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Conserved domains on  [gi|1889077426|ref|XP_035597863|]
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aspartyl/asparaginyl beta-hydroxylase-like isoform X8 [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 ...
 551-705 7.21e-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: 233.31  E-value: 7.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 551 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 627
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077426 628 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 705
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 ...
 37-113 2.83e-26

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: 102.23  E-value: 2.83e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLL 113
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 299-520 1.08e-20

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: 92.48  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 299 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 378
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 379 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 458
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077426 459 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 520
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 215-281 2.30e-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: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426 215 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
rne super family cl35953
ribonuclease E; Reviewed
 138-281 3.43e-03

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426  138 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 214
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077426  215 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
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 ...
 551-705 7.21e-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: 233.31  E-value: 7.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 551 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 627
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077426 628 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 705
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 525-713 1.63e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.32  E-value: 1.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 525 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 599
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 600 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 675
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077426 676 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 713
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-113 2.83e-26

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: 102.23  E-value: 2.83e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLL 113
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 299-520 1.08e-20

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: 92.48  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 299 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 378
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 379 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 458
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077426 459 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 520
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 215-281 2.30e-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: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426 215 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 298-481 1.02e-05

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 298 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 370
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 371 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 449
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077426 450 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 481
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
TPR_19 pfam14559
Tetratricopeptide repeat;
394-447 1.03e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077426 394 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 447
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
rne PRK10811
ribonuclease E; Reviewed
 138-281 3.43e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426  138 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 214
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077426  215 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
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 ...
 551-705 7.21e-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: 233.31  E-value: 7.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 551 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 627
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077426 628 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 705
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 525-713 1.63e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.32  E-value: 1.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 525 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 599
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 600 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 675
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077426 676 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 713
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-113 2.83e-26

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: 102.23  E-value: 2.83e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIaerakefrfnfsevlqGKLSAYDADGDGDFDVEDAKVLL 113
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL----------------GKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 299-520 1.08e-20

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: 92.48  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 299 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 378
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 379 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 458
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077426 459 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 520
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 331-512 3.36e-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: 3.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 331 YPQSPRCRYGKALAEDGLAEKMLSNDMLQKAIGtykEASELPNATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIF 410
Cdd:COG3914    33 EAAALAAALGLALLLLAALAEAAAAALLALAAG---EAAAAAAALLLLAAL-LELAALLLQALGRYEEALALYRRALALN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 411 PEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGRFYFH 490
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALEL-DP--DNAEALNN 185

                         170       180
                  ....*....|....*....|...
gi 1889077426 491 LGDALQRMGD-DSAYKWYERGHQ 512
Cdd:COG3914   186 LGNALQDLGRlEEAIAAYRRALE 208
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 385-513 5.66e-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: 5.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 385 KRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKI 464
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889077426 465 AESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQR 513
Cdd:COG4783    89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALEKALEL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
311-476 1.22e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.49  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 311 LRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDGLAEkmlsndmLQKAIGTYKEASELpnaTPDLIKAtLKKRAERQ 390
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGR-------YEEALADYEQALEL---DPDDAEA-LNNLGLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 391 QFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPF 470
Cdd:COG0457    87 QALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALEL 166


                  ....*.
gi 1889077426 471 LRDGLE 476
Cdd:COG0457   167 LEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
393-509 6.75e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.18  E-value: 6.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 393 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 472
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1889077426 473 DGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 509
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYER 135
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 393-477 1.96e-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: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 393 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 472
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 1889077426 473 DGLES 477
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 306-490 1.18e-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: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 306 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASELPnatPDLIKAtLKK 385
Cdd:COG3914    83 LAALLLQALGRYEEALALYRRALALNPDNA-----EALFN--LGNLLLALGRLEEALAALRRALALN---PDFAEA-YLN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 386 RAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIA 465
Cdd:COG3914   152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWE 231

                         170       180
                  ....*....|....*....|....*
gi 1889077426 466 ESIPFLRDGLESGDPGTDDGRFYFH 490
Cdd:COG3914   232 VYDRFEELLAALARGPSELSPFALL 256
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 393-483 1.42e-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: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 393 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 472
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1889077426 473 DGLESGDPGTD 483
Cdd:COG4235   110 KLLALLPADAP 120
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 399-509 2.21e-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: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 399 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESg 478
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL- 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1889077426 479 DPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 509
Cdd:COG4235    81 DP--DNPEALYLLGLAAFQQGDyAEAIAAWQK 110
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 304-447 4.63e-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: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 304 EIDAAEKLRKKGKVEEAVRAFETLVLQYPQSP--RCRYGKALAEDGlaekmlsndMLQKAIGTYKEASELPNATPDLika 381
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPeaFALLGEILLQLG---------DLDEAIVLLHEALELDPDEPEA--- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077426 382 tLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 447
Cdd:COG4783    75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 412-522 1.35e-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: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 412 EDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLEsGDPgtDDGRFYFHL 491
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE-LDP--DEPEARLNL 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1889077426 492 GDALQRMGD-DSAYKWYERGHQRG-HFASVWQR 522
Cdd:COG4783    79 GLALLKAGDyDEALALLEKALKLDpEHPEAYLR 111
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
407-509 1.54e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.09  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 407 VQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGR 486
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|....
gi 1889077426 487 FYFHLGDALQRMGD-DSAYKWYER 509
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYDK 101
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
423-513 7.31e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.86  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 423 AHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRdGLESgDPgtDDGRFYFHLGDALQRMGD-D 501
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEK-ALKL-DP--NNAEALLNLAELLLELGDyD 76

                          90
                  ....*....|..
gi 1889077426 502 SAYKWYERGHQR 513
Cdd:COG3063    77 EALAYLERALEL 88
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 310-412 8.91e-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: 8.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 310 KLRKKGKVEEAVRAFETLVLQYPQSPRcrygKALAEDGLAEKMLSNDMLQKAIGTYKEASELPNATPDLIKATLkKRAER 389
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPL----APDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALL-KLGLS 76

                          90       100
                  ....*....|....*....|...
gi 1889077426 390 QQFLGRMRGALATLEKLVQIFPE 412
Cdd:COG1729    77 YLELGDYDKARATLEELIKKYPD 99
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 215-281 2.30e-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: 2.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077426 215 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 225-278 3.29e-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: 47.09  E-value: 3.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077426 225 NAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHP 278
Cdd:pfam05887  58 DPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 111
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
393-476 3.55e-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: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 393 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRvYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 472
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1889077426 473 DGLE 476
Cdd:COG3063    84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 378-509 6.66e-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: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 378 LIKATLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFI 457
Cdd:COG5010    18 TKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889077426 458 LKSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 509
Cdd:COG5010    98 YSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDEAKAALQR 147
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 298-481 1.02e-05

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 298 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 370
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 371 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 449
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077426 450 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 481
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 358-445 1.11e-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: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 358 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 437
Cdd:COG5010    70 FEESLALLEQALQL---DPNNPEL-YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAAL 145


                  ....*...
gi 1889077426 438 EEVLATAP 445
Cdd:COG5010   146 QRALGTSP 153
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 179-263 1.36e-05

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: 45.17  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 179 EDENDAIDTKGElveKAQPQQTLEESKQYNNQPGSPETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVES 258
Cdd:pfam05887  29 EGPEDKGLTKGG---KGKGKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 105


                  ....*
gi 1889077426 259 VLELE 263
Cdd:pfam05887 106 EPEPE 110
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 319-447 1.75e-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: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 319 EAVRAFETLVLQYPQSPRcrygkALAEdgLAEKMLSNDMLQKAIGTYKEASELPNATPDLikatLKKRAERQQFLGRMRG 398
Cdd:COG4235     1 EAIARLRQALAANPNDAE-----GWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADA----LLDLAEALLAAGDTEE 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1889077426 399 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 447
Cdd:COG4235    70 AEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 301-487 8.30e-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: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 301 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALA-------EDGL--AEKMLSND-----------MLQK 360
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVdfqkknyEDARetLQDALKSApeylpalllagASEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 361 AIGTYKEASELPN----ATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRV 436
Cdd:TIGR02917 307 QLGNLEQAYQYLNqilkYAPNSHQA-RRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1889077426 437 YEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESGDPGTDDGRF 487
Cdd:TIGR02917 386 LAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
301-450 9.65e-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: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 301 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDglaekmlsndmLQKAIGTYKEASELPNATPDLIK 380
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAA-----------ALAAAALAAERIDRALALPDLAQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 381 AtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFA 450
Cdd:COG4785    75 L-YYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 297-476 3.96e-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: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 297 FEKTIKTEID---AAEKL----RKKGKVEEAVRAFETLVLQYPQSPRcrygkalAEDGLAEKMLSNDMLQKAIGTYKEAS 369
Cdd:TIGR02917 488 FEKALSIEPDffpAAANLaridIQEGNPDDAIQRFEKVLTIDPKNLR-------AILALAGLYLRTGNEEEAVAWLEKAA 560

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 370 ELPNAtpDLIKATLKKRAERQQflGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 449
Cdd:TIGR02917 561 ELNPQ--EIEPALALAQYYLGK--GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSAL 636

                         170       180
                  ....*....|....*....|....*..
gi 1889077426 450 AKVHYGFILKSENKIAESIPFLRDGLE 476
Cdd:TIGR02917 637 ALLLLADAYAVMKNYAKAITSLKRALE 663
TPR_19 pfam14559
Tetratricopeptide repeat;
394-447 1.03e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077426 394 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 447
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 308-413 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 308 AEKLRKKGKVEEAVRAFETLVLQYPQSPRcrygkALAedGLAEKMLSNDMLQKAIGTYKEASELpnaTPDLIKAtLKKRA 387
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNAD-----ALL--DLAEALLAAGDTEEAEELLERALAL---DPDNPEA-LYLLG 92

                          90       100
                  ....*....|....*....|....*.
gi 1889077426 388 ERQQFLGRMRGALATLEKLVQIFPED 413
Cdd:COG4235    93 LAAFQQGDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 307-468 1.41e-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: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 307 AAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAedglaeKMLSNDM------LQKAIGTykeASELPNATPDLIK 380
Cdd:TIGR02917 369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS------KLSQGDPseaiadLETAAQL---DPELGRADLLLIL 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 381 ATLKkraerqqfLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKS 460
Cdd:TIGR02917 440 SYLR--------SGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQ 511


                  ....*...
gi 1889077426 461 ENKIAESI 468
Cdd:TIGR02917 512 EGNPDDAI 519
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 257-473 1.98e-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: 41.61  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 257 ESVLELEAEFVPELKENA-----EDHPKDqlkekakkkkpkLLNKFEKTIK---TEIDA----AEKLRKKGKVEEAVRAF 324
Cdd:TIGR02917 489 EKALSIEPDFFPAAANLAridiqEGNPDD------------AIQRFEKVLTidpKNLRAilalAGLYLRTGNEEEAVAWL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 325 ETLVLQYPQSprcrYGKALAedgLAEKMLSNDMLQKAIGTYKEASELPNATPDLIkaTLKKRAerQQFLGRMRGALATLE 404
Cdd:TIGR02917 557 EKAAELNPQE----IEPALA---LAQYYLGKGQLKKALAILNEAADAAPDSPEAW--LMLGRA--QLAAGDLNKAVSSFK 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077426 405 KLVQIFPEDmalkndlGVAHLLIGD-----NNSAK--RVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRD 473
Cdd:TIGR02917 626 KLLALQPDS-------ALALLLLADayavmKNYAKaiTSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKS 694
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 306-448 3.24e-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: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 306 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrYGkALAEDGLAEKMLSNDMLQKAIGTYKEASElpNATPDLIKATLKK 385
Cdd:COG2976    58 EQLLEALAAGDAAAAAAAAEKLIDDYGGTA---YA-ALAALLLAKAAVDAGDLDKAAAQLQWVLD--NAKDPALKALARL 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077426 386 RAERQQF-LGRMRGALATLEklvQIFPED-MALKNDL-GVAHLLIGDNNSAKRVYEEVLATAPSDG 448
Cdd:COG2976   132 RLARVLLaQKKYDEALATLD---AVKPEAfAALYAELrGDILLAQGDKAEARAAYQKALAALPEDA 194
rne PRK10811
ribonuclease E; Reviewed
 138-281 3.43e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426  138 SVSLREAKEESAVKEPAAVPLPPISDDFIPDDSRDDATHPYED---ENDAIDTKGELVEKAQPQqTLEESKQYNNQPGSP 214
Cdd:PRK10811   855 VEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEpvvVAEPQPEEVVVVETTHPE-VIAAPVTEQPQVITE 933

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889077426  215 ETkETVQLRYNAEAESVPEPEADVEPEVES-------VPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 281
Cdd:PRK10811   934 SD-VAVAQEVAEHAEPVVEPQDETADIEEAaetaevvVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQV 1006
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 315-477 3.72e-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: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 315 GKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASEL--------------------PNA 374
Cdd:TIGR02917 615 GDLNKAVSSFKKLLALQPDSA-----LALLL--LADAYAVMKNYAKAITSLKRALELkpdnteaqiglaqlllaakrTES 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 375 TPDLIKATLKKR---AERQQFLGR--MR-----GALATLEKLVQIFPEDMALKNdLGVAHLLIGDNNSAKRVYEEVLATA 444
Cdd:TIGR02917 688 AKKIAKSLQKQHpkaALGFELEGDlyLRqkdypAAIQAYRKALKRAPSSQNAIK-LHRALLASGNTAEAVKTLEAWLKTH 766

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1889077426 445 PSDGFAKVHYGFILKSENKIAESIPFLRDGLES 477
Cdd:TIGR02917 767 PNDAVLRTALAELYLAQKDYDKAIKHYQTVVKK 799
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
358-446 3.77e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.07  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426 358 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALAtLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 437
Cdd:COG3063     8 LEEAEEYYEKALEL---DPDNADA-LNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                  ....*....
gi 1889077426 438 EEVLATAPS 446
Cdd:COG3063    83 ERALELDPS 91
rne PRK10811
ribonuclease E; Reviewed
 106-273 9.35e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 39.25  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426  106 VEDAKVL-LDEKEIKVPAPKMErlkkglkESPVSVSLREAKEESAVKEPAAVPLPP--ISDDFIPDDSRDDATHPyEDEN 182
Cdd:PRK10811   850 PQDVQVEeQREAEEVQVQPVVA-------EVPVAAAVEPVVSAPVVEAVAEVVEEPvvVAEPQPEEVVVVETTHP-EVIA 921

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077426  183 DAIDTKGELVEK---AQPQQTLEESkqynnQPGSPETKETVQLRYNAEA--ESVPEPEADVEPEVESVPEPEADV--EPE 255
Cdd:PRK10811   922 APVTEQPQVITEsdvAVAQEVAEHA-----EPVVEPQDETADIEEAAETaeVVVAEPEVVAQPAAPVVAEVAAEVetVTA 996

                          170
                   ....*....|....*...
gi 1889077426  256 VESVLELEAEFVPELKEN 273
Cdd:PRK10811   997 VEPEVAPAQVPEATVEHN 1014
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 308-374 9.88e-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: 9.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889077426 308 AEKLRKKGKVEEAVRAFETLVLQYPQSPRC-----RYGKALAEDGLAEKmlSNDMLQKAIGTYKEASELPNA 374
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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