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Conserved domains on  [gi|927173031|ref|XP_013923374|]
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PREDICTED: aspartyl/asparaginyl beta-hydroxylase [Thamnophis sirtalis]

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 ...
 215-369 2.17e-75

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: 230.61  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  215 EKNWKVIRDEGLSVMDRSKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKSCALLERF-TEATGCRRGQIKY 291
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPgVKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927173031  292 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAEETRFWEEGKILIFDDSFEHEVWQDANAYRLIFIVDVWHP 369
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 49-172 2.69e-14

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: 69.45  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  49 RRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKI 128
Cdd:COG4783    9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 927173031 129 EESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG4783   89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALE 130
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 215-369 2.17e-75

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: 230.61  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  215 EKNWKVIRDEGLSVMDRSKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKSCALLERF-TEATGCRRGQIKY 291
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPgVKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927173031  292 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAEETRFWEEGKILIFDDSFEHEVWQDANAYRLIFIVDVWHP 369
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 214-372 2.36e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 181.23  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 214 LEKNWKVIRDEGLSVMDRSKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKSCALLERFteatgcrrGQ 288
Cdd:COG3555   23 LEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI--------PG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 289 IK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCAEETRFWEEGKILIFDDSFEHEVWQDANAYRLIFIV 364
Cdd:COG3555   95 VKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVVLFC 174


                 ....*...
gi 927173031 365 DVWHPELT 372
Cdd:COG3555  175 DVWRPMLS 182
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 49-172 2.69e-14

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: 69.45  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  49 RRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKI 128
Cdd:COG4783    9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 927173031 129 EESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG4783   89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALE 130
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 57-140 1.16e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031   57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:TIGR02917 580 KGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLK 659


                  ....
gi 927173031  137 EGLE 140
Cdd:TIGR02917 660 RALE 663
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 67-176 4.31e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 38.76  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  67 LQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKvhygfilksenkieesipylkeglesgdpgt 146
Cdd:cd24142   23 LQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK------------------------------- 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 927173031 147 ddgrfYFHLGdamQRVGNKEAYKWYELGYQ 176
Cdd:cd24142   72 -----YLYLG---QLSGGEEALQYYEKGIE 93
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 215-369 2.17e-75

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: 230.61  E-value: 2.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  215 EKNWKVIRDEGLSVMDRSKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACNSVPKSCALLERF-TEATGCRRGQIKY 291
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPgVKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927173031  292 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCRIRCAEETRFWEEGKILIFDDSFEHEVWQDANAYRLIFIVDVWHP 369
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 214-372 2.36e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 181.23  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 214 LEKNWKVIRDEGLSVMDRSKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACNSVPKSCALLERFteatgcrrGQ 288
Cdd:COG3555   23 LEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI--------PG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 289 IK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCRIRCAEETRFWEEGKILIFDDSFEHEVWQDANAYRLIFIV 364
Cdd:COG3555   95 VKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVVLFC 174


                 ....*...
gi 927173031 365 DVWHPELT 372
Cdd:COG3555  175 DVWRPMLS 182
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 49-172 2.69e-14

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: 69.45  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  49 RRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKI 128
Cdd:COG4783    9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 927173031 129 EESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG4783   89 DEALALLEKALKL-DP--EHPEAYLRLARAYRALGRpDEAIAALE 130
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
57-172 1.82e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.57  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG0457   21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 927173031 137 EGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG0457  101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 47-176 4.96e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 67.33  E-value: 4.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  47 LKRRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSEN 126
Cdd:COG3914   81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927173031 127 KIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYELGYQ 176
Cdd:COG3914  161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYRRALE 208
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 57-141 8.81e-12

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: 62.67  E-value: 8.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG5010   67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                 ....*
gi 927173031 137 EGLES 141
Cdd:COG5010  147 RALGT 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
57-190 3.74e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.72  E-value: 3.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG0457   55 LGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYE 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927173031 137 EGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYELGYQRGHFASVWQRSLYN 190
Cdd:COG0457  135 RALEL-DP--DDADALYNLGIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 22-184 5.94e-11

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: 62.44  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  22 LQRSITTYGEVANL-PNVPDVLVKMtlkrrADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKI 100
Cdd:COG2956   92 LDRAEELLEKLLELdPDDAEALRLL-----AEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 101 YQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYELGYQRGH 179
Cdd:COG2956  167 LEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLRKALELDP 243


                 ....*
gi 927173031 180 FASVW 184
Cdd:COG2956  244 SDDLL 248
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 57-140 7.19e-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: 56.74  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG4783   51 LGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALE 130


                 ....
gi 927173031 137 EGLE 140
Cdd:COG4783  131 KALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
71-172 1.03e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  71 VDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESgDPgtDDGR 150
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                         90       100
                 ....*....|....*....|...
gi 927173031 151 FYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG0457   78 ALNNLGLALQALGRyEEALEDYD 100
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 64-172 5.48e-09

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 53.86  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  64 LVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESgD 143
Cdd:COG4235    3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 927173031 144 PgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG4235   82 P--DNPEALYLLGLAAFQQGDyAEAIAAWQ 109
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 57-147 7.18e-09

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 53.86  E-value: 7.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG4235   30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                         90
                 ....*....|.
gi 927173031 137 EGLESGDPGTD 147
Cdd:COG4235  110 KLLALLPADAP 120
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
46-140 1.86e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.63  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  46 TLKRRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSE 125
Cdd:COG0457   78 ALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKL 157

                         90
                 ....*....|....*
gi 927173031 126 NKIEESIPYLKEGLE 140
Cdd:COG0457  158 GRYEEALELLEKLEA 172
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
88-172 2.41e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 51.32  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  88 YLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYlKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KE 166
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                 ....*.
gi 927173031 167 AYKWYE 172
Cdd:COG3063   78 ALAYLE 83
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 67-172 6.51e-08

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: 53.19  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  67 LQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESGDpgt 146
Cdd:COG2956   65 HQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGP--- 141

                         90       100
                 ....*....|....*....|....*..
gi 927173031 147 DDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG2956  142 ENAHAYCELAELYLEQGDyDEAIEALE 168
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
57-140 1.14e-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: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKiYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG3063    5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                 ....
gi 927173031 137 EGLE 140
Cdd:COG3063   84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 88-172 2.38e-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: 49.96  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  88 YLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESgDPgtDDGRFYFHLGDAMQRVGN-KE 166
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                 ....*.
gi 927173031 167 AYKWYE 172
Cdd:COG5010  141 AKAALQ 146
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 66-172 3.00e-05

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: 45.11  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  66 TLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESGDpg 145
Cdd:COG2956   30 LLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDP-- 107

                         90       100
                 ....*....|....*....|....*...
gi 927173031 146 tDDGRFYFHLGDAMQRVGN-KEAYKWYE 172
Cdd:COG2956  108 -DDAEALRLLAEIYEQEGDwEKAIEVLE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 57-109 4.80e-05

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.41  E-value: 4.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAP 109
Cdd:COG5010  101 SGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 57-154 4.34e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:COG3914  159 LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEE 238

                         90
                 ....*....|....*...
gi 927173031 137 EGLESGDPGTDDGRFYFH 154
Cdd:COG3914  239 LLAALARGPSELSPFALL 256
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 57-140 1.16e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031   57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:TIGR02917 580 KGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLK 659


                  ....
gi 927173031  137 EGLE 140
Cdd:TIGR02917 660 RALE 663
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 84-172 1.84e-03

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: 39.71  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  84 LGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGLESGDpgtDDGRFYFHLGDAMQRVG 163
Cdd:COG2956   14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDP---DRAEALLELAQDYLKAG 90

                         90
                 ....*....|
gi 927173031 164 N-KEAYKWYE 172
Cdd:COG2956   91 LlDRAEELLE 100
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 88-172 2.50e-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: 37.28  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  88 YLLIGDNNNAKKIYQEVLSLAPNDGFA-KVHY--GFILKSENKIEESIPYLKEGLESGDPGTDDGRFYFHLGDAMQRVGN 164
Cdd:COG1729    3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                 ....*....
gi 927173031 165 KE-AYKWYE 172
Cdd:COG1729   83 YDkARATLE 91
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
75-218 3.23e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 38.74  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  75 PNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPndGFAKVHY--GFILKSENKIEESIPYLKEGLESgDPgtDDGRFY 152
Cdd:COG4785   70 PDLAQLYYERGVAYDSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAY 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031 153 FHLGDAMQRVGN-KEAYKWYELGYQRGH---FASVWQrslynvnglkaqpWWTAKETGYTELIKSLEKNW 218
Cdd:COG4785  145 LNRGIALYYLGRyELAIADLEKALELDPndpERALWL-------------YLAERKLDPEKALALLLEDW 201
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 57-151 3.61e-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: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031   57 LGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLK 136
Cdd:TIGR02917 342 LGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLE 421

                          90
                  ....*....|....*
gi 927173031  137 EGLESGDPGTDDGRF 151
Cdd:TIGR02917 422 TAAQLDPELGRADLL 436
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 67-176 4.31e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 38.76  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  67 LQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKvhygfilksenkieesipylkeglesgdpgt 146
Cdd:cd24142   23 LQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK------------------------------- 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 927173031 147 ddgrfYFHLGdamQRVGNKEAYKWYELGYQ 176
Cdd:cd24142   72 -----YLYLG---QLSGGEEALQYYEKGIE 93
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 49-115 5.80e-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: 36.12  E-value: 5.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031  49 RRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKN---NLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAK 115
Cdd:COG1729   35 WLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDallKLGLSYLELGDYDKARATLEELIKKYPDSEAAK 104
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 68-145 6.08e-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: 38.91  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927173031   68 QKLVDLFPNDTSFKNN--------LGVGYLLIGDNNNAKKIYQEVLSLAPNDGFAKVHYGFILKSENKIEESIPYLKEGL 139
Cdd:TIGR02917 107 QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVL 186


                  ....*.
gi 927173031  140 eSGDPG 145
Cdd:TIGR02917 187 -TADPG 191
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
46-114 8.11e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 37.59  E-value: 8.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927173031  46 TLKRRADRQQFLGRMRGSLVTLQKLVDLFPNDTSFKNNLGVGYLLIGDNNNAKKIYQEVLSLAPNDGFA 114
Cdd:COG4785   75 LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
 
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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