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Conserved domains on  [gi|2069539933|ref|XP_042319649|]
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aspartyl/asparaginyl beta-hydroxylase isoform X5 [Sceloporus undulatus]

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 ...
 637-791 2.82e-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: 236.01  E-value: 2.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 637 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 713
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539933 714 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 791
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 6.50e-35

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: 126.88  E-value: 6.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539933 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 381-594 5.96e-17

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: 81.70  E-value: 5.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 381 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 446
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 447 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 526
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539933 527 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 124-335 3.05e-07

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: 54.41  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  124 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 199
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  200 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQ--PESPDETEITL 277
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEydEENVEEIEENI 1076

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  278 EDTLEHNTElEN--EDFIEIQDTDGEPFTEHHYENkqdkpsASDSFTEHIESVDDSEPTE 335
Cdd:PTZ00341  1077 EENIEENVE-ENveENVEEIEENVEENVEENAEEN------AEENAEENAEEYDDENPEE 1129
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 637-791 2.82e-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: 236.01  E-value: 2.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 637 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 713
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539933 714 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 791
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 633-798 8.83e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 8.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 633 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 707
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 708 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 783
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539933 784 FIVDVWHPELTPQQR 798
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 6.50e-35

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: 126.88  E-value: 6.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539933 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 381-594 5.96e-17

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: 81.70  E-value: 5.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 381 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 446
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 447 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 526
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539933 527 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 388-501 1.47e-08

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: 53.44  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 388 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 464
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539933 465 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 501
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 124-335 3.05e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.41  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  124 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 199
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  200 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQ--PESPDETEITL 277
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEydEENVEEIEENI 1076

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  278 EDTLEHNTElEN--EDFIEIQDTDGEPFTEHHYENkqdkpsASDSFTEHIESVDDSEPTE 335
Cdd:PTZ00341  1077 EENIEENVE-ENveENVEEIEENVEENVEENAEEN------AEENAEENAEEYDDENPEE 1129
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 229-353 2.19e-04

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 43.70  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 229 HESIQEEPASDYQPE--EPEADDAHVTYEYHTHMEEVMDQPESPDETEITLEDTLEHNTELENEDFIEIQ-DTDGEPFTE 305
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETEPESDIESETEFETEPEtEPDTAPTTE 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539933 306 HHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 353
Cdd:pfam06390 148 PETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 637-791 2.82e-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: 236.01  E-value: 2.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 637 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 713
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539933 714 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 791
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 633-798 8.83e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 8.83e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 633 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 707
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 708 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 783
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539933 784 FIVDVWHPELTPQQR 798
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 6.50e-35

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: 126.88  E-value: 6.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539933 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 381-594 5.96e-17

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: 81.70  E-value: 5.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 381 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 446
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 447 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 526
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539933 527 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
397-562 2.21e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.72  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 397 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSeddLAEKKRsneiLQRSINTYGEVASL-PNIPDdlvklALKRRADR 475
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 476 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIP 555
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2069539933 556 YLKEGLE 562
Cdd:COG0457   166 LLEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
468-594 8.41e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.10  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 468 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 547
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539933 548 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG0457    90 GRYEEALEDYDKALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 390-562 8.78e-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: 60.59  E-value: 8.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 390 ELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseddlaekkrsneILQRsintygevaslpnipddlvklal 469
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ----------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 470 krradrqqfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENK 549
Cdd:COG4783    51 ---------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                         170
                  ....*....|...
gi 2069539933 550 IEESIPYLKEGLE 562
Cdd:COG4783   122 PDEAIAALEKALE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 479-563 1.15e-10

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: 60.74  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 479 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 558
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2069539933 559 EGLES 563
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 464-594 1.46e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 64.63  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 464 LVKLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFI 543
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2069539933 544 LKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG3914   156 LRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
418-612 4.83e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.79  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 418 PQSPRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNIPDdlvklALKRRADRQQFLGHMRGSLVTLQKLVNLFP 497
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELD------PDDAE-----ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 498 NDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHL 577
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2069539933 578 GDAMQRVGN-SEAYKWYELGHQRGHFASVWQRSLYN 612
Cdd:COG0457   151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 486-594 5.60e-09

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: 55.01  E-value: 5.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 486 LVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgD 565
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069539933 566 PgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG4235    82 P--DNPEALYLLGLAAFQQGDyAEAIAAWQ 109
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 388-501 1.47e-08

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: 53.44  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 388 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 464
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539933 465 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 501
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
493-594 2.44e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.78  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 493 VNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGR 572
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2069539933 573 FYFHLGDAMQRVGN-SEAYKWYE 594
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 396-498 2.62e-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: 52.69  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 396 KLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGEvaslpnipDDLVKLALKRR 472
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD--------SPKAPDALLKL 73

                          90       100
                  ....*....|....*....|....*.
gi 2069539933 473 ADRQQFLGHMRGSLVTLQKLVNLFPN 498
Cdd:COG1729    74 GLSYLELGDYDKARATLEELIKKYPD 99
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 391-576 1.50e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 55.00  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 391 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkaqsedDLAEKKRSNEILQRSINTYGEVASLPniPDDLvkLALK 470
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN--PDFA--EAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 471 RRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKI 550
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDW 230

                         170       180
                  ....*....|....*....|....*.
gi 2069539933 551 EESIPYLKEGLESGDPGTDDGRFYFH 576
Cdd:COG3914   231 EVYDRFEELLAALARGPSELSPFALL 256
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
510-594 2.36e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.40  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 510 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 588
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2069539933 589 AYKWYE 594
Cdd:COG3063    78 ALAYLE 83
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 124-335 3.05e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.41  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  124 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 199
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  200 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQ--PESPDETEITL 277
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEydEENVEEIEENI 1076

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  278 EDTLEHNTElEN--EDFIEIQDTDGEPFTEHHYENkqdkpsASDSFTEHIESVDDSEPTE 335
Cdd:PTZ00341  1077 EENIEENVE-ENveENVEEIEENVEENVEENAEEN------AEENAEENAEEYDDENPEE 1129
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 461-569 3.49e-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: 50.00  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 461 PDDLVKLALkrRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHY 540
Cdd:COG4235    14 PNDAEGWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91

                          90       100
                  ....*....|....*....|....*....
gi 2069539933 541 GFILKAENKIEESIPYLKEGLESGDPGTD 569
Cdd:COG4235    92 GLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
479-562 7.77e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.86  E-value: 7.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 479 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRvYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 558
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2069539933 559 EGLE 562
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 510-594 8.68e-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: 49.57  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 510 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 588
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2069539933 589 AYKWYE 594
Cdd:COG5010   141 AKAALQ 146
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 387-573 2.40e-06

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: 51.24  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 387 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSE----------DDLAEKKRSN-------------EI 443
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSApeylpalllagasEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 444 LQRSINTYGE-----VASLPNIPddlvkLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNN 518
Cdd:TIGR02917 307 QLGNLEQAYQylnqiLKYAPNSH-----QARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539933 519 AKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESGDPGTDDGRF 573
Cdd:TIGR02917 382 AAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 468-594 5.00e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.99  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 468 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 547
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2069539933 548 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGNSEAYKWYE 594
Cdd:COG3914   194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFE 237
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 400-582 1.11e-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: 48.93  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 400 KGKVEEALKAFETLVSKYPQSPRARYGKAQ---SEDDLAE-KKRSNEILQrsintygevASLPNIPddlvklALKRRADR 475
Cdd:TIGR02917 138 LGQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEaRALIDEVLT---------ADPGNVD------ALLLKGDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 476 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAkvHYgfiLKA-----ENKI 550
Cdd:TIGR02917 203 LLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNY 277

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2069539933 551 EESIPYLKEGLESgDPGTDDGRFY-----FHLGDAMQ 582
Cdd:TIGR02917 278 EDARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 381-562 1.17e-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: 48.93  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 381 NKFDKGIKteldAAEKLRK------------------KGKVEEALKAFETLVSKYPQSPRARYGKA----QSEDDLAEKK 438
Cdd:TIGR02917 445 GQFDKALA----AAKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 439 RSNEILQ------RSINTYGEVASLPNIPDD----LVKLALKRRAD---RQQFLGHMRG------SLVTLQKLVNLFPND 499
Cdd:TIGR02917 521 RFEKVLTidpknlRAILALAGLYLRTGNEEEavawLEKAAELNPQEiepALALAQYYLGkgqlkkALAILNEAADAAPDS 600

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539933 500 TSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLE 562
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 394-473 4.18e-05

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: 43.44  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 394 AEKLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNipDDLVKLALK 470
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY------PD--SEAAKEARA 108


                  ...
gi 2069539933 471 RRA 473
Cdd:COG1729   109 RLA 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
387-536 4.22e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 387 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSEDDLAEKKRSNEIlqrsintYGEVASLPNIPDdlvk 466
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQ---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 467 lALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFA 536
Cdd:COG4785    75 -LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 125-309 6.36e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.70  E-value: 6.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  125 ERSVQEQpVLKDAEEVIQPAKETHTraERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYEEPNIQEDMESN 202
Cdd:PTZ00341   964 EENVEEN-VEENVEENVEENVEENV--EENVEENVEEnvEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEE 1040

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933  203 KIPEVptleevyveelEDKIPEVLEahESIqEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDqpESPDETEITLEDTLE 282
Cdd:PTZ00341  1041 NVEEI-----------EENAEENVE--ENI-EENIEEYDEENVEEIEENIEENIEENVEENVE--ENVEEIEENVEENVE 1104

                          170       180
                   ....*....|....*....|....*....
gi 2069539933  283 HNTELENEDFIE--IQDTDGEPFTEHHYE 309
Cdd:PTZ00341  1105 ENAEENAEENAEenAEEYDDENPEEHNEE 1133
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 391-589 1.90e-04

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: 45.07  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 391 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARY--GKAQSE--DDLAEKKRSNEILQRSintYGEVASLPnipdDLVK 466
Cdd:TIGR02917  26 IEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLAlgDYAAAEKELRKALSLG---YPKNQVLP----LLAR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 467 LALKRRADrqqflghmrgslvtlQKLVNLFPNDTSFKNN--------LGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKV 538
Cdd:TIGR02917  99 AYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069539933 539 HYGFILKAENKIEESIPYLKEGLeSGDPGTDDGrfYFHLGDAMQRVGNSEA 589
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVL-TADPGNVDA--LLLKGDLLLSLGNIEL 211
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 229-353 2.19e-04

Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian neuroendocrine-specific golgi protein P55 (NESP55) sequences. NESP55 is a novel member of the chromogranin family and is a soluble, acidic, heat-stable secretory protein that is expressed exclusively in endocrine and nervous tissues, although less widely than chromogranins.


Pssm-ID: 115071 [Multi-domain]  Cd Length: 261  Bit Score: 43.70  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 229 HESIQEEPASDYQPE--EPEADDAHVTYEYHTHMEEVMDQPESPDETEITLEDTLEHNTELENEDFIEIQ-DTDGEPFTE 305
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHEDEDFEPELARPECLEYDEDDFDTETDSETEPESDIESETEFETEPEtEPDTAPTTE 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539933 306 HHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 353
Cdd:pfam06390 148 PETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 397-531 2.55e-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: 42.25  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 397 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAqseddlaekkrsneilqrsintygevaslpnipddlvkLALKRradrq 476
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLA--------------------------------------LLYSR----- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539933 477 qfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAP 531
Cdd:COG5010   101 --SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 392-498 6.24e-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: 42.18  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 392 DAAEKLRKKGKVEEALKAFETLVSKYPQSP---RARYGKAQSEDDLAEKKRSNEILQRSINTYgevASLPNIPDDLVKLA 468
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAYYKQGDYEEAIAAADRFIKLY---PNSPNADYAYYLRG 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2069539933 469 L-----KRRADRQQflGHMRGSLVTLQKLVNLFPN 498
Cdd:COG4105   114 LsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 392-498 7.61e-04

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: 41.77  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 392 DAAEKLRKKGKVEEALKAFETLVSKYPQSPRARygkaQSEDDLAEKKRSNEILQRSINTYGEVASL-PNIPD-D------ 463
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhPNHPDaDyayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2069539933 464 -LVKLALKRRADRQQflGHMRGSLVTLQKLVNLFPN 498
Cdd:TIGR03302 114 gLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYPN 147
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 380-528 5.40e-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: 40.45  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 380 LNKFDKGIKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRAR------YGKAQSEDDLAEKKRSNEIlqrsintyge 453
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLnnlawlYLELKDPRALEYAERALKL---------- 832

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539933 454 VASLPNIPDDLVKLALKRradrqqflGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLD 528
Cdd:TIGR02917 833 APNIPAILDTLGWLLVEK--------GEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 380-554 7.72e-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: 39.68  E-value: 7.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 380 LNKFDKGIKTELDA------AEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkAQSEDDLAEKKRSN------EILQRS 447
Cdd:TIGR02917 723 IQAYRKALKRAPSSqnaiklHRALLASGNTAEAVKTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDKaikhyqTVVKKA 800

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539933 448 INtygEVASLPNipddLVKLALKRRADRQqfLGHMRGSLvtlqKLVnlfPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVL 527
Cdd:TIGR02917 801 PD---NAVVLNN----LAWLYLELKDPRA--LEYAERAL----KLA---PNIPAILDTLGWLLVEKGEADRALPLLRKAV 864

                         170       180
                  ....*....|....*....|....*..
gi 2069539933 528 DLAPNDGFAKVHYGFILKAENKIEESI 554
Cdd:TIGR02917 865 NIAPEAAAIRYHLALALLATGRKAEAR 891
 
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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