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Conserved domains on  [gi|2069539931|ref|XP_042319648|]
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aspartyl/asparaginyl beta-hydroxylase isoform X4 [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 ...
 638-792 5.52e-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: 235.23  E-value: 5.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 638 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 714
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931 715 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 792
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 ...
 16-96 1.52e-34

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: 125.72  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  16 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 95
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539931  96 G 96
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 382-595 1.66e-16

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: 80.54  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 382 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 447
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 448 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 527
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539931 528 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 113-336 1.49e-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: 52.10  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  113 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 188
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  189 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 268
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931  269 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 336
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 638-792 5.52e-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: 235.23  E-value: 5.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 638 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 714
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931 715 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 792
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 634-799 1.02e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 634 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 708
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 709 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 784
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539931 785 FIVDVWHPELTPQQR 799
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 16-96 1.52e-34

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: 125.72  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  16 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 95
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539931  96 G 96
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 382-595 1.66e-16

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: 80.54  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 382 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 447
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 448 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 527
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539931 528 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
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 ...
 389-502 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 2069539931 389 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 465
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539931 466 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 502
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 113-336 1.49e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 52.10  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  113 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 188
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  189 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 268
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931  269 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 336
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 218-354 4.18e-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: 42.93  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 218 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 295
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539931 296 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 354
Cdd:pfam06390 134 TEpetEPDTAPTTEPETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 638-792 5.52e-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: 235.23  E-value: 5.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 638 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 714
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931 715 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 792
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 634-799 1.02e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 634 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 708
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 709 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 784
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539931 785 FIVDVWHPELTPQQR 799
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 16-96 1.52e-34

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: 125.72  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  16 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 95
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539931  96 G 96
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 382-595 1.66e-16

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: 80.54  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 382 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 447
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 448 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 527
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539931 528 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
398-563 4.58e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 398 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSeddLAEKKRsneiLQRSINTYGEVASL-PNIPDdlvklALKRRADR 476
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 477 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIP 556
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2069539931 557 YLKEGLE 563
Cdd:COG0457   166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 391-563 1.32e-10

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 59.82  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 391 ELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseddlaekkrsneILQRsintygevaslpnipddlvklal 470
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ----------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 471 krradrqqfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENK 550
Cdd:COG4783    51 ---------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                         170
                  ....*....|...
gi 2069539931 551 IEESIPYLKEGLE 563
Cdd:COG4783   122 PDEAIAALEKALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
469-595 1.40e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.33  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 469 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 548
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539931 549 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
Cdd:COG0457    90 GRYEEALEDYDKALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 465-595 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 2069539931 465 LVKLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFI 544
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2069539931 545 LKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
Cdd:COG3914   156 LRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 480-564 1.70e-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: 60.36  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 480 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 559
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2069539931 560 EGLES 564
Cdd:COG5010   147 RALGT 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
469-613 8.29e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.02  E-value: 8.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 469 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 548
Cdd:COG0457    44 ALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLEL 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539931 549 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYELGHQRGHFASVWQRSLYN 613
Cdd:COG0457   124 GRYDEAIEAYERALEL-DP--DDADALYNLGIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 487-595 7.49e-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: 54.63  E-value: 7.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 487 LVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgD 566
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069539931 567 PgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 595
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 ...
 389-502 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 2069539931 389 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 465
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539931 466 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 502
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 397-499 3.12e-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: 52.30  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 397 KLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGEvaslpnipDDLVKLALKRR 473
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD--------SPKAPDALLKL 73

                          90       100
                  ....*....|....*....|....*.
gi 2069539931 474 ADRQQFLGHMRGSLVTLQKLVNLFPN 499
Cdd:COG1729    74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
494-595 4.10e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.01  E-value: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 494 VNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGR 573
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2069539931 574 FYFHLGDAMQRVGN-SEAYKWYE 595
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 392-577 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 2069539931 392 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkaqsedDLAEKKRSNEILQRSINTYGEVASLPniPDDLvkLALK 471
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN--PDFA--EAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 472 RRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKI 551
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDW 230

                         170       180
                  ....*....|....*....|....*.
gi 2069539931 552 EESIPYLKEGLESGDPGTDDGRFYFH 577
Cdd:COG3914   231 EVYDRFEELLAALARGPSELSPFALL 256
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
511-595 3.60e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.63  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 511 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 589
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2069539931 590 AYKWYE 595
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 462-570 4.41e-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: 49.62  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 462 PDDLVKLALkrRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHY 541
Cdd:COG4235    14 PNDAEGWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91

                          90       100
                  ....*....|....*....|....*....
gi 2069539931 542 GFILKAENKIEESIPYLKEGLESGDPGTD 570
Cdd:COG4235    92 GLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
480-563 1.06e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.47  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 480 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRvYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 559
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2069539931 560 EGLE 563
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 511-595 1.31e-06

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: 48.80  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 511 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 589
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2069539931 590 AYKWYE 595
Cdd:COG5010   141 AKAALQ 146
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 113-336 1.49e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 52.10  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  113 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 188
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  189 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 268
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539931  269 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 336
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 388-574 2.49e-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: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 388 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSE----------DDLAEKKRSN-------------EI 444
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSApeylpalllagasEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 445 LQRSINTYGE-----VASLPNIPddlvkLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNN 519
Cdd:TIGR02917 307 QLGNLEQAYQylnqiLKYAPNSH-----QARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539931 520 AKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESGDPGTDDGRF 574
Cdd:TIGR02917 382 AAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 469-595 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 2069539931 469 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 548
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2069539931 549 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGNSEAYKWYE 595
Cdd:COG3914   194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFE 237
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 401-583 1.16e-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: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 401 KGKVEEALKAFETLVSKYPQSPRARYGKAQ---SEDDLAE-KKRSNEILQrsintygevASLPNIPddlvklALKRRADR 476
Cdd:TIGR02917 138 LGQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEaRALIDEVLT---------ADPGNVD------ALLLKGDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 477 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAkvHYgfiLKA-----ENKI 551
Cdd:TIGR02917 203 LLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNY 277

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2069539931 552 EESIPYLKEGLESgDPGTDDGRFY-----FHLGDAMQ 583
Cdd:TIGR02917 278 EDARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 382-563 1.21e-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: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 382 NKFDKGIKteldAAEKLRK------------------KGKVEEALKAFETLVSKYPQSPRARYGKA----QSEDDLAEKK 439
Cdd:TIGR02917 445 GQFDKALA----AAKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 440 RSNEILQ------RSINTYGEVASLPNIPDD----LVKLALKRRAD---RQQFLGHMRG------SLVTLQKLVNLFPND 500
Cdd:TIGR02917 521 RFEKVLTidpknlRAILALAGLYLRTGNEEEavawLEKAAELNPQEiepALALAQYYLGkgqlkkALAILNEAADAAPDS 600

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539931 501 TSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLE 563
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 395-454 4.75e-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: 4.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539931 395 AEKLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGE 454
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKYPD 99
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
388-537 5.27e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.29  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 388 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSEDDLAEKKRSNEIlqrsintYGEVASLPNIPDdlvk 467
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQ---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 468 lALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFA 537
Cdd:COG4785    75 -LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 392-590 2.04e-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: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 392 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARY--GKAQSE--DDLAEKKRSNEILQRSintYGEVASLPnipdDLVK 467
Cdd:TIGR02917  26 IEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLAlgDYAAAEKELRKALSLG---YPKNQVLP----LLAR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 468 LALKRRADrqqflghmrgslvtlQKLVNLFPNDTSFKNN--------LGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKV 539
Cdd:TIGR02917  99 AYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069539931 540 HYGFILKAENKIEESIPYLKEGLeSGDPGTDDGrfYFHLGDAMQRVGNSEA 590
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVL-TADPGNVDA--LLLKGDLLLSLGNIEL 211
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 398-532 3.91e-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: 41.87  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 398 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAqseddlaekkrsneilqrsintygevaslpnipddlvkLALKRradrq 477
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLA--------------------------------------LLYSR----- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539931 478 qfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAP 532
Cdd:COG5010   101 --SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 218-354 4.18e-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: 42.93  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 218 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 295
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539931 296 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 354
Cdd:pfam06390 134 TEpetEPDTAPTTEPETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 106-310 7.11e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.24  E-value: 7.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  106 KAKVKGLKERSVQ---EQPVLKDAEEVIQPAKETHTraERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIye 180
Cdd:PTZ00341   944 EANIEEDAEENVEedaEENVEENVEENVEENVEENV--EENVEENVEEnvEENVEENVEENIEENVEENVEENIEENV-- 1019

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931  181 epniqEDMESNKIPEVPTLEEVYVEELEDKIPEVLEAH-ESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDqpESP 259
Cdd:PTZ00341  1020 -----EEYDEENVEEVEENVEEYDEENVEEIEENAEENvEENIEENIEEYDEENVEEIEENIEENIEENVEENVE--ENV 1092

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069539931  260 DETEITLEDTLEHNTEDTehhdyVDERELENedfieIQDTDGEPFTEHHYE 310
Cdd:PTZ00341  1093 EEIEENVEENVEENAEEN-----AEENAEEN-----AEEYDDENPEEHNEE 1133
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 393-499 7.76e-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: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 393 DAAEKLRKKGKVEEALKAFETLVSKYPQSP---RARYGKAQSEDDLAEKKRSNEILQRSINTYgevASLPNIPDDLVKLA 469
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAYYKQGDYEEAIAAADRFIKLY---PNSPNADYAYYLRG 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2069539931 470 L-----KRRADRQQflGHMRGSLVTLQKLVNLFPN 499
Cdd:COG4105   114 LsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 393-499 9.47e-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: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 393 DAAEKLRKKGKVEEALKAFETLVSKYPQSPRARygkaQSEDDLAEKKRSNEILQRSINTYGEVASL-PNIPD-D------ 464
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhPNHPDaDyayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2069539931 465 -LVKLALKRRADRQQflGHMRGSLVTLQKLVNLFPN 499
Cdd:TIGR03302 114 gLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYPN 147
ATG27 pfam09451
Autophagy-related protein 27;
1-39 2.19e-03

Autophagy-related protein 27;


Pssm-ID: 430622  Cd Length: 261  Bit Score: 40.78  E-value: 2.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539931   1 MDTYQL-LKTKHG--------GNKNGKKEGISGSSFFTWFMVIALLGV 39
Cdd:pfam09451 159 DDKLRLeWKTKYAcekdesdpDDGDGGGNGGSGWGWFTWFFIILFLFT 206
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 381-529 5.45e-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: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 381 LNKFDKGIKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRAR------YGKAQSEDDLAEKKRSNEIlqrsintyge 454
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLnnlawlYLELKDPRALEYAERALKL---------- 832

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539931 455 VASLPNIPDDLVKLALKRradrqqflGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLD 529
Cdd:TIGR02917 833 APNIPAILDTLGWLLVEK--------GEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 381-555 7.86e-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: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 381 LNKFDKGIKTELDA------AEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkAQSEDDLAEKKRSN------EILQRS 448
Cdd:TIGR02917 723 IQAYRKALKRAPSSqnaiklHRALLASGNTAEAVKTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDKaikhyqTVVKKA 800

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539931 449 INtygEVASLPNipddLVKLALKRRADRQqfLGHMRGSLvtlqKLVnlfPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVL 528
Cdd:TIGR02917 801 PD---NAVVLNN----LAWLYLELKDPRA--LEYAERAL----KLA---PNIPAILDTLGWLLVEKGEADRALPLLRKAV 864

                         170       180
                  ....*....|....*....|....*..
gi 2069539931 529 DLAPNDGFAKVHYGFILKAENKIEESI 555
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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