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Conserved domains on  [gi|2024475664|ref|XP_040522180|]
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aspartyl/asparaginyl beta-hydroxylase isoform X6 [Gallus gallus]

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 ...
 595-749 9.39e-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: 9.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 595 EKNWKLIRDEGLDVMDKKRSLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGVPKTCALLERFP-EATGCRRGQIKY 671
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024475664 672 SVMLPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAQENRTWEEGKVLIFDDSFEHEVWQDAESYRLIFIVDVWHP 749
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 29-94 5.25e-37

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: 132.66  E-value: 5.25e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024475664  29 NGKKEGLSGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 94
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 343-564 6.22e-19

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: 87.48  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 343 KTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARYGkaqseddLAEKMRSNEMLQKAINTYDEVVSL-PNVPSD 421
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELdPDDAEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 422 LIKLslkreADRQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFI 501
Cdd:COG2956   113 LRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024475664 502 LKAENKIAESIPYLKEGLESgDPgtDDGRFYFHLGDALQRIGD-KEAYKWYELGYQRGHFASVW 564
Cdd:COG2956   188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 97-308 5.54e-05

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.70  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664   97 ERSVPEQPASPVSEETIQPAEQSFTKSEHKNVDVELEEEIQpvlhdalhsqpgeghEDVDESISDQWQEKEEihaETFET 176
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVE---------------ENVEENVEENVEENVE---ENIEE 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664  177 PATDDTLRELEnEMTEDYETPDSFQKDADFVADDPGATEPETYEVPGDSELTLEDAVEHYTEPEYEK-ETETQDTAVEDL 255
Cdd:PTZ00341  1006 NVEENVEENIE-ENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEiEENIEENIEENV 1084

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024475664  256 PEEVHEATEPVRDETVEDLEMEKKLPVEskHTEEDNVAAGPEESeVPVQTEDY 308
Cdd:PTZ00341  1085 EENVEENVEEIEENVEENVEENAEENAE--ENAEENAEEYDDEN-PEEHNEEY 1134
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 595-749 9.39e-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: 9.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 595 EKNWKLIRDEGLDVMDKKRSLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGVPKTCALLERFP-EATGCRRGQIKY 671
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024475664 672 SVMLPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAQENRTWEEGKVLIFDDSFEHEVWQDAESYRLIFIVDVWHP 749
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 591-756 1.18e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 187.39  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 591 VKSLEKNWKLIRDEGLDVMDKKRSL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGVPKTCALLERFPeatgcr 665
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 666 rgQIK---YSVMLPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCAQENRTWEEGKVLIFDDSFEHEVWQDAESYRLI 741
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2024475664 742 FIVDVWHPELTAQQR 756
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 29-94 5.25e-37

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: 132.66  E-value: 5.25e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024475664  29 NGKKEGLSGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 94
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 343-564 6.22e-19

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: 87.48  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 343 KTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARYGkaqseddLAEKMRSNEMLQKAINTYDEVVSL-PNVPSD 421
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELdPDDAEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 422 LIKLslkreADRQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFI 501
Cdd:COG2956   113 LRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024475664 502 LKAENKIAESIPYLKEGLESgDPgtDDGRFYFHLGDALQRIGD-KEAYKWYELGYQRGHFASVW 564
Cdd:COG2956   188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 97-308 5.54e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.70  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664   97 ERSVPEQPASPVSEETIQPAEQSFTKSEHKNVDVELEEEIQpvlhdalhsqpgeghEDVDESISDQWQEKEEihaETFET 176
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVE---------------ENVEENVEENVEENVE---ENIEE 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664  177 PATDDTLRELEnEMTEDYETPDSFQKDADFVADDPGATEPETYEVPGDSELTLEDAVEHYTEPEYEK-ETETQDTAVEDL 255
Cdd:PTZ00341  1006 NVEENVEENIE-ENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEiEENIEENIEENV 1084

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024475664  256 PEEVHEATEPVRDETVEDLEMEKKLPVEskHTEEDNVAAGPEESeVPVQTEDY 308
Cdd:PTZ00341  1085 EENVEENVEEIEENVEENVEENAEENAE--ENAEENAEEYDDEN-PEEHNEEY 1134
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 342-525 2.94e-04

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.30  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 342 DKTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARY--GKAQSED-DL--AEKmrsnemlqkainTYDEVVSLp 416
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK------------ELRKALSL- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 417 NVPSDLIKLSLKREADRQ-QFlgrmrgslitlQKLVHLFPSDTSFKND--------LGVGYLLIGDNSNAKQVYEEVLRM 487
Cdd:TIGR02917  86 GYPKNQVLPLLARAYLLQgKF-----------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024475664 488 APDDGFAKVHYGFILKAENKIAESIPYLKEGLeSGDPG 525
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDEVL-TADPG 191
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 595-749 9.39e-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: 9.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 595 EKNWKLIRDEGLDVMDKKRSLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGVPKTCALLERFP-EATGCRRGQIKY 671
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024475664 672 SVMLPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAQENRTWEEGKVLIFDDSFEHEVWQDAESYRLIFIVDVWHP 749
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 591-756 1.18e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 187.39  E-value: 1.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 591 VKSLEKNWKLIRDEGLDVMDKKRSL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGVPKTCALLERFPeatgcr 665
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 666 rgQIK---YSVMLPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCAQENRTWEEGKVLIFDDSFEHEVWQDAESYRLI 741
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2024475664 742 FIVDVWHPELTAQQR 756
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 29-94 5.25e-37

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: 132.66  E-value: 5.25e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024475664  29 NGKKEGLSGSSFFTWFMVIALLGVWTSVAVVWFELVDYEEVLGKLGIYDADGDGDFDVEDAKVLLG 94
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 343-564 6.22e-19

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: 87.48  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 343 KTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARYGkaqseddLAEKMRSNEMLQKAINTYDEVVSL-PNVPSD 421
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELdPDDAEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 422 LIKLslkreADRQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFI 501
Cdd:COG2956   113 LRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024475664 502 LKAENKIAESIPYLKEGLESgDPgtDDGRFYFHLGDALQRIGD-KEAYKWYELGYQRGHFASVW 564
Cdd:COG2956   188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDPSDDLL 248
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 347-556 4.22e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 69.64  E-value: 4.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 347 AELDAAEKLRKKGKVEEALRAFEALVNQYPE--SPRARYGKAQSEDDLAEKMRSNEMLQKAINTYDEVvslpNVPSDLIK 424
Cdd:COG3914     3 AAALLALAALAAAALLAAAAAAELALAAELEaaALAAALGLALLLLAALAEAAAAALLALAAGEAAAA----AAALLLLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 425 LSLKREADRQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKA 504
Cdd:COG3914    79 ALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024475664 505 ENKIAESIPYLKEGLESgDPgtDDGRFYFHLGDALQRIGD-KEAYKWYELGYQ 556
Cdd:COG3914   159 LGRLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYRRALE 208
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
355-520 4.24e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 355 LRKKGKVEEALRAFEALVNQYPESPRARYGKAQSEDDLaekmrsnEMLQKAINTYDEVVSL-PNVPSDLIKLslkreADR 433
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRL-------GRYEEALADYEQALELdPDDAEALNNL-----GLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 434 QQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIP 513
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 2024475664 514 YLKEGLE 520
Cdd:COG0457   166 LLEKLEA 172
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
376-570 1.47e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.33  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 376 PESPRARYGKAQSEDDLAEkmrsnemLQKAINTYDEVVSL-PNVPSDLIKLSLKREAdrqqfLGRMRGSLITLQKLVHLF 454
Cdd:COG0457     5 PDDAEAYNNLGLAYRRLGR-------YEEAIEDYEKALELdPDDAEALYNLGLAYLR-----LGRYEEALADYEQALELD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 455 PSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLKEGLESgDPgtDDGRFYFH 534
Cdd:COG0457    73 PDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYN 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2024475664 535 LGDALQRIGD-KEAYKWYELGYQRGHFASVWQRSLYN 570
Cdd:COG0457   150 LGIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 347-520 4.61e-10

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: 58.28  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 347 AELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARYGKAQSeddlaekmrsnemlqkaintydevvslpnvpsdlikls 426
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI-------------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 427 lkreadrQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAEN 506
Cdd:COG4783    48 -------LLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                         170
                  ....*....|....
gi 2024475664 507 KIAESIPYLKEGLE 520
Cdd:COG4783   121 RPDEAIAALEKALE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 437-521 6.76e-09

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: 55.35  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 437 LGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLK 516
Cdd:COG5010    67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*
gi 2024475664 517 EGLES 521
Cdd:COG5010   147 RALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 447-552 1.11e-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: 54.24  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 447 LQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLKEGLESgDPgt 526
Cdd:COG4235     6 LRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-DP-- 82

                          90       100
                  ....*....|....*....|....*..
gi 2024475664 527 DDGRFYFHLGDALQRIGD-KEAYKWYE 552
Cdd:COG4235    83 DNPEALYLLGLAAFQQGDyAEAIAAWQ 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
451-552 9.90e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.86  E-value: 9.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 451 VHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLKEGLESgDPgtDDGR 530
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 2024475664 531 FYFHLGDALQRIGD-KEAYKWYE 552
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
468-552 1.89e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.40  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 468 YLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYlKEGLESgDPgtDDGRFYFHLGDALQRIGD-KE 546
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 2024475664 547 AYKWYE 552
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 437-527 3.59e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 49.62  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 437 LGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLK 516
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 2024475664 517 EGLESGDPGTD 527
Cdd:COG4235   110 KLLALLPADAP 120
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 468-552 4.39e-07

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 50.34  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 468 YLLIGDNSNAKQVYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLKEGLESgDPgtDDGRFYFHLGDALQRIGD-KE 546
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                  ....*.
gi 2024475664 547 AYKWYE 552
Cdd:COG5010   141 AKAALQ 146
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 354-456 4.59e-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: 48.83  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 354 KLRKKGKVEEALRAFEALVNQYPES---PRARYGKAQSeddlaekMRSNEMLQKAINTYDEVVSL-PNvpSDLIKLSLKR 429
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA-------YYALGDYDEAAEAFEKLLKRyPD--SPKAPDALLK 72

                          90       100
                  ....*....|....*....|....*..
gi 2024475664 430 EADRQQFLGRMRGSLITLQKLVHLFPS 456
Cdd:COG1729    73 LGLSYLELGDYDKARATLEELIKKYPD 99
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
437-520 8.92e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.78  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 437 LGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQvYEEVLRMAPDDGFAKVHYGFILKAENKIAESIPYLK 516
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 2024475664 517 EGLE 520
Cdd:COG3063    84 RALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 352-409 3.19e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.83  E-value: 3.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024475664 352 AEKLRKKGKVEEALRAFEALVNQYPES---PRARYGKAQSEDDLAEKMRSNEMLQKAINTY 409
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 97-308 5.54e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.70  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664   97 ERSVPEQPASPVSEETIQPAEQSFTKSEHKNVDVELEEEIQpvlhdalhsqpgeghEDVDESISDQWQEKEEihaETFET 176
Cdd:PTZ00341   944 EANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVE---------------ENVEENVEENVEENVE---ENIEE 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664  177 PATDDTLRELEnEMTEDYETPDSFQKDADFVADDPGATEPETYEVPGDSELTLEDAVEHYTEPEYEK-ETETQDTAVEDL 255
Cdd:PTZ00341  1006 NVEENVEENIE-ENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEiEENIEENIEENV 1084

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024475664  256 PEEVHEATEPVRDETVEDLEMEKKLPVEskHTEEDNVAAGPEESeVPVQTEDY 308
Cdd:PTZ00341  1085 EENVEENVEEIEENVEENVEENAEENAE--ENAEENAEEYDDEN-PEEHNEEY 1134
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 342-525 2.94e-04

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.30  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 342 DKTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARY--GKAQSED-DL--AEKmrsnemlqkainTYDEVVSLp 416
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK------------ELRKALSL- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 417 NVPSDLIKLSLKREADRQ-QFlgrmrgslitlQKLVHLFPSDTSFKND--------LGVGYLLIGDNSNAKQVYEEVLRM 487
Cdd:TIGR02917  86 GYPKNQVLPLLARAYLLQgKF-----------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024475664 488 APDDGFAKVHYGFILKAENKIAESIPYLKEGLeSGDPG 525
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDEVL-TADPG 191
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 347-489 1.34e-03

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.94  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 347 AELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARYGKAQSEDDLAEKMRSNemLQKAINTYDEVVSL-PNVPSDLIKL 425
Cdd:COG5010    17 LTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGD--FEESLALLEQALQLdPNNPELYYNL 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024475664 426 slkreADRQQFLGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAP 489
Cdd:COG5010    95 -----ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 350-455 1.57e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 41.00  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 350 DAAEKLRKKGKVEEALRAFEALVNQYPESPRARygkaQSEDDLAEKMRSNEMLQKAINTYDEVVSL----PNVP------ 419
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE----QAQLDLAYAYYKSGDYAEAIAAADRFIRLhpnhPDADyayylr 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2024475664 420 ----SDLIKLSlkreaDRQQflGRMRGSLITLQKLVHLFP 455
Cdd:TIGR03302 114 glsnYNQIDRV-----DRDQ--TAAREAFEAFQELIRRYP 146
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 342-455 3.08e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 40.25  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 342 DKTIKAELDAAEKLRKKGKVEEALRAFEALVNQYPESPRARygkaQSEDDLAE-KMRSNEMLQkAINTYDEVVSL----P 416
Cdd:COG4105    29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPYAE----QAQLMLAYaYYKQGDYEE-AIAAADRFIKLypnsP 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024475664 417 NVP-----SDLIKLSLKREADRQQflGRMRGSLITLQKLVHLFP 455
Cdd:COG4105   104 NADyayylRGLSYYEQSPDSDRDQ--TSTRKAIEAFQELINRYP 145
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 468-552 3.57e-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: 38.05  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 468 YLLIGDNSNAKQVYEEVLRMAPDDGFA-KVHY--GFILKAENKIAESIPYLKEGLESGDPGTDDGRFYFHLGDALQRIGD 544
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                  ....*....
gi 2024475664 545 KE-AYKWYE 552
Cdd:COG1729    83 YDkARATLE 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 355-457 4.79e-03

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: 38.25  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 355 LRKKGKVEEALRAFEALVNQYPESPRARYgkaqsedDLAEKMRSNEMLQKAINTYDEVVSL-PNVPSDLIKLslkreADR 433
Cdd:COG4783    48 LLQLGDLDEAIVLLHEALELDPDEPEARL-------NLGLALLKAGDYDEALALLEKALKLdPEHPEAYLRL-----ARA 115

                          90       100
                  ....*....|....*....|....
gi 2024475664 434 QQFLGRMRGSLITLQKLVHLFPSD 457
Cdd:COG4783   116 YRALGRPDEAIAALEKALELDPDD 139
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 352-457 6.49e-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: 37.68  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 352 AEKLRKKGKVEEALRAFEALVNQYPESPRARYgkaqsedDLAEKMRSNEMLQKAINTYDEVVSLpnVPSDLIKLSLKREA 431
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALL-------DLAEALLAAGDTEEAEELLERALAL--DPDNPEALYLLGLA 94

                          90       100
                  ....*....|....*....|....*.
gi 2024475664 432 DRQQflGRMRGSLITLQKLVHLFPSD 457
Cdd:COG4235    95 AFQQ--GDYAEAIAAWQKLLALLPAD 118
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 357-520 8.49e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 357 KKGKVEEALRAFEALVNQYPESPRARYGKA----QSEDDLAEKMRSNEMLQ------KAINTYDEVVSLPNVPSD-LIKL 425
Cdd:TIGR02917 477 GKGDLAKAREAFEKALSIEPDFFPAAANLAridiQEGNPDDAIQRFEKVLTidpknlRAILALAGLYLRTGNEEEaVAWL 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 426 SLKREADRQQF------------LGRMRGSLITLQKLVHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDDGF 493
Cdd:TIGR02917 557 EKAAELNPQEIepalalaqyylgKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSAL 636

                         170       180
                  ....*....|....*....|....*..
gi 2024475664 494 AKVHYGFILKAENKIAESIPYLKEGLE 520
Cdd:TIGR02917 637 ALLLLADAYAVMKNYAKAITSLKRALE 663
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
451-556 9.03e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 38.36  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024475664 451 VHLFPSDTSFKNDLGVGYLLIGDNSNAKQVYEEVLRMAPDdgFAKVHY--GFILKAENKIAESIPYLKEGLESgDPgtDD 528
Cdd:COG4785    66 ALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPD--LAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DY 140

                          90       100
                  ....*....|....*....|....*....
gi 2024475664 529 GRFYFHLGDALQRIGD-KEAYKWYELGYQ 556
Cdd:COG4785   141 AYAYLNRGIALYYLGRyELAIADLEKALE 169
 
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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