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Conserved domains on  [gi|1621831544|gb|THG23875|]
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hypothetical protein TEA_023535 [Camellia sinensis var. sinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 101-248 1.80e-40

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member PLN02917:

Pssm-ID: 472172  Cd Length: 293  Bit Score: 145.75  E-value: 1.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLKKKKnvrhrgarsqvlgaavvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:PLN02917  107 FGADVIMTSESCRNGTERCNEALKKLEKKY-------------------------------------------------- 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621831544 181 rtrcnetlqklkkkknDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDACDPNRVK 248
Cdd:PLN02917  137 ----------------DIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVK 188
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
264-324 2.78e-15

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 75.38  E-value: 2.78e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642   169 DGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRH 229
Inhibitor_I29 super family cl48006
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 36-57 1.42e-03

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin Swiss:Q70SU8. This family is classified as I29 by MEROPS.


The actual alignment was detected with superfamily member pfam08246:

Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 36.47  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|..
gi 1621831544  36 FSLFKSKFGKSYATKEEHDHRF 57
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRF 22
 
Name Accession Description Interval E-value
PLN02917 PLN02917
CMP-KDO synthetase
 101-248 1.80e-40

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 145.75  E-value: 1.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLKKKKnvrhrgarsqvlgaavvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:PLN02917  107 FGADVIMTSESCRNGTERCNEALKKLEKKY-------------------------------------------------- 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621831544 181 rtrcnetlqklkkkknDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDACDPNRVK 248
Cdd:PLN02917  137 ----------------DIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVK 188
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 101-248 7.41e-21

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 90.61  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLKKKknvrhrgarsqvlgaavvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:cd02517    61 FGGKVVMTSPDHPSGTDRIAEVAEKLDAD--------------------------------------------------- 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621831544 181 rtrcnetlqklkkkkNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLK-PEDACDPNRVK 248
Cdd:cd02517    90 ---------------DDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISdEEELFNPNVVK 143
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 101-248 9.45e-18

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 82.03  E-value: 9.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNEtlqklkkkknvrhrgarsqvlgAAvvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:COG1212    62 FGGEVVMTSPDHPSGTDRIAE----------------------AA----------------------------------- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621831544 181 rtrcnetlQKLKKKKNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLK-PEDACDPNRVK 248
Cdd:COG1212    85 --------EKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITdEEELFNPNVVK 145
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
264-324 2.78e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 75.38  E-value: 2.78e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642   169 DGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRH 229
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 120-248 1.21e-09

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 58.39  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 120 NETLQKLKKKKNVRHRGARSQVLGAAVVSRRTSGEVYAGVPQAVwstcGGAGCPARRK-GSGRTRCNETLQKLKKKKNDV 198
Cdd:TIGR00466  15 GKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKF----GIEVCMTSKHhNSGTERLAEVVEKLALKDDER 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1621831544 199 VVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDACDPNRVK 248
Cdd:TIGR00466  91 IVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVK 140
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 259-324 1.85e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 56.38  E-value: 1.85e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621831544 259 KYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:PLN03185  117 KYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKD 182
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 169-248 6.69e-08

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 52.72  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 169 GAGCPARRKG--SGRTRCNETLQKLKKKKNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSL-KPEDACDPN 245
Cdd:pfam02348  60 GAGVVMTSGSlsSGTDRFYEVVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVgSAEEVLNAN 139


                  ...
gi 1621831544 246 RVK 248
Cdd:pfam02348 140 ALK 142
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
266-287 7.52e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 39.25  E-value: 7.52e-05
                           10        20
                   ....*....|....*....|..
gi 1621831544  266 DVYAGEYFADKMHGFGVYRFAN 287
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 268-288 7.09e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 36.62  E-value: 7.09e-04
                          10        20
                  ....*....|....*....|.
gi 1621831544 268 YAGEYFADKMHGFGVYRFANG 288
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 36-57 1.42e-03

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 36.47  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|..
gi 1621831544  36 FSLFKSKFGKSYATKEEHDHRF 57
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRF 22
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 36-57 1.59e-03

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 36.45  E-value: 1.59e-03
                           10        20
                   ....*....|....*....|..
gi 1621831544   36 FSLFKSKFGKSYATKEEHDHRF 57
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRF 22
 
Name Accession Description Interval E-value
PLN02917 PLN02917
CMP-KDO synthetase
 101-248 1.80e-40

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 145.75  E-value: 1.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLKKKKnvrhrgarsqvlgaavvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:PLN02917  107 FGADVIMTSESCRNGTERCNEALKKLEKKY-------------------------------------------------- 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621831544 181 rtrcnetlqklkkkknDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDACDPNRVK 248
Cdd:PLN02917  137 ----------------DIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVK 188
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 101-248 7.41e-21

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 90.61  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLKKKknvrhrgarsqvlgaavvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:cd02517    61 FGGKVVMTSPDHPSGTDRIAEVAEKLDAD--------------------------------------------------- 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621831544 181 rtrcnetlqklkkkkNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLK-PEDACDPNRVK 248
Cdd:cd02517    90 ---------------DDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISdEEELFNPNVVK 143
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 101-248 9.45e-18

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 82.03  E-value: 9.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNEtlqklkkkknvrhrgarsqvlgAAvvsrrtsgevyagvpqavwstcggagcparrkgsg 180
Cdd:COG1212    62 FGGEVVMTSPDHPSGTDRIAE----------------------AA----------------------------------- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621831544 181 rtrcnetlQKLKKKKNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLK-PEDACDPNRVK 248
Cdd:COG1212    85 --------EKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITdEEELFNPNVVK 145
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 101-248 3.34e-17

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 80.55  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 101 FGADVIMTSESCRNGTERCNETLQKLkkkknvrhrgarsqvlgaavvsrrtsgevyaGVPQAvwstcggagcparrkgsg 180
Cdd:PRK05450   61 FGGEVVMTSPDHPSGTDRIAEAAAKL-------------------------------GLADD------------------ 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621831544 181 rtrcnetlqklkkkknDVVVNIQGDEPLIDSDVIDGIVKALqATPDTVFSTAVTSLK-PEDACDPNRVK 248
Cdd:PRK05450   92 ----------------DIVVNVQGDEPLIPPEIIDQVAEPL-ANPEADMATLAVPIHdAEEAFNPNVVK 143
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
264-324 2.78e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 75.38  E-value: 2.78e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642   169 DGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRH 229
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
258-321 3.46e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 75.38  E-value: 3.46e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621831544 258 RKYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNG 321
Cdd:COG4642   140 GIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNG 203
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
259-324 4.10e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 74.99  E-value: 4.10e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621831544 259 KYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642   187 TLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRH 252
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
264-320 4.34e-15

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 74.99  E-value: 4.34e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNN 320
Cdd:COG4642   215 DGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEWKN 271
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 179-248 8.95e-13

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 67.68  E-value: 8.95e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621831544 179 SGRTRCNETLQKLKkkkNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDAC-DPNRVK 248
Cdd:PRK13368   75 SGTDRLAEVMLKIE---ADIYINVQGDEPMIRPRDIDTLIQPMLDDPSINVATLCAPISTEEEFeSPNVVK 142
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 120-248 1.21e-09

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 58.39  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 120 NETLQKLKKKKNVRHRGARSQVLGAAVVSRRTSGEVYAGVPQAVwstcGGAGCPARRK-GSGRTRCNETLQKLKKKKNDV 198
Cdd:TIGR00466  15 GKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKF----GIEVCMTSKHhNSGTERLAEVVEKLALKDDER 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1621831544 199 VVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSLKPEDACDPNRVK 248
Cdd:TIGR00466  91 IVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVK 140
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
247-324 2.04e-09

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 58.04  E-value: 2.04e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621831544 247 VKEKKIWEGMCRKYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642   106 GGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRH 183
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 259-324 1.85e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 56.38  E-value: 1.85e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621831544 259 KYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:PLN03185  117 KYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKD 182
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 260-321 2.04e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 56.38  E-value: 2.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1621831544 260 YGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNG 321
Cdd:PLN03185   72 YTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGG 133
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 169-248 6.69e-08

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 52.72  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 169 GAGCPARRKG--SGRTRCNETLQKLKKKKNDVVVNIQGDEPLIDSDVIDGIVKALQATPDTVFSTAVTSL-KPEDACDPN 245
Cdd:pfam02348  60 GAGVVMTSGSlsSGTDRFYEVVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVgSAEEVLNAN 139


                  ...
gi 1621831544 246 RVK 248
Cdd:pfam02348 140 ALK 142
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 264-323 1.06e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 50.99  E-value: 1.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGIL 323
Cdd:PLN03185   99 NGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMM 158
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 264-306 2.59e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 46.36  E-value: 2.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMY 306
Cdd:PLN03185  145 SGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
260-324 5.03e-05

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 44.56  E-value: 5.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621831544 260 YGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGILD 324
Cdd:COG4642    96 GGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPH 160
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
266-287 7.52e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 39.25  E-value: 7.52e-05
                           10        20
                   ....*....|....*....|..
gi 1621831544  266 DVYAGEYFADKMHGFGVYRFAN 287
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 264-333 3.41e-04

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 42.90  E-value: 3.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621831544 264 NGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHWNNGIL----DIPSTQNTTY 333
Cdd:PLN03185    7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMhgsgTYTGTDGTTY 80
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 268-288 7.09e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 36.62  E-value: 7.09e-04
                          10        20
                  ....*....|....*....|.
gi 1621831544 268 YAGEYFADKMHGFGVYRFANG 288
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDG 21
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
248-324 8.29e-04

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 40.05  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 248 KEKKIWEGMCRKYgNRNGDVYA-GEYFADKMHGFGVYRFANGH-WYEGAWHEGRRQGLGMYTFRNGETQS-GHWNNGILD 324
Cdd:COG2849    61 KYKKGKLGEWKTY-YPNGQLKSeGTYKNGKLEGEWKEYYENGKlKSEGNYKNGKLHGEWKEYYENGKLKEeGNYKNGKKD 139
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 36-57 1.42e-03

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 36.47  E-value: 1.42e-03
                          10        20
                  ....*....|....*....|..
gi 1621831544  36 FSLFKSKFGKSYATKEEHDHRF 57
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRF 22
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 36-57 1.59e-03

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 36.45  E-value: 1.59e-03
                           10        20
                   ....*....|....*....|..
gi 1621831544   36 FSLFKSKFGKSYATKEEHDHRF 57
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRF 22
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 291-313 1.66e-03

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 35.46  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|...
gi 1621831544 291 YEGAWHEGRRQGLGMYTFRNGET 313
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 259-318 1.72e-03

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 40.59  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621831544 259 KYGNRNGDVYAGEYFADKMHGFGVYRFANGHWYEGAWHEGRRQGLGMYTFRNGETQSGHW 318
Cdd:PLN03185   25 KYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRW 84
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
291-310 5.56e-03

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 34.24  E-value: 5.56e-03
                           10        20
                   ....*....|....*....|
gi 1621831544  291 YEGAWHEGRRQGLGMYTFRN 310
Cdd:smart00698   3 YEGEWRNGKRHGRGVYTYAN 22
 
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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