e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.88  E-value: 8.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG0457  23 RYEEAIEDYEKALELDPDDAEALYNLGLAYLRL---GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDY 99


                .
gi 22095349 456 D 456
Cdd:COG0457 100 D 100
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 356-456 9.00e-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: 9.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 356 ELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAH 435
Cdd:COG5010  49 KLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRS---GDKDEAKEYYEKALALSPDNPNAY 125

                        90       100
                ....*....|....*....|.
gi 22095349 436 FRLARCLFELKYVAEALECLD 456
Cdd:COG5010 126 SNLAALLLSLGQDDEAKAALQ 146
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-456 1.02e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 65.41  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG0457  91 RYEEALEDYDKALELDPDDAEALYNLGLALLEL---GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELL 167


                .
gi 22095349 456 D 456
Cdd:COG0457 168 E 168
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 366-476 2.27e-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: 2.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 366 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 445
Cdd:COG4783   9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQL---GDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 22095349 446 KYVAEALECLDDFKGKFPEqaHSSACDALGR 476
Cdd:COG4783  86 GDYDEALALLEKALKLDPE--HPEAYLRLAR 114
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 368-466 2.30e-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: 2.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 368 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKY 447
Cdd:COG4235  24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAA---GDTEEAEELLERALALDPDNPEALYLLGLAAFQQGD 100

                        90
                ....*....|....*....
gi 22095349 448 VAEALECLDDFKGKFPEQA 466
Cdd:COG4235 101 YAEAIAAWQKLLALLPADA 119
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
376-464 6.96e-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: 6.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKwdgdHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG3063   7 DLEEAEEYYEKALELDPDNADALNNLGLLLLEQG----RYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                ....*....
gi 22095349 456 DDFKGKFPE 464
Cdd:COG3063  83 ERALELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 376-465 3.42e-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: 3.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG4783  53 DLDEAIVLLHEALELDPDEPEARLNLGLALLKA---GDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAAL 129

                        90
                ....*....|
gi 22095349 456 DDFKGKFPEQ 465
Cdd:COG4783 130 EKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 355-466 2.62e-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: 2.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 355 VELPPYLERVKQQANEAFACQ-QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLK 433
Cdd:COG2956 103 LELDPDDAEALRLLAEIYEQEgDWEKAIEVLERLLKLGPENAHAYCELAELYLEQ---GDYDEAIEALEKALKLDPDCAR 179

                        90       100       110
                ....*....|....*....|....*....|...
gi 22095349 434 AHFRLARCLFELKYVAEALECLDDFKGKFPEQA 466
Cdd:COG2956 180 ALLLLAELYLEQGDYEEAIAALERALEQDPDYL 212
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 545-625 2.78e-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: 2.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                .
gi 22095349 625 G 625
Cdd:cd00200 217 G 217
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 376-467 5.06e-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: 5.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 455
Cdd:COG2956  57 EYDRAIRIHQKLLERDPDRAEALLELAQDYLKA---GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL 133

                        90
                ....*....|..
gi 22095349 456 DDFKGKFPEQAH 467
Cdd:COG2956 134 ERLLKLGPENAH 145
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
357-481 5.40e-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: 5.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 357 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 436
Cdd:COG4785  69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLL---GDYDAALEDFDRALELDPDYAYAYL 145

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 22095349 437 RLARCLFELKYVAEALEcldDFKgKFPEQAHSSACDALGRDITAA 481
Cdd:COG4785 146 NRGIALYYLGRYELAIA---DLE-KALELDPNDPERALWLYLAER 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 366-481 5.59e-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: 5.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 366 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 445
Cdd:COG2956 149 ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQ---GDYEEAIAALERALEQDPDYLPALPRLAELYEKL 225

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 22095349 446 KYVAEALECLDDFKGKFPEqahSSACDALGRDITAA 481
Cdd:COG2956 226 GDPEEALELLRKALELDPS---DDLLLALADLLERK 258
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
388-456 5.65e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 5.65e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22095349 388 VQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 456
Cdd:COG0457   1 LELDPDDAEAYNNLGLAYRRL---GRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYE 66
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 545-607 6.02e-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: 6.02e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 607
Cdd:cd00200 227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 524-607 6.71e-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: 57.73  E-value: 6.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 524 DYQFRYCGHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVV 603
Cdd:cd00200  42 ELLRTLKGHTGPVRDVA----ASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTI 117


                ....
gi 22095349 604 RLWN 607
Cdd:cd00200 118 KVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 521-625 7.03e-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: 7.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 521 RSYDYQFRYC-----GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLA 595
Cdd:cd00200  76 RLWDLETGECvrtltGHTSYVSSVA----FSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVA 151

                        90       100       110
                ....*....|....*....|....*....|
gi 22095349 596 TSGIDPVVRLWNPRpesedlTGRVVEDMEG 625
Cdd:cd00200 152 SSSQDGTIKLWDLR------TGKCVATLTG 175
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 367-437 1.34e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22095349  367 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 437
Cdd:PLN03088   8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
WD40 COG2319
WD40 repeat [General function prediction only];
545-625 2.34e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319 170 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------TGKLLRTLT 243


                .
gi 22095349 625 G 625
Cdd:COG2319 244 G 244
WD40 COG2319
WD40 repeat [General function prediction only];
545-625 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 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319 254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 327


                .
gi 22095349 625 G 625
Cdd:COG2319 328 G 328
WD40 COG2319
WD40 repeat [General function prediction only];
545-625 5.63e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 5.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319 128 FSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 201


                .
gi 22095349 625 G 625
Cdd:COG2319 202 G 202
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 375-464 7.23e-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: 7.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 375 QQWTQAIQLYSKAVQRAPHNAML---YGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLK---AHFRLARCLFELKYV 448
Cdd:COG1729   7 GDYDEAIAAFKAFLKRYPNSPLApdaLYWLGEAYYAL---GDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDY 83

                        90
                ....*....|....*.
gi 22095349 449 AEALECLDDFKGKFPE 464
Cdd:COG1729  84 DKARATLEELIKKYPD 99
WD40 COG2319
WD40 repeat [General function prediction only];
545-629 1.01e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.92  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319 212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA------TGELLRTLT 285


                ....*
gi 22095349 625 GASQA 629
Cdd:COG2319 286 GHSGG 290
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 39-75 3.42e-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: 3.42e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 22095349     39 LEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWD 75
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 366-466 5.19e-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: 5.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 366 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 445
Cdd:COG2956  13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRR---GEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA 89

                        90       100
                ....*....|....*....|.
gi 22095349 446 KYVAEALECLDDFKGKFPEQA 466
Cdd:COG2956  90 GLLDRAEELLEKLLELDPDDA 110
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 366-456 6.79e-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: 6.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 366 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 445
Cdd:COG3914  49 AALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQAL---GRYEEALALYRRALALNPDNAEALFNLGNLLLAL 125

                        90
                ....*....|.
gi 22095349 446 KYVAEALECLD 456
Cdd:COG3914 126 GRLEEALAALR 136
WD40 pfam00400
WD domain, G-beta repeat;
39-75 8.63e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 8.63e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 22095349    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 ...
 544-616 9.96e-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: 9.96e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095349 544 FFGSNAQyIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLT 616
Cdd:cd00200 185 FSPDGEK-LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
WD40 COG2319
WD40 repeat [General function prediction only];
545-609 1.55e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.07  E-value: 1.55e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPR 609
Cdd:COG2319 296 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 531-629 1.71e-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: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 531 GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRp 610
Cdd:cd00200   7 GHTGGVTCVA----FSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81

                        90
                ....*....|....*....
gi 22095349 611 esedlTGRVVEDMEGASQA 629
Cdd:cd00200  82 -----TGECVRTLTGHTSY 95
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 379-456 3.31e-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: 3.31e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22095349 379 QAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 456
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLLLGRAYLRL---GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 360-466 7.68e-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: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349   360 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 439
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 22095349   440 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 466
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
372-456 1.69e-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: 1.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 372 FACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYvAEA 451
Cdd:COG4785 118 LLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYL---GRYELAIADLEKALELDPNDPERALWLYLAERKLDP-EKA 193


                ....*
gi 22095349 452 LECLD 456
Cdd:COG4785 194 LALLL 198
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 357-455 4.86e-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: 4.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 357 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 436
Cdd:COG5010  16 LLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKL---GDFEESLALLEQALQLDPNNPELYY 92

                        90
                ....*....|....*....
gi 22095349 437 RLARCLFELKYVAEALECL 455
Cdd:COG5010  93 NLALLYSRSGDKDEAKEYY 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
352-456 5.62e-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: 5.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 352 SPQVELPPYLERVKQQANEAFACQQW----TQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISL 427
Cdd:COG4785  26 LAALLFAAVLALAIALADLALALAAAalaaAALAAERIDRALALPDLAQLYYERGVAYDSL---GDYDLAIADFDQALEL 102

                        90       100
                ....*....|....*....|....*....
gi 22095349 428 NPCHLKAHFRLARCLFELKYVAEALECLD 456
Cdd:COG4785 103 DPDLAEAYNNRGLAYLLLGDYDAALEDFD 131
WD40 COG2319
WD40 repeat [General function prediction only];
545-629 1.07e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095349 545 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 624
Cdd:COG2319  86 FSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA------TGKLLRTLT 159


                ....*
gi 22095349 625 GASQA 629
Cdd:COG2319 160 GHSGA 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 568-607 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 22095349    568 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 607
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
570-607 3.45e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 3.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 22095349   570 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 607
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
395-429 5.33e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 22095349   395 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 429
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 401-459 9.34e-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: 9.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22095349    401 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 459
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 376-429 1.11e-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: 40.33  E-value: 1.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 22095349 376 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 429
Cdd:COG5010 103 DKDEAKEYYEKALALSPDNPNAYSNLAALLLSL---GQDDEAKAALQRALGTSP 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
404-453 1.39e-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: 1.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 22095349 404 AYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALE 453
Cdd:COG3063   1 LYLKL---GDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA 47
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 366-464 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 22095349 366 QQANEAFACQQWTQAIQLYSKAVQRAP-----HNAMLYgnRAAAYMKrkwDGDHYDALRDCLKAISLNPCHLK---AHFR 437
Cdd:COG4105  37 EEAKEALEKGDYEKAIKLFEELEPRYPgspyaEQAQLM--LAYAYYK---QGDYEEAIAAADRFIKLYPNSPNadyAYYL 111

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22095349 438 LARCLFEL--------KYVAEALECLDDFKGKFPE 464
Cdd:COG4105 112 RGLSYYEQspdsdrdqTSTRKAIEAFQELINRYPD 146
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 395-429 1.81e-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: 1.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 22095349    395 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 429
Cdd:smart00028   1 AEALYNLGNAYLKL---GDYDEALEYYEKALELDP 32
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 362-429 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 22095349 362 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 429
Cdd:cd24142   1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
TPR_19 pfam14559
Tetratricopeptide repeat;
411-456 2.43e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.79  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 22095349   411 DGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 456
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLA 46
WD40 COG2319
WD40 repeat [General function prediction only];
34-76 4.09e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 4.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 22095349  34 IRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDP 76
Cdd:COG2319 359 LATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
ANAPC3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
 393-458 6.82e-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: 6.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22095349   393 HNAMLYGNRAAAYMKRK-----W-------DGDHYDALrDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDF 458
Cdd:pfam12895   6 KNAIFLAERLLAAEPESpedayLlaqclflNGQYKRAY-ELLRKAKLNGSSLGCRYLFAQCLLKLKKYDEALDALGKA 82
TPR_11 pfam13414
TPR repeat;
368-407 9.26e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 34.37  E-value: 9.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 22095349   368 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMK 407
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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