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Conserved domains on  [gi|2462506423|ref|XP_054191242|]
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WD and tetratricopeptide repeats protein 1 isoform X4 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

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
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 275-384 1.59e-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: 73.49  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 275 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 354
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506423 355 LARCLFELKYVAEALECLDDFKGKFPEQAH 384
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 ...
 3-132 7.53e-11

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: 63.12  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmwPNTF-WSAAEDGLIRQYDLR 81
Cdd:cd00200    90 TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLR 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462506423  82 eNSKHSEVLIDLTEYCgqlveaKCLTVNPqDNNCLAVGASGPFVRLYDIRM 132
Cdd:cd00200   166 -TGKCVATLTGHTGEV------NSVAFSP-DGEKLLSSSSDGTIKLWDLST 208
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 462-542 1.69e-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: 59.27  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506423 542 G 542
Cdd:cd00200   217 G 217
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 275-384 1.59e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.49  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 275 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 354
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506423 355 LARCLFELKYVAEALECLDDFKGKFPEQAH 384
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-132 7.53e-11

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: 63.12  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmwPNTF-WSAAEDGLIRQYDLR 81
Cdd:cd00200    90 TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLR 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462506423  82 eNSKHSEVLIDLTEYCgqlveaKCLTVNPqDNNCLAVGASGPFVRLYDIRM 132
Cdd:cd00200   166 -TGKCVATLTGHTGEV------NSVAFSP-DGEKLLSSSSDGTIKLWDLST 208
WD40 COG2319
WD40 repeat [General function prediction only];
3-222 1.42e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPhagD-RILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 81
Cdd:COG2319   159 TGHSGAVTSVAFSP---DgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLA 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423  82 ENskhsEVLIDLTeycGQLVEAKCLTVNPqDNNCLAVGASGPFVRLYDIRmiHNHRKSMKQSPSAGVHTFCdrqkPLPDG 161
Cdd:COG2319   235 TG----KLLRTLT---GHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLA--TGELLRTLTGHSGGVNSVA----FSPDG 300

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 162 aaQYYVAGHL--PVKLPDYNNR--LRVLVA-----TYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTF 222
Cdd:COG2319   301 --KLLASGSDdgTVRLWDLATGklLRTLTGhtgavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 462-542 1.69e-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: 59.27  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506423 542 G 542
Cdd:cd00200   217 G 217
WD40 COG2319
WD40 repeat [General function prediction only];
462-526 7.53e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.00  E-value: 7.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPR 526
Cdd:COG2319   338 FSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 284-354 1.11e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506423 284 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 354
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 277-383 6.38e-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: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 277 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 356
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462506423 357 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 383
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 485-524 1.99e-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: 1.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462506423  485 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 524
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
487-524 2.44e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462506423 487 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 524
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
312-346 5.02e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.02e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462506423 312 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 346
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 318-376 5.19e-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: 40.75  E-value: 5.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506423  318 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 376
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 279-346 1.68e-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: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506423 279 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 346
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 275-384 1.59e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.49  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 275 PPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 354
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL---GRLEEAIAALRRALELDPDNAEALNN 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506423 355 LARCLFELKYVAEALECLDDFKGKFPEQAH 384
Cdd:COG3914   186 LGNALQDLGRLEEAIAAYRRALELDPDNAD 215
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
293-373 1.99e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG0457    57 RYEEALADYEQALELDPDDAEALNNLGLALQAL---GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAY 133


                  .
gi 2462506423 373 D 373
Cdd:COG0457   134 E 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 279-373 3.02e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 72.72  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 279 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARC 358
Cdd:COG3914    79 ALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLAL---GRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90
                  ....*....|....*
gi 2462506423 359 LFELKYVAEALECLD 373
Cdd:COG3914   156 LRRLGRLEEAIAALR 170
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
293-373 5.34e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.88  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG0457    23 RYEEAIEDYEKALELDPDDAEALYNLGLAYLRL---GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDY 99


                  .
gi 2462506423 373 D 373
Cdd:COG0457   100 D 100
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 273-373 6.07e-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: 63.83  E-value: 6.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 273 ELPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAH 352
Cdd:COG5010    49 KLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRS---GDKDEAKEYYEKALALSPDNPNAY 125

                          90       100
                  ....*....|....*....|.
gi 2462506423 353 FRLARCLFELKYVAEALECLD 373
Cdd:COG5010   126 SNLAALLLSLGQDDEAKAALQ 146
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
293-373 7.21e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 65.80  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG0457    91 RYEEALEDYDKALELDPDDAEALYNLGLALLEL---GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELL 167


                  .
gi 2462506423 373 D 373
Cdd:COG0457   168 E 168
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 285-383 1.75e-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: 61.95  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 285 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKY 364
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAA---GDTEEAEELLERALALDPDNPEALYLLGLAAFQQGD 100

                          90
                  ....*....|....*....
gi 2462506423 365 VAEALECLDDFKGKFPEQA 383
Cdd:COG4235   101 YAEAIAAWQKLLALLPADA 119
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 283-393 1.82e-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: 62.13  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 283 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 362
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQL---GDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462506423 363 KYVAEALECLDDFKGKFPEqaHSSACDALGR 393
Cdd:COG4783    86 GDYDEALALLEKALKLDPE--HPEAYLRLAR 114
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
293-381 5.48e-11

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 59.41  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRKwdgdHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG3063     7 DLEEAEEYYEKALELDPDNADALNNLGLLLLEQG----RYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                  ....*....
gi 2462506423 373 DDFKGKFPE 381
Cdd:COG3063    83 ERALELDPS 91
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-132 7.53e-11

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: 63.12  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmwPNTF-WSAAEDGLIRQYDLR 81
Cdd:cd00200    90 TGHTSYVSSVAFSPD--GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLR 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462506423  82 eNSKHSEVLIDLTEYCgqlveaKCLTVNPqDNNCLAVGASGPFVRLYDIRM 132
Cdd:cd00200   166 -TGKCVATLTGHTGEV------NSVAFSP-DGEKLLSSSSDGTIKLWDLST 208
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 293-382 2.78e-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: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG4783    53 DLDEAIVLLHEALELDPDEPEARLNLGLALLKA---GDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAAL 129

                          90
                  ....*....|
gi 2462506423 373 DDFKGKFPEQ 382
Cdd:COG4783   130 EKALELDPDD 139
WD40 COG2319
WD40 repeat [General function prediction only];
3-222 1.42e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPhagD-RILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 81
Cdd:COG2319   159 TGHSGAVTSVAFSP---DgKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLA 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423  82 ENskhsEVLIDLTeycGQLVEAKCLTVNPqDNNCLAVGASGPFVRLYDIRmiHNHRKSMKQSPSAGVHTFCdrqkPLPDG 161
Cdd:COG2319   235 TG----KLLRTLT---GHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLA--TGELLRTLTGHSGGVNSVA----FSPDG 300

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 162 aaQYYVAGHL--PVKLPDYNNR--LRVLVA-----TYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTF 222
Cdd:COG2319   301 --KLLASGSDdgTVRLWDLATGklLRTLTGhtgavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 462-542 1.69e-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: 59.27  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS------TGKCLGTLR 216


                  .
gi 2462506423 542 G 542
Cdd:cd00200   217 G 217
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 272-383 2.17e-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: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 272 VELPPYLERVKQQANEAFACQ-QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLK 350
Cdd:COG2956   103 LELDPDDAEALRLLAEIYEQEgDWEKAIEVLERLLKLGPENAHAYCELAELYLEQ---GDYDEAIEALEKALKLDPDCAR 179

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462506423 351 AHFRLARCLFELKYVAEALECLDDFKGKFPEQA 383
Cdd:COG2956   180 ALLLLAELYLEQGDYEEAIAALERALEQDPDYL 212
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 462-524 3.59e-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: 58.12  E-value: 3.59e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 524
Cdd:cd00200   227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 441-524 3.93e-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: 58.12  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 441 DYQFRYCGHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVV 520
Cdd:cd00200    42 ELLRTLKGHTGPVRDVA----ASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTI 117


                  ....
gi 2462506423 521 RLWN 524
Cdd:cd00200   118 KVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 438-542 4.00e-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: 58.12  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 438 RSYDYQFRYC-----GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLA 512
Cdd:cd00200    76 RLWDLETGECvrtltGHTSYVSSVA----FSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVA 151

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462506423 513 TSGIDPVVRLWNPRpesedlTGRVVEDMEG 542
Cdd:cd00200   152 SSSQDGTIKLWDLR------TGKCVATLTG 175
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 293-384 4.12e-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: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECL 372
Cdd:COG2956    57 EYDRAIRIHQKLLERDPDRAEALLELAQDYLKA---GLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL 133

                          90
                  ....*....|..
gi 2462506423 373 DDFKGKFPEQAH 384
Cdd:COG2956   134 ERLLKLGPENAH 145
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
305-373 4.18e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 4.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506423 305 VQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 373
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRL---GRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYE 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 283-398 4.64e-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: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 283 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 362
Cdd:COG2956   149 ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQ---GDYEEAIAALERALEQDPDYLPALPRLAELYEKL 225

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462506423 363 KYVAEALECLDDFKGKFPEqahSSACDALGRDITAA 398
Cdd:COG2956   226 GDPEEALELLRKALELDPS---DDLLLALADLLERK 258
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
274-398 4.88e-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: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 274 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 353
Cdd:COG4785    69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLL---GDYDAALEDFDRALELDPDYAYAYL 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462506423 354 RLARCLFELKYVAEALEcldDFKgKFPEQAHSSACDALGRDITAA 398
Cdd:COG4785   146 NRGIALYYLGRYELAIA---DLE-KALELDPNDPERALWLYLAER 186
WD40 COG2319
WD40 repeat [General function prediction only];
462-526 7.53e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.00  E-value: 7.53e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPR 526
Cdd:COG2319   338 FSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 284-354 1.11e-08

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 57.10  E-value: 1.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462506423 284 QANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFR 354
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKL---GNFTEAVADANKAIELDPSLAKAYLR 75
WD40 COG2319
WD40 repeat [General function prediction only];
3-222 1.90e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPhaGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIAtapMWPN--TFWSAAEDGLIRQYDL 80
Cdd:COG2319   117 TGHTGAVRSVAFSP--DGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423  81 RENSKhsevlidLTEYCGQLVEAKCLTVNPqDNNCLAVGASGPFVRLYD------IRMIHNHrksmkqspSAGVHT--Fc 152
Cdd:COG2319   192 ATGKL-------LRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDlatgklLRTLTGH--------SGSVRSvaF- 254

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506423 153 drqkpLPDGaaQYYVAGHLP--VKL--PDYNNRLRVL-----VATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTF 222
Cdd:COG2319   255 -----SPDG--RLLASGSADgtVRLwdLATGELLRTLtghsgGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL 326
WD40 COG2319
WD40 repeat [General function prediction only];
462-542 1.93e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:COG2319   170 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------TGKLLRTLT 243


                  .
gi 2462506423 542 G 542
Cdd:COG2319   244 G 244
WD40 COG2319
WD40 repeat [General function prediction only];
462-542 2.16e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.46  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:COG2319   254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 327


                  .
gi 2462506423 542 G 542
Cdd:COG2319   328 G 328
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-129 4.32e-08

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: 55.03  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   2 HTGHTANIFSVKFLPhaGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 81
Cdd:cd00200   173 LTGHTGEVNSVAFSP--DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLR 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462506423  82 ENSKHSEVlidlteyCGQLVEAKCLTVNPqDNNCLAVGASGPFVRLYD 129
Cdd:cd00200   250 TGECVQTL-------SGHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
462-542 4.65e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:COG2319   128 FSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA------TGKLLRTLT 201


                  .
gi 2462506423 542 G 542
Cdd:COG2319   202 G 202
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 292-381 8.38e-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: 50.76  E-value: 8.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 292 QQWTQAIQLYSKAVQRAPHNAML---YGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLK---AHFRLARCLFELKYV 365
Cdd:COG1729     7 GDYDEAIAAFKAFLKRYPNSPLApdaLYWLGEAYYAL---GDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDY 83

                          90
                  ....*....|....*.
gi 2462506423 366 AEALECLDDFKGKFPE 381
Cdd:COG1729    84 DKARATLEELIKKYPD 99
WD40 COG2319
WD40 repeat [General function prediction only];
462-546 8.38e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.92  E-value: 8.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:COG2319   212 FSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA------TGELLRTLT 285


                  ....*
gi 2462506423 542 GASQA 546
Cdd:COG2319   286 GHSGG 290
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-148 2.73e-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: 52.34  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   3 TGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPMwPNTFWSAAEDGLIRQYDLRE 82
Cdd:cd00200   132 RGHTDWVNSVAFSPD--GTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLST 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506423  83 nSKHSEVLIdlteycGQLVEAKCLTVNPqDNNCLAVGASGPFVRLYDIRMI--------HNHR-KSMKQSPSAGV 148
Cdd:cd00200   209 -GKCLGTLR------GHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGecvqtlsgHTNSvTSLAWSPDGKR 275
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 283-383 4.28e-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: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 283 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 362
Cdd:COG2956    13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRR---GEYDRAIRIHQKLLERDPDRAEALLELAQDYLKA 89

                          90       100
                  ....*....|....*....|.
gi 2462506423 363 KYVAEALECLDDFKGKFPEQA 383
Cdd:COG2956    90 GLLDRAEELLEKLLELDPDDA 110
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 283-373 5.09e-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: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 283 QQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFEL 362
Cdd:COG3914    49 AALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQAL---GRYEEALALYRRALALNPDNAEALFNLGNLLLAL 125

                          90
                  ....*....|.
gi 2462506423 363 KYVAEALECLD 373
Cdd:COG3914   126 GRLEEALAALR 136
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 461-533 6.38e-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: 51.18  E-value: 6.38e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462506423 461 FFGSNAQyIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLT 533
Cdd:cd00200   185 FSPDGEK-LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
WD40 COG2319
WD40 repeat [General function prediction only];
2-81 9.59e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.45  E-value: 9.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   2 HTGHTANIFSVKFLPHagDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 81
Cdd:COG2319   326 LTGHTGAVRSVAFSPD--GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 448-546 1.04e-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: 50.80  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 448 GHCNTTTDIKeanfFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRp 527
Cdd:cd00200     7 GHTGGVTCVA----FSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81

                          90
                  ....*....|....*....
gi 2462506423 528 esedlTGRVVEDMEGASQA 546
Cdd:cd00200    82 -----TGECVRTLTGHTSY 95
WD40 COG2319
WD40 repeat [General function prediction only];
462-526 1.29e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.07  E-value: 1.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPR 526
Cdd:COG2319   296 FSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLA 360
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 296-373 2.70e-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: 2.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506423 296 QAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 373
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRL---GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 277-383 6.38e-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: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 277 YLERVKQQANEAFACQQWTQAIQLYSKAVQRAPhNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLA 356
Cdd:TIGR00990 126 YAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNAL---GDWEKVVEDTTAALELDPDYSKALNRRA 201

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462506423 357 RCLFELKYVAEAL-----ECL-DDFKGKFPEQA 383
Cdd:TIGR00990 202 NAYDGLGKYADALldltaSCIiDGFRNEQSAQA 234
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
289-373 1.43e-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: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 289 FACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYvAEA 368
Cdd:COG4785   118 LLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYL---GRYELAIADLEKALELDPNDPERALWLYLAERKLDP-EKA 193


                  ....*
gi 2462506423 369 LECLD 373
Cdd:COG4785   194 LALLL 198
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 274-372 3.83e-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: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 274 LPPYLERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHF 353
Cdd:COG5010    16 LLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKL---GDFEESLALLEQALQLDPNNPELYY 92

                          90
                  ....*....|....*....
gi 2462506423 354 RLARCLFELKYVAEALECL 372
Cdd:COG5010    93 NLALLYSRSGDKDEAKEYY 111
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-131 3.85e-05

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: 45.79  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423   2 HTGHTANIFSVKFLPHAgdRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPmWPNTFWSAAEDGLIRQYDLR 81
Cdd:cd00200     5 LKGHTGGVTCVAFSPDG--KLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASA-DGTYLASGSSDKTIRLWDLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462506423  82 ENSKHSEvlidLTEYCGQLveaKCLTVNPqDNNCLAVGASGPFVRLYDIR 131
Cdd:cd00200    82 TGECVRT----LTGHTSYV---SSVAFSP-DGRILSSSSRDKTIKVWDVE 123
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
269-373 4.91e-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: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 269 SPQVELPPYLERVKQQANEAFACQQW----TQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISL 344
Cdd:COG4785    26 LAALLFAAVLALAIALADLALALAAAalaaAALAAERIDRALALPDLAQLYYERGVAYDSL---GDYDLAIADFDQALEL 102

                          90       100
                  ....*....|....*....|....*....
gi 2462506423 345 NPCHLKAHFRLARCLFELKYVAEALECLD 373
Cdd:COG4785   103 DPDLAEAYNNRGLAYLLLGDYDAALEDFD 131
WD40 COG2319
WD40 repeat [General function prediction only];
462-546 9.02e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 462 FGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRpesedlTGRVVEDME 541
Cdd:COG2319    86 FSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA------TGKLLRTLT 159


                  ....*
gi 2462506423 542 GASQA 546
Cdd:COG2319   160 GHSGA 164
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 485-524 1.99e-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: 1.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462506423  485 TTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 524
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
487-524 2.44e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462506423 487 NLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWN 524
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
TPR_1 pfam00515
Tetratricopeptide repeat;
312-346 5.02e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.79  E-value: 5.02e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462506423 312 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 346
Cdd:pfam00515   1 AKALYNLGNAYFKL---GKYDEALEYYEKALELNP 32
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
 318-376 5.19e-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: 40.75  E-value: 5.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462506423  318 RAAAYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFK 376
Cdd:smart01043  67 LAEALLAL---GRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLR 122
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 293-346 8.52e-04

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: 8.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462506423 293 QWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 346
Cdd:COG5010   103 DKDEAKEYYEKALALSPDNPNAYSNLAALLLSL---GQDDEAKAALQRALGTSP 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
321-370 1.15e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.61  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462506423 321 AYMKRkwdGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALE 370
Cdd:COG3063     1 LYLKL---GDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA 47
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 279-346 1.68e-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: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506423 279 ERVKQQANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMKrkwDGDHYDALRDCLKAISLNP 346
Cdd:cd24142     1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLE---LGDVEEAREVLLRAIELDP 65
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 312-346 1.68e-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: 1.68e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2462506423  312 AMLYGNRAAAYMKRkwdGDHYDALRDCLKAISLNP 346
Cdd:smart00028   1 AEALYNLGNAYLKL---GDYDEALEYYEKALELDP 32
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 283-381 1.73e-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: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462506423 283 QQANEAFACQQWTQAIQLYSKAVQRAP-----HNAMLYgnRAAAYMKrkwDGDHYDALRDCLKAISLNPCHLK---AHFR 354
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPgspyaEQAQLM--LAYAYYK---QGDYEEAIAAADRFIKLYPNSPNadyAYYL 111

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462506423 355 LARCLFEL--------KYVAEALECLDDFKGKFPE 381
Cdd:COG4105   112 RGLSYYEQspdsdrdqTSTRKAIEAFQELINRYPD 146
TPR_19 pfam14559
Tetratricopeptide repeat;
328-373 2.06e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.79  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462506423 328 DGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLD 373
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLA 46
ANAPC3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
 310-375 5.94e-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: 5.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462506423 310 HNAMLYGNRAAAYMKRK-----W-------DGDHYDALrDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDF 375
Cdd:pfam12895   6 KNAIFLAERLLAAEPESpedayLlaqclflNGQYKRAY-ELLRKAKLNGSSLGCRYLFAQCLLKLKKYDEALDALGKA 82
TPR_11 pfam13414
TPR repeat;
285-324 9.14e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 34.37  E-value: 9.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462506423 285 ANEAFACQQWTQAIQLYSKAVQRAPHNAMLYGNRAAAYMK 324
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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