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Conserved domains on  [gi|2069539939|ref|XP_042319652|]
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aspartyl/asparaginyl beta-hydroxylase isoform X8 [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 ...
 634-788 6.46e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 6.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 634 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 710
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939 711 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 788
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 ...
 27-92 2.19e-38

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: 136.51  E-value: 2.19e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539939  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 92
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 378-591 3.82e-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: 82.47  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 378 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 443
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 444 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 523
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539939 524 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 109-332 1.13e-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: 52.48  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  109 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 184
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  185 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 264
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939  265 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 332
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 ...
 634-788 6.46e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 6.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 634 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 710
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939 711 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 788
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 630-795 1.10e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 1.10e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 630 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 704
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 705 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 780
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539939 781 FIVDVWHPELTPQQR 795
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-92 2.19e-38

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: 136.51  E-value: 2.19e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539939  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 92
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 378-591 3.82e-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: 82.47  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 378 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 443
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 444 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 523
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539939 524 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
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 ...
 385-498 1.46e-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: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 385 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 461
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539939 462 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 498
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 109-332 1.13e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 52.48  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  109 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 184
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  185 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 264
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939  265 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 332
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 214-350 9.89e-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: 41.77  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 214 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 291
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539939 292 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 350
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 ...
 634-788 6.46e-73

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 234.85  E-value: 6.46e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 634 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 710
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939 711 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 788
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 630-795 1.10e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 1.10e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 630 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 704
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 705 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 780
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539939 781 FIVDVWHPELTPQQR 795
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-92 2.19e-38

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: 136.51  E-value: 2.19e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539939  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 92
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 378-591 3.82e-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: 82.47  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 378 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 443
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 444 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 523
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539939 524 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
394-559 1.51e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.11  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 394 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSeddLAEKKRsneiLQRSINTYGEVASL-PNIPDdlvklALKRRADR 472
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 473 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIP 552
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2069539939 553 YLKEGLE 559
Cdd:COG0457   166 LLEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
465-591 5.93e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.49  E-value: 5.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 465 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 544
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539939 545 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
Cdd:COG0457    90 GRYEEALEDYDKALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 387-559 7.27e-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: 7.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 387 ELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseddlaekkrsneILQRsintygevaslpnipddlvklal 466
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ----------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 467 krradrqqfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENK 546
Cdd:COG4783    51 ---------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                         170
                  ....*....|...
gi 2069539939 547 IEESIPYLKEGLE 559
Cdd:COG4783   122 PDEAIAALEKALE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 476-560 7.85e-11

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: 61.13  E-value: 7.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 476 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 555
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2069539939 556 EGLES 560
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 461-591 1.45e-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: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 461 LVKLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFI 540
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2069539939 541 LKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
Cdd:COG3914   156 LRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
415-609 3.35e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 415 PQSPRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNIPDdlvklALKRRADRQQFLGHMRGSLVTLQKLVNLFP 494
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELD------PDDAE-----ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 495 NDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHL 574
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2069539939 575 GDAMQRVGN-SEAYKWYELGHQRGHFASVWQRSLYN 609
Cdd:COG0457   151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 483-591 4.59e-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: 55.40  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 483 LVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgD 562
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069539939 563 PgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 591
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 ...
 385-498 1.46e-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: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 385 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 461
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539939 462 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 498
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 393-495 1.84e-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: 53.07  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 393 KLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGEvaslpnipDDLVKLALKRR 469
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD--------SPKAPDALLKL 73

                          90       100
                  ....*....|....*....|....*.
gi 2069539939 470 ADRQQFLGHMRGSLVTLQKLVNLFPN 495
Cdd:COG1729    74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
490-591 2.08e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.78  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 490 VNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGR 569
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2069539939 570 FYFHLGDAMQRVGN-SEAYKWYE 591
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 388-573 1.49e-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: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 388 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkaqsedDLAEKKRSNEILQRSINTYGEVASLPniPDDLvkLALK 467
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN--PDFA--EAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 468 RRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKI 547
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDW 230

                         170       180
                  ....*....|....*....|....*.
gi 2069539939 548 EESIPYLKEGLESGDPGTDDGRFYFH 573
Cdd:COG3914   231 EVYDRFEELLAALARGPSELSPFALL 256
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
507-591 1.88e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.78  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 507 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 585
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2069539939 586 AYKWYE 591
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 458-566 2.84e-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: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 458 PDDLVKLALkrRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHY 537
Cdd:COG4235    14 PNDAEGWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91

                          90       100
                  ....*....|....*....|....*....
gi 2069539939 538 GFILKAENKIEESIPYLKEGLESGDPGTD 566
Cdd:COG4235    92 GLAAFQQGDYAEAIAAWQKLLALLPADAP 120
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 507-591 5.79e-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: 49.96  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 507 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 585
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2069539939 586 AYKWYE 591
Cdd:COG5010   141 AKAALQ 146
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
476-559 6.43e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.24  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 476 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRvYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 555
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2069539939 556 EGLE 559
Cdd:COG3063    84 RALE 87
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 109-332 1.13e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 52.48  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  109 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 184
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  185 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 264
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539939  265 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 332
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 ...
 384-570 1.76e-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: 51.62  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 384 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSE----------DDLAEKKRSN-------------EI 440
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSApeylpalllagasEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 441 LQRSINTYGE-----VASLPNIPddlvkLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNN 515
Cdd:TIGR02917 307 QLGNLEQAYQylnqiLKYAPNSH-----QARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539939 516 AKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESGDPGTDDGRF 570
Cdd:TIGR02917 382 AAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 465-591 4.97e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.99  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 465 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 544
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2069539939 545 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGNSEAYKWYE 591
Cdd:COG3914   194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFE 237
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 397-579 7.43e-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: 49.70  E-value: 7.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 397 KGKVEEALKAFETLVSKYPQSPRARYGKAQ---SEDDLAE-KKRSNEILQrsintygevASLPNIPddlvklALKRRADR 472
Cdd:TIGR02917 138 LGQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEaRALIDEVLT---------ADPGNVD------ALLLKGDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 473 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAkvHYgfiLKA-----ENKI 547
Cdd:TIGR02917 203 LLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNY 277

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2069539939 548 EESIPYLKEGLESgDPGTDDGRFY-----FHLGDAMQ 579
Cdd:TIGR02917 278 EDARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 378-559 8.09e-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: 49.70  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 378 NKFDKGIKteldAAEKLRK------------------KGKVEEALKAFETLVSKYPQSPRARYGKA----QSEDDLAEKK 435
Cdd:TIGR02917 445 GQFDKALA----AAKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 436 RSNEILQ------RSINTYGEVASLPNIPDD----LVKLALKRRAD---RQQFLGHMRG------SLVTLQKLVNLFPND 496
Cdd:TIGR02917 521 RFEKVLTidpknlRAILALAGLYLRTGNEEEavawLEKAAELNPQEiepALALAQYYLGkgqlkkALAILNEAADAAPDS 600

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539939 497 TSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLE 559
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 391-470 2.99e-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: 43.83  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 391 AEKLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNipDDLVKLALK 467
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY------PD--SEAAKEARA 108


                  ...
gi 2069539939 468 RRA 470
Cdd:COG1729   109 RLA 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
384-533 3.63e-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: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 384 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSEDDLAEKKRSNEIlqrsintYGEVASLPNIPDdlvk 463
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQ---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 464 lALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFA 533
Cdd:COG4785    75 -LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 388-586 1.37e-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: 45.46  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 388 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARY--GKAQSE--DDLAEKKRSNEILQRSintYGEVASLPnipdDLVK 463
Cdd:TIGR02917  26 IEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLAlgDYAAAEKELRKALSLG---YPKNQVLP----LLAR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 464 LALKRRADrqqflghmrgslvtlQKLVNLFPNDTSFKNN--------LGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKV 535
Cdd:TIGR02917  99 AYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069539939 536 HYGFILKAENKIEESIPYLKEGLeSGDPGTDDGrfYFHLGDAMQRVGNSEA 586
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVL-TADPGNVDA--LLLKGDLLLSLGNIEL 211
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 394-528 1.77e-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: 42.64  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 394 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAqseddlaekkrsneilqrsintygevaslpnipddlvkLALKRradrq 473
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLA--------------------------------------LLYSR----- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539939 474 qfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAP 528
Cdd:COG5010   101 --SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 389-495 5.24e-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: 42.56  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 389 DAAEKLRKKGKVEEALKAFETLVSKYPQSP---RARYGKAQSEDDLAEKKRSNEILQRSINTYgevASLPNIPDDLVKLA 465
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAYYKQGDYEEAIAAADRFIKLY---PNSPNADYAYYLRG 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2069539939 466 L-----KRRADRQQflGHMRGSLVTLQKLVNLFPN 495
Cdd:COG4105   114 LsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 102-306 5.34e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.62  E-value: 5.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  102 KAKVKGLKERSVQ---EQPVLKDAEEVIQPAKETHTraERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIye 176
Cdd:PTZ00341   944 EANIEEDAEENVEedaEENVEENVEENVEENVEENV--EENVEENVEEnvEENVEENVEENIEENVEENVEENIEENV-- 1019

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939  177 epniqEDMESNKIPEVPTLEEVYVEELEDKIPEVLEAH-ESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDqpESP 255
Cdd:PTZ00341  1020 -----EEYDEENVEEVEENVEEYDEENVEEIEENAEENvEENIEENIEEYDEENVEEIEENIEENIEENVEENVE--ENV 1092

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2069539939  256 DETEITLEDTLEHNTEDTehhdyVDERELENedfieIQDTDGEPFTEHHYE 306
Cdd:PTZ00341  1093 EEIEENVEENVEENAEEN-----AEENAEEN-----AEEYDDENPEEHNEE 1133
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 389-495 6.98e-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: 42.15  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 389 DAAEKLRKKGKVEEALKAFETLVSKYPQSPRARygkaQSEDDLAEKKRSNEILQRSINTYGEVASL-PNIPD-D------ 460
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhPNHPDaDyayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2069539939 461 -LVKLALKRRADRQQflGHMRGSLVTLQKLVNLFPN 495
Cdd:TIGR03302 114 gLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYPN 147
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 214-350 9.89e-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: 41.77  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 214 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 291
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539939 292 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 350
Cdd:pfam06390 134 TEpetEPDTAPTTEPETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 377-525 4.20e-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: 40.84  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 377 LNKFDKGIKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRAR------YGKAQSEDDLAEKKRSNEIlqrsintyge 450
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLnnlawlYLELKDPRALEYAERALKL---------- 832

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539939 451 VASLPNIPDDLVKLALKRradrqqflGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLD 525
Cdd:TIGR02917 833 APNIPAILDTLGWLLVEK--------GEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 377-551 6.05e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.07  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 377 LNKFDKGIKTELDA------AEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkAQSEDDLAEKKRSN------EILQRS 444
Cdd:TIGR02917 723 IQAYRKALKRAPSSqnaiklHRALLASGNTAEAVKTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDKaikhyqTVVKKA 800

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539939 445 INtygEVASLPNipddLVKLALKRRADRQqfLGHMRGSLvtlqKLVnlfPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVL 524
Cdd:TIGR02917 801 PD---NAVVLNN----LAWLYLELKDPRA--LEYAERAL----KLA---PNIPAILDTLGWLLVEKGEADRALPLLRKAV 864

                         170       180
                  ....*....|....*....|....*..
gi 2069539939 525 DLAPNDGFAKVHYGFILKAENKIEESI 551
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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