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Conserved domains on  [gi|2114306222|ref|XP_029195696|]
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LOW QUALITY PROTEIN: aspartyl/asparaginyl beta-hydroxylase-like [Acropora millepora]

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 ...
 376-529 4.38e-78

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: 242.55  E-value: 4.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 376 EGNWKVIRDEGLEVLDQKSGGFIPEEENLRQQGD--WKQFTLYQRGRKNTAACRRTPRTCAIVDSIA-DAASCKRGQIKY 452
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2114306222 453 SVMLPGTHVWPHTGPTNCRLRLHLGLVIPKNVAIRVGHETRTWKEGKAIIIDDSFDHEVWHNGSTFRLIFIVDFWHP 529
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 136-376 3.93e-16

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


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 78.62  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 136 KGQIEDALKKYEGLVNKYPKSPLAMYgkaqsldKLSEIRQSNEILQQSIHAYGNVIDLPEcplqLKHQAMRRQADRLSFL 215
Cdd:COG2956    55 RGEYDRAIRIHQKLLERDPDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELDP----DDAEALRLLAEIYEQE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 216 GKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IKTDhlRYKEAIPLL 294
Cdd:COG2956   124 GDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELyLEQG--DYEEAIAAL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 295 REGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKkgiflsalqrsLYNADTPLTARPWWAPEQTGYLEAIRK 374
Cdd:COG2956   202 ERAL---EQDPDYLPALPRLAELYEKLGDPEEALELLRKALE-----------LDPSDDLLLALADLLERKEGLEAALAL 267


                  ..
gi 2114306222 375 LE 376
Cdd:COG2956   268 LE 269
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 376-529 4.38e-78

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: 242.55  E-value: 4.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 376 EGNWKVIRDEGLEVLDQKSGGFIPEEENLRQQGD--WKQFTLYQRGRKNTAACRRTPRTCAIVDSIA-DAASCKRGQIKY 452
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2114306222 453 SVMLPGTHVWPHTGPTNCRLRLHLGLVIPKNVAIRVGHETRTWKEGKAIIIDDSFDHEVWHNGSTFRLIFIVDFWHP 529
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 372-537 6.11e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 181.61  E-value: 6.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 372 IRKLEGNWKVIRDEGLEVLDQKSG-----GFIPEEENLRQQGDWKQFTLYQRGRKNTAACRRTPRTCAIVDSIadaasck 446
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEAlppyhDISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 447 rGQIK---YSVMLPGTHVWPHTGPTNCRLRLHLGLVIPK--NVAIRVGHETRTWKEGKAIIIDDSFDHEVWHNGSTFRLI 521
Cdd:COG3555    93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNddRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*.
gi 2114306222 522 FIVDFWHPDLTPRQRA 537
Cdd:COG3555   172 LFCDVWRPMLSPWERA 187
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 136-376 3.93e-16

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 78.62  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 136 KGQIEDALKKYEGLVNKYPKSPLAMYgkaqsldKLSEIRQSNEILQQSIHAYGNVIDLPEcplqLKHQAMRRQADRLSFL 215
Cdd:COG2956    55 RGEYDRAIRIHQKLLERDPDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELDP----DDAEALRLLAEIYEQE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 216 GKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IKTDhlRYKEAIPLL 294
Cdd:COG2956   124 GDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELyLEQG--DYEEAIAAL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 295 REGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKkgiflsalqrsLYNADTPLTARPWWAPEQTGYLEAIRK 374
Cdd:COG2956   202 ERAL---EQDPDYLPALPRLAELYEKLGDPEEALELLRKALE-----------LDPSDDLLLALADLLERKEGLEAALAL 267


                  ..
gi 2114306222 375 LE 376
Cdd:COG2956   268 LE 269
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 126-337 3.45e-08

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: 56.25  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 126 ELTKAQSVLDKGQIEDALKKYEGLVNKYPKSPLAMYGKAQ----------SLDKLSEIRQSN-------------EILQQ 182
Cdd:TIGR02917 230 LLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALvdfqkknyedARETLQDALKSApeylpalllagasEYQLG 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 183 SIHAYGNVIDLPECPLQLKHQAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKV 262
Cdd:TIGR02917 310 NLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 263 VNMDPSNGFAKSHLG--FIIKTDHlrykeaipllREGIASGETGA----DDGRFYFHLGDAFTRIGKPDEAYKVYEEAAK 336
Cdd:TIGR02917 390 TELDPENAAARTQLGisKLSQGDP----------SEAIADLETAAqldpELGRADLLLILSYLRSGQFDKALAAAKKLEK 459


                  .
gi 2114306222 337 K 337
Cdd:TIGR02917 460 K 460
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 286-338 4.10e-05

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 41.55  E-value: 4.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2114306222 286 RYKEAIPLLREGIASGETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKKG 338
Cdd:pfam13432  12 DYDDAAAALEAALARFPESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAA 64
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 376-529 4.38e-78

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: 242.55  E-value: 4.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 376 EGNWKVIRDEGLEVLDQKSGGFIPEEENLRQQGD--WKQFTLYQRGRKNTAACRRTPRTCAIVDSIA-DAASCKRGQIKY 452
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2114306222 453 SVMLPGTHVWPHTGPTNCRLRLHLGLVIPKNVAIRVGHETRTWKEGKAIIIDDSFDHEVWHNGSTFRLIFIVDFWHP 529
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPPGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 372-537 6.11e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 181.61  E-value: 6.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 372 IRKLEGNWKVIRDEGLEVLDQKSG-----GFIPEEENLRQQGDWKQFTLYQRGRKNTAACRRTPRTCAIVDSIadaasck 446
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEAlppyhDISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 447 rGQIK---YSVMLPGTHVWPHTGPTNCRLRLHLGLVIPK--NVAIRVGHETRTWKEGKAIIIDDSFDHEVWHNGSTFRLI 521
Cdd:COG3555    93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNddRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*.
gi 2114306222 522 FIVDFWHPDLTPRQRA 537
Cdd:COG3555   172 LFCDVWRPMLSPWERA 187
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 136-376 3.93e-16

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 78.62  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 136 KGQIEDALKKYEGLVNKYPKSPLAMYgkaqsldKLSEIRQSNEILQQSIHAYGNVIDLPEcplqLKHQAMRRQADRLSFL 215
Cdd:COG2956    55 RGEYDRAIRIHQKLLERDPDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELDP----DDAEALRLLAEIYEQE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 216 GKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IKTDhlRYKEAIPLL 294
Cdd:COG2956   124 GDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELyLEQG--DYEEAIAAL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 295 REGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKkgiflsalqrsLYNADTPLTARPWWAPEQTGYLEAIRK 374
Cdd:COG2956   202 ERAL---EQDPDYLPALPRLAELYEKLGDPEEALELLRKALE-----------LDPSDDLLLALADLLERKEGLEAALAL 267


                  ..
gi 2114306222 375 LE 376
Cdd:COG2956   268 LE 269
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 203-337 7.53e-16

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: 74.46  E-value: 7.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 203 QAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IK 281
Cdd:COG4783     5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAlLK 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2114306222 282 TDhlRYKEAIPLLREGIASGEtgaDDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKK 337
Cdd:COG4783    85 AG--DYDEALALLEKALKLDP---EHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
154-407 1.90e-15

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 76.20  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 154 PKSPLAMYGKAQSLDKLSEIRQSNEILQQSIHaygnvIDlPECPlqlkhQAMRRQADRLSFLGKIGQAISTLKKLLNLFP 233
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALE-----LD-PDDA-----EALYNLGLAYLRLGRYEEALADYEQALELDP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 234 HDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGfIIKTDHLRYKEAIPLLREGIasgETGADDGRFYFH 313
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLG-LALLELGRYDEAIEAYERAL---ELDPDDADALYN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 314 LGDAFTRIGKPDEAYKVYEEAAKKGIFLSALQRSLYNADTPLTARPWWAPEQTGYLEAIRKLEGNWKVIRDEGLEVLDQK 393
Cdd:COG0457   150 LGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALAL 229

                         250
                  ....*....|....
gi 2114306222 394 SGGFIPEEENLRQQ 407
Cdd:COG0457   230 LLALRLAALALYQY 243
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
134-351 8.99e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.11  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 134 LDKGQIEDALKKYEGLVNKYPKSPLAMYGKAQSLDKLSEirqsneiLQQSIHAYGNVIDL-PECPlqlkhQAMRRQADRL 212
Cdd:COG0457    19 RRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGR-------YEEALADYEQALELdPDDA-----EALNNLGLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 213 SFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGfIIKTDHLRYKEAIP 292
Cdd:COG0457    87 QALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG-IALEKLGRYEEALE 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2114306222 293 LLREGIASGETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKKGIFLSALQRSLYNA 351
Cdd:COG0457   166 LLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLL 224
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 235-337 1.57e-12

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: 64.83  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 235 DLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIIKTDHlRYKEAIPLLREGIasgETGADDGRFYFHL 314
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEAL---ELDPDEPEARLNL 78

                          90       100
                  ....*....|....*....|...
gi 2114306222 315 GDAFTRIGKPDEAYKVYEEAAKK 337
Cdd:COG4783    79 GLALLKAGDYDEALALLEKALKL 101
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 130-334 3.04e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 69.25  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 130 AQSVLDKGQIEDALKKYEGLVNKYPKSPLAMYGKAQSLDKLSEIRQSNEILQQSIHAygNVIDLPECPLQLKHQAMRRQA 209
Cdd:COG3914     8 ALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAA--GEAAAAAAALLLLAALLELAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 210 DRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIIKTDHlRYKE 289
Cdd:COG3914    86 LLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG-RLEE 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2114306222 290 AIPLLREGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEA 334
Cdd:COG3914   165 AIAALRRAL---ELDPDNAEALNNLGNALQDLGRLEEAIAAYRRA 206
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
229-334 3.92e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.41  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 229 LNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGfIIKTDHLRYKEAIPLLREGIasgETGADDG 308
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLG-LAYLRLGRYEEALADYEQAL---ELDPDDA 76

                          90       100
                  ....*....|....*....|....*.
gi 2114306222 309 RFYFHLGDAFTRIGKPDEAYKVYEEA 334
Cdd:COG0457    77 EALNNLGLALQALGRYEEALEDYDKA 102
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 215-300 6.67e-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: 58.05  E-value: 6.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 215 LGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIIKTDHlRYKEAIPLL 294
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLG-QDDEAKAAL 145


                  ....*.
gi 2114306222 295 REGIAS 300
Cdd:COG5010   146 QRALGT 151
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 208-338 1.74e-09

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: 58.97  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 208 QADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFiiktDHLR- 286
Cdd:COG2956    14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ----DYLKa 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2114306222 287 --YKEAIPLLREGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKKG 338
Cdd:COG2956    90 glLDRAEELLEKLL---ELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLG 140
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 220-336 3.43e-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: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 220 QAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IKTDhlRYKEAIPLLREGI 298
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEAlLAAG--DTEEAEELLERAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2114306222 299 AsgeTGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAK 336
Cdd:COG4235    79 A---LDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLA 113
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 134-280 7.45e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 58.47  E-value: 7.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 134 LDKGQIEDALKKYEGLVNKYPKSPLAMYgkaqsldKLSEIRQSNEILQQSIHAYGNVIDL-PECPlqlkhQAMRRQADRL 212
Cdd:COG3914    89 QALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFA-----EAYLNLGEAL 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2114306222 213 SFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFII 280
Cdd:COG3914   157 RRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFAL 224
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 126-269 9.15e-09

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: 54.04  E-value: 9.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 126 ELTKAQSVLDKGQIEDALKKYEGLVNKYPKSPLAMYGKAQSLDKLSEIRQSNEILQQSIHAYgnvidlPECPlqlkhQAM 205
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELD------PDEP-----EAR 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2114306222 206 RRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSN 269
Cdd:COG4783    76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 131-233 1.80e-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: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 131 QSVLDKGQIEDALKKYEGLVNKYPKSPL---AMYGKAQSLDKLSEIRQSNEILQQSIHAYGNVIDLPEcplqlkhqAMRR 207
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRYPNSPLapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPD--------ALLK 72

                          90       100
                  ....*....|....*....|....*.
gi 2114306222 208 QADRLSFLGKIGQAISTLKKLLNLFP 233
Cdd:COG1729    73 LGLSYLELGDYDKARATLEELIKKYP 98
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 126-337 3.45e-08

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: 56.25  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 126 ELTKAQSVLDKGQIEDALKKYEGLVNKYPKSPLAMYGKAQ----------SLDKLSEIRQSN-------------EILQQ 182
Cdd:TIGR02917 230 LLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALvdfqkknyedARETLQDALKSApeylpalllagasEYQLG 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 183 SIHAYGNVIDLPECPLQLKHQAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKV 262
Cdd:TIGR02917 310 NLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 263 VNMDPSNGFAKSHLG--FIIKTDHlrykeaipllREGIASGETGA----DDGRFYFHLGDAFTRIGKPDEAYKVYEEAAK 336
Cdd:TIGR02917 390 TELDPENAAARTQLGisKLSQGDP----------SEAIADLETAAqldpELGRADLLLILSYLRSGQFDKALAAAKKLEK 459


                  .
gi 2114306222 337 K 337
Cdd:TIGR02917 460 K 460
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 185-336 4.32e-08

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: 52.66  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 185 HAYGNVIDLPECPLQLKHQAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVN 264
Cdd:COG5010     3 ALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2114306222 265 MDPSNGFAKSHLGfIIKTDHLRYKEAIPLLREGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAK 336
Cdd:COG5010    83 LDPNNPELYYNLA-LLYSRSGDKDEAKEYYEKAL---ALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALG 150
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
246-337 2.27e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.01  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 246 YLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIIkTDHLRYKEAIPLLRegiaSGETGADDGRFYFHLGDAFTRIGKPD 325
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLL-LEQGRYDEAIALEK----ALKLDPNNAEALLNLAELLLELGDYD 76

                          90
                  ....*....|..
gi 2114306222 326 EAYKVYEEAAKK 337
Cdd:COG3063    77 EALAYLERALEL 88
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 203-306 6.88e-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: 48.46  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 203 QAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGfIIKT 282
Cdd:COG4235    18 EGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLG-LAAF 96

                          90       100
                  ....*....|....*....|....
gi 2114306222 283 DHLRYKEAIPLLREGIASGETGAD 306
Cdd:COG4235    97 QQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
215-299 1.92e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.32  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 215 LGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENiYNKVVNMDPSNGFAKSHLGFIIKTDHlRYKEAIPLL 294
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELG-DYDEALAYL 82


                  ....*
gi 2114306222 295 REGIA 299
Cdd:COG3063    83 ERALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 244-337 2.51e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.44  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 244 VQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIIKTDHL--RYKEAIPLLREGIASGETGADDGRFYFHLGDAFTRI 321
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRYPNSPLAPDALYWLGEAYYAlgDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLEL 80

                          90
                  ....*....|....*.
gi 2114306222 322 GKPDEAYKVYEEAAKK 337
Cdd:COG1729    81 GDYDKARATLEELIKK 96
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 286-338 4.10e-05

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 41.55  E-value: 4.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2114306222 286 RYKEAIPLLREGIASGETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKKG 338
Cdd:pfam13432  12 DYDDAAAALEAALARFPESPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAA 64
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
203-334 5.82e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.52  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 203 QAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIikt 282
Cdd:COG4785    74 QLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIA--- 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2114306222 283 dHL---RYKEAI---------------PLLREGIASGETGADDGRFYF--HLGDAFTRIGKPDEAYKVYEEA 334
Cdd:COG4785   151 -LYylgRYELAIadlekaleldpndpeRALWLYLAERKLDPEKALALLleDWATAYLLQGDTEEARELFKLA 221
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 130-189 5.95e-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: 42.67  E-value: 5.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2114306222 130 AQSVLDKGQIEDALKKYEGLVNKYPKSPL---AMYGKAQSLDKLSEIRQSNEILQQSIHAYGN 189
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELGDYDKARATLEELIKKYPD 99
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 127-336 1.79e-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: 44.30  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 127 LTKAQSVLDKGQIEDALKKYEGLVNKYPKSPLAmygkaQSLDKLSEIRQSNeiLQQSIHAYGNVIDLpecplQLKHQAMR 206
Cdd:TIGR02917 673 IGLAQLLLAAKRTESAKKIAKSLQKQHPKAALG-----FELEGDLYLRQKD--YPAAIQAYRKALKR-----APSSQNAI 740

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 207 RQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFI-IKTDH- 284
Cdd:TIGR02917 741 KLHRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNNLAWLyLELKDp 820

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 285 --LRY----------------------------KEAIPLLREGIasgETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEA 334
Cdd:TIGR02917 821 raLEYaeralklapnipaildtlgwllvekgeaDRALPLLRKAV---NIAPEAAAIRYHLALALLATGRKAEARKELDKL 897


                  ..
gi 2114306222 335 AK 336
Cdd:TIGR02917 898 LN 899
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 130-187 3.80e-03

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: 37.26  E-value: 3.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2114306222 130 AQSVLDKGQIEDALKKYEGLVNKYPKS---PLAMYGKAQSLDKLSEIRQSNEILQQSIHAY 187
Cdd:TIGR02795  44 GEAYYAQGDYADAAKAFLAVVKKYPKSpkaPDALLKLGMSLQELGDKEKAKATLQQVIKRY 104
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 130-337 4.64e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 130 AQSVLDKGQIEDALKKYEGLVNKYPKSPLAMygkaQSLDKLSEIRQSNEilqqsihaygNVIDLPECPLQLKHQAmrrQA 209
Cdd:TIGR02917 506 ARIDIQEGNPDDAIQRFEKVLTIDPKNLRAI----LALAGLYLRTGNEE----------EAVAWLEKAAELNPQE---IE 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 210 DRLSF------LGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENIYNKVVNMDPSNGFAKSHLGFIiktd 283
Cdd:TIGR02917 569 PALALaqyylgKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADA---- 644

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2114306222 284 HLRYKEAIPLLREGIASGETGADDGRFYFHLGDAFTRIGKPDEAYKVYEEAAKK 337
Cdd:TIGR02917 645 YAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQ 698
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 180-267 9.01e-03

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: 37.25  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2114306222 180 LQQSIHAYGNVIDL-PECPlqlkhQAMRRQADRLSFLGKIGQAISTLKKLLNLFPHDLKLMNEIGVQYLLSGRNRDAENI 258
Cdd:COG5010    70 FEESLALLEQALQLdPNNP-----ELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAA 144


                  ....*....
gi 2114306222 259 YNKVVNMDP 267
Cdd:COG5010   145 LQRALGTSP 153
 
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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