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Conserved domains on  [gi|2069539945|ref|XP_042319655|]
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aspartyl/asparaginyl beta-hydroxylase isoform X11 [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 ...
 621-775 6.86e-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: 234.46  E-value: 6.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 621 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 697
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945 698 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 775
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 ...
 14-79 4.39e-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: 135.74  E-value: 4.39e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539945  14 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 365-578 9.02e-17

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


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.31  E-value: 9.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 365 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 430
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 431 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 510
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539945 511 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 96-319 2.06e-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: 51.71  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945   96 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 171
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945  172 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 251
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945  252 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 319
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 ...
 621-775 6.86e-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: 234.46  E-value: 6.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 621 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 697
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945 698 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 775
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 617-782 9.22e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 9.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 617 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 691
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 692 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 767
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539945 768 FIVDVWHPELTPQQR 782
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 14-79 4.39e-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: 135.74  E-value: 4.39e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539945  14 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 365-578 9.02e-17

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.31  E-value: 9.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 365 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 430
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 431 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 510
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539945 511 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
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 ...
 372-485 1.43e-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: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 372 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 448
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539945 449 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 485
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 96-319 2.06e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 51.71  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945   96 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 171
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945  172 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 251
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945  252 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 319
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 201-337 6.49e-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: 42.16  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 201 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 278
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539945 279 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 337
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 ...
 621-775 6.86e-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: 234.46  E-value: 6.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 621 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 697
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945 698 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 775
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 617-782 9.22e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.55  E-value: 9.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 617 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 691
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 692 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 767
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539945 768 FIVDVWHPELTPQQR 782
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 14-79 4.39e-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: 135.74  E-value: 4.39e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539945  14 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 365-578 9.02e-17

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.31  E-value: 9.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 365 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 430
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 431 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 510
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539945 511 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
381-546 2.85e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 381 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSeddLAEKKRsneiLQRSINTYGEVASL-PNIPDdlvklALKRRADR 459
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 460 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIP 539
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2069539945 540 YLKEGLE 546
Cdd:COG0457   166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 374-546 9.64e-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: 60.21  E-value: 9.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 374 ELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseddlaekkrsneILQRsintygevaslpnipddlvklal 453
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ----------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 454 krradrqqfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENK 533
Cdd:COG4783    51 ---------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                         170
                  ....*....|...
gi 2069539945 534 IEESIPYLKEGLE 546
Cdd:COG4783   122 PDEAIAALEKALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
452-578 1.03e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.72  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 452 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 531
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539945 532 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
Cdd:COG0457    90 GRYEEALEDYDKALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 463-547 1.09e-10

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 60.74  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 463 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 542
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2069539945 543 EGLES 547
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 448-578 1.42e-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: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 448 LVKLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFI 527
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2069539945 528 LKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
Cdd:COG3914   156 LRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
402-596 5.57e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.41  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 402 PQSPRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNIPDdlvklALKRRADRQQFLGHMRGSLVTLQKLVNLFP 481
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELD------PDDAE-----ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 482 NDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHL 561
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2069539945 562 GDAMQRVGN-SEAYKWYELGHQRGHFASVWQRSLYN 596
Cdd:COG0457   151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 470-578 5.47e-09

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.01  E-value: 5.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 470 LVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgD 549
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069539945 550 PgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 578
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 ...
 372-485 1.43e-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: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 372 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 448
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539945 449 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 485
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 380-482 2.05e-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: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 380 KLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGEvaslpnipDDLVKLALKRR 456
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD--------SPKAPDALLKL 73

                          90       100
                  ....*....|....*....|....*.
gi 2069539945 457 ADRQQFLGHMRGSLVTLQKLVNLFPN 482
Cdd:COG1729    74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
477-578 2.95e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.40  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 477 VNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGR 556
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2069539945 557 FYFHLGDAMQRVGN-SEAYKWYE 578
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 375-560 1.46e-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: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 375 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkaqsedDLAEKKRSNEILQRSINTYGEVASLPniPDDLvkLALK 454
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN--PDFA--EAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 455 RRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKI 534
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDW 230

                         170       180
                  ....*....|....*....|....*.
gi 2069539945 535 EESIPYLKEGLESGDPGTDDGRFYFH 560
Cdd:COG3914   231 EVYDRFEELLAALARGPSELSPFALL 256
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
494-578 2.41e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.40  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 494 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 572
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2069539945 573 AYKWYE 578
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 445-553 3.42e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 50.00  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 445 PDDLVKLALkrRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHY 524
Cdd:COG4235    14 PNDAEGWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91

                          90       100
                  ....*....|....*....|....*....
gi 2069539945 525 GFILKAENKIEESIPYLKEGLESGDPGTD 553
Cdd:COG4235    92 GLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
463-546 7.68e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.86  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 463 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRvYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 542
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2069539945 543 EGLE 546
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 494-578 8.48e-07

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 49.57  E-value: 8.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 494 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 572
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2069539945 573 AYKWYE 578
Cdd:COG5010   141 AKAALQ 146
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 371-557 1.80e-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: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 371 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSE----------DDLAEKKRSN-------------EI 427
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSApeylpalllagasEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 428 LQRSINTYGE-----VASLPNIPddlvkLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNN 502
Cdd:TIGR02917 307 QLGNLEQAYQylnqiLKYAPNSH-----QARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539945 503 AKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESGDPGTDDGRF 557
Cdd:TIGR02917 382 AAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 96-319 2.06e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 51.71  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945   96 KERSVQEQPVLKDAEEVIQPAKETHtrAERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDM 171
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEANIEED--AEENVEEDAEEnvEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENI 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945  172 ESNKIPEVptleevyVEELEDKIPEVLEAHESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDQPESPDETEItlED 251
Cdd:PTZ00341  1004 EENVEENV-------EENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEI--EE 1074

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539945  252 TLEHNTEDTehhdyVDERELENEDFIEiqdtdgEPFTEHHYENKQDkpSASDSFTEHIESVDDSEPTE 319
Cdd:PTZ00341  1075 NIEENIEEN-----VEENVEENVEEIE------ENVEENVEENAEE--NAEENAEENAEEYDDENPEE 1129
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 452-578 4.86e-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: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 452 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 531
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2069539945 532 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGNSEAYKWYE 578
Cdd:COG3914   194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFE 237
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 384-566 7.99e-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: 7.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 384 KGKVEEALKAFETLVSKYPQSPRARYGKAQ---SEDDLAE-KKRSNEILQrsintygevASLPNIPddlvklALKRRADR 459
Cdd:TIGR02917 138 LGQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEaRALIDEVLT---------ADPGNVD------ALLLKGDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 460 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAkvHYgfiLKA-----ENKI 534
Cdd:TIGR02917 203 LLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNY 277

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2069539945 535 EESIPYLKEGLESgDPGTDDGRFY-----FHLGDAMQ 566
Cdd:TIGR02917 278 EDARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 365-546 9.15e-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: 49.31  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 365 NKFDKGIKteldAAEKLRK------------------KGKVEEALKAFETLVSKYPQSPRARYGKA----QSEDDLAEKK 422
Cdd:TIGR02917 445 GQFDKALA----AAKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 423 RSNEILQ------RSINTYGEVASLPNIPDD----LVKLALKRRAD---RQQFLGHMRG------SLVTLQKLVNLFPND 483
Cdd:TIGR02917 521 RFEKVLTidpknlRAILALAGLYLRTGNEEEavawLEKAAELNPQEiepALALAQYYLGkgqlkkALAILNEAADAAPDS 600

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539945 484 TSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLE 546
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 378-457 3.21e-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: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 378 AEKLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNipDDLVKLALK 454
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY------PD--SEAAKEARA 108


                  ...
gi 2069539945 455 RRA 457
Cdd:COG1729   109 RLA 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
371-520 4.04e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 371 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSEDDLAEKKRSNEIlqrsintYGEVASLPNIPDdlvk 450
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQ---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 451 lALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFA 520
Cdd:COG4785    75 -LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 375-573 1.47e-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: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 375 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARY--GKAQSE--DDLAEKKRSNEILQRSintYGEVASLPnipdDLVK 450
Cdd:TIGR02917  26 IEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLAlgDYAAAEKELRKALSLG---YPKNQVLP----LLAR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 451 LALKRRADrqqflghmrgslvtlQKLVNLFPNDTSFKNN--------LGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKV 522
Cdd:TIGR02917  99 AYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069539945 523 HYGFILKAENKIEESIPYLKEGLeSGDPGTDDGrfYFHLGDAMQRVGNSEA 573
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVL-TADPGNVDA--LLLKGDLLLSLGNIEL 211
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 381-515 2.38e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.25  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 381 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAqseddlaekkrsneilqrsintygevaslpnipddlvkLALKRradrq 460
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLA--------------------------------------LLYSR----- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539945 461 qfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAP 515
Cdd:COG5010   101 --SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 376-482 6.04e-04

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 42.18  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 376 DAAEKLRKKGKVEEALKAFETLVSKYPQSP---RARYGKAQSEDDLAEKKRSNEILQRSINTYgevASLPNIPDDLVKLA 452
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAYYKQGDYEEAIAAADRFIKLY---PNSPNADYAYYLRG 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2069539945 453 L-----KRRADRQQflGHMRGSLVTLQKLVNLFPN 482
Cdd:COG4105   114 LsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
NESP55 pfam06390
Neuroendocrine-specific golgi protein P55 (NESP55); This family consists of several mammalian ...
 201-337 6.49e-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: 42.16  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 201 HESIQEEPASDYQPE--EPEADDAhvtyeyHTHMEEVMDQPESPDETEITLEDTLEHNTEdtehhdyvDERELENEDFIE 278
Cdd:pfam06390  68 HRSAAAAAAAQVFPEpsEPESDHE------DEDFEPELARPECLEYDEDDFDTETDSETE--------PESDIESETEFE 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539945 279 IQ---DTDGEPFTEHHYENKQDK-------PSASDSFTEHIESVDDSEPTEDHAAAQP--HETEVPVQVEE 337
Cdd:pfam06390 134 TEpetEPDTAPTTEPETEPEDEPgpvvpkgATFHQSLTERLHALKLQSADASPRRAPPstQEPESAREGEE 204
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 376-482 7.92e-04

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


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 41.77  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 376 DAAEKLRKKGKVEEALKAFETLVSKYPQSPRARygkaQSEDDLAEKKRSNEILQRSINTYGEVASL-PNIPD-D------ 447
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhPNHPDaDyayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2069539945 448 -LVKLALKRRADRQQflGHMRGSLVTLQKLVNLFPN 482
Cdd:TIGR03302 114 gLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYPN 147
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 102-293 9.64e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 42.85  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945  102 EQPVLKDAEEVIQPAKETHTR------AERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIyeepniqEDMES 173
Cdd:PTZ00341   952 EENVEEDAEENVEENVEENVEenveenVEENVEENVEEnvEENVEENVEENIEENVEENVEENIEENV-------EEYDE 1024

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945  174 NKIPEVPTLEEVYVEELEDKIPEVLEAH-ESIQEEPASDYQPEEPEADDAHVTYEYHTHMEEVMDqpESPDETEITLEDT 252
Cdd:PTZ00341  1025 ENVEEVEENVEEYDEENVEEIEENAEENvEENIEENIEEYDEENVEEIEENIEENIEENVEENVE--ENVEEIEENVEEN 1102

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2069539945  253 LEHNTEDTehhdyVDERELENedfieIQDTDGEPFTEHHYE 293
Cdd:PTZ00341  1103 VEENAEEN-----AEENAEEN-----AEEYDDENPEEHNEE 1133
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 364-512 4.33e-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: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 364 LNKFDKGIKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRAR------YGKAQSEDDLAEKKRSNEIlqrsintyge 437
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLnnlawlYLELKDPRALEYAERALKL---------- 832

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539945 438 VASLPNIPDDLVKLALKRradrqqflGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLD 512
Cdd:TIGR02917 833 APNIPAILDTLGWLLVEK--------GEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 364-538 6.57e-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: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 364 LNKFDKGIKTELDA------AEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkAQSEDDLAEKKRSN------EILQRS 431
Cdd:TIGR02917 723 IQAYRKALKRAPSSqnaiklHRALLASGNTAEAVKTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDKaikhyqTVVKKA 800

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539945 432 INtygEVASLPNipddLVKLALKRRADRQqfLGHMRGSLvtlqKLVnlfPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVL 511
Cdd:TIGR02917 801 PD---NAVVLNN----LAWLYLELKDPRA--LEYAERAL----KLA---PNIPAILDTLGWLLVEKGEADRALPLLRKAV 864

                         170       180
                  ....*....|....*....|....*..
gi 2069539945 512 DLAPNDGFAKVHYGFILKAENKIEESI 538
Cdd:TIGR02917 865 NIAPEAAAIRYHLALALLATGRKAEAR 891
ATG27 pfam09451
Autophagy-related protein 27;
4-37 9.46e-03

Autophagy-related protein 27;


Pssm-ID: 430622  Cd Length: 261  Bit Score: 38.85  E-value: 9.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2069539945   4 DSETKHGGNKNGKKEGISGSSFFTWFMVIALLGV 37
Cdd:pfam09451 173 EKDESDPDDGDGGGNGGSGWGWFTWFFIILFLFT 206
 
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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