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Conserved domains on  [gi|2069539951|ref|XP_042319659|]
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aspartyl/asparaginyl beta-hydroxylase isoform X14 [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 ...
 613-767 2.44e-73

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


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 235.62  E-value: 2.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 613 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 689
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539951 690 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 767
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 1.49e-34

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 125.72  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539951 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 357-570 5.73e-17

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


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.70  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 357 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 422
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 423 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 502
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539951 503 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 130-311 1.70e-08

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: 58.26  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  130 EQPVLKDAEEVIQPAKETHTR--AERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDMESNK 203
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEenVEENVEENVEEnvEENVEENVEENVEENVEENVEENIEENVEEnvEENIEENVEEYD 1023

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  204 IPEVPTLEEVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEHNTEDTEHH--DYVDERELEN--EDFIEIQDTDGEPF 279
Cdd:PTZ00341  1024 EENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENieENIEENVEENveENVEEIEENVEENV 1103

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069539951  280 TEHHYENkqdkpsASDSFTEHIESVDDSEPTE 311
Cdd:PTZ00341  1104 EENAEEN------AEENAEENAEEYDDENPEE 1129
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 613-767 2.44e-73

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


Pssm-ID: 461552  Cd Length: 157  Bit Score: 235.62  E-value: 2.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 613 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 689
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539951 690 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 767
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 609-774 6.78e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.94  E-value: 6.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 609 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 683
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 684 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 759
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539951 760 FIVDVWHPELTPQQR 774
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 1.49e-34

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 125.72  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539951 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 357-570 5.73e-17

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.70  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 357 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 422
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 423 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 502
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539951 503 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
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 ...
 364-477 1.42e-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: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 364 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 440
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539951 441 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 477
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 130-311 1.70e-08

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 58.26  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  130 EQPVLKDAEEVIQPAKETHTR--AERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDMESNK 203
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEenVEENVEENVEEnvEENVEENVEENVEENVEENVEENIEENVEEnvEENIEENVEEYD 1023

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  204 IPEVPTLEEVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEHNTEDTEHH--DYVDERELEN--EDFIEIQDTDGEPF 279
Cdd:PTZ00341  1024 EENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENieENIEENVEENveENVEEIEENVEENV 1103

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069539951  280 TEHHYENkqdkpsASDSFTEHIESVDDSEPTE 311
Cdd:PTZ00341  1104 EENAEEN------AEENAEENAEEYDDENPEE 1129
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 107-344 2.13e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.52  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  107 GQSPGGVIKRKAKVKGLK-ERSVQEQPVLKDAEEVIQPAKETHTRAERRIADEVEPEDEIESLLHEVLDSQLEEQTSNMD 185
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENgEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGET 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  186 E-ENIYEEPNIQ--------EDMESNKIpEVPTLEEVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEH--NTEDTEH 254
Cdd:TIGR00927  722 EaEGTEDEGEIEtgeegeevEDEGEGEA-EGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMkgDEGAEGK 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  255 HDYVDERELENEDFIEIQDTDGEPFTEHHYENKQDKPSASDsfteHIESVDDSEPTEDHAAAQPHETEVPVQVEEYSNDE 334
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN----QGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEE 876

                          250
                   ....*....|
gi 2069539951  335 SVGQEKETQQ 344
Cdd:TIGR00927  877 EEEEEEEEEE 886
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 613-767 2.44e-73

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


Pssm-ID: 461552  Cd Length: 157  Bit Score: 235.62  E-value: 2.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 613 ERNWKMIRDEGLAVMDRGKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKTCAFLERFP-EATGCRRGQIKY 689
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539951 690 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPNeGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLIFIVDVWHP 767
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 609-774 6.78e-57

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.94  E-value: 6.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 609 VKSLERNWKMIRDEGLAVMDRGKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKTCAFLERFPeatgcr 683
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 684 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIPN-EGCRIRCAQETRFWEEGKVLIFDDSFEHEVWQDAQAYRLI 759
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNdDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2069539951 760 FIVDVWHPELTPQQR 774
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 27-107 1.49e-34

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 125.72  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  27 NGKKEGISGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVEDAKVLL 106
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2069539951 107 G 107
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 357-570 5.73e-17

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 81.70  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 357 NKFDKGIKTELDAAEK--------------LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseDDLAEKKrsneiLQR 422
Cdd:COG2956    22 GQPDKAIDLLEEALELdpetveahlalgnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 423 SINTYGEVASLPniPDDLVklALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEV 502
Cdd:COG2956    95 AEELLEKLLELD--PDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539951 503 LDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
Cdd:COG2956   171 LKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
373-538 1.85e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.11  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 373 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSeddLAEKKRsneiLQRSINTYGEVASL-PNIPDdlvklALKRRADR 451
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 452 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIP 531
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2069539951 532 YLKEGLE 538
Cdd:COG0457   166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 366-538 6.67e-11

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 60.98  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 366 ELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQseddlaekkrsneILQRsintygevaslpnipddlvklal 445
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGE-------------ILLQ----------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 446 krradrqqfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENK 525
Cdd:COG4783    51 ---------LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                         170
                  ....*....|...
gi 2069539951 526 IEESIPYLKEGLE 538
Cdd:COG4783   122 PDEAIAALEKALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
444-570 6.97e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.10  E-value: 6.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 444 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 523
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2069539951 524 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
Cdd:COG0457    90 GRYEEALEDYDKALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 455-539 9.97e-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: 60.74  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 455 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 534
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2069539951 535 EGLES 539
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 440-570 1.39e-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: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 440 LVKLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFI 519
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2069539951 520 LKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
Cdd:COG3914   156 LRRLGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
394-588 4.08e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.79  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 394 PQSPRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNIPDdlvklALKRRADRQQFLGHMRGSLVTLQKLVNLFP 473
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELD------PDDAE-----ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 474 NDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHL 553
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2069539951 554 GDAMQRVGN-SEAYKWYELGHQRGHFASVWQRSLYN 588
Cdd:COG0457   151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 462-570 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 2069539951 462 LVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgD 541
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2069539951 542 PgtDDGRFYFHLGDAMQRVGN-SEAYKWYE 570
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 ...
 364-477 1.42e-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: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 364 KTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPR---ARYGKAQSEDDLAEKKRSNEILQRSINTYGEVaslPNIPDDL 440
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYWLGEAYYAQGDYADAAKAFLAVVKKYPKS---PKAPDAL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2069539951 441 VKLALKrradrQQFLGHMRGSLVTLQKLVNLFPNDTS 477
Cdd:TIGR02795  78 LKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 130-311 1.70e-08

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 58.26  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  130 EQPVLKDAEEVIQPAKETHTR--AERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDMESNK 203
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEenVEENVEENVEEnvEENVEENVEENVEENVEENVEENIEENVEEnvEENIEENVEEYD 1023

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  204 IPEVPTLEEVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEHNTEDTEHH--DYVDERELEN--EDFIEIQDTDGEPF 279
Cdd:PTZ00341  1024 EENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENieENIEENVEENveENVEEIEENVEENV 1103

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2069539951  280 TEHHYENkqdkpsASDSFTEHIESVDDSEPTE 311
Cdd:PTZ00341  1104 EENAEEN------AEENAEENAEEYDDENPEE 1129
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 372-474 2.11e-08

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 52.69  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 372 KLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYGEvaslpnipDDLVKLALKRR 448
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPD--------SPKAPDALLKL 73

                          90       100
                  ....*....|....*....|....*.
gi 2069539951 449 ADRQQFLGHMRGSLVTLQKLVNLFPN 474
Cdd:COG1729    74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
469-570 2.27e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.78  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 469 VNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGR 548
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2069539951 549 FYFHLGDAMQRVGN-SEAYKWYE 570
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 367-552 1.44e-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: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 367 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkaqsedDLAEKKRSNEILQRSINTYGEVASLPniPDDLvkLALK 446
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN--PDFA--EAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 447 RRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKI 526
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDW 230

                         170       180
                  ....*....|....*....|....*.
gi 2069539951 527 EESIPYLKEGLESGDPGTDDGRFYFH 552
Cdd:COG3914   231 EVYDRFEELLAALARGPSELSPFALL 256
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
486-570 2.14e-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: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 486 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 564
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2069539951 565 AYKWYE 570
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 437-545 2.95e-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: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 437 PDDLVKLALkrRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHY 516
Cdd:COG4235    14 PNDAEGWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91

                          90       100
                  ....*....|....*....|....*....
gi 2069539951 517 GFILKAENKIEESIPYLKEGLESGDPGTD 545
Cdd:COG4235    92 GLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
455-538 7.24e-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: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 455 LGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRvYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLK 534
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2069539951 535 EGLE 538
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 486-570 7.70e-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: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 486 YLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-SE 564
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2069539951 565 AYKWYE 570
Cdd:COG5010   141 AKAALQ 146
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 363-549 1.95e-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: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 363 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSE----------DDLAEKKRSN-------------EI 419
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDfqkknyedarETLQDALKSApeylpalllagasEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 420 LQRSINTYGE-----VASLPNIPddlvkLALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNN 494
Cdd:TIGR02917 307 QLGNLEQAYQylnqiLKYAPNSH-----QARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539951 495 AKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLESGDPGTDDGRF 549
Cdd:TIGR02917 382 AAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 134-341 3.48e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.94  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  134 LKDAEEVIQPAKETHTRAERRIADEVEPEDEIESLLHEVLDSQLEEQTSNMDEENIYE--EPNIQEDMESNKIPEVptlE 211
Cdd:PTZ00341   928 LKNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEEnvEENVEENVEENVEENI---E 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  212 EVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEHNTEDTEHHdyVDERELEN--EDFIEIQDTDGEPFTEHHYENKQD 289
Cdd:PTZ00341  1005 ENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEEN--AEENVEENieENIEEYDEENVEEIEENIEENIEE 1082

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2069539951  290 kpSASDSFTEHIESVDDS-EPTEDHAAAQPHETEVPVQVEEYsNDESVGQEKE 341
Cdd:PTZ00341  1083 --NVEENVEENVEEIEENvEENVEENAEENAEENAEENAEEY-DDENPEEHNE 1132
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 444-570 4.80e-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: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 444 ALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAE 523
Cdd:COG3914   114 ALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDL 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2069539951 524 NKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGNSEAYKWYE 570
Cdd:COG3914   194 GRLEEAIAAYRRALEL-DP--DNADAHSNLLFALRQACDWEVYDRFE 237
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 376-558 9.27e-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: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 376 KGKVEEALKAFETLVSKYPQSPRARYGKAQ---SEDDLAE-KKRSNEILQrsintygevASLPNIPddlvklALKRRADR 451
Cdd:TIGR02917 138 LGQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEaRALIDEVLT---------ADPGNVD------ALLLKGDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 452 QQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAkvHYgfiLKA-----ENKI 526
Cdd:TIGR02917 203 LLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNY 277

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2069539951 527 EESIPYLKEGLESgDPGTDDGRFY-----FHLGDAMQ 558
Cdd:TIGR02917 278 EDARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 357-538 1.07e-05

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 357 NKFDKGIKteldAAEKLRK------------------KGKVEEALKAFETLVSKYPQSPRARYGKA----QSEDDLAEKK 414
Cdd:TIGR02917 445 GQFDKALA----AAKKLEKkqpdnaslhnllgaiylgKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQ 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 415 RSNEILQ------RSINTYGEVASLPNIPDD----LVKLALKRRAD---RQQFLGHMRG------SLVTLQKLVNLFPND 475
Cdd:TIGR02917 521 RFEKVLTidpknlRAILALAGLYLRTGNEEEavawLEKAAELNPQEiepALALAQYYLGkgqlkkALAILNEAADAAPDS 600

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539951 476 TSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKVHYGFILKAENKIEESIPYLKEGLE 538
Cdd:TIGR02917 601 PEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALE 663
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 370-449 3.33e-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: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 370 AEKLRKKGKVEEALKAFETLVSKYPQS---PRARYGKAQSEDDLAEKKRSNEILQRSINTYgevaslPNipDDLVKLALK 446
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY------PD--SEAAKEARA 108


                  ...
gi 2069539951 447 RRA 449
Cdd:COG1729   109 RLA 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
363-512 3.82e-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: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 363 IKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARYGKAQSEDDLAEKKRSNEIlqrsintYGEVASLPNIPDdlvk 442
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQ---- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 443 lALKRRADRQQFLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAPNDGFA 512
Cdd:COG4785    75 -LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 125-285 1.37e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.55  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  125 ERSVQEQpVLKDAEEVIQPAKETHTraERRIADEVEP--EDEIESLLHEVLDSQLEEQTSNM---DEENIYE-EPNIQED 198
Cdd:PTZ00341   976 EENVEEN-VEENVEENVEENVEENV--EENIEENVEEnvEENIEENVEEYDEENVEEVEENVeeyDEENVEEiEENAEEN 1052

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  199 MESNKIPEVPTLEEVYVEELEDKIPEVLEAH--ESIQEDETEItlEDTLEHNTEDTEHHDyVDERELENedfieIQDTDG 276
Cdd:PTZ00341  1053 VEENIEENIEEYDEENVEEIEENIEENIEENveENVEENVEEI--EENVEENVEENAEEN-AEENAEEN-----AEEYDD 1124


                   ....*....
gi 2069539951  277 EPFTEHHYE 285
Cdd:PTZ00341  1125 ENPEEHNEE 1133
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 367-565 1.64e-04

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.07  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 367 LDAAEKLRKKGKVEEALKAFETLVSKYPQSPRARY--GKAQSE--DDLAEKKRSNEILQRSintYGEVASLPnipdDLVK 442
Cdd:TIGR02917  26 IEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLAlgDYAAAEKELRKALSLG---YPKNQVLP----LLAR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 443 LALKRRADrqqflghmrgslvtlQKLVNLFPNDTSFKNN--------LGVGYLLIGDNNNAKRVYEEVLDLAPNDGFAKV 514
Cdd:TIGR02917  99 AYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2069539951 515 HYGFILKAENKIEESIPYLKEGLeSGDPGTDDGrfYFHLGDAMQRVGNSEA 565
Cdd:TIGR02917 164 GLAQLALAENRFDEARALIDEVL-TADPGNVDA--LLLKGDLLLSLGNIEL 211
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 373-507 2.18e-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: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 373 LRKKGKVEEALKAFETLVSKYPQSPRARYGKAqseddlaekkrsneilqrsintygevaslpnipddlvkLALKRradrq 452
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLA--------------------------------------LLYSR----- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2069539951 453 qfLGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLDLAP 507
Cdd:COG5010   101 --SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 368-474 4.81e-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: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 368 DAAEKLRKKGKVEEALKAFETLVSKYPQSP---RARYGKAQSEDDLAEKKRSNEILQRSINTYgevASLPNIPDDLVKLA 444
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAYYKQGDYEEAIAAADRFIKLY---PNSPNADYAYYLRG 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2069539951 445 L-----KRRADRQQflGHMRGSLVTLQKLVNLFPN 474
Cdd:COG4105   114 LsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 368-474 5.80e-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: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 368 DAAEKLRKKGKVEEALKAFETLVSKYPQSPRARygkaQSEDDLAEKKRSNEILQRSINTYGEVASL-PNIPD-D------ 439
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhPNHPDaDyayylr 113

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2069539951 440 -LVKLALKRRADRQQflGHMRGSLVTLQKLVNLFPN 474
Cdd:TIGR03302 114 gLSNYNQIDRVDRDQ--TAAREAFEAFQELIRRYPN 147
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 107-344 2.13e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.52  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  107 GQSPGGVIKRKAKVKGLK-ERSVQEQPVLKDAEEVIQPAKETHTRAERRIADEVEPEDEIESLLHEVLDSQLEEQTSNMD 185
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENgEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGET 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  186 E-ENIYEEPNIQ--------EDMESNKIpEVPTLEEVYVEELEDKIPEVLEAHESIQEDETEITLEDTLEH--NTEDTEH 254
Cdd:TIGR00927  722 EaEGTEDEGEIEtgeegeevEDEGEGEA-EGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMkgDEGAEGK 800

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951  255 HDYVDERELENEDFIEIQDTDGEPFTEHHYENKQDKPSASDsfteHIESVDDSEPTEDHAAAQPHETEVPVQVEEYSNDE 334
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN----QGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEE 876

                          250
                   ....*....|
gi 2069539951  335 SVGQEKETQQ 344
Cdd:TIGR00927  877 EEEEEEEEEE 886
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 356-504 4.50e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.45  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 356 LNKFDKGIKTELDAAEKLRKKGKVEEALKAFETLVSKYPQSPRAR------YGKAQSEDDLAEKKRSNEIlqrsintyge 429
Cdd:TIGR02917 763 LKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLnnlawlYLELKDPRALEYAERALKL---------- 832

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539951 430 VASLPNIPDDLVKLALKRradrqqflGHMRGSLVTLQKLVNLFPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVLD 504
Cdd:TIGR02917 833 APNIPAILDTLGWLLVEK--------GEADRALPLLRKAVNIAPEAAAIRYHLALALLATGRKAEARKELDKLLN 899
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 356-530 6.94e-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: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 356 LNKFDKGIKTELDA------AEKLRKKGKVEEALKAFETLVSKYPQSPRARYgkAQSEDDLAEKKRSN------EILQRS 423
Cdd:TIGR02917 723 IQAYRKALKRAPSSqnaiklHRALLASGNTAEAVKTLEAWLKTHPNDAVLRT--ALAELYLAQKDYDKaikhyqTVVKKA 800

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539951 424 INtygEVASLPNipddLVKLALKRRADRQqfLGHMRGSLvtlqKLVnlfPNDTSFKNNLGVGYLLIGDNNNAKRVYEEVL 503
Cdd:TIGR02917 801 PD---NAVVLNN----LAWLYLELKDPRA--LEYAERAL----KLA---PNIPAILDTLGWLLVEKGEADRALPLLRKAV 864

                         170       180
                  ....*....|....*....|....*..
gi 2069539951 504 DLAPNDGFAKVHYGFILKAENKIEESI 530
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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