|
Name |
Accession |
Description |
Interval |
E-value |
| Asp_Arg_Hydrox |
pfam05118 |
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
844-998 |
1.94e-72 |
|
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.
Pssm-ID: 461552 Cd Length: 157 Bit Score: 236.39 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 844 EANWKLIRDEGLAVIDTEKGLFVPEDENLREKGD--WSQYTLWQQGRKNEKSCAAAPRTCALLERFP-ESTGCRRGQIKY 920
Cdd:pfam05118 1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785372442 921 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCANDTRSWEEGKVLIFDDSFEHEVWQEANSYRLIFIVDVWHP 998
Cdd:pfam05118 81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
|
|
| LpxO2 |
COG3555 |
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
840-1001 |
4.02e-56 |
|
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442776 Cd Length: 220 Bit Score: 193.55 E-value: 4.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 840 VRTLEANWKLIRDEGLAVIDTEKGL-----FVPEDENLREKGDWSQYTLWQQGRKNEKSCAAAPRTCALLERFPestgcr 914
Cdd:COG3555 20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 915 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCANDTRSWEEGKVLIFDDSFEHEVWQEANSYRLI 990
Cdd:COG3555 94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171
|
170
....*....|.
gi 1785372442 991 FIVDVWHPELT 1001
Cdd:COG3555 172 LFCDVWRPMLS 182
|
|
| Asp-B-Hydro_N |
pfam05279 |
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ... |
27-103 |
4.51e-21 |
|
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.
Pssm-ID: 428406 Cd Length: 66 Bit Score: 87.59 E-value: 4.51e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785372442 27 EGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakaqdfrynlsealqGKLGVYDTDGDGDFDVDDAKILLG 103
Cdd:pfam05279 5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
592-800 |
3.59e-14 |
|
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: 74.00 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 592 KTIKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYgkaqsedALAEKMRSNDILLQAINTYGEVAEL-PNAPAE 670
Cdd:COG2956 40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELdPDDAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 671 LIKLtlkrrADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFI 750
Cdd:COG2956 113 LRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785372442 751 LKAENYIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGSQEAYIWY 800
Cdd:COG2956 188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDPEEALEL 234
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
385-567 |
9.88e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.65 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 385 QETEHEP-ETHRDEEAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEAPAvien 463
Cdd:PRK10811 849 RPQDVQVeEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPV---- 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 464 eDEDSEPVEErldeaepPTASDQEEINEEILHVIEDKIVKAFEQlqnpaEQAQSEPEEiqdVLTEEILQDDKAEESLLVP 543
Cdd:PRK10811 925 -TEQPQVITE-------SDVAVAQEVAEHAEPVVEPQDETADIE-----EAAETAEVV---VAEPEVVAQPAAPVVAEVA 988
|
170 180
....*....|....*....|....
gi 1785372442 544 EEQQETPTDEHKEVPEEKTEQPAG 567
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
594-744 |
4.06e-05 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.77 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 594 IKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQSE----------DALAEKMRSNDILLQAINTYGEVA- 662
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSAPEYLPALLLAGASEy 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 663 ---ELPNAPAELIKlTLK--------RR--ADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAV 729
Cdd:TIGR02917 307 qlgNLEQAYQYLNQ-ILKyapnshqaRRllASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY 385
|
170
....*....|....*
gi 1785372442 730 FEQVLAMSPNDGFAK 744
Cdd:TIGR02917 386 LAKATELDPENAAAR 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-568 |
5.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 114 AEDSEDDHPATQATAEPDDVEEEdiqdvfQPQDEADDLDKDLEEIVQ-DSLHESADDLDKDLQEVVEEIHEEAVDDLGKA 192
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKE------EAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 193 FDEEVQDSPH-----ESTDDLDQDLKEIVEDSYTEAAAADDLDKDLEEIVQESLHAEEDASETHEEADQVAEEEAHDEEP 267
Cdd:PTZ00121 1426 KAEEKKKADEakkkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 268 EVEKEVEAVETANVEAVFVEEQLELEvqDDEQAETTEEVPETEEADDNTVVEEAKVEIETesddQELDQDVKAEPEIEEI 347
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEK----KKAEEAKKAEEDKNMA 1579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 348 YKEELLEEDAEEQPEPEVIEETEPEEEREEQVALDDNQETEHEPETHRDEEA--PSESQVTEDLQEVIVDEHVTYEQEEE 425
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 426 HHTEDEPQHTEHLEVEESQTPDEEFEPEMLEAPAVIENEDEDSEPVEERLDEAEPPTASDQEEINEEILHVIEDKIVKAF 505
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785372442 506 EQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHKEVPEEKTEQPAGD 568
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
319-565 |
6.45e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 319 EEAKVEIETESDDQELDQDVKAEPEIEEIYKEELLEEDAEEQPEPEVIEETEPEEEREEQVALDDNQETEHEPETHRD-E 397
Cdd:TIGR00927 647 EEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEgT 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 398 EAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEmLEAPAVIENEDEDSEPVEERLDE 477
Cdd:TIGR00927 727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE-IQAGEDGEMKGDEGAEGKVEHEG 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 478 AEPPTASDQEEINEEILHVIEDKIVKAFEQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHKEV 557
Cdd:TIGR00927 806 ETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEE 885
|
....*...
gi 1785372442 558 PEEKTEQP 565
Cdd:TIGR00927 886 EEEENEEP 893
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Asp_Arg_Hydrox |
pfam05118 |
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ... |
844-998 |
1.94e-72 |
|
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.
Pssm-ID: 461552 Cd Length: 157 Bit Score: 236.39 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 844 EANWKLIRDEGLAVIDTEKGLFVPEDENLREKGD--WSQYTLWQQGRKNEKSCAAAPRTCALLERFP-ESTGCRRGQIKY 920
Cdd:pfam05118 1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785372442 921 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCANDTRSWEEGKVLIFDDSFEHEVWQEANSYRLIFIVDVWHP 998
Cdd:pfam05118 81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
|
|
| LpxO2 |
COG3555 |
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ... |
840-1001 |
4.02e-56 |
|
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442776 Cd Length: 220 Bit Score: 193.55 E-value: 4.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 840 VRTLEANWKLIRDEGLAVIDTEKGL-----FVPEDENLREKGDWSQYTLWQQGRKNEKSCAAAPRTCALLERFPestgcr 914
Cdd:COG3555 20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 915 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCANDTRSWEEGKVLIFDDSFEHEVWQEANSYRLI 990
Cdd:COG3555 94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171
|
170
....*....|.
gi 1785372442 991 FIVDVWHPELT 1001
Cdd:COG3555 172 LFCDVWRPMLS 182
|
|
| Asp-B-Hydro_N |
pfam05279 |
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ... |
27-103 |
4.51e-21 |
|
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.
Pssm-ID: 428406 Cd Length: 66 Bit Score: 87.59 E-value: 4.51e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785372442 27 EGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakaqdfrynlsealqGKLGVYDTDGDGDFDVDDAKILLG 103
Cdd:pfam05279 5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
592-800 |
3.59e-14 |
|
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: 74.00 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 592 KTIKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYgkaqsedALAEKMRSNDILLQAINTYGEVAEL-PNAPAE 670
Cdd:COG2956 40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELdPDDAEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 671 LIKLtlkrrADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFI 750
Cdd:COG2956 113 LRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1785372442 751 LKAENYIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGSQEAYIWY 800
Cdd:COG2956 188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDPEEALEL 234
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
596-769 |
2.11e-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: 59.82 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 596 AELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQsedalaekmrsndILLQaintygevaelpnapaeliklt 675
Cdd:COG4783 6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ---------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 676 lkrradrqqfLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAEN 755
Cdd:COG4783 51 ----------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120
|
170
....*....|....
gi 1785372442 756 YIAESIPYLKEGLE 769
Cdd:COG4783 121 RPDEAIAALEKALE 134
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
604-769 |
8.73e-10 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 60.41 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 604 LRKKGKVDEALRAFESLVDKYPQSPKARYGKAQsedALAEKMRSNdillQAINTYGEVAEL-PNAPAeliklTLKRRADR 682
Cdd:COG0457 18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGL---AYLRLGRYE----EALADYEQALELdPDDAE-----ALNNLGLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 683 QQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIP 762
Cdd:COG0457 86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165
|
....*..
gi 1785372442 763 YLKEGLE 769
Cdd:COG0457 166 LLEKLEA 172
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
628-801 |
1.32e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 61.93 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 628 PKARYGKAQSEDALAEKMRSNDILLQAINTYGEVAELPNAPAELIKLTLKRRADRQQFLGRTRGSVVTLHKLVQLYPEDV 707
Cdd:COG3914 33 EAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 708 TFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLKEGLESgEPgtDDGRFYFHLGDA 787
Cdd:COG3914 113 EALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNA 189
|
170
....*....|....*
gi 1785372442 788 LQRVG-SQEAYIWYE 801
Cdd:COG3914 190 LQDLGrLEEAIAAYR 204
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
594-783 |
2.18e-08 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 58.08 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 594 IKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYgkaqsedALAEKMRSNDILLQAINTYGEVAEL-PNAPAELI 672
Cdd:COG3914 78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 673 KLTLKRRAdrqqfLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILK 752
Cdd:COG3914 151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225
|
170 180 190
....*....|....*....|....*....|.
gi 1785372442 753 AENYIAESIPYLKEGLESGEPGTDDGRFYFH 783
Cdd:COG3914 226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
630-770 |
1.58e-07 |
|
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: 51.88 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 630 ARYGKAQSEDALAEKMRSNDILLQAINTYGEVAELPNAPAELIKLTLKRRADRQQFLGRTRGSVVTLHKLVQLYPEDVTF 709
Cdd:COG5010 11 PLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPEL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785372442 710 RNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLKEGLES 770
Cdd:COG5010 91 YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
603-705 |
1.81e-06 |
|
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: 47.68 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 603 KLRKKGKVDEALRAFESLVDKYPQS---PKARYGKAQSEDALAEKMRSNDILLQAINTYGEVAELPNApaelikltLKRR 679
Cdd:COG1729 2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA--------LLKL 73
|
90 100
....*....|....*....|....*.
gi 1785372442 680 ADRQQFLGRTRGSVVTLHKLVQLYPE 705
Cdd:COG1729 74 GLSYLELGDYDKARATLEELIKKYPD 99
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
596-802 |
2.97e-06 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 51.15 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 596 AELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQSEDALAEKMRSNDILLQAINTYGEVAEL-PNAPAELIKL 674
Cdd:COG3914 39 AALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALnPDNAEALFNL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 675 tlkrrADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAE 754
Cdd:COG3914 119 -----GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1785372442 755 NYIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGSQEAYIWYEA 802
Cdd:COG3914 194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFEE 238
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
700-801 |
9.34e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 48.08 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 700 VQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLKEGLESgEPgtDDGR 779
Cdd:COG0457 1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77
|
90 100
....*....|....*....|...
gi 1785372442 780 FYFHLGDALQRVG-SQEAYIWYE 801
Cdd:COG0457 78 ALNNLGLALQALGrYEEALEDYD 100
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
385-567 |
9.88e-06 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 49.65 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 385 QETEHEP-ETHRDEEAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEAPAvien 463
Cdd:PRK10811 849 RPQDVQVeEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPV---- 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 464 eDEDSEPVEErldeaepPTASDQEEINEEILHVIEDKIVKAFEQlqnpaEQAQSEPEEiqdVLTEEILQDDKAEESLLVP 543
Cdd:PRK10811 925 -TEQPQVITE-------SDVAVAQEVAEHAEPVVEPQDETADIE-----EAAETAEVV---VAEPEVVAQPAAPVVAEVA 988
|
170 180
....*....|....*....|....
gi 1785372442 544 EEQQETPTDEHKEVPEEKTEQPAG 567
Cdd:PRK10811 989 AEVETVTAVEPEVAPAQVPEATVE 1012
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
693-792 |
1.26e-05 |
|
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: 45.77 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 693 VVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLKEGLESgE 772
Cdd:COG4235 3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81
|
90 100
....*....|....*....|
gi 1785372442 773 PgtDDGRFYFHLGDALQRVG 792
Cdd:COG4235 82 P--DNPEALYLLGLAAFQQG 99
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
612-740 |
1.37e-05 |
|
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: 45.77 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 612 EALRAFESLVDKYPQSPKARYGKAQSEdalaekMRSNDiLLQAINTYGEVAEL-PNAPAELIKLtlkrrADRQQFLGRTR 690
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAY------LRLGR-YDEALAAYEKALRLdPDNADALLDL-----AEALLAAGDTE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1785372442 691 GSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPND 740
Cdd:COG4235 69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
686-776 |
1.98e-05 |
|
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: 45.00 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 686 LGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLK 765
Cdd:COG4235 30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109
|
90
....*....|.
gi 1785372442 766 EGLESGEPGTD 776
Cdd:COG4235 110 KLLALLPADAP 120
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
381-560 |
3.19e-05 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 48.24 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 381 LDDNQETEHEPETHRDEEAPSESQVTEDLQEVI---VDEHVTYEQEE--EHHTEDEPQHTEHLEVEESQTPDEEFEPEML 455
Cdd:PTZ00341 963 VEENVEENVEENVEENVEENVEENVEENVEENVeenVEENIEENVEEnvEENIEENVEEYDEENVEEVEENVEEYDEENV 1042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 456 EapaviENEDEDSEPVEERLDE-AEPPTASDQEEINEEILHVIEDKIVKAFEQlqNPAEQAQSEPEEIQDVLTEEIlqDD 534
Cdd:PTZ00341 1043 E-----EIEENAEENVEENIEEnIEEYDEENVEEIEENIEENIEENVEENVEE--NVEEIEENVEENVEENAEENA--EE 1113
|
170 180
....*....|....*....|....*.
gi 1785372442 535 KAEESLlvpEEQQETPTDEHKEVPEE 560
Cdd:PTZ00341 1114 NAEENA---EEYDDENPEEHNEEYDE 1136
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
594-744 |
4.06e-05 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.77 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 594 IKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQSE----------DALAEKMRSNDILLQAINTYGEVA- 662
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSAPEYLPALLLAGASEy 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 663 ---ELPNAPAELIKlTLK--------RR--ADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAV 729
Cdd:TIGR02917 307 qlgNLEQAYQYLNQ-ILKyapnshqaRRllASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY 385
|
170
....*....|....*
gi 1785372442 730 FEQVLAMSPNDGFAK 744
Cdd:TIGR02917 386 LAKATELDPENAAAR 400
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
686-769 |
4.11e-05 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 43.24 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 686 LGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAvFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLK 765
Cdd:COG3063 5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83
|
....
gi 1785372442 766 EGLE 769
Cdd:COG3063 84 RALE 87
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
591-743 |
1.20e-04 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 44.52 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 591 DKTIKAELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQSEDALAekmrsndILLQAINTYGEVAELPNApAE 670
Cdd:COG4785 3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALA-------AAALAAERIDRALALPDL-AQ 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785372442 671 LikltLKRRADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFA 743
Cdd:COG4785 75 L----YYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
|
|
| tol_pal_ybgF |
TIGR02795 |
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ... |
601-669 |
1.48e-04 |
|
tol-pal system protein YbgF; Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.
Pssm-ID: 188247 [Multi-domain] Cd Length: 117 Bit Score: 42.27 E-value: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785372442 601 AEKLRKKGKVDEALRAFESLVDKYPQSPKArygkaqsEDAL------AEKMRSNDillQAINTYGEVAEL-PNAPA 669
Cdd:TIGR02795 44 GEAYYAQGDYADAAKAFLAVVKKYPKSPKA-------PDALlklgmsLQELGDKE---KAKATLQQVIKRyPGSSA 109
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
378-544 |
1.51e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.93 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 378 QVALDDNQETEHEPETHRDEEAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEA 457
Cdd:PTZ00341 422 QKYMDMLDGSEDESVEDNEEEHSGDANEEELSVDEHVEEHNADDSGEQQSDDESGEHQSVNEIVEEQSVNEHVEEPTVAD 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 458 PAVIENEDEDSEpvEERLDEAEPPTASDQeeineeilHVIEDKIvkAFEQLQNPAEQAQSEPEEIqdvlTEEILQDDKAE 537
Cdd:PTZ00341 502 IVEQETVDEHVE--EPAVDENEEQQTADE--------HVEEPTI--AEEHVEEEISTAEEHIEEP----ASDVQQDSEAA 565
|
....*..
gi 1785372442 538 ESLLVPE 544
Cdd:PTZ00341 566 PTIEIPD 572
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
601-674 |
1.66e-04 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 41.90 E-value: 1.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785372442 601 AEKLRKKGKVDEALRAFESLVDKYPQSPK---ARYGKAQSEDALAEKMRSNDILLQAINTYGEVAELPNAPAELIKL 674
Cdd:COG1729 37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-568 |
5.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 114 AEDSEDDHPATQATAEPDDVEEEdiqdvfQPQDEADDLDKDLEEIVQ-DSLHESADDLDKDLQEVVEEIHEEAVDDLGKA 192
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKE------EAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 193 FDEEVQDSPH-----ESTDDLDQDLKEIVEDSYTEAAAADDLDKDLEEIVQESLHAEEDASETHEEADQVAEEEAHDEEP 267
Cdd:PTZ00121 1426 KAEEKKKADEakkkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 268 EVEKEVEAVETANVEAVFVEEQLELEvqDDEQAETTEEVPETEEADDNTVVEEAKVEIETesddQELDQDVKAEPEIEEI 347
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEK----KKAEEAKKAEEDKNMA 1579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 348 YKEELLEEDAEEQPEPEVIEETEPEEEREEQVALDDNQETEHEPETHRDEEA--PSESQVTEDLQEVIVDEHVTYEQEEE 425
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 426 HHTEDEPQHTEHLEVEESQTPDEEFEPEMLEAPAVIENEDEDSEPVEERLDEAEPPTASDQEEINEEILHVIEDKIVKAF 505
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785372442 506 EQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHKEVPEEKTEQPAGD 568
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
319-565 |
6.45e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.83 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 319 EEAKVEIETESDDQELDQDVKAEPEIEEIYKEELLEEDAEEQPEPEVIEETEPEEEREEQVALDDNQETEHEPETHRD-E 397
Cdd:TIGR00927 647 EEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEgT 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 398 EAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEmLEAPAVIENEDEDSEPVEERLDE 477
Cdd:TIGR00927 727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE-IQAGEDGEMKGDEGAEGKVEHEG 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 478 AEPPTASDQEEINEEILHVIEDKIVKAFEQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHKEV 557
Cdd:TIGR00927 806 ETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEE 885
|
....*...
gi 1785372442 558 PEEKTEQP 565
Cdd:TIGR00927 886 EEEENEEP 893
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
115-256 |
8.55e-04 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 43.62 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 115 EDSEDDHPATQATAEPDDVEEEDIQDVFQPQDEADDLDKDLEEIVQDSLHESADDLDKDLQEVVEEIHEEAVddlgkafD 194
Cdd:PTZ00341 1009 ENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENI-------E 1081
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785372442 195 EEVQDSPHESTDDLDQDLKEIVEDSYTEaaaadDLDKDLEEIVQEslHAEEDASETHEEADQ 256
Cdd:PTZ00341 1082 ENVEENVEENVEEIEENVEENVEENAEE-----NAEENAEENAEE--YDDENPEEHNEEYDE 1136
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
717-801 |
1.04e-03 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 39.38 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 717 YLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYlKEGLESGEpgtDDGRFYFHLGDALQRVG-SQE 795
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDP---NNAEALLNLAELLLELGdYDE 77
|
....*.
gi 1785372442 796 AYIWYE 801
Cdd:COG3063 78 ALAYLE 83
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
588-769 |
1.43e-03 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 42.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 588 NKFDKTIKAeldaAEKLRK------------------KGKVDEALRAFESLVDKYPQSPKARYGKA----QSEDALAEKM 645
Cdd:TIGR02917 445 GQFDKALAA----AKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 646 RSNDIL------LQAINTYGEVAELPNAPAE-LIKLTLKRRADRQQF------------LGRTRGSVVTLHKLVQLYPED 706
Cdd:TIGR02917 521 RFEKVLtidpknLRAILALAGLYLRTGNEEEaVAWLEKAAELNPQEIepalalaqyylgKGQLKKALAILNEAADAAPDS 600
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785372442 707 VTFRNELGVGYLLLGDNSNAKAVFEQVLAMSPNDGFAKVHYGFILKAENYIAESIPYLKEGLE 769
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
385-566 |
2.06e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 42.08 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 385 QETEHEPETHRDEEApsESQVTEDLQEViVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEapAVIENE 464
Cdd:PTZ00341 937 EHLKEHAEANIEEDA--EENVEEDAEEN-VEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEE--NVEENV 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 465 DED-SEPVEERLDEAEPPTASDQEEINEEILHVIEDKIVKAFEQ--LQNPAEQAQSEPEEIQDVLTEEILQ--DDKAEES 539
Cdd:PTZ00341 1012 EENiEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEEniEENIEEYDEENVEEIEENIEENIEEnvEENVEEN 1091
|
170 180
....*....|....*....|....*...
gi 1785372442 540 LLVPEEQQETPTDEH-KEVPEEKTEQPA 566
Cdd:PTZ00341 1092 VEEIEENVEENVEENaEENAEENAEENA 1119
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
596-738 |
3.52e-03 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 39.17 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 596 AELDAAEKLRKKGKVDEALRAFESLVDKYPQSPKARYGKAQSEDALAEKMRSNDILL-------QAINTYGEVAEL-PNA 667
Cdd:COG5010 8 DRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYnklgdfeESLALLEQALQLdPNN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785372442 668 PAeliklTLKRRADRQQFLGRTRGSVVTLHKLVQLYPEDVTFRNELGVGYLLLGDNSNAKAVFEQVLAMSP 738
Cdd:COG5010 88 PE-----LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
396-567 |
4.99e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 40.34 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 396 DEEAPSESQVTEDLQEVIVDEHVTYEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEAPavienEDEDSEPVEERL 475
Cdd:PHA03169 101 GSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQP-----SSFLQPSHEDSP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 476 DEAEPPTASDQEEINEEILHVIEDKIVKAFEQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHK 555
Cdd:PHA03169 176 EEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSY 255
|
170
....*....|...
gi 1785372442 556 EVPEEK-TEQPAG 567
Cdd:PHA03169 256 TVVGWKpSTRPGG 268
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
315-564 |
5.47e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 40.93 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 315 NTVVEEAKVEIETESDDQELDQDVKAEPEIEEiykeeLLEEDAEEQPEPEVIEEtepeeereeqvaLDDNQETEHEPETH 394
Cdd:PTZ00341 922 NLINKELKNQNENVPEHLKEHAEANIEEDAEE-----NVEEDAEENVEENVEEN------------VEENVEENVEENVE 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 395 RDEEAPSESQVTEDLQEVIvDEHVtyEQEEEHHTEDEPQHTEHLEVEESQTPDEEFEPEMLEapaviENEDEDSEPVEER 474
Cdd:PTZ00341 985 ENVEENVEENVEENVEENI-EENV--EENVEENIEENVEEYDEENVEEVEENVEEYDEENVE-----EIEENAEENVEEN 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 475 LDEaepptasDQEEINEEILHVIEDKIVKAFEqlQNPAEQAQSEPEEIQDVLTEEIlqDDKAEESllVPEEQQETPTDEH 554
Cdd:PTZ00341 1057 IEE-------NIEEYDEENVEEIEENIEENIE--ENVEENVEENVEEIEENVEENV--EENAEEN--AEENAEENAEEYD 1123
|
250
....*....|
gi 1785372442 555 KEVPEEKTEQ 564
Cdd:PTZ00341 1124 DENPEEHNEE 1133
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
135-341 |
7.23e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 40.54 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 135 EEDIQDVFQpQDEADDLDKDLEEIVQDSLHESADD-LDKDLQEVVEEIHEEAVDD-LGKAFDEEVQDSPHESTDDLDQDL 212
Cdd:PTZ00341 948 EEDAEENVE-EDAEENVEENVEENVEENVEENVEEnVEENVEENVEENVEENVEEnIEENVEENVEENIEENVEEYDEEN 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 213 KEIVEDSYTEAAAADDLDKdlEEIVQESLhaEEDASETHEEADQvaeeeahdeepevekeveavetANVEAVfvEEQLEL 292
Cdd:PTZ00341 1027 VEEVEENVEEYDEENVEEI--EENAEENV--EENIEENIEEYDE----------------------ENVEEI--EENIEE 1078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1785372442 293 EVQDDEQAETTEEVPETEEADDNTVVE--EAKVEIETESDDQELDQDVKAE 341
Cdd:PTZ00341 1079 NIEENVEENVEENVEEIEENVEENVEEnaEENAEENAEENAEEYDDENPEE 1129
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
432-566 |
9.03e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.02 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785372442 432 PQHTEHLEVEESQTPDEEFEPEMLEAPAVIENEDEDSEPVEERLD----------EAEPPTASDQEEINEEIL------- 494
Cdd:PRK10811 848 VRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAevveepvvvaEPQPEEVVVVETTHPEVIaapvteq 927
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785372442 495 -HVIEDKIVKAFEQLQNPAEQAQSEPEEIQDVLTEEILQDDKAEESLLVPEEQQETPTDEHKEVPEEKTEQPA 566
Cdd:PRK10811 928 pQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPE 1000
|
|
| |
