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Conserved domains on  [gi|564350298|ref|XP_006237924|]
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aspartyl/asparaginyl beta-hydroxylase isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 511-665 1.68e-73

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: 234.08  E-value: 1.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  511 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCTLLEKFS-ETTGCRRGQIKY 587
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298  588 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 665
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 253-468 2.80e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.55  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 253 LLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAASL- 331
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 332 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAK 411
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298 412 VHYGFILKAQNRIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
Asp-B-Hydro_N super family cl25755
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 25-94 3.53e-17

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.


The actual alignment was detected with superfamily member pfam05279:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 76.03  E-value: 3.53e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298   25 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 94
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 109-242 3.02e-06

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  109 EAETQAELEEQAPEGAEaQNVEDEVKEQIQSLLQESVHT------DHDTEDSYHVEETASQNHPNDAEEVMSEQESSDHG 182
Cdd:PTZ00341  992 EENVEENVEENIEENVE-ENVEENIEENVEEYDEENVEEveenveEYDEENVEEIEENAEENVEENIEENIEEYDEENVE 1070

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564350298  183 EavTDDGLQQHAEEVRHEDYDEPVYEPSEN--ERIE--ISDNAIDDSNIISEEINVASVEEQQD 242
Cdd:PTZ00341 1071 E--IEENIEENIEENVEENVEENVEEIEENveENVEenAEENAEENAEENAEEYDDENPEEHNE 1132
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 511-665 1.68e-73

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: 234.08  E-value: 1.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  511 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCTLLEKFS-ETTGCRRGQIKY 587
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298  588 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 665
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 507-672 1.43e-53

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 183.15  E-value: 1.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 507 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCTLLEKFsettgcr 581
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 582 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLI 657
Cdd:COG3555   93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 564350298 658 FIVDVWHPELTPQQR 672
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 253-468 2.80e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.55  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 253 LLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAASL- 331
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 332 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAK 411
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298 412 VHYGFILKAQNRIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 25-94 3.53e-17

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: 76.03  E-value: 3.53e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298   25 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 94
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 261-447 2.68e-07

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: 53.93  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  261 IKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAASL-PDAPTD-- 337
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  338 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLMGDN 390
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564350298  391 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTDDGRF 447
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 109-242 3.02e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  109 EAETQAELEEQAPEGAEaQNVEDEVKEQIQSLLQESVHT------DHDTEDSYHVEETASQNHPNDAEEVMSEQESSDHG 182
Cdd:PTZ00341  992 EENVEENVEENIEENVE-ENVEENIEENVEEYDEENVEEveenveEYDEENVEEIEENAEENVEENIEENIEEYDEENVE 1070

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564350298  183 EavTDDGLQQHAEEVRHEDYDEPVYEPSEN--ERIE--ISDNAIDDSNIISEEINVASVEEQQD 242
Cdd:PTZ00341 1071 E--IEENIEENIEENVEENVEENVEEIEENveENVEenAEENAEENAEENAEEYDDENPEEHNE 1132
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 265-329 3.26e-05

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 42.32  E-value: 3.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298  265 LDAAEKLRKRGKIEEAVSAFEELVRRYPQSP---RARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAA 329
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 511-665 1.68e-73

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: 234.08  E-value: 1.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  511 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCTLLEKFS-ETTGCRRGQIKY 587
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298  588 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 665
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 507-672 1.43e-53

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 183.15  E-value: 1.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 507 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCTLLEKFsettgcr 581
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 582 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRSWEEGKVLIFDDSFEHEVWQDASSFRLI 657
Cdd:COG3555   93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 564350298 658 FIVDVWHPELTPQQR 672
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 253-468 2.80e-18

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 85.55  E-value: 2.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 253 LLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAASL- 331
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 332 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAK 411
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298 412 VHYGFILKAQNRIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 25-94 3.53e-17

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: 76.03  E-value: 3.53e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298   25 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLLG 94
Cdd:pfam05279  12 FFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
271-436 3.08e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 3.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 271 LRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAASL-PDAPTdlvklSLKRRSER 349
Cdd:COG0457   18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 350 QQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIP 429
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ....*..
gi 564350298 430 YLKEGIE 436
Cdd:COG0457  166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 263-436 5.43e-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: 60.98  E-value: 5.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 263 AELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAaslpdaptdlvkls 342
Cdd:COG4783    6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHEA-------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 343 lkrrserqqflghmrgslltlqrlVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQN 422
Cdd:COG4783   65 ------------------------LELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                        170
                 ....*....|....
gi 564350298 423 RIAESIPYLKEGIE 436
Cdd:COG4783  121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 261-450 5.82e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.32  E-value: 5.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 261 IKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYgkaqcedDLAEKQRSNEVLRRAIETYQEAASL-PDAPTDLV 339
Cdd:COG3914   78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 340 KLSLKRRSerqqfLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILK 419
Cdd:COG3914  151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                        170       180       190
                 ....*....|....*....|....*....|.
gi 564350298 420 AQNRIAESIPYLKEGIESGDPGTDDGRFYFH 450
Cdd:COG3914  226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
353-468 6.25e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.02  E-value: 6.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 353 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLK 432
Cdd:COG0457   21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564350298 433 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG0457  101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 287-437 3.66e-09

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: 56.12  E-value: 3.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 287 LVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRL 366
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564350298 367 VQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIES 437
Cdd:COG5010   81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
367-468 5.91e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.24  E-value: 5.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 367 VQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESgDPgtDDGR 446
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                         90       100
                 ....*....|....*....|...
gi 564350298 447 FYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG0457   78 ALNNLGLALQALGRyEEALEDYD 100
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 270-372 6.03e-08

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 51.53  E-value: 6.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 270 KLRKRGKIEEAVSAFEELVRRYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAptdLVKLslkrr 346
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA---LLKL----- 73

                         90       100
                 ....*....|....*....|....*.
gi 564350298 347 SERQQFLGHMRGSLLTLQRLVQLFPS 372
Cdd:COG1729   74 GLSYLELGDYDKARATLEELIKKYPD 99
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 320-443 2.01e-07

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: 50.39  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 320 RAIETYQEAASL-PDAPTDLVKLSlkrRSERQQflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYE 398
Cdd:COG4235    1 EAIARLRQALAAnPNDAEGWLLLG---RAYLRL--GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564350298 399 EVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTD 443
Cdd:COG4235   76 RALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
384-468 2.26e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.01  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 384 YLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 462
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                 ....*.
gi 564350298 463 AYKWYE 468
Cdd:COG3063   78 ALAYLE 83
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 261-447 2.68e-07

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: 53.93  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  261 IKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAASL-PDAPTD-- 337
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  338 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLMGDN 390
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564350298  391 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDPGTDDGRF 447
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 268-341 3.02e-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: 46.52  E-value: 3.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564350298 268 AEKLRKRGKIEEAVSAFEELVRRYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLPDAPTDLVKL 341
Cdd:COG1729   37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 109-242 3.02e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  109 EAETQAELEEQAPEGAEaQNVEDEVKEQIQSLLQESVHT------DHDTEDSYHVEETASQNHPNDAEEVMSEQESSDHG 182
Cdd:PTZ00341  992 EENVEENVEENIEENVE-ENVEENIEENVEEYDEENVEEveenveEYDEENVEEIEENAEENVEENIEENIEEYDEENVE 1070

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564350298  183 EavTDDGLQQHAEEVRHEDYDEPVYEPSEN--ERIE--ISDNAIDDSNIISEEINVASVEEQQD 242
Cdd:PTZ00341 1071 E--IEENIEENIEENVEENVEENVEEIEENveENVEenAEENAEENAEENAEEYDDENPEEHNE 1132
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 109-239 3.90e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.17  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  109 EAETQAELEEQAPEGAEaQNVEDEVKEQIQSLLQESVHTDHDTEDSYHVEETASQN-HPNDAEEVMSEQESSDHGEAVTD 187
Cdd:PTZ00341  964 EENVEENVEENVEENVE-ENVEENVEENVEENVEENVEENIEENVEENVEENIEENvEEYDEENVEEVEENVEEYDEENV 1042

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564350298  188 DGLQQHAEEVRHEDYDEPVYEPSENERIEISDNAidDSNI---ISEEI--NVASVEE 239
Cdd:PTZ00341 1043 EEIEENAEENVEENIEENIEEYDEENVEEIEENI--EENIeenVEENVeeNVEEIEE 1097
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 107-239 8.05e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 49.40  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  107 PEEAE--TQAELEEQAPEGAEaQNVEDEVKEQIQSLLQESVHTDHDTEDSYHVEETASQNHPNDAEEVMSEQESSDHGEA 184
Cdd:PTZ00341  948 EEDAEenVEEDAEENVEENVE-ENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEEN 1026

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564350298  185 VtddglqQHAEEVRHEDYDEPVYEPSENERIEISDNaIDDSNIISEEINVASVEE 239
Cdd:PTZ00341 1027 V------EEVEENVEEYDEENVEEIEENAEENVEEN-IEENIEEYDEENVEEIEE 1074
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
353-436 1.05e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.39  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 353 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKvYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLK 432
Cdd:COG3063    5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                 ....
gi 564350298 433 EGIE 436
Cdd:COG3063   84 RALE 87
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 258-441 1.23e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.54  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  258 DKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARY--GKAQCED-DL--AEKQrsnevLRRAIET-YQEAASL 331
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEKE-----LRKALSLgYPKNQVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  332 PDaptdLVKLSLKRRSerqqflghmrgslltLQRLVQLFPSDTTLKND--------LGVGYLLMGDNDSAKKVYEEVLNV 403
Cdd:TIGR02917  94 PL----LARAYLLQGK---------------FQQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 564350298  404 TPNDGFAKVHYGFILKAQNRIAESIPYLKEgIESGDPG 441
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 268-436 1.37e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.54  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  268 AEKLRKRGKIEEAVSAFEELVRRYPQSPRARygkaqceDDLAEKQRSNEVLRRAIETYQEAASL-PDAPTDLVKLSlkrr 346
Cdd:TIGR02917 574 AQYYLGKGQLKKALAILNEAADAAPDSPEAW-------LMLGRAQLAAGDLNKAVSSFKKLLALqPDSALALLLLA---- 642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  347 sERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAE 426
Cdd:TIGR02917 643 -DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPA 721

                         170
                  ....*....|
gi 564350298  427 SIPYLKEGIE 436
Cdd:TIGR02917 722 AIQAYRKALK 731
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 279-407 1.48e-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: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 279 EAVSAFEELVRRYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAASL-PDAPTDLVKLslkrrSERQQFLGHMR 357
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLL-------LGRAYLRLGRYDEALAAYEKALRLdPDNADALLDL-----AEALLAAGDTE 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 564350298 358 GSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPND 407
Cdd:COG4235   69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 265-329 3.26e-05

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 42.32  E-value: 3.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564350298  265 LDAAEKLRKRGKIEEAVSAFEELVRRYPQSP---RARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAA 329
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLAALRQGRLAEAAAAYRAALRAAPGDP 68
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 272-436 9.52e-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: 45.84  E-value: 9.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  272 RKRGKIEEAVSAFEELVRRYPQSPRARYGKAqcedDLAEKQRSNEvlrRAIETYQEAASLpdAPTDL-VKLSLKRRSERQ 350
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALA----GLYLRTGNEE---EAVAWLEKAAEL--NPQEIePALALAQYYLGK 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  351 qflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPY 430
Cdd:TIGR02917 581 ---GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITS 657


                  ....*.
gi 564350298  431 LKEGIE 436
Cdd:TIGR02917 658 LKRALE 663
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 108-204 1.46e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.16  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  108 EEAETQAE--LEEQAPEGAE------AQNVEDEVKEQIQSLLQESVHtdhdtEDSYHVEETASQNHPNDAEEvMSEQESS 179
Cdd:PTZ00341 1043 EEIEENAEenVEENIEENIEeydeenVEEIEENIEENIEENVEENVE-----ENVEEIEENVEENVEENAEE-NAEENAE 1116

                          90       100
                  ....*....|....*....|....*
gi 564350298  180 DHGEAVTDDGLQQHAEEvrhedYDE 204
Cdd:PTZ00341 1117 ENAEEYDDENPEEHNEE-----YDE 1136
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 263-327 1.49e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.49  E-value: 1.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564350298 263 AELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQE 327
Cdd:COG4783   74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 265-345 2.32e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 265 LDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAASL--PDAPTDLVKLS 342
Cdd:COG4235   55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                 ...
gi 564350298 343 LKR 345
Cdd:COG4235  128 IAE 130
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 253-373 2.51e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 253 LLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAASL- 331
Cdd:COG4783   30 ALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLd 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564350298 332 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSD 373
Cdd:COG4783  103 PEHPE-----AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 268-373 2.53e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 268 AEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAASLpdAPTDLVKLSLKRRS 347
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEELLERALAL--DPDNPEALYLLGLA 94

                         90       100
                 ....*....|....*....|....*.
gi 564350298 348 ERQQflGHMRGSLLTLQRLVQLFPSD 373
Cdd:COG4235   95 AFQQ--GDYAEAIAAWQKLLALLPAD 118
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 278-353 3.77e-04

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 42.56  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 278 EEAVSAFEELVRRYPQSPRARYGKA---QCEDDLAEK---------QRSNEV-----LRRAIETYQEAASLPDAPTDLVK 340
Cdd:COG4105  131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                         90
                 ....*....|....*
gi 564350298 341 --LSLKRRSERQQFL 353
Cdd:COG4105  211 ayYALGRYDEAQDAA 225
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 271-405 4.12e-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: 41.48  E-value: 4.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 271 LRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAaslpdaptdlvklslkrrserq 350
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYEKA---------------------- 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564350298 351 qflghmrgslltlqrlVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTP 405
Cdd:COG5010  115 ----------------LALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 108-239 5.37e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.24  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  108 EEAETQAE-LEEQAPEGAEAqNVEDEVKEQIQSLLQESVhtDHDTEDSyhVEETASQNHPNDAEEVMSEQESSDHGEAVt 186
Cdd:PTZ00341  926 KELKNQNEnVPEHLKEHAEA-NIEEDAEENVEEDAEENV--EENVEEN--VEENVEENVEENVEENVEENVEENVEENV- 999

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564350298  187 DDGLQQHAEEVRHEDYDEPVYEPSENERIEISDNAIDdsniiSEEINVASVEE 239
Cdd:PTZ00341 1000 EENIEENVEENVEENIEENVEEYDEENVEEVEENVEE-----YDEENVEEIEE 1047
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 362-468 6.70e-04

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: 42.02  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 362 TLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESIPYLKEGIESGDpg 441
Cdd:COG2956   30 LLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDP-- 107

                         90       100
                 ....*....|....*....|....*...
gi 564350298 442 tDDGRFYFHLGDAMQRVGN-KEAYKWYE 468
Cdd:COG2956  108 -DDAEALRLLAEIYEQEGDwEKAIEVLE 134
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
258-428 1.59e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 40.67  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 258 DKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASLpdaptd 337
Cdd:COG4785    3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLY------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 338 lvklslKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFI 417
Cdd:COG4785   77 ------YERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIA 150

                        170
                 ....*....|.
gi 564350298 418 LKAQNRIAESI 428
Cdd:COG4785  151 LYYLGRYELAI 161
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 277-351 1.70e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 40.61  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  277 IEEAVSAFEELVRRYPQSPRARYGKAQ---CEDDLAEK---------QRSNEV-----LRRAIETYQEAASLPDAPTDLV 339
Cdd:TIGR03302 131 AREAFEAFQELIRRYPNSEYAPDAKKRmdyLRNRLAGKelyvarfylKRGAYVaainrFQTVVENYPDTPATEEALARLV 210

                          90
                  ....*....|....
gi 564350298  340 K--LSLKRRSERQQ 351
Cdd:TIGR03302 211 EayLKLGLTDLAQD 224
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 266-371 1.87e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 40.61  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  266 DAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARygKAQCedDLAEKQRSNEVLRRAIETYQEAASL----PDAPT----- 336
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE--QAQL--DLAYAYYKSGDYAEAIAAADRFIRLhpnhPDADYayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564350298  337 DLVKLSLKRRSERQQflGHMRGSLLTLQRLVQLFP 371
Cdd:TIGR03302 114 GLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYP 146
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 262-327 2.02e-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: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 262 KAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPR---ARYGKAQCEDDLAEK-QRSNEVLRRAIETYQE 327
Cdd:COG4105   70 QAQLMLAYAYYKQGDYEEAIAAADRFIKLYPNSPNadyAYYLRGLSYYEQSPDsDRDQTSTRKAIEAFQE 139
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 258-371 3.66e-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: 39.86  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 258 DKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSP---RARYGKAQC---EDDLAEkqrsnevlrrAIETYQEAASL 331
Cdd:COG4105   29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564350298 332 ----PDAPTDLVKLSL-----KRRSERQQflGHMRGSLLTLQRLVQLFP 371
Cdd:COG4105   99 ypnsPNADYAYYLRGLsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYP 145
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
271-406 3.76e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.07  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 271 LRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCeddLAEKQRsnevlrraietYQEAaslpdaptdlvklslkrrserq 350
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLL---LLEQGR-----------YDEA---------------------- 45

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564350298 351 qflghmrgslLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPN 406
Cdd:COG3063   46 ----------IALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 253-303 4.76e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.28  E-value: 4.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564350298 253 LLNKFDKTIKAE---LDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQ 303
Cdd:COG1729   56 LLKRYPDSPKAPdalLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 253-334 5.93e-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: 39.09  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298 253 LLNKFDKTIKAElDAAEKLR------------------KRGKIEEAVSAFEELVRRYPQSP---RARYGKAQCEDDLAEK 311
Cdd:COG4105  140 LINRYPDSEYAE-DAKKRIDelrdklarkelevaryylKRGAYVAAINRFQNVLEDYPDTPaveEALYLLVEAYYALGRY 218

                         90       100
                 ....*....|....*....|...
gi 564350298 312 QRSNEVLRRAIETYQEAASLPDA 334
Cdd:COG4105  219 DEAQDAAAVLGKNYPDSPYLKDA 241
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 214-428 5.98e-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: 40.07  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  214 RIEISDNAIDDSNIISEEINVASVEEQQ------DTPPVKKKKPKLLNKFDKTIKAELDA------AEKLRKRGKIEEAV 281
Cdd:TIGR02917 677 QLLLAAKRTESAKKIAKSLQKQHPKAALgfelegDLYLRQKDYPAAIQAYRKALKRAPSSqnaiklHRALLASGNTAEAV 756

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  282 SAFEELVRRYPQSPRARYgkAQCEDDLAEKQRSNevlrrAIETYQEAASLpdAPTDLVKL------SLKRRSERqqflgh 355
Cdd:TIGR02917 757 KTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDK-----AIKHYQTVVKK--APDNAVVLnnlawlYLELKDPR------ 821

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564350298  356 mrgSLLTLQRLVQLFPSDTTLKNDLGVGYLLMGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNRIAESI 428
Cdd:TIGR02917 822 ---ALEYAERALKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEAR 891
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 253-331 6.82e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 38.94  E-value: 6.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564350298 253 LLNKFDKTIKAELDAAEKLRKRGKIEEAVSAFEELVRRYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAASL 331
Cdd:COG2956  170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLL 248
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 72-243 7.46e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 39.77  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298   72 KLGVYDADGDGDFDVDDAKVLLGLKERSTSERTFPPEEAETQAELEEQAPEGAEAQNVEDEVKEQiqsllqesvhtdHDT 151
Cdd:PTZ00341  396 KDGKYLDDDSSDALYTDEDLLFDLEKQKYMDMLDGSEDESVEDNEEEHSGDANEEELSVDEHVEE------------HNA 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350298  152 EDSYHVEETASQNHPNDAEEVMSEQESSDHGEAVTDDglqqhaEEVRHEDYDEPVYEPS--ENERIEISDNAIDDSNI-- 227
Cdd:PTZ00341  464 DDSGEQQSDDESGEHQSVNEIVEEQSVNEHVEEPTVA------DIVEQETVDEHVEEPAvdENEEQQTADEHVEEPTIae 537

                         170       180
                  ....*....|....*....|....*
gi 564350298  228 --ISEEINVA--SVEE-----QQDT 243
Cdd:PTZ00341  538 ehVEEEISTAeeHIEEpasdvQQDS 562
 
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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