NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1889077420|ref|XP_035597860|]
View 

aspartyl/asparaginyl beta-hydroxylase-like isoform X5 [Oncorhynchus keta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 558-712 5.20e-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: 233.69  E-value: 5.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 558 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077420 635 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 712
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 ...
 37-97 7.36e-30

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: 112.24  E-value: 7.36e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889077420  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIGKLSAYDADGDGDFDVEDAKVLL 97
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 306-527 6.23e-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: 93.26  E-value: 6.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 306 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 385
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 386 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 465
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077420 466 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 527
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP super family cl42451
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 222-288 1.94e-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: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077420 222 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 288
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 558-712 5.20e-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: 233.69  E-value: 5.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 558 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077420 635 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 712
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 532-720 9.03e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.09  E-value: 9.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 532 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 606
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 607 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 682
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077420 683 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 720
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-97 7.36e-30

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: 112.24  E-value: 7.36e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889077420  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIGKLSAYDADGDGDFDVEDAKVLL 97
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 306-527 6.23e-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: 93.26  E-value: 6.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 306 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 385
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 386 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 465
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077420 466 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 527
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 222-288 1.94e-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: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077420 222 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 288
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 305-488 8.40e-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: 8.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 305 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 377
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 378 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 456
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077420 457 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 488
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
TPR_19 pfam14559
Tetratricopeptide repeat;
401-454 9.29e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 9.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077420 401 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 454
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 558-712 5.20e-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: 233.69  E-value: 5.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 558 ERNWRIIRDEAQSVMDKTTGLFVPEEENLREKGE--WGQFTLWQQGKKAGESCRSVPKTCGLLERYP-EATGCKRGQIKF 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889077420 635 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKtGCKIRCTNDTRAWEEGKVLIFDDSFEHEVWQDADSYRLIFIVDVWHP 712
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 532-720 9.03e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.09  E-value: 9.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 532 YNVDGLKAQPWWtpkDTGYMDLVKTLERNWRIIRDEAQSVMDKTTGL-----FVPEEENLREKGEWGQFTLWQQGKKAGE 606
Cdd:COG3555     1 YRFSGLPTTPFF---DRAQFPWLAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 607 SCRSVPKTCGLLERYPeatgckrgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKT-GCKIRCTNDTRAWEEGK 682
Cdd:COG3555    78 NCALCPKTAALLEQIP--------GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGE 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1889077420 683 VLIFDDSFEHEVWQDADSYRLIFIVDVWHPELTQYQRQ 720
Cdd:COG3555   150 AVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWERA 187
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 37-97 7.36e-30

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: 112.24  E-value: 7.36e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889077420  37 GGFSGTKIFTWFMVLALLGVWSSVAVVWFDLVDYDNVIGKLSAYDADGDGDFDVEDAKVLL 97
Cdd:pfam05279   5 GGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLL 65
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 306-527 6.23e-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: 93.26  E-value: 6.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 306 KTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYgkALAEDglaekMLSNDMLQKAIGTYKEASELPnatPDL 385
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALL--ELAQD-----YLKAGLLDRAEELLEKLLELD---PDD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 386 IKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFIL 465
Cdd:COG2956   110 AEA-LRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889077420 466 KSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQRGHFASVW 527
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 338-519 3.42e-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: 3.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 338 YPQSPRCRYGKALAEDGLAEKMLSNDMLQKAIGtykEASELPNATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIF 417
Cdd:COG3914    33 EAAALAAALGLALLLLAALAEAAAAALLALAAG---EAAAAAAALLLLAAL-LELAALLLQALGRYEEALALYRRALALN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 418 PEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGRFYFH 497
Cdd:COG3914   109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALEL-DP--DNAEALNN 185

                         170       180
                  ....*....|....*....|...
gi 1889077420 498 LGDALQRMGD-DSAYKWYERGHQ 519
Cdd:COG3914   186 LGNALQDLGRlEEAIAAYRRALE 208
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 392-520 4.08e-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: 67.14  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 392 KRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKI 471
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1889077420 472 AESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYERGHQR 520
Cdd:COG4783    89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALEKALEL 135
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
318-483 8.73e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.88  E-value: 8.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 318 LRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDGLAEkmlsndmLQKAIGTYKEASELpnaTPDLIKAtLKKRAERQ 397
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGR-------YEEALADYEQALEL---DPDDAEA-LNNLGLAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 398 QFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPF 477
Cdd:COG0457    87 QALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALEL 166


                  ....*.
gi 1889077420 478 LRDGLE 483
Cdd:COG0457   167 LEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
400-516 4.79e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.57  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 400 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 479
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1889077420 480 DGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 516
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYER 135
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 400-484 1.28e-10

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 60.36  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 400 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 479
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 1889077420 480 DGLES 484
Cdd:COG5010   147 RALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 313-497 1.20e-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: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 313 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASELPnatPDLIKAtLKK 392
Cdd:COG3914    83 LAALLLQALGRYEEALALYRRALALNPDNA-----EALFN--LGNLLLALGRLEEALAALRRALALN---PDFAEA-YLN 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 393 RAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIA 472
Cdd:COG3914   152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWE 231

                         170       180
                  ....*....|....*....|....*
gi 1889077420 473 ESIPFLRDGLESGDPGTDDGRFYFH 497
Cdd:COG3914   232 VYDRFEELLAALARGPSELSPFALL 256
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 400-490 1.26e-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: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 400 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 479
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1889077420 480 DGLESGDPGTD 490
Cdd:COG4235   110 KLLALLPADAP 120
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 406-516 1.74e-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: 53.47  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 406 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESg 485
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL- 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1889077420 486 DPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 516
Cdd:COG4235    81 DP--DNPEALYLLGLAAFQQGDyAEAIAAWQK 110
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 311-454 3.47e-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: 52.89  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 311 EIDAAEKLRKKGKVEEAVRAFETLVLQYPQSP--RCRYGKALAEDGlaekmlsndMLQKAIGTYKEASELPNATPDLika 388
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPeaFALLGEILLQLG---------DLDEAIVLLHEALELDPDEPEA--- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077420 389 tLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 454
Cdd:COG4783    75 -RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 419-529 1.05e-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: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 419 EDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLEsGDPgtDDGRFYFHL 498
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE-LDP--DEPEARLNL 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1889077420 499 GDALQRMGD-DSAYKWYERGHQRG-HFASVWQR 529
Cdd:COG4783    79 GLALLKAGDyDEALALLEKALKLDpEHPEAYLR 111
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
414-516 1.10e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.47  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 414 VQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESgDPgtDDGR 493
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|....
gi 1889077420 494 FYFHLGDALQRMGD-DSAYKWYER 516
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYDK 101
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
430-520 4.95e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.24  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 430 AHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRdGLESgDPgtDDGRFYFHLGDALQRMGD-D 508
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEK-ALKL-DP--NNAEALLNLAELLLELGDyD 76

                          90
                  ....*....|..
gi 1889077420 509 SAYKWYERGHQR 520
Cdd:COG3063    77 EALAYLERALEL 88
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 317-419 6.35e-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: 48.45  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 317 KLRKKGKVEEAVRAFETLVLQYPQSPRcrygKALAEDGLAEKMLSNDMLQKAIGTYKEASELPNATPDLIKATLkKRAER 396
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPL----APDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALL-KLGLS 76

                          90       100
                  ....*....|....*....|...
gi 1889077420 397 QQFLGRMRGALATLEKLVQIFPE 419
Cdd:COG1729    77 YLELGDYDKARATLEELIKKYPD 99
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 222-288 1.94e-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: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889077420 222 ETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHPKDQ 288
Cdd:pfam05887  44 GKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPE 110
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
400-483 2.68e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.32  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 400 LGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRvYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLR 479
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1889077420 480 DGLE 483
Cdd:COG3063    84 RALE 87
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 232-285 2.88e-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: 2.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077420 232 NAEAESVPEPEADVEPEVESVPEPEADVEPEVESVLELEAEFVPELKENAEDHP 285
Cdd:pfam05887  58 DPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 111
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 385-516 4.14e-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: 47.26  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 385 LIKATLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFI 464
Cdd:COG5010    18 TKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1889077420 465 LKSENKIAESIPFLRDGLESgDPgtDDGRFYFHLGDALQRMGD-DSAYKWYER 516
Cdd:COG5010    98 YSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDEAKAALQR 147
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 365-452 7.77e-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: 46.49  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 365 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 444
Cdd:COG5010    70 FEESLALLEQALQL---DPNNPEL-YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAAL 145


                  ....*...
gi 1889077420 445 EEVLATAP 452
Cdd:COG5010   146 QRALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 305-488 8.40e-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: 8.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 305 EKTIKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRY--GKALAEDG---LAEKMLsndmlQKA--IGTYKEAse 377
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALGdyaAAEKEL-----RKAlsLGYPKNQ-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 378 lpnATPDLIKATLKKRAERQqflgrmrgALATLEKLVQIFPEDMA-LKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 456
Cdd:TIGR02917  92 ---VLPLLARAYLLQGKFQQ--------VLDELPGKTLLDDEGAAeLLALRGLAYLGLGQLELAQKSYEQALAIDPRSLY 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1889077420 457 AKVHYGFILKSENKIAESIPFLRDGLeSGDPG 488
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVL-TADPG 191
Trypan_PARP pfam05887
Procyclic acidic repetitive protein (PARP); This family consists of several Trypanosoma brucei ...
 186-270 1.22e-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: 45.55  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 186 EDENDAIDTKGElveKAQPQQTLEESKQYNNQPGSPETKETVQLRYNAEAESVPEPEADVEPEVESVPEPEADVEPEVES 265
Cdd:pfam05887  29 EGPEDKGLTKGG---KGKGKGTKVSDDDTNGTDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEP 105


                  ....*
gi 1889077420 266 VLELE 270
Cdd:pfam05887 106 EPEPE 110
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 326-454 1.43e-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: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 326 EAVRAFETLVLQYPQSPRcrygkALAEdgLAEKMLSNDMLQKAIGTYKEASELPNATPDLikatLKKRAERQQFLGRMRG 405
Cdd:COG4235     1 EAIARLRQALAANPNDAE-----GWLL--LGRAYLRLGRYDEALAAYEKALRLDPDNADA----LLDLAEALLAAGDTEE 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1889077420 406 ALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 454
Cdd:COG4235    70 AEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 308-494 7.66e-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: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 308 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALA-------EDGL--AEKMLSND-----------MLQK 367
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVdfqkknyEDARetLQDALKSApeylpalllagASEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 368 AIGTYKEASELPN----ATPDLIKAtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRV 443
Cdd:TIGR02917 307 QLGNLEQAYQYLNqilkYAPNSHQA-RRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEY 385

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1889077420 444 YEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRDGLESGDPGTDDGRF 494
Cdd:TIGR02917 386 LAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
308-457 7.69e-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: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 308 IKTEIDAAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAEDglaekmlsndmLQKAIGTYKEASELPNATPDLIK 387
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAA-----------ALAAAALAAERIDRALALPDLAQ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 388 AtLKKRAERQQFLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFA 457
Cdd:COG4785    75 L-YYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 304-483 3.55e-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: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 304 FEKTIKTEID---AAEKL----RKKGKVEEAVRAFETLVLQYPQSPRcrygkalAEDGLAEKMLSNDMLQKAIGTYKEAS 376
Cdd:TIGR02917 488 FEKALSIEPDffpAAANLaridIQEGNPDDAIQRFEKVLTIDPKNLR-------AILALAGLYLRTGNEEEAVAWLEKAA 560

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 377 ELPNAtpDLIKATLKKRAERQQflGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGF 456
Cdd:TIGR02917 561 ELNPQ--EIEPALALAQYYLGK--GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSAL 636

                         170       180
                  ....*....|....*....|....*..
gi 1889077420 457 AKVHYGFILKSENKIAESIPFLRDGLE 483
Cdd:TIGR02917 637 ALLLLADAYAVMKNYAKAITSLKRALE 663
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 315-420 8.95e-04

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: 39.99  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 315 AEKLRKKGKVEEAVRAFETLVLQYPQSPRcrygkALAedGLAEKMLSNDMLQKAIGTYKEASELpnaTPDLIKAtLKKRA 394
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNAD-----ALL--DLAEALLAAGDTEEAEELLERALAL---DPDNPEA-LYLLG 92

                          90       100
                  ....*....|....*....|....*.
gi 1889077420 395 ERQQFLGRMRGALATLEKLVQIFPED 420
Cdd:COG4235    93 LAAFQQGDYAEAIAAWQKLLALLPAD 118
TPR_19 pfam14559
Tetratricopeptide repeat;
401-454 9.29e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.95  E-value: 9.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1889077420 401 GRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSD 454
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD 55
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 314-475 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 314 AAEKLRKKGKVEEAVRAFETLVLQYPQSPRCRYGKALAedglaeKMLSNDM------LQKAIGTykeASELPNATPDLIK 387
Cdd:TIGR02917 369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS------KLSQGDPseaiadLETAAQL---DPELGRADLLLIL 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 388 ATLKkraerqqfLGRMRGALATLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVYEEVLATAPSDGFAKVHYGFILKS 467
Cdd:TIGR02917 440 SYLR--------SGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQ 511


                  ....*...
gi 1889077420 468 ENKIAESI 475
Cdd:TIGR02917 512 EGNPDDAI 519
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 264-480 1.71e-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: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 264 ESVLELEAEFVPELKENA-----EDHPKDqlkekakkkkpkLLNKFEKTIK---TEIDA----AEKLRKKGKVEEAVRAF 331
Cdd:TIGR02917 489 EKALSIEPDFFPAAANLAridiqEGNPDD------------AIQRFEKVLTidpKNLRAilalAGLYLRTGNEEEAVAWL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 332 ETLVLQYPQSprcrYGKALAedgLAEKMLSNDMLQKAIGTYKEASELPNATPDLIkaTLKKRAerQQFLGRMRGALATLE 411
Cdd:TIGR02917 557 EKAAELNPQE----IEPALA---LAQYYLGKGQLKKALAILNEAADAAPDSPEAW--LMLGRA--QLAAGDLNKAVSSFK 625

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077420 412 KLVQIFPEDmalkndlGVAHLLIGD-----NNSAK--RVYEEVLATAPSDGFAKVHYGFILKSENKIAESIPFLRD 480
Cdd:TIGR02917 626 KLLALQPDS-------ALALLLLADayavmKNYAKaiTSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKS 694
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
365-453 2.87e-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: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 365 LQKAIGTYKEASELpnaTPDLIKAtLKKRAERQQFLGRMRGALAtLEKLVQIFPEDMALKNDLGVAHLLIGDNNSAKRVY 444
Cdd:COG3063     8 LEEAEEYYEKALEL---DPDNADA-LNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYL 82


                  ....*....
gi 1889077420 445 EEVLATAPS 453
Cdd:COG3063    83 ERALELDPS 91
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 313-455 3.19e-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: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 313 DAAEKLRKKGKVEEAVRAFETLVLQYPQSPrcrYGkALAEDGLAEKMLSNDMLQKAIGTYKEASElpNATPDLIKATLKK 392
Cdd:COG2976    58 EQLLEALAAGDAAAAAAAAEKLIDDYGGTA---YA-ALAALLLAKAAVDAGDLDKAAAQLQWVLD--NAKDPALKALARL 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889077420 393 RAERQQF-LGRMRGALATLEklvQIFPED-MALKNDL-GVAHLLIGDNNSAKRVYEEVLATAPSDG 455
Cdd:COG2976   132 RLARVLLaQKKYDEALATLD---AVKPEAfAALYAELrGDILLAQGDKAEARAAYQKALAALPEDA 194
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 322-484 3.43e-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: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 322 GKVEEAVRAFETLVLQYPQSPrcrygKALAEdgLAEKMLSNDMLQKAIGTYKEASEL--------------------PNA 381
Cdd:TIGR02917 615 GDLNKAVSSFKKLLALQPDSA-----LALLL--LADAYAVMKNYAKAITSLKRALELkpdnteaqiglaqlllaakrTES 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889077420 382 TPDLIKATLKKR---AERQQFLGR--MR-----GALATLEKLVQIFPEDMALKNdLGVAHLLIGDNNSAKRVYEEVLATA 451
Cdd:TIGR02917 688 AKKIAKSLQKQHpkaALGFELEGDlyLRqkdypAAIQAYRKALKRAPSSQNAIK-LHRALLASGNTAEAVKTLEAWLKTH 766

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1889077420 452 PSDGFAKVHYGFILKSENKIAESIPFLRDGLES 484
Cdd:TIGR02917 767 PNDAVLRTALAELYLAQKDYDKAIKHYQTVVKK 799
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 315-381 7.69e-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: 36.89  E-value: 7.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889077420 315 AEKLRKKGKVEEAVRAFETLVLQYPQSPRC-----RYGKALAEDGLAEKmlSNDMLQKAIGTYKEASELPNA 381
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH