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Conserved domains on  [gi|1889077434|ref|XP_035597867|]
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aspartyl/asparaginyl beta-hydroxylase-like isoform X12 [Oncorhynchus keta]

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 ...
 534-688 6.87e-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: 232.92  E-value: 6.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 534 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 610
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434 611 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 688
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 ...
 37-114 8.91e-27

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: 103.38  E-value: 8.91e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLLG 114
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 282-503 8.35e-21

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: 92.87  E-value: 8.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 282 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 361
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 362 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 441
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077434 442 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 503
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 198-264 1.62e-06

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


The actual alignment was detected with superfamily member pfam05887:

Pssm-ID: 368653  Cd Length: 134  Bit Score: 47.86  E-value: 1.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077434 198 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
rne super family cl35953
ribonuclease E; Reviewed
 121-264 2.98e-03

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434  121 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 197
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077434  198 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:PRK10811   934 SD-VAVAQEVAEHAEPVVEPQDETADIEEAaetaevvVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 534-688 6.87e-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: 232.92  E-value: 6.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 534 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 610
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434 611 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 688
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 508-696 1.41e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 188.93  E-value: 1.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 508 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 582
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 583 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 658
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077434 659 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 696
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-114 8.91e-27

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: 103.38  E-value: 8.91e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLLG 114
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 282-503 8.35e-21

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: 92.87  E-value: 8.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 282 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 361
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 362 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 441
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077434 442 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 503
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 198-264 1.62e-06

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 47.86  E-value: 1.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077434 198 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 281-464 7.89e-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: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 281 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 353
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 354 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 432
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077434 433 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 464
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
TPR_19 pfam14559
Tetratricopeptide repeat;
377-430 9.71e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 9.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077434 377 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 430
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
rne PRK10811
ribonuclease E; Reviewed
 121-264 2.98e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434  121 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 197
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077434  198 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:PRK10811   934 SD-VAVAQEVAEHAEPVVEPQDETADIEEAaetaevvVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 534-688 6.87e-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: 232.92  E-value: 6.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 534 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 610
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434 611 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 688
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 508-696 1.41e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 188.93  E-value: 1.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 508 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 582
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 583 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 658
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077434 659 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 696
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-114 8.91e-27

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: 103.38  E-value: 8.91e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077434  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLLG 114
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 282-503 8.35e-21

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: 92.87  E-value: 8.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 282 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 361
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 362 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 441
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077434 442 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 503
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 314-495 3.23e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.10  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 314 YPQSPRCRYGKALAEDGLAEKMLSNDMLQKAIGtykEASELPNATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIF 393
Cdd:COG3914    33 EAAALAAALGLALLLLAALAEAAAAALLALAAG---EAAAAAAALLLLAAL-LELAALLLQALGRYEEALALYRRALALN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 394 PEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGRFYFH 473
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALEL-DP--DNAEALNN 185

                         170       180
                  ....*....|....*....|...
gi 1889077434 474 LGDALQRMGD-DSAYKWYERGHQ 495
Cdd:COG3914   186 LGNALQDLGRlEEAIAAYRRALE 208
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 368-496 5.05e-13

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: 66.75  E-value: 5.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 368 KRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKI 447
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889077434 448 AESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQR 496
Cdd:COG4783    89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALEKALEL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
294-459 1.26e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.11  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 294 LRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDGLAEkmlsndmLQKAIGTYKEASELpnaTPDLIKAtLKKRAERQ 373
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGR-------YEEALADYEQALEL---DPDDAEA-LNNLGLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 374 QFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPF 453
Cdd:COG0457    87 QALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALEL 166


                  ....*.
gi 1889077434 454 LRDGLE 459
Cdd:COG0457   167 LEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-492 7.12e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.18  E-value: 7.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 376 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 455
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1889077434 456 DGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 492
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYER 135
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 376-460 1.90e-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: 59.97  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 376 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 455
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 1889077434 456 DGLES 460
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 289-473 1.14e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 61.55  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 289 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASELPnatPDLIKAtLKK 368
Cdd:COG3914    83 LAALLLQALGRYEEALALYRRALALNPDNA-----EALFN--LGNLLLALGRLEEALAALRRALALN---PDFAEA-YLN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 369 RAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIA 448
Cdd:COG3914   152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWE 231

                         170       180
                  ....*....|....*....|....*
gi 1889077434 449 ESIPFLRDGLESGDPGTDDGRFYFH 473
Cdd:COG3914   232 VYDRFEELLAALARGPSELSPFALL 256
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 376-466 1.38e-08

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: 53.86  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 376 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 455
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1889077434 456 DGLESGDPGTD 466
Cdd:COG4235   110 KLLALLPADAP 120
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 382-492 2.15e-08

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: 53.09  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 382 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESg 461
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL- 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1889077434 462 DPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 492
Cdd:COG4235    81 DP--DNPEALYLLGLAAFQQGDyAEAIAAWQK 110
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 287-430 4.06e-08

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: 52.50  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 287 EIDAAEKLRKKGKVEEAVRAFETLVLQYPQSP--RCRYGKALAEDGlaekmlsndMLQKAIGTYKEASELPNATPDLika 364
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPeaFALLGEILLQLG---------DLDEAIVLLHEALELDPDEPEA--- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077434 365 tLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 430
Cdd:COG4783    75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 395-505 1.19e-07

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: 51.35  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 395 EDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLEsGDPgtDDGRFYFHL 474
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE-LDP--DEPEARLNL 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1889077434 475 GDALQRMGD-DSAYKWYERGHQRG-HFASVWQR 505
Cdd:COG4783    79 GLALLKAGDyDEALALLEKALKLDpEHPEAYLR 111
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
390-492 1.47e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.09  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 390 VQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGR 469
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|....
gi 1889077434 470 FYFHLGDALQRMGD-DSAYKWYER 492
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYDK 101
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
406-496 6.78e-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: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 406 AHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRdGLESgDPgtDDGRFYFHLGDALQRMGD-D 484
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEK-ALKL-DP--NNAEALLNLAELLLELGDyD 76

                          90
                  ....*....|..
gi 1889077434 485 SAYKWYERGHQR 496
Cdd:COG3063    77 EALAYLERALEL 88
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 293-395 7.81e-07

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: 48.06  E-value: 7.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 293 KLRKKGKVEEAVRAFETLVLQYPQSPRcrygKALAEDGLAEKMLSNDMLQKAIGTYKEASELPNATPDLIKATLkKRAER 372
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPL----APDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALL-KLGLS 76

                          90       100
                  ....*....|....*....|...
gi 1889077434 373 QQFLGRMRGALATLEKLVQIFPE 395
Cdd:COG1729    77 YLELGDYDKARATLEELIKKYPD 99
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 198-264 1.62e-06

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 47.86  E-value: 1.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077434 198 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 210-261 2.24e-06

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 47.48  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1889077434 210 EAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHP 261
Cdd:pfam05887  60 EPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 111
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
376-459 3.33e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.93  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 376 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRvYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 455
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1889077434 456 DGLE 459
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 361-492 6.48e-06

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 46.88  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 361 LIKATLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFI 440
Cdd:COG5010    18 TKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889077434 441 LKSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 492
Cdd:COG5010    98 YSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDEAKAALQR 147
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 281-464 7.89e-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: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 281 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 353
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 354 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 432
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077434 433 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 464
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 162-246 9.49e-06

Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei procyclic acidic repetitive protein (PARP) like sequences. The procyclic acidic repetitive protein (parp) genes of Trypanosoma brucei encode a small family of abundant surface proteins whose expression is restricted to the procyclic form of the parasite. They are found at two unlinked loci, parpA and parpB; transcription of both loci is developmentally regulated.


Pssm-ID: 368653  Cd Length: 134  Bit Score: 45.55  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 162 EDENDAIDTKGElveKAQPQQTLEESKQYNNQPGSPETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVES 241
Cdd:pfam05887  29 EGPEDKGLTKGG---KGKGKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 105


                  ....*
gi 1889077434 242 VLELE 246
Cdd:pfam05887 106 EPEPE 110
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 341-428 1.08e-05

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: 46.11  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 341 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 420
Cdd:COG5010    70 FEESLALLEQALQL---DPNNPEL-YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAAL 145


                  ....*...
gi 1889077434 421 EEVLATAP 428
Cdd:COG5010   146 QRALGTSP 153
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 302-430 1.71e-05

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: 45.00  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 302 EAVRAFETLVLQYPQSPRcrygkALAEdgLAEKMLSNDMLQKAIGTYKEASELPNATPDLikatLKKRAERQQFLGRMRG 381
Cdd:COG4235     1 EAIARLRQALAANPNDAE-----GWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADA----LLDLAEALLAAGDTEE 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1889077434 382 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 430
Cdd:COG4235    70 AEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 284-470 7.08e-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: 46.23  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 284 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALA-------EDGL--AEKMLSND-----------MLQK 343
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVdfqkknyEDARetLQDALKSApeylpalllagASEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 344 AIGTYKEASELPN----ATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRV 419
Cdd:TIGR02917 307 QLGNLEQAYQYLNqilkYAPNSHQA-RRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1889077434 420 YEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESGDPGTDDGRF 470
Cdd:TIGR02917 386 LAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
284-433 1.04e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 44.14  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 284 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDglaekmlsndmLQKAIGTYKEASELPNATPDLIK 363
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAA-----------ALAAAALAAERIDRALALPDLAQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 364 AtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFA 433
Cdd:COG4785    75 L-YYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 280-459 3.40e-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: 43.92  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 280 FEKTIKTEID---AAEKL----RKKGKVEEAVRAFETLVLQYPQSPRcrygkalAEDGLAEKMLSNDMLQKAIGTYKEAS 352
Cdd:TIGR02917 488 FEKALSIEPDffpAAANLaridIQEGNPDDAIQRFEKVLTIDPKNLR-------AILALAGLYLRTGNEEEAVAWLEKAA 560

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 353 ELPNAtpDLIKATLKKRAERQQflGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 432
Cdd:TIGR02917 561 ELNPQ--EIEPALALAQYYLGK--GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSAL 636

                         170       180
                  ....*....|....*....|....*..
gi 1889077434 433 AKVHYGFILKSENKIAESIPFLRDGLE 459
Cdd:TIGR02917 637 ALLLLADAYAVMKNYAKAITSLKRALE 663
TPR_19 pfam14559
Tetratricopeptide repeat;
377-430 9.71e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 9.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077434 377 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 430
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 291-396 1.00e-03

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: 39.60  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 291 AEKLRKKGKVEEAVRAFETLVLQYPQSPRcrygkALAedGLAEKMLSNDMLQKAIGTYKEASELpnaTPDLIKAtLKKRA 370
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNAD-----ALL--DLAEALLAAGDTEEAEELLERALAL---DPDNPEA-LYLLG 92

                          90       100
                  ....*....|....*....|....*.
gi 1889077434 371 ERQQFLGRMRGALATLEKLVQIFPED 396
Cdd:COG4235    93 LAAFQQGDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 290-451 1.16e-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: 42.38  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 290 AAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAedglaeKMLSNDM------LQKAIGTykeASELPNATPDLIK 363
Cdd:TIGR02917 369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS------KLSQGDPseaiadLETAAQL---DPELGRADLLLIL 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 364 ATLKkraerqqfLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKS 443
Cdd:TIGR02917 440 SYLR--------SGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQ 511


                  ....*...
gi 1889077434 444 ENKIAESI 451
Cdd:TIGR02917 512 EGNPDDAI 519
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 240-456 1.62e-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: 41.99  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 240 ESVLELEAEFVPELKENA-----EDHPKDqlkekakkkkpkLLNKFEKTIK---TEIDA----AEKLRKKGKVEEAVRAF 307
Cdd:TIGR02917 489 EKALSIEPDFFPAAANLAridiqEGNPDD------------AIQRFEKVLTidpKNLRAilalAGLYLRTGNEEEAVAWL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 308 ETLVLQYPQSprcrYGKALAedgLAEKMLSNDMLQKAIGTYKEASELPNATPDLIkaTLKKRAerQQFLGRMRGALATLE 387
Cdd:TIGR02917 557 EKAAELNPQE----IEPALA---LAQYYLGKGQLKKALAILNEAADAAPDSPEAW--LMLGRA--QLAAGDLNKAVSSFK 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077434 388 KLVQIFPEDmalkndlGVAHLLIGD-----NNSAK--RVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRD 456
Cdd:TIGR02917 626 KLLALQPDS-------ALALLLLADayavmKNYAKaiTSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKS 694
rne PRK10811
ribonuclease E; Reviewed
 121-264 2.98e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434  121 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 197
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077434  198 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 264
Cdd:PRK10811   934 SD-VAVAQEVAEHAEPVVEPQDETADIEEAaetaevvVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 289-431 3.15e-03

Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];


Pssm-ID: 442215 [Multi-domain]  Cd Length: 207  Bit Score: 39.45  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 289 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrYGkALAEDGLAEKMLSNDMLQKAIGTYKEASElpNATPDLIKATLKK 368
Cdd:COG2976    58 EQLLEALAAGDAAAAAAAAEKLIDDYGGTA---YA-ALAALLLAKAAVDAGDLDKAAAQLQWVLD--NAKDPALKALARL 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077434 369 RAERQQF-LGRMRGALATLEklvQIFPED-MALKNDL-GVAHLLIGDNNSAKRVYEEVLATAPSDG 431
Cdd:COG2976   132 RLARVLLaQKKYDEALATLD---AVKPEAfAALYAELrGDILLAQGDKAEARAAYQKALAALPEDA 194
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 298-460 3.15e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 298 GKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASEL--------------------PNA 357
Cdd:TIGR02917 615 GDLNKAVSSFKKLLALQPDSA-----LALLL--LADAYAVMKNYAKAITSLKRALELkpdnteaqiglaqlllaakrTES 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 358 TPDLIKATLKKR---AERQQFLGR--MR-----GALATLEKLVQIFPEDMALKNdLGVAHLLIGDNNSAKRVYEEVLATA 427
Cdd:TIGR02917 688 AKKIAKSLQKQHpkaALGFELEGDlyLRqkdypAAIQAYRKALKRAPSSQNAIK-LHRALLASGNTAEAVKTLEAWLKTH 766

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1889077434 428 PSDGFAKVHYGFILKSENKIAESIPFLRDGLES 460
Cdd:TIGR02917 767 PNDAVLRTALAELYLAQKDYDKAIKHYQTVVKK 799
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
341-429 3.61e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434 341 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALAtLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 420
Cdd:COG3063     8 LEEAEEYYEKALEL---DPDNADA-LNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                  ....*....
gi 1889077434 421 EEVLATAPS 429
Cdd:COG3063    83 ERALELDPS 91
rne PRK10811
ribonuclease E; Reviewed
 117-256 8.92e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 39.64  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077434  117 ESPVSVSLREAKEESAVKEPAAVPLPP--ISDDFIPDDSRDDATHPyEDENDAIDTKGELVEK---AQPQQTLEESkqyn 191
Cdd:PRK10811   872 EVPVAAAVEPVVSAPVVEAVAEVVEEPvvVAEPQPEEVVVVETTHP-EVIAAPVTEQPQVITEsdvAVAQEVAEHA---- 946

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889077434  192 nQPGSPETKETVQLRYNAEA--ESVPEPEADVEPEVESVPEPEADV--EPEVESVLELEAEFVPELKEN 256
Cdd:PRK10811   947 -EPVVEPQDETADIEEAAETaeVVVAEPEVVAQPAAPVVAEVAAEVetVTAVEPEVAPAQVPEATVEHN 1014
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 291-357 9.44e-03

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: 36.51  E-value: 9.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889077434 291 AEKLRKKGKVEEAVRAFETLVLQYPQSPRC-----RYGKALAEDGLAEKmlSNDMLQKAIGTYKEASELPNA 357
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSPKApdallKLGLSYLELGDYDK--ARATLEELIKKYPDSEAAKEA 106
 
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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